메뉴 건너뛰기




Volumn 65, Issue 1, 2001, Pages 1-105

Glutamate uptake

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; CYTOKINE; GLUTAMATE TRANSPORTER; GLUTAMIC ACID; GLUTATHIONE; GROWTH FACTOR; ION CHANNEL; MESSENGER RNA;

EID: 0035001341     PISSN: 03010082     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-0082(00)00067-8     Document Type: Review
Times cited : (4126)

References (1244)
  • 1
    • 0027175886 scopus 로고
    • Redistribution of glutamate and glutamine in slices of human neocortex exposed to combined hypoxia and glucose deprivation in vitro
    • Aas J.E., Berg-Johnsen J., Hegstad E., Laake J.H., Langmoen I.A., Ottersen O.P. Redistribution of glutamate and glutamine in slices of human neocortex exposed to combined hypoxia and glucose deprivation in vitro. J. Cereb. Blood Flow Metab. 13:1993;503-515.
    • (1993) J. Cereb. Blood Flow Metab. , vol.13 , pp. 503-515
    • Aas, J.E.1    Berg-Johnsen, J.2    Hegstad, E.3    Laake, J.H.4    Langmoen, I.A.5    Ottersen, O.P.6
  • 2
    • 0031021063 scopus 로고    scopus 로고
    • Alzheimer's disease research: A game of connect the dots
    • Adams C. Alzheimer's disease research: a game of connect the dots. Gerontology. 43:1997;8-19.
    • (1997) Gerontology , vol.43 , pp. 8-19
    • Adams, C.1
  • 3
    • 0031027249 scopus 로고    scopus 로고
    • Impairment of excitatory amino acid transporter activity by oxidative stress conditions in retinal cells: Effect of antioxidants
    • Agostinho P., Duarte C.B., Oliveira C.R. Impairment of excitatory amino acid transporter activity by oxidative stress conditions in retinal cells: Effect of antioxidants. FASEB J. 11:1997;154-163.
    • (1997) FASEB J. , vol.11 , pp. 154-163
    • Agostinho, P.1    Duarte, C.B.2    Oliveira, C.R.3
  • 5
    • 0031562362 scopus 로고    scopus 로고
    • Expression of glial glutamate transporters GLT-1 and GLAST is unchanged in the hippocampus in fully kindled rats
    • Akbar M.T., Torp R., Danbolt N.C., Levy L.M., Meldrum B.S., Ottersen O.P. Expression of glial glutamate transporters GLT-1 and GLAST is unchanged in the hippocampus in fully kindled rats. Neuroscience. 78:1997;351-359.
    • (1997) Neuroscience , vol.78 , pp. 351-359
    • Akbar, M.T.1    Torp, R.2    Danbolt, N.C.3    Levy, L.M.4    Meldrum, B.S.5    Ottersen, O.P.6
  • 6
    • 17644446163 scopus 로고    scopus 로고
    • Reduction of GABA and glutamate transporter messenger RNAs in the severe-seizure genetically epilepsy-prone rat
    • Akbar M.T., Rattray M., Williams R.J., Chong N.W.S., Meldrum B.S. Reduction of GABA and glutamate transporter messenger RNAs in the severe-seizure genetically epilepsy-prone rat. Neuroscience. 85:1998;1235-1251.
    • (1998) Neuroscience , vol.85 , pp. 1235-1251
    • Akbar, M.T.1    Rattray, M.2    Williams, R.J.3    Chong, N.W.S.4    Meldrum, B.S.5
  • 7
    • 0026609559 scopus 로고
    • Alternative excitotoxic hypotheses
    • Albin R.L., Greenamyre J.T. Alternative excitotoxic hypotheses. Neurology. 42:1992;733-738.
    • (1992) Neurology , vol.42 , pp. 733-738
    • Albin, R.L.1    Greenamyre, J.T.2
  • 8
    • 0029902775 scopus 로고    scopus 로고
    • Glutamate: A potential mediator of inorganic mercury neurotoxicity
    • Albrecht J., Matyja E. Glutamate: a potential mediator of inorganic mercury neurotoxicity. Metab. Brain. Dis. 11:1996;175-184.
    • (1996) Metab. Brain. Dis. , vol.11 , pp. 175-184
    • Albrecht, J.1    Matyja, E.2
  • 9
    • 0027400784 scopus 로고
    • The role of sulfhydryl groups and calcium in the mercuric chloride-induced inhibition of glutamate uptake in rat primary astrocyte cultures
    • Albrecht J., Talbot M., Kimelberg H.K., Aschner M. The role of sulfhydryl groups and calcium in the mercuric chloride-induced inhibition of glutamate uptake in rat primary astrocyte cultures. Brain Res. 607:1993;249-254.
    • (1993) Brain Res. , vol.607 , pp. 249-254
    • Albrecht, J.1    Talbot, M.2    Kimelberg, H.K.3    Aschner, M.4
  • 10
    • 0034099564 scopus 로고    scopus 로고
    • Elevated cortical extracellular fluid glutamate in transgenic mice expressing human mutant (G93A) Cu/Zn superoxide dismutase
    • Alexander G.M., Deitch J.S., Seeburger J.L., Del Valle L., Heiman-Patterson T.D. Elevated cortical extracellular fluid glutamate in transgenic mice expressing human mutant (G93A) Cu/Zn superoxide dismutase. J. Neurochem. 74:2000;1666-1673.
    • (2000) J. Neurochem. , vol.74 , pp. 1666-1673
    • Alexander, G.M.1    Deitch, J.S.2    Seeburger, J.L.3    Del Valle, L.4    Heiman-Patterson, T.D.5
  • 11
    • 0025171558 scopus 로고
    • Synthesis and activity of a potent N-methyl-D-aspartic acid agonist, trans-1-aminocyclobutane-1,3-dicarboxylic acid, and related phosphonic and carboxylic acids
    • Allan R.D., Hanrahan J.R., Hambley T.W., Johnston G.A.R., Mewett K.N., Mitrovic A.D. Synthesis and activity of a potent N-methyl-D-aspartic acid agonist, trans-1-aminocyclobutane-1,3-dicarboxylic acid, and related phosphonic and carboxylic acids. J. Med. Chem. 33:1990;2905-2915.
    • (1990) J. Med. Chem. , vol.33 , pp. 2905-2915
    • Allan, R.D.1    Hanrahan, J.R.2    Hambley, T.W.3    Johnston, G.A.R.4    Mewett, K.N.5    Mitrovic, A.D.6
  • 12
    • 84943442523 scopus 로고
    • Surgery of experimental lesion of spinal cord equivalent to crush injury of fracture dislocation of spinal column
    • Allen A.R. Surgery of experimental lesion of spinal cord equivalent to crush injury of fracture dislocation of spinal column. JAMA. 57:1911;878-880.
    • (1911) JAMA , vol.57 , pp. 878-880
    • Allen, A.R.1
  • 13
    • 0027253959 scopus 로고
    • Beta-N-methylamino-L-alanine in the presence of bicarbonate is an agonist at non-N-methyl-D-aspartate-type receptors
    • Allen C.N., Spencer P.S., Carpenter D.O. Beta-N-methylamino-L-alanine in the presence of bicarbonate is an agonist at non-N-methyl-D-aspartate-type receptors. Neuroscience. 54:1993;567-574.
    • (1993) Neuroscience , vol.54 , pp. 567-574
    • Allen, C.N.1    Spencer, P.S.2    Carpenter, D.O.3
  • 15
    • 0025284844 scopus 로고
    • Transmitter release from synapses: Does a preassembled fusion pore initiate exocytosis?
    • Almers W., Tse F.W. Transmitter release from synapses: does a preassembled fusion pore initiate exocytosis? Neuron. 4:1990;813-818.
    • (1990) Neuron , vol.4 , pp. 813-818
    • Almers, W.1    Tse, F.W.2
  • 16
    • 0019433958 scopus 로고
    • Development of the mossy fibers of the dentate gyrus: I. A light and electron microscopic study of the mossy fibers and their expansions
    • Amaral D.G., Dent J.A. Development of the mossy fibers of the dentate gyrus: I. A light and electron microscopic study of the mossy fibers and their expansions. J. Comp. Neurol. 195:1981;51-86.
    • (1981) J. Comp. Neurol. , vol.195 , pp. 51-86
    • Amaral, D.G.1    Dent, J.A.2
  • 17
    • 0028062679 scopus 로고
    • Intracellular pH changes produced by glutamate uptake in rat hippocampal slices
    • Amato A., Ballerini L., Attwell D. Intracellular pH changes produced by glutamate uptake in rat hippocampal slices. J. Neurophysiol. 72:1994;1686-1696.
    • (1994) J. Neurophysiol. , vol.72 , pp. 1686-1696
    • Amato, A.1    Ballerini, L.2    Attwell, D.3
  • 19
    • 0025988136 scopus 로고
    • Increased density of excitatory amino acid transport sites in the hippocampal formation following an entorhinal lesion
    • Anderson K.J., Bridges R.J., Cotman C.W. Increased density of excitatory amino acid transport sites in the hippocampal formation following an entorhinal lesion. Brain Res. 562:1991;285-290.
    • (1991) Brain Res. , vol.562 , pp. 285-290
    • Anderson, K.J.1    Bridges, R.J.2    Cotman, C.W.3
  • 23
    • 0030612096 scopus 로고    scopus 로고
    • 3H]D-aspartate binding to glutamate uptake sites in striatal and accumbens tissue in patients with schizophrenia
    • 3H]D-aspartate binding to glutamate uptake sites in striatal and accumbens tissue in patients with schizophrenia. Neurosci. Lett. 232:1997;13-16.
    • (1997) Neurosci. Lett. , vol.232 , pp. 13-16
    • Aparicio-Legarza, M.I.1    Cutts, A.J.2    Davis, B.3    Reynolds, G.P.4
  • 24
    • 0027329175 scopus 로고
    • Excitotoxic neuronal cell death in amyotrophic lateral sclerosis
    • Appel S.H. Excitotoxic neuronal cell death in amyotrophic lateral sclerosis. Trends Neurosci. 16:1993;3-5.
    • (1993) Trends Neurosci. , vol.16 , pp. 3-5
    • Appel, S.H.1
  • 25
    • 0029685043 scopus 로고    scopus 로고
    • Immune-mediated cell death in neurodegenerative disease
    • Appel S.H., Smith R.G., Le W.D. Immune-mediated cell death in neurodegenerative disease. Adv. Neurol. 69:1996;153-159.
    • (1996) Adv. Neurol. , vol.69 , pp. 153-159
    • Appel, S.H.1    Smith, R.G.2    Le, W.D.3
  • 26
    • 0034651087 scopus 로고    scopus 로고
    • SNARE protein-dependent glutamate release from astrocytes
    • Araque A., Li N.Z., Doyle R.T., Haydon P.G. SNARE protein-dependent glutamate release from astrocytes. J. Neurosci. 20:2000;666-673.
    • (2000) J. Neurosci. , vol.20 , pp. 666-673
    • Araque, A.1    Li, N.Z.2    Doyle, R.T.3    Haydon, P.G.4
  • 27
    • 0010283905 scopus 로고
    • A family series of fatal and dangerous cases of icterus neonatorum - Fourteen cases in one family, with four survivors
    • Arkwright J.A. A family series of fatal and dangerous cases of icterus neonatorum - fourteen cases in one family, with four survivors. Edinb. Med. J. 2:1902;156-158.
    • (1902) Edinb. Med. J. , vol.2 , pp. 156-158
    • Arkwright, J.A.1
  • 28
    • 0027327563 scopus 로고
    • Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family
    • Arriza J.L., Kavanaugh M.P., Fairman W.A., Wu Y.N., Murdoch G.H., North R.A., Amara S.G. Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J. Biol. Chem. 268:1993;15329-15332.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15329-15332
    • Arriza, J.L.1    Kavanaugh, M.P.2    Fairman, W.A.3    Wu, Y.N.4    Murdoch, G.H.5    North, R.A.6    Amara, S.G.7
  • 30
    • 0030932152 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance
    • Arriza J.L., Eliasof S., Kavanaugh M.P., Amara S.G. Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance. Proc. Natl. Acad. Sci. USA. 94:1997;4155-4160.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4155-4160
    • Arriza, J.L.1    Eliasof, S.2    Kavanaugh, M.P.3    Amara, S.G.4
  • 31
    • 0025011377 scopus 로고
    • Interactions of methylmercury with rat primary astrocyte cultures - Inhibition of rubidium and glutamate uptake and induction of swelling
    • Aschner M., Eberle N.B., Miller K., Kimelberg H.K. Interactions of methylmercury with rat primary astrocyte cultures - inhibition of rubidium and glutamate uptake and induction of swelling. Brain Res. 530:1990;245-250.
    • (1990) Brain Res. , vol.530 , pp. 245-250
    • Aschner, M.1    Eberle, N.B.2    Miller, K.3    Kimelberg, H.K.4
  • 32
    • 0027480552 scopus 로고
    • Methylmercury-induced alterations in excitatory amino acid transport in rat primary astrocyte cultures
    • Aschner M., Du Y.L., Gannon M., Kimelberg H.K. Methylmercury-induced alterations in excitatory amino acid transport in rat primary astrocyte cultures. Brain Res. 602:1993;181-186.
    • (1993) Brain Res. , vol.602 , pp. 181-186
    • Aschner, M.1    Du, Y.L.2    Gannon, M.3    Kimelberg, H.K.4
  • 34
    • 0034256934 scopus 로고    scopus 로고
    • Methylmercury alters glutamate transport in astrocytes
    • Aschner M., Yao C.P., Allen J.W., Tan K.H. Methylmercury alters glutamate transport in astrocytes. Neurochem. Int. 37:2000;199-206.
    • (2000) Neurochem. Int. , vol.37 , pp. 199-206
    • Aschner, M.1    Yao, C.P.2    Allen, J.W.3    Tan, K.H.4
  • 35
    • 0031046153 scopus 로고    scopus 로고
    • Extrasynaptic glutamate spillover in the hippocampus: Dependence on temperature and the role of active glutamate uptake
    • Asztely F., Erdemli G., Kullmann D.M. Extrasynaptic glutamate spillover in the hippocampus: dependence on temperature and the role of active glutamate uptake. Neuron. 18:1997;281-293.
    • (1997) Neuron , vol.18 , pp. 281-293
    • Asztely, F.1    Erdemli, G.2    Kullmann, D.M.3
  • 36
    • 0028291438 scopus 로고
    • Neurobiology-glia and neurons in dialogue
    • Attwell D. Neurobiology-glia and neurons in dialogue. Nature. 369:1994;707-708.
    • (1994) Nature , vol.369 , pp. 707-708
    • Attwell, D.1
  • 37
    • 26344480693 scopus 로고    scopus 로고
    • An energy budget for signalling in the grey matter of the brain
    • Attwell, D., Laughlin, S.B., 2000. An energy budget for signalling in the grey matter of the brain, J. Physiol. 525, 61P.
    • (2000) J. Physiol. , vol.525
    • Attwell, D.1    Laughlin, S.B.2
  • 38
    • 0343769581 scopus 로고
    • Patch-clamp studies of electrogenic glutamate uptake: Ionic dependence, modulation and failure in anoxia
    • H. Wheal, & A. Thomson. New York: Academic Press
    • Attwell D., Sarantis M., Szatkowski M., Barbour B., Brew H. Patch-clamp studies of electrogenic glutamate uptake: ionic dependence, modulation and failure in anoxia. Wheal H., Thomson A. Excitatory Amino Acids and Synaptic Transmission. 1991;223-237 Academic Press, New York.
    • (1991) Excitatory Amino Acids and Synaptic Transmission , pp. 223-237
    • Attwell, D.1    Sarantis, M.2    Szatkowski, M.3    Barbour, B.4    Brew, H.5
  • 39
    • 0033636982 scopus 로고    scopus 로고
    • Fast removal of synaptic glutamate by postsynaptic transporters
    • Auger C., Attwell D. Fast removal of synaptic glutamate by postsynaptic transporters. Neuron. 28:2000;547-558.
    • (2000) Neuron , vol.28 , pp. 547-558
    • Auger, C.1    Attwell, D.2
  • 41
    • 0034698248 scopus 로고    scopus 로고
    • Riluzole increases high-affinity glutamate uptake in rat spinal cord synaptosomes
    • Azbill R.D., Mu X., Springer J.E. Riluzole increases high-affinity glutamate uptake in rat spinal cord synaptosomes. Brain Res. 871:2000;175-180.
    • (2000) Brain Res. , vol.871 , pp. 175-180
    • Azbill, R.D.1    Mu, X.2    Springer, J.E.3
  • 42
    • 0032412545 scopus 로고    scopus 로고
    • Pathophysiology of the ischemic penumbra - Revision of a concept
    • Back T. Pathophysiology of the ischemic penumbra - revision of a concept. Cell. Mol. Neurobiol. 18:1998;621-638.
    • (1998) Cell. Mol. Neurobiol. , vol.18 , pp. 621-638
    • Back, T.1
  • 44
    • 0028018273 scopus 로고
    • Kainate receptor gene expression in the developing rat brain
    • Bahn S., Volk B., Wisden W. Kainate receptor gene expression in the developing rat brain. J. Neurosci. 14:1994;5525-5547.
    • (1994) J. Neurosci. , vol.14 , pp. 5525-5547
    • Bahn, S.1    Volk, B.2    Wisden, W.3
  • 45
    • 0027295901 scopus 로고
    • Excitatory amino acids in cerebrospinal fluid following traumatic brain injury in humans
    • Baker A.J., Moulton R.J., MacMillan V.H., Shedden P.M. Excitatory amino acids in cerebrospinal fluid following traumatic brain injury in humans. J. Neurosurg. 79:1993;369-372.
    • (1993) J. Neurosurg. , vol.79 , pp. 369-372
    • Baker, A.J.1    Moulton, R.J.2    MacMillan, V.H.3    Shedden, P.M.4
  • 46
    • 0026572491 scopus 로고
    • +-dependent high-affinity uptake of L-glutamate in cultured fibroblasts
    • +-dependent high-affinity uptake of L-glutamate in cultured fibroblasts. FEBS Lett. 300:1992;203-207.
    • (1992) FEBS Lett. , vol.300 , pp. 203-207
    • Balcar, V.J.1
  • 47
    • 0015455754 scopus 로고
    • Glutamate uptake by brain slices and its relation to the depolarization of neurones by acidic amino acids
    • Balcar V.J., Johnston G.A.R. Glutamate uptake by brain slices and its relation to the depolarization of neurones by acidic amino acids. J. Neurobiol. 3:1972a;295-301.
    • (1972) J. Neurobiol. , vol.3 , pp. 295-301
    • Balcar, V.J.1    Johnston, G.A.R.2
  • 48
    • 0015426691 scopus 로고
    • The structural specificity of the high affinity uptake of L-glutamate and L-aspartate by rat brain slices
    • Balcar V.J., Johnston G.A.R. The structural specificity of the high affinity uptake of L-glutamate and L-aspartate by rat brain slices. J. Neurochem. 19:1972b;2657-2666.
    • (1972) J. Neurochem. , vol.19 , pp. 2657-2666
    • Balcar, V.J.1    Johnston, G.A.R.2
  • 49
    • 0016690770 scopus 로고
    • High affinity uptake of L-glutamine in rat brain slices
    • Balcar V.J., Johnston G.A.R. High affinity uptake of L-glutamine in rat brain slices. J. Neurochem. 24:1975;875-879.
    • (1975) J. Neurochem. , vol.24 , pp. 875-879
    • Balcar, V.J.1    Johnston, G.A.R.2
  • 50
    • 0026705561 scopus 로고
    • Heterogeneity of high affinity uptake of L-glutamate and L-aspartate in the mammalian central nervous system
    • Balcar V.J., Li Y. Heterogeneity of high affinity uptake of L-glutamate and L-aspartate in the mammalian central nervous system. Life Sci. 51:1992;1467-1478.
    • (1992) Life Sci. , vol.51 , pp. 1467-1478
    • Balcar, V.J.1    Li, Y.2
  • 51
    • 0017389588 scopus 로고
    • Stereospecificity of the inhibition of L-glutamate and L-aspartate high affinity uptake in rat brain slices by threo-3-hydroxyaspartate
    • Balcar V.J., Johnston G.A.R., Twitchin B. Stereospecificity of the inhibition of L-glutamate and L-aspartate high affinity uptake in rat brain slices by threo-3-hydroxyaspartate. J. Neurochem. 28:1977;1145-1146.
    • (1977) J. Neurochem. , vol.28 , pp. 1145-1146
    • Balcar, V.J.1    Johnston, G.A.R.2    Twitchin, B.3
  • 52
    • 0028294291 scopus 로고
    • +-dependent high affinity uptake of L-glutamate is primary cultures of human fibroblasts isolated from three different types of tissue
    • +-dependent high affinity uptake of L-glutamate is primary cultures of human fibroblasts isolated from three different types of tissue. FEBS Lett. 339:1994;50-54.
    • (1994) FEBS Lett. , vol.339 , pp. 50-54
    • Balcar, V.J.1    Shen, J.2    Bao, S.S.3    King, N.J.C.4
  • 53
    • 0028987411 scopus 로고
    • 3H]alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA)
    • 3H]kainate studied by autoradiography in rat forebrain. Neurochem. Int. 26:1995;155-164.
    • (1995) Neurochem. Int. , vol.26 , pp. 155-164
    • Balcar, V.J.1    Li, Y.2    Killinger, S.3
  • 54
    • 0021215013 scopus 로고
    • Transport of cystine and cysteine in mammalian cells
    • Bannai S. Transport of cystine and cysteine in mammalian cells. Biochim. Biophys. Acta. 779:1984;289-306.
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 289-306
    • Bannai, S.1
  • 55
    • 0022969399 scopus 로고
    • Exchange of cystine and glutamate across plasma membrane of human fibroblasts
    • Bannai S. Exchange of cystine and glutamate across plasma membrane of human fibroblasts. J. Biol. Chem. 261:1986;2256-2263.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2256-2263
    • Bannai, S.1
  • 56
    • 0018963749 scopus 로고
    • Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture
    • Bannai S., Kitamura E. Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture. J. Biol. Chem. 255:1980;2372-2376.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2372-2376
    • Bannai, S.1    Kitamura, E.2
  • 57
    • 0019410188 scopus 로고
    • Role of proton dissociation in the transport of cystine and glutamine in human diploid fibroblasts in culture
    • Bannai S., Kitamura E. Role of proton dissociation in the transport of cystine and glutamine in human diploid fibroblasts in culture. J. Biol. Chem. 256:1981;5770-5772.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5770-5772
    • Bannai, S.1    Kitamura, E.2
  • 61
    • 0343376117 scopus 로고    scopus 로고
    • Intersynaptic diffusion of neurotransmitter
    • Barbour B., Häusser M. Intersynaptic diffusion of neurotransmitter. Trends Neurosci. 20:1997;377-384.
    • (1997) Trends Neurosci. , vol.20 , pp. 377-384
    • Barbour, B.1    Häusser, M.2
  • 62
    • 0023678757 scopus 로고
    • Electrogenic glutamate uptake in glial cells is activated by intracellular potassium
    • Barbour B., Brew H., Attwell D. Electrogenic glutamate uptake in glial cells is activated by intracellular potassium. Nature. 335:1988;433-435.
    • (1988) Nature , vol.335 , pp. 433-435
    • Barbour, B.1    Brew, H.2    Attwell, D.3
  • 63
    • 0024822252 scopus 로고
    • Arachidonic acid induces a prolonged inhibition of glutamate uptake into glial cells
    • Barbour B., Szatkowski M., Ingledew N., Attwell D. Arachidonic acid induces a prolonged inhibition of glutamate uptake into glial cells. Nature. 342:1989;918-920.
    • (1989) Nature , vol.342 , pp. 918-920
    • Barbour, B.1    Szatkowski, M.2    Ingledew, N.3    Attwell, D.4
  • 64
    • 0025765234 scopus 로고
    • Electrogenic uptake of glutamate and aspartate into glial cells isolated from the salamander (Ambystoma) retina
    • Barbour B., Brew H., Attwell D. Electrogenic uptake of glutamate and aspartate into glial cells isolated from the salamander (Ambystoma) retina. J. Physiol. (Lond.). 436:1991;169-193.
    • (1991) J. Physiol. (Lond.) , vol.436 , pp. 169-193
    • Barbour, B.1    Brew, H.2    Attwell, D.3
  • 65
    • 0028238967 scopus 로고
    • Prolonged presence of glutamate during excitatory synaptic transmission to cerebellar Purkinje cells
    • Barbour B., Keller B.U., Llano I., Marty A. Prolonged presence of glutamate during excitatory synaptic transmission to cerebellar Purkinje cells. Neuron. 12:1994;1331-1343.
    • (1994) Neuron , vol.12 , pp. 1331-1343
    • Barbour, B.1    Keller, B.U.2    Llano, I.3    Marty, A.4
  • 66
    • 0031948064 scopus 로고    scopus 로고
    • An altered invariant chain protein with an antigenic peptide in place of CLIP forms SDS-stable complexes with class II alpha beta dimers and facilitates highly efficient peptide loading
    • Barton G.M., Rudensky A.Y. An altered invariant chain protein with an antigenic peptide in place of CLIP forms SDS-stable complexes with class II alpha beta dimers and facilitates highly efficient peptide loading. Int. Immunol. 10:1998;1159-1165.
    • (1998) Int. Immunol. , vol.10 , pp. 1159-1165
    • Barton, G.M.1    Rudensky, A.Y.2
  • 67
    • 0034020619 scopus 로고    scopus 로고
    • Glutamine and glutamate exchange between the fetal liver and the placenta
    • Battaglia F.C. Glutamine and glutamate exchange between the fetal liver and the placenta. J. Nutr. 130:2000;974S-977S.
    • (2000) J. Nutr. , vol.130
    • Battaglia, F.C.1
  • 68
    • 0019394905 scopus 로고
    • 3H]glutamate binding sites in rat hippocampal membranes
    • 3H]glutamate binding sites in rat hippocampal membranes. J. Neurochem. 36:1981;811-820.
    • (1981) J. Neurochem. , vol.36 , pp. 811-820
    • Baudry, M.1    Lynch, G.2
  • 69
    • 0019186424 scopus 로고
    • Aspartate and glutamate as possible neurotransmitters of cells in layer 6 of the visual cortex
    • Baughman R.W., Gilbert C.D. Aspartate and glutamate as possible neurotransmitters of cells in layer 6 of the visual cortex. Nature. 287:1980;848-850.
    • (1980) Nature , vol.287 , pp. 848-850
    • Baughman, R.W.1    Gilbert, C.D.2
  • 70
    • 0028802503 scopus 로고
    • Mediators of injury in neurotrauma: Intracellular signal transduction and gene expression
    • Bazan N.G., Deturco E.B.R., Allan G. Mediators of injury in neurotrauma: intracellular signal transduction and gene expression. J. Neurotrauma. 12:1995;791-814.
    • (1995) J. Neurotrauma , vol.12 , pp. 791-814
    • Bazan, N.G.1    Deturco, E.B.R.2    Allan, G.3
  • 71
    • 0027477946 scopus 로고
    • Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases
    • Beal M.F., Hyman B.T., Koroshetz W. Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases. Trends Neurosci. 16:1993;125-131.
    • (1993) Trends Neurosci. , vol.16 , pp. 125-131
    • Beal, M.F.1    Hyman, B.T.2    Koroshetz, W.3
  • 72
    • 0032127681 scopus 로고    scopus 로고
    • Neurotransmitter transporters: Regulators of function and functional regulation
    • Beckman M.L., Quick M.W. Neurotransmitter transporters: regulators of function and functional regulation. J. Membr. Biol. 164:1998;1-10.
    • (1998) J. Membr. Biol. , vol.164 , pp. 1-10
    • Beckman, M.L.1    Quick, M.W.2
  • 73
    • 0033556396 scopus 로고    scopus 로고
    • Interindividual differences in the levels of the glutamate transporters GLAST and GLT, but no clear correlation with Alzheimer's disease
    • Beckstrøm H., Julsrud L., Haugeto Ø., Dewar D., Graham D.I., Lehre K.P., Storm-Mathisen J., Danbolt N.C. Interindividual differences in the levels of the glutamate transporters GLAST and GLT, but no clear correlation with Alzheimer's disease. J. Neurosci. Res. 55:1999;218-229.
    • (1999) J. Neurosci. Res. , vol.55 , pp. 218-229
    • Beckstrøm, H.1    Julsrud, L.2    Haugeto Ø3    Dewar, D.4    Graham, D.I.5    Lehre, K.P.6    Storm-Mathisen, J.7    Danbolt, N.C.8
  • 75
    • 0032211134 scopus 로고    scopus 로고
    • The localization of the brain-specific inorganic phosphate transporter suggests a specific presynaptic role in glutamatergic transmission
    • Bellocchio E.E., Hu H., Pohorille A., Chan J., Pickel V.M., Edwards R.H. The localization of the brain-specific inorganic phosphate transporter suggests a specific presynaptic role in glutamatergic transmission. J. Neurosci. 18:1998;8648-8659.
    • (1998) J. Neurosci. , vol.18 , pp. 8648-8659
    • Bellocchio, E.E.1    Hu, H.2    Pohorille, A.3    Chan, J.4    Pickel, V.M.5    Edwards, R.H.6
  • 76
    • 0034637146 scopus 로고    scopus 로고
    • Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter
    • Bellocchio E.E., Reimer R.J., Fremeau R.T.J.r., Edwards R.H. Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter. Science. 289:2000;957-960.
    • (2000) Science , vol.289 , pp. 957-960
    • Bellocchio, E.E.1    Reimer, R.J.2    Fremeau, R.T.J.R.3    Edwards, R.H.4
  • 77
    • 0034529012 scopus 로고    scopus 로고
    • Arginine-447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter
    • Bendahan A., Armon A., Madani N., Kavanaugh M.P., Kanner B.I. Arginine-447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter. J. Biol. Chem. 275:2000;37436-37442.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37436-37442
    • Bendahan, A.1    Armon, A.2    Madani, N.3    Kavanaugh, M.P.4    Kanner, B.I.5
  • 78
    • 0024363933 scopus 로고
    • Beta-DL-methylene-aspartate, an inhibitor of aspartate aminotransferase, potently inhibits L-glutamate uptake into astrocytes
    • Bender A.S., Woodbury D.M., White H.S. Beta-DL-methylene-aspartate, an inhibitor of aspartate aminotransferase, potently inhibits L-glutamate uptake into astrocytes. Neurochem. Res. 14:1989;641-646.
    • (1989) Neurochem. Res. , vol.14 , pp. 641-646
    • Bender, A.S.1    Woodbury, D.M.2    White, H.S.3
  • 79
    • 0017262503 scopus 로고
    • Cerebral uptakes and exchange diffusion in vitro of L- And D-glutamates
    • Benjamin A.M., Quastel J.H. Cerebral uptakes and exchange diffusion in vitro of L- and D-glutamates. J. Neurochem. 26:1976;431-441.
    • (1976) J. Neurochem. , vol.26 , pp. 431-441
    • Benjamin, A.M.1    Quastel, J.H.2
  • 80
    • 0015712111 scopus 로고
    • Amino acids as central nervous transmitters: The influence of ions, amino acid analogues and ontogeny on transport systems for L-glutamic and L-aspartic acids and glycine into central nervous synaptosomes of the rat
    • Bennett J.P. Jr, Logan W.J., Snyder S.H. Amino acids as central nervous transmitters: the influence of ions, amino acid analogues and ontogeny on transport systems for L-glutamic and L-aspartic acids and glycine into central nervous synaptosomes of the rat. J. Neurochem. 21:1973;1533-1550.
    • (1973) J. Neurochem. , vol.21 , pp. 1533-1550
    • Bennett J.P., Jr.1    Logan, W.J.2    Snyder, S.H.3
  • 81
    • 0021707433 scopus 로고
    • Elevation of the extracellular concentrations of glutamate and aspartate in rat hippocampus during transient cerebral ischemia monitored by intracerebral microdialysis
    • Benveniste H., Drejer J., Schousboe A., Diemer N.H. Elevation of the extracellular concentrations of glutamate and aspartate in rat hippocampus during transient cerebral ischemia monitored by intracerebral microdialysis. J. Neurochem. 43:1984;1369-1374.
    • (1984) J. Neurochem. , vol.43 , pp. 1369-1374
    • Benveniste, H.1    Drejer, J.2    Schousboe, A.3    Diemer, N.H.4
  • 83
    • 0033981056 scopus 로고    scopus 로고
    • Detection and cellular localization of enterovirus RNA sequences in spinal cord of patients with ALS
    • Berger M.M., Kopp N., Vital C., Redl B., Aymard M., Lina B. Detection and cellular localization of enterovirus RNA sequences in spinal cord of patients with ALS. Neurology. 54:2000;20-25.
    • (2000) Neurology , vol.54 , pp. 20-25
    • Berger, M.M.1    Kopp, N.2    Vital, C.3    Redl, B.4    Aymard, M.5    Lina, B.6
  • 84
    • 0031853290 scopus 로고    scopus 로고
    • Comparative analysis of glutamate transporter expression in rat brain using differential double in situ hybridization
    • Berger U.V., Hediger M.A. Comparative analysis of glutamate transporter expression in rat brain using differential double in situ hybridization. Anat. Embryol. 198:1998;13-30.
    • (1998) Anat. Embryol. , vol.198 , pp. 13-30
    • Berger, U.V.1    Hediger, M.A.2
  • 85
    • 0034608271 scopus 로고    scopus 로고
    • Distribution of the glutamate transporters GLAST and GLT-1 in rat circumventricular organs, meninges and dorsal root ganglia
    • Berger U.V., Hediger M.A. Distribution of the glutamate transporters GLAST and GLT-1 in rat circumventricular organs, meninges and dorsal root ganglia. J. Comp. Neurol. 421:2000;385-399.
    • (2000) J. Comp. Neurol. , vol.421 , pp. 385-399
    • Berger, U.V.1    Hediger, M.A.2
  • 86
    • 0034608271 scopus 로고    scopus 로고
    • Distribution of the glutamate transporters GLAST and GLT-1 in rat circumventricular organs, meninges and dorsal root ganglia
    • Berger U.V., Hediger M.A. Distribution of the glutamate transporters GLAST and GLT-1 in rat circumventricular organs, meninges and dorsal root ganglia. J. Comp. Neurol. 421:2000;385-399.
    • (2000) J. Comp. Neurol. , vol.421 , pp. 385-399
    • Berger, U.V.1    Hediger, M.A.2
  • 87
    • 0031472475 scopus 로고    scopus 로고
    • Synaptic activation of glutamate transporters in hippocampal astrocytes
    • Bergles D.E., Jahr C.E. Synaptic activation of glutamate transporters in hippocampal astrocytes. Neuron. 19:1997;1297-1308.
    • (1997) Neuron , vol.19 , pp. 1297-1308
    • Bergles, D.E.1    Jahr, C.E.2
  • 88
    • 0032189544 scopus 로고    scopus 로고
    • Glial contribution to glutamate uptake at Schaffer collateral-commissural synapses in the hippocampus
    • Bergles D.E., Jahr C.E. Glial contribution to glutamate uptake at Schaffer collateral-commissural synapses in the hippocampus. J. Neurosci. 18:1998;7709-7716.
    • (1998) J. Neurosci. , vol.18 , pp. 7709-7716
    • Bergles, D.E.1    Jahr, C.E.2
  • 89
    • 0031434844 scopus 로고    scopus 로고
    • Glutamate transporter currents in Bergmann glial cells follow the time course of extrasynaptic glutamate
    • Bergles D.E., Dzubay J.A., Jahr C.E. Glutamate transporter currents in Bergmann glial cells follow the time course of extrasynaptic glutamate. Proc. Natl. Acad. Sci. USA. 94:1997;14821-14825.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14821-14825
    • Bergles, D.E.1    Dzubay, J.A.2    Jahr, C.E.3
  • 91
    • 0034636493 scopus 로고    scopus 로고
    • Glutamatergic synapses on oligodendrocyte precursor cells in the hippocampus
    • Bergles D.E., Roberts J.D., Somogyi P., Jahr C.E. Glutamatergic synapses on oligodendrocyte precursor cells in the hippocampus. Nature. 405:2000;187-191.
    • (2000) Nature , vol.405 , pp. 187-191
    • Bergles, D.E.1    Roberts, J.D.2    Somogyi, P.3    Jahr, C.E.4
  • 92
    • 84982337275 scopus 로고
    • Amino acid and protein metabolism. VI. Cerebral compartments of glutamic acid metabolism
    • Berl S., Lajtha A., Waelsch H. Amino acid and protein metabolism. VI. Cerebral compartments of glutamic acid metabolism. J. Neurochem. 7:1961;186-197.
    • (1961) J. Neurochem. , vol.7 , pp. 186-197
    • Berl, S.1    Lajtha, A.2    Waelsch, H.3
  • 93
    • 73049161747 scopus 로고
    • Metabolic compartments in vivo: Ammonia and glutamic acid metabolism in brain and liver
    • Berl S., Takagaki G., Clarke D.D., Waelsch H. Metabolic compartments in vivo: ammonia and glutamic acid metabolism in brain and liver. J. Biol. Chem. 237:1962;2562-2569.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2562-2569
    • Berl, S.1    Takagaki, G.2    Clarke, D.D.3    Waelsch, H.4
  • 94
    • 0030857351 scopus 로고    scopus 로고
    • Inhibition of glutamate transport in synaptosomes by dopamine oxidation and reactive oxygen species
    • Berman S.B., Hastings T.G. Inhibition of glutamate transport in synaptosomes by dopamine oxidation and reactive oxygen species. J. Neurochem. 69:1997;1185-1195.
    • (1997) J. Neurochem. , vol.69 , pp. 1185-1195
    • Berman, S.B.1    Hastings, T.G.2
  • 95
    • 0030739639 scopus 로고    scopus 로고
    • Domoic acid neurotoxicity in cultured cerebellar granule neurons is mediated predominantly by NMDA receptors that are activated as a consequence of excitatory amino acid release
    • Berman F.W., Murray T.F. Domoic acid neurotoxicity in cultured cerebellar granule neurons is mediated predominantly by NMDA receptors that are activated as a consequence of excitatory amino acid release. J. Neurochem. 69:1997;693-703.
    • (1997) J. Neurochem. , vol.69 , pp. 693-703
    • Berman, F.W.1    Murray, T.F.2
  • 96
    • 0033534449 scopus 로고    scopus 로고
    • Regulation of gamma-aminobutyric acid (GABA) transporters by extracellular GABA
    • Bernstein E.M., Quick M.W. Regulation of gamma-aminobutyric acid (GABA) transporters by extracellular GABA. J. Biol. Chem. 274:1999;889-895.
    • (1999) J. Biol. Chem. , vol.274 , pp. 889-895
    • Bernstein, E.M.1    Quick, M.W.2
  • 97
    • 0026520891 scopus 로고
    • Evidence for a glutamate receptor of the AMPA subtype which mediates insulin release from rat perfused pancreas
    • Bertrand G., Gross R., Puech R., Loubatieres-Mariani M.M., Bockaert J. Evidence for a glutamate receptor of the AMPA subtype which mediates insulin release from rat perfused pancreas. Br. J. Pharmacol. 106:1992;354-359.
    • (1992) Br. J. Pharmacol. , vol.106 , pp. 354-359
    • Bertrand, G.1    Gross, R.2    Puech, R.3    Loubatieres-Mariani, M.M.4    Bockaert, J.5
  • 98
    • 0027302112 scopus 로고
    • Glutamate stimulates glucagon secretion via an excitatory amino acid receptor of the AMPA subtype in rat pancreas
    • Bertrand G., Gross R., Puech R., Loubatieres-Mariani M.M., Bockaert J. Glutamate stimulates glucagon secretion via an excitatory amino acid receptor of the AMPA subtype in rat pancreas. Eur. J. Pharmacol. 237:1993;45-50.
    • (1993) Eur. J. Pharmacol. , vol.237 , pp. 45-50
    • Bertrand, G.1    Gross, R.2    Puech, R.3    Loubatieres-Mariani, M.M.4    Bockaert, J.5
  • 99
    • 0028833216 scopus 로고
    • Glutamate stimulates insulin secretion and improves glucose tolerance in rats
    • Bertrand G., Puech R., Loubatieresmariani M.M., Bockaert J. Glutamate stimulates insulin secretion and improves glucose tolerance in rats. Am. J. Physiol. 32:1995;E551-E556.
    • (1995) Am. J. Physiol. , vol.32 , pp. 551-E556
    • Bertrand, G.1    Puech, R.2    Loubatieresmariani, M.M.3    Bockaert, J.4
  • 100
    • 0032992792 scopus 로고    scopus 로고
    • Identification and structural characterization of two genes encoding glutamate transporter homologues differently expressed in the nervous system of Drosophila melanogaster
    • Besson M.T., Soustelle L., Birman S. Identification and structural characterization of two genes encoding glutamate transporter homologues differently expressed in the nervous system of Drosophila melanogaster. FEBS Lett. 443:1999;97-104.
    • (1999) FEBS Lett. , vol.443 , pp. 97-104
    • Besson, M.T.1    Soustelle, L.2    Birman, S.3
  • 102
    • 0027241403 scopus 로고
    • Structural requirements for the development of potent N-methyl-D-aspartic acid (NMDA) receptor antagonists
    • Bigge C.F. Structural requirements for the development of potent N-methyl-D-aspartic acid (NMDA) receptor antagonists. Biochem. Pharmacol. 45:1993;1547-1561.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 1547-1561
    • Bigge, C.F.1
  • 103
    • 0030048785 scopus 로고    scopus 로고
    • Modulation of non-vesicular glutamate release by pH
    • Billups B., Attwell D. Modulation of non-vesicular glutamate release by pH. Nature. 379:1996;171-174.
    • (1996) Nature , vol.379 , pp. 171-174
    • Billups, B.1    Attwell, D.2
  • 104
    • 0029973191 scopus 로고    scopus 로고
    • Anion conductance behavior of the glutamate uptake carrier in salamander retinal glial cells
    • Billups B., Rossi D., Attwell D. Anion conductance behavior of the glutamate uptake carrier in salamander retinal glial cells. J. Neurosci. 16:1996;6722-6731.
    • (1996) J. Neurosci. , vol.16 , pp. 6722-6731
    • Billups, B.1    Rossi, D.2    Attwell, D.3
  • 105
    • 0031717627 scopus 로고    scopus 로고
    • Patch-clamp, ion-sensing, and glutamate-sensing techniques to study glutamate transport in isolated retinal glial cells
    • Billups B., Szatkowski M., Rossi D., Attwell D. Patch-clamp, ion-sensing, and glutamate-sensing techniques to study glutamate transport in isolated retinal glial cells. Methods Enzymol. 296:1998;617-632.
    • (1998) Methods Enzymol. , vol.296 , pp. 617-632
    • Billups, B.1    Szatkowski, M.2    Rossi, D.3    Attwell, D.4
  • 108
    • 0031870450 scopus 로고    scopus 로고
    • Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer
    • Blackman S.M., Piston D.W., Beth A.H. Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer. Biophys. J. 75:1998;1117-1130.
    • (1998) Biophys. J. , vol.75 , pp. 1117-1130
    • Blackman, S.M.1    Piston, D.W.2    Beth, A.H.3
  • 109
    • 73049129675 scopus 로고
    • Special axo-dendritic synapses in the hippocampal cortex: Electron and light microscopic studies of the layer of mossy fibers
    • Blackstad T.W., Kjaerheim A. Special axo-dendritic synapses in the hippocampal cortex: electron and light microscopic studies of the layer of mossy fibers. J. Comp. Neurol. 117:1961;133-159.
    • (1961) J. Comp. Neurol. , vol.117 , pp. 133-159
    • Blackstad, T.W.1    Kjaerheim, A.2
  • 110
    • 0025890297 scopus 로고
    • Vaccinia-T7 RNA polymerase expression system: Evaluation for the expression cloning of plasma membrane transporters
    • Blakely R.D., Clark J.A., Rudnick G., Amara S.G. Vaccinia-T7 RNA polymerase expression system: evaluation for the expression cloning of plasma membrane transporters. Anal. Biochem. 194:1991;302-308.
    • (1991) Anal. Biochem. , vol.194 , pp. 302-308
    • Blakely, R.D.1    Clark, J.A.2    Rudnick, G.3    Amara, S.G.4
  • 112
    • 0032005805 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, a lipid peroxidation product, impairs glutamate transport in cortical astrocytes
    • Blanc E.M., Keller J.N., Fernandez S., Mattson M.P. 4-Hydroxynonenal, a lipid peroxidation product, impairs glutamate transport in cortical astrocytes. Glia. 22:1998;149-160.
    • (1998) Glia , vol.22 , pp. 149-160
    • Blanc, E.M.1    Keller, J.N.2    Fernandez, S.3    Mattson, M.P.4
  • 113
    • 0032712791 scopus 로고    scopus 로고
    • Kainate receptor pharmacology and physiology
    • Bleakman D. Kainate receptor pharmacology and physiology. Cell. Mol. Life Sci. 56:1999;558-566.
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 558-566
    • Bleakman, D.1
  • 114
    • 0032828311 scopus 로고    scopus 로고
    • Pathophysiology of cerebral edema in fulminant hepatic failure
    • Blei A.T., Larsen F.S. Pathophysiology of cerebral edema in fulminant hepatic failure. J. Hepatol. 31:1999;771-776.
    • (1999) J. Hepatol. , vol.31 , pp. 771-776
    • Blei, A.T.1    Larsen, F.S.2
  • 115
    • 0029815360 scopus 로고    scopus 로고
    • The glutamate transport inhibitor L-trans-pyrrolidine-2,4-dicarboxylate indirectly evokes NMDA receptor mediated neurotoxicity in rat cortical cultures
    • Blitzblau R., Gupta S., Djali S., Robinson M.B., Rosenberg P.A. The glutamate transport inhibitor L-trans-pyrrolidine-2,4-dicarboxylate indirectly evokes NMDA receptor mediated neurotoxicity in rat cortical cultures. Eur. J. Neurosci. 8:1996;1840-1852.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 1840-1852
    • Blitzblau, R.1    Gupta, S.2    Djali, S.3    Robinson, M.B.4    Rosenberg, P.A.5
  • 116
    • 0028043521 scopus 로고
    • Release-regulating presynaptic heterocarriers
    • Bonanno G., Raiteri M. Release-regulating presynaptic heterocarriers. Prog. Neurobiol. 44:1994;451-462.
    • (1994) Prog. Neurobiol. , vol.44 , pp. 451-462
    • Bonanno, G.1    Raiteri, M.2
  • 117
    • 0027322513 scopus 로고
    • Glutamic acid and gamma-aminobutyric acid modulate each other's release through heterocarriers sited on the axon terminals of rat brain
    • Bonanno G., Pittaluga A., Fedele E., Fontana G., Raiteri M. Glutamic acid and gamma-aminobutyric acid modulate each other's release through heterocarriers sited on the axon terminals of rat brain. J. Neurochem. 61:1993;222-230.
    • (1993) J. Neurochem. , vol.61 , pp. 222-230
    • Bonanno, G.1    Pittaluga, A.2    Fedele, E.3    Fontana, G.4    Raiteri, M.5
  • 118
    • 0027955885 scopus 로고
    • Heterocarrier-mediated reciprocal modulation of glutamate and glycine release in rat cerebral cortex and spinal cord synaptosomes
    • Bonanno G., Vallebuona F., Donadini F., Fontana G., Fedele E., Raiteri M. Heterocarrier-mediated reciprocal modulation of glutamate and glycine release in rat cerebral cortex and spinal cord synaptosomes. Eur. J. Pharmacol. 252:1994;61-67.
    • (1994) Eur. J. Pharmacol. , vol.252 , pp. 61-67
    • Bonanno, G.1    Vallebuona, F.2    Donadini, F.3    Fontana, G.4    Fedele, E.5    Raiteri, M.6
  • 119
    • 0027251608 scopus 로고
    • Oxidative stress induced by glutamate receptor agonists
    • Bondy S.C., Lee D.K. Oxidative stress induced by glutamate receptor agonists. Brain Res. 610:1993;229-233.
    • (1993) Brain Res. , vol.610 , pp. 229-233
    • Bondy, S.C.1    Lee, D.K.2
  • 120
    • 0031763592 scopus 로고    scopus 로고
    • AMPA receptors: Molecular and functional diversity
    • Borges K., Dingledine R. AMPA receptors: molecular and functional diversity. Prog. Brain Res. 116:1998;153-170.
    • (1998) Prog. Brain Res. , vol.116 , pp. 153-170
    • Borges, K.1    Dingledine, R.2
  • 121
    • 0029199308 scopus 로고
    • Neurotransmitter transporters: Molecular biology, function, and regulation
    • Borowsky B., Hoffman B.J. Neurotransmitter transporters: molecular biology, function, and regulation. Int. Rev. Neurobiol. 38:1995;139-199.
    • (1995) Int. Rev. Neurobiol. , vol.38 , pp. 139-199
    • Borowsky, B.1    Hoffman, B.J.2
  • 122
    • 0026463206 scopus 로고
    • The glial cell glutamate uptake carrier countertransports pH-changing anions
    • Bouvier M., Szatkowski M., Amato A., Attwell D. The glial cell glutamate uptake carrier countertransports pH-changing anions. Nature. 360:1992;471-474.
    • (1992) Nature , vol.360 , pp. 471-474
    • Bouvier, M.1    Szatkowski, M.2    Amato, A.3    Attwell, D.4
  • 123
    • 0018141863 scopus 로고
    • Glutamine - A major substrate for nerve endings
    • Bradford H.F., Ward H.K., Thomas A.J. Glutamine - a major substrate for nerve endings. J. Neurochem. 30:1978;1453-1459.
    • (1978) J. Neurochem. , vol.30 , pp. 1453-1459
    • Bradford, H.F.1    Ward, H.K.2    Thomas, A.J.3
  • 124
    • 0034061665 scopus 로고    scopus 로고
    • Interactions between AMPA receptors and intracellular proteins
    • Braithwaite S.P., Meyer G., Henley J.M. Interactions between AMPA receptors and intracellular proteins. Neuropharmacology. 39:2000;919-930.
    • (2000) Neuropharmacology , vol.39 , pp. 919-930
    • Braithwaite, S.P.1    Meyer, G.2    Henley, J.M.3
  • 125
    • 0025696512 scopus 로고
    • Distribution of glutamate-like immunoreactivity in excitatory hippocampal pathways: A semiquantitative electron microscopic study in rats
    • Bramham C.R., Torp R., Zhang N., Storm-Mathisen J., Ottersen O.P. Distribution of glutamate-like immunoreactivity in excitatory hippocampal pathways: a semiquantitative electron microscopic study in rats. Neuroscience. 39:1990;405-417.
    • (1990) Neuroscience , vol.39 , pp. 405-417
    • Bramham, C.R.1    Torp, R.2    Zhang, N.3    Storm-Mathisen, J.4    Ottersen, O.P.5
  • 126
    • 0032123276 scopus 로고    scopus 로고
    • The increasing power of immunohistochemistry and immunocytochemistry
    • Brandtzaeg P. The increasing power of immunohistochemistry and immunocytochemistry. J. Immunol. Methods. 216:1998;49-67.
    • (1998) J. Immunol. Methods , vol.216 , pp. 49-67
    • Brandtzaeg, P.1
  • 130
    • 0033754407 scopus 로고    scopus 로고
    • Imaging the glutamatergic system in vivo - Relevance to schizophrenia
    • Bressan R.A., Pilowsky L.S. Imaging the glutamatergic system in vivo - relevance to schizophrenia. Eur. J. Nucl. Med. 27:2000;1723-1731.
    • (2000) Eur. J. Nucl. Med. , vol.27 , pp. 1723-1731
    • Bressan, R.A.1    Pilowsky, L.S.2
  • 131
    • 0030665014 scopus 로고    scopus 로고
    • Arachidonic acid inhibits uptake of amino acids and potentiates PKC effects on glutamate, but not GABA, exocytosis in isolated hippocampal nerve terminals
    • Breukel A.I.M., Besselsen E., Dasilva F.H.L., Ghijsen W.E.J.M. Arachidonic acid inhibits uptake of amino acids and potentiates PKC effects on glutamate, but not GABA, exocytosis in isolated hippocampal nerve terminals. Brain Res. 773:1997;90-97.
    • (1997) Brain Res. , vol.773 , pp. 90-97
    • Breukel, A.I.M.1    Besselsen, E.2    Dasilva, F.H.L.3    Ghijsen, W.E.J.M.4
  • 132
    • 0023260545 scopus 로고
    • Electrogenic glutamate uptake is a major current carrier in the membrane of axolotal retinal glial cells
    • Brew H., Attwell D. Electrogenic glutamate uptake is a major current carrier in the membrane of axolotal retinal glial cells. Nature. 327:1987;707-709.
    • (1987) Nature , vol.327 , pp. 707-709
    • Brew, H.1    Attwell, D.2
  • 133
    • 0026080845 scopus 로고
    • Conformationally defined neurotransmitter analogues. Selective inhibition of glutamate uptake by one pyrrolidine-2,4-dicarboxylate diastereomer
    • Bridges R.J., Stanley M.S., Anderson M.W., Cotman C.W., Chamberlin A.R. Conformationally defined neurotransmitter analogues. Selective inhibition of glutamate uptake by one pyrrolidine-2,4-dicarboxylate diastereomer. J. Med. Chem. 34:1991;717-725.
    • (1991) J. Med. Chem. , vol.34 , pp. 717-725
    • Bridges, R.J.1    Stanley, M.S.2    Anderson, M.W.3    Cotman, C.W.4    Chamberlin, A.R.5
  • 136
    • 0028341707 scopus 로고
    • A conformationally constrained competitive inhibitor of the sodium-dependent glutamate transporter in forebrain synaptosomes: L-anti-endo-3,4-methanopyrrolidine dicarboxylate
    • Bridges R.J., Lovering F.E., Koch H., Cotman C.W., Chamberlin A.R. A conformationally constrained competitive inhibitor of the sodium-dependent glutamate transporter in forebrain synaptosomes: L-anti-endo-3,4-methanopyrrolidine dicarboxylate. Neurosci. Lett. 174:1994;193-197.
    • (1994) Neurosci. Lett. , vol.174 , pp. 193-197
    • Bridges, R.J.1    Lovering, F.E.2    Koch, H.3    Cotman, C.W.4    Chamberlin, A.R.5
  • 137
    • 0032937403 scopus 로고    scopus 로고
    • A pharmacological review of competitive inhibitors and substrates of high-affinity, sodium-dependent glutamate transport in the central nervous system
    • Bridges R.J., Kavanaugh M.P., Chamberlin A.R. A pharmacological review of competitive inhibitors and substrates of high-affinity, sodium-dependent glutamate transport in the central nervous system. Curr. Pharm. Des. 5:1999;363-379.
    • (1999) Curr. Pharm. Des. , vol.5 , pp. 363-379
    • Bridges, R.J.1    Kavanaugh, M.P.2    Chamberlin, A.R.3
  • 138
    • 0029024072 scopus 로고
    • The cardiac glycoside ouabain potentiates excitotoxic injury of adult neurons in rat hippocampus
    • Brines M.L., Dare A.O., de Lanerolle N.C. The cardiac glycoside ouabain potentiates excitotoxic injury of adult neurons in rat hippocampus. Neurosci. Lett. 191:1995;145-148.
    • (1995) Neurosci. Lett. , vol.191 , pp. 145-148
    • Brines, M.L.1    Dare, A.O.2    De Lanerolle, N.C.3
  • 139
    • 0032142757 scopus 로고    scopus 로고
    • Discrimination of two amino acid transport activities in 4F2 heavy chain- expressing Xenopus laevis oocytes
    • Bröer A., Hamprecht B., Bröer S. Discrimination of two amino acid transport activities in 4F2 heavy chain- expressing Xenopus laevis oocytes. Biochem. J. 333:(3):1998;549-554.
    • (1998) Biochem. J. , vol.333 , Issue.3 , pp. 549-554
    • Bröer, A.1    Hamprecht, B.2    Bröer, S.3
  • 141
    • 70350302198 scopus 로고    scopus 로고
    • Biochemistry and anatomy of transmitter glutamate
    • O.P. Ottersen, & J. Storm-Mathisen. Amsterdam: Elsevier
    • Broman J., Hassel B., Rinvik E., Ottersen O.P. Biochemistry and anatomy of transmitter glutamate. Ottersen O.P., Storm-Mathisen J. Glutamate. 2000;1-44 Elsevier, Amsterdam.
    • (2000) Glutamate , pp. 1-44
    • Broman, J.1    Hassel, B.2    Rinvik, E.3    Ottersen, O.P.4
  • 142
    • 0023885049 scopus 로고
    • 2 of glutamate transport in astrocyte cultures
    • 2 of glutamate transport in astrocyte cultures. J. Neurochem. 50:1988;1117-1122.
    • (1988) J. Neurochem. , vol.50 , pp. 1117-1122
    • Brookes, N.1
  • 143
    • 0032143556 scopus 로고    scopus 로고
    • The glutamate transporter, GLT-1, is expressed in cultured hippocampal neurons
    • Brooks-Kayal A.R., Munir M., Jin H., Robinson M.B. The glutamate transporter, GLT-1, is expressed in cultured hippocampal neurons. Neurochem. Int. 33:1998;95-100.
    • (1998) Neurochem. Int. , vol.33 , pp. 95-100
    • Brooks-Kayal, A.R.1    Munir, M.2    Jin, H.3    Robinson, M.B.4
  • 144
    • 0025314266 scopus 로고
    • A chloride-dependent and calcium-dependent glutamate-binding protein from rat brain - Identification as a ubiquitous constituent of the inner mitochondrial membrane
    • Brose N., Thomas A., Weber M.G., Jahn R. A chloride-dependent and calcium-dependent glutamate-binding protein from rat brain - identification as a ubiquitous constituent of the inner mitochondrial membrane. J. Biol. Chem. 265:1990;10604-10610.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10604-10610
    • Brose, N.1    Thomas, A.2    Weber, M.G.3    Jahn, R.4
  • 145
    • 0028841852 scopus 로고
    • The release of glutamate and aspartate from rat brain synaptosomes in response to domoic acid (amnesic shellfish toxin) and kainic acid
    • Brown J.A., Nijjar M.S. The release of glutamate and aspartate from rat brain synaptosomes in response to domoic acid (amnesic shellfish toxin) and kainic acid. Mol. Cell. Biochem. 151:1995;49-54.
    • (1995) Mol. Cell. Biochem. , vol.151 , pp. 49-54
    • Brown, J.A.1    Nijjar, M.S.2
  • 146
    • 85009295914 scopus 로고    scopus 로고
    • Clinical significance of CSF glutamate concentrations following severe traumatic brain injury in humans
    • Brown J.I.M., Baker A.J., Konasiewicz S.J., Moulton R.J. Clinical significance of CSF glutamate concentrations following severe traumatic brain injury in humans. J. Neurotrauma. 15:1998;253-263.
    • (1998) J. Neurotrauma , vol.15 , pp. 253-263
    • Brown, J.I.M.1    Baker, A.J.2    Konasiewicz, S.J.3    Moulton, R.J.4
  • 147
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice
    • Brown R.H. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell. 80:1995;687-692.
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown, R.H.1
  • 148
    • 14444268768 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Insights from genetics
    • Brown R.H. Amyotrophic lateral sclerosis: insights from genetics. Arch. Neurol. 54:1997;1246-1250.
    • (1997) Arch. Neurol. , vol.54 , pp. 1246-1250
    • Brown, R.H.1
  • 152
    • 0025813176 scopus 로고
    • GABA and glycine in synaptic vesicles - Storage and transport characteristics
    • Burger P.M., Hell J., Mehl E., Krasel C., Lottspeich F., Jahn R. GABA and glycine in synaptic vesicles - storage and transport characteristics. Neuron. 7:1991;287-293.
    • (1991) Neuron , vol.7 , pp. 287-293
    • Burger, P.M.1    Hell, J.2    Mehl, E.3    Krasel, C.4    Lottspeich, F.5    Jahn, R.6
  • 153
    • 0030928406 scopus 로고    scopus 로고
    • Beta-amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • Butterfield D.A. Beta-amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem. Res. Toxicol. 10:1997;495-506.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 495-506
    • Butterfield, D.A.1
  • 154
    • 0031879678 scopus 로고    scopus 로고
    • Effects of hyperammonaemia on brain function
    • Butterworth R.F. Effects of hyperammonaemia on brain function. J. Inherit. Metab. Dis. 21:1998;6-20.
    • (1998) J. Inherit. Metab. Dis. , vol.21 , pp. 6-20
    • Butterworth, R.F.1
  • 155
    • 0031828634 scopus 로고    scopus 로고
    • Pathogenesis of acute hepatic encephalopathy
    • Butterworth R.F. Pathogenesis of acute hepatic encephalopathy. Digestion. 59:1998;16-21.
    • (1998) Digestion , vol.59 , pp. 16-21
    • Butterworth, R.F.1
  • 157
    • 0029671435 scopus 로고    scopus 로고
    • Channel behavior in a gamma-aminobutyrate transporter
    • Cammack J.N., Schwartz E.A. Channel behavior in a gamma-aminobutyrate transporter. Proc. Natl. Acad. Sci. USA. 93:1996;723-727.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 723-727
    • Cammack, J.N.1    Schwartz, E.A.2
  • 158
    • 0028020417 scopus 로고
    • A GABA transporter operates asymmetrically and with variable stoichiometry
    • Cammack J.N., Rakhilin S.V., Schwartz E.A. A GABA transporter operates asymmetrically and with variable stoichiometry. Neuron. 13:1994;949-960.
    • (1994) Neuron , vol.13 , pp. 949-960
    • Cammack, J.N.1    Rakhilin, S.V.2    Schwartz, E.A.3
  • 159
    • 0032579962 scopus 로고    scopus 로고
    • Glutamate uptake is decreased tardively in the spinal cord of FALS mice
    • Canton T., Pratt J., Stutzmann J.M., Imperato A., Boireau A. Glutamate uptake is decreased tardively in the spinal cord of FALS mice. Neuroreport. 9:1998;775-778.
    • (1998) Neuroreport , vol.9 , pp. 775-778
    • Canton, T.1    Pratt, J.2    Stutzmann, J.M.3    Imperato, A.4    Boireau, A.5
  • 160
    • 0032190185 scopus 로고    scopus 로고
    • Amino acid residues that control pH modulation of transport-associated current in mammalian serotonin transporters
    • Cao Y.W., Li M., Mager S., Lester H.A. Amino acid residues that control pH modulation of transport-associated current in mammalian serotonin transporters. J. Neurosci. 18:1998;7739-7749.
    • (1998) J. Neurosci. , vol.18 , pp. 7739-7749
    • Cao, Y.W.1    Li, M.2    Mager, S.3    Lester, H.A.4
  • 161
    • 0030943091 scopus 로고    scopus 로고
    • Neurotransmitter aberrations in schizophrenia: New perspectives and therapeutic implications
    • Carlsson A., Hansson L.O., Waters N., Carlsson M.L. Neurotransmitter aberrations in schizophrenia: new perspectives and therapeutic implications. Life Sci. 61:1997;75-94.
    • (1997) Life Sci. , vol.61 , pp. 75-94
    • Carlsson, A.1    Hansson, L.O.2    Waters, N.3    Carlsson, M.L.4
  • 163
    • 0344809958 scopus 로고    scopus 로고
    • The schizophrenia ketamine challenge study debate
    • Carpenter W.T. The schizophrenia ketamine challenge study debate. Biol. Psychiatry. 46:1999;1081-1091.
    • (1999) Biol. Psychiatry , vol.46 , pp. 1081-1091
    • Carpenter, W.T.1
  • 164
    • 0000392593 scopus 로고    scopus 로고
    • Protein kinase C modulation of the human excitatory amino acid transporter 2 subtype of glutamate transporter
    • Carrick T., Dunlop J. Protein kinase C modulation of the human excitatory amino acid transporter 2 subtype of glutamate transporter. Soc. Neurosci. Abstr. 25:(1):1999;426.
    • (1999) Soc. Neurosci. Abstr. , vol.25 , Issue.1 , pp. 426
    • Carrick, T.1    Dunlop, J.2
  • 165
    • 0034659742 scopus 로고    scopus 로고
    • Prolonged synaptic currents and glutamate spillover at the parallel fiber to stellate cell synapse
    • Carter A.G., Regehr W.G. Prolonged synaptic currents and glutamate spillover at the parallel fiber to stellate cell synapse. J. Neurosci. 20:2000;4423-4434.
    • (2000) J. Neurosci. , vol.20 , pp. 4423-4434
    • Carter, A.G.1    Regehr, W.G.2
  • 166
    • 0026000567 scopus 로고
    • Activation of high-affinity uptake of glutamate by phorbol esters in primary glial cell cultures
    • Casado M., Zafra F., Aragón C., Gimenez C. Activation of high-affinity uptake of glutamate by phorbol esters in primary glial cell cultures. J. Neurochem. 57:1991;1185-1190.
    • (1991) J. Neurochem. , vol.57 , pp. 1185-1190
    • Casado, M.1    Zafra, F.2    Aragón, C.3    Gimenez, C.4
  • 170
    • 0025138490 scopus 로고
    • Differential alterations of cortical glutamatergic binding sites in senile dementia of the Alzheimer type
    • Chalmers D.T., Dewar D., Graham D.I., Brooks D.N., McCulloch J. Differential alterations of cortical glutamatergic binding sites in senile dementia of the Alzheimer type. Proc. Natl. Acad. Sci. USA. 87:1990;1352-1356.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1352-1356
    • Chalmers, D.T.1    Dewar, D.2    Graham, D.I.3    Brooks, D.N.4    McCulloch, J.5
  • 171
    • 0031660297 scopus 로고    scopus 로고
    • Design and synthesis of conformationally constrained inhibitors of high-affinity, sodium-dependent glutamate transporters
    • Chamberlin A.R., Koch H.P., Bridges R.J. Design and synthesis of conformationally constrained inhibitors of high-affinity, sodium-dependent glutamate transporters. Methods Enzymol. 296:1998;175-189.
    • (1998) Methods Enzymol. , vol.296 , pp. 175-189
    • Chamberlin, A.R.1    Koch, H.P.2    Bridges, R.J.3
  • 172
    • 0002837109 scopus 로고
    • Conformationally constrained acidic amino acids as probes of glutamate receptors and transporters
    • A.P. Kozikowski. New York: Raven Press
    • Chamberlin R., Bridges R. Conformationally constrained acidic amino acids as probes of glutamate receptors and transporters. Kozikowski A.P. Drug Design for Neuroscience. 1993;231-259 Raven Press, New York.
    • (1993) Drug Design for Neuroscience , pp. 231-259
    • Chamberlin, R.1    Bridges, R.2
  • 173
    • 0032702799 scopus 로고    scopus 로고
    • Evidence for an astrocytic glutamate transporter deficit in hepatic encephalopathy
    • Chan H., Butterworth R.F. Evidence for an astrocytic glutamate transporter deficit in hepatic encephalopathy. Neurochem. Res. 24:1999;1397-1401.
    • (1999) Neurochem. Res. , vol.24 , pp. 1397-1401
    • Chan, H.1    Butterworth, R.F.2
  • 174
    • 0034257046 scopus 로고    scopus 로고
    • Effects of ammonia on glutamate transporter (GLAST) protein and mRNA in cultured rat cortical astrocytes
    • Chan H., Hazell A.S., Desjardins P., Butterworth R.F. Effects of ammonia on glutamate transporter (GLAST) protein and mRNA in cultured rat cortical astrocytes. Neurochem. Int. 37:2000;243-248.
    • (2000) Neurochem. Int. , vol.37 , pp. 243-248
    • Chan, H.1    Hazell, A.S.2    Desjardins, P.3    Butterworth, R.F.4
  • 175
    • 0020683087 scopus 로고
    • +)-ATPase activity in brain slices and synaptosomes by arachidonic acid
    • +)-ATPase activity in brain slices and synaptosomes by arachidonic acid. J. Neurochem. 40:1983;309-316.
    • (1983) J. Neurochem. , vol.40 , pp. 309-316
    • Chan, P.H.1    Kerlan, R.2    Fishman, R.A.3
  • 176
    • 0027055105 scopus 로고
    • Adult onset motor neuron disease - Worldwide mortality, incidence and distribution since 1950
    • Chancellor A.M., Warlow C.P. Adult onset motor neuron disease - worldwide mortality, incidence and distribution since 1950. J. Neurol. Neurosurg. Psychiatry. 55:1992;1106-1115.
    • (1992) J. Neurol. Neurosurg. Psychiatry , vol.55 , pp. 1106-1115
    • Chancellor, A.M.1    Warlow, C.P.2
  • 177
    • 0033058120 scopus 로고    scopus 로고
    • Chronic ethanol upregulates NMDA and AMPA, but not kainate receptor subunit proteins in rat primary cortical cultures
    • Chandler L.J., Norwood D., Sutton G. Chronic ethanol upregulates NMDA and AMPA, but not kainate receptor subunit proteins in rat primary cortical cultures. Alcohol Clin. Exp. Res. 23:1999;363-370.
    • (1999) Alcohol Clin. Exp. Res. , vol.23 , pp. 363-370
    • Chandler, L.J.1    Norwood, D.2    Sutton, G.3
  • 178
    • 0029114107 scopus 로고
    • Glutamate transporters in glial plasma membranes: Highly differentiated localizations revealed by quantitative ultrastructural immunocytochemistry
    • Chaudhry F.A., Lehre K.P., Campagne M.V., Ottersen O.P., Danbolt N.C., Storm-Mathisen J. Glutamate transporters in glial plasma membranes: highly differentiated localizations revealed by quantitative ultrastructural immunocytochemistry. Neuron. 15:1995;711-720.
    • (1995) Neuron , vol.15 , pp. 711-720
    • Chaudhry, F.A.1    Lehre, K.P.2    Campagne, M.V.3    Ottersen, O.P.4    Danbolt, N.C.5    Storm-Mathisen, J.6
  • 179
    • 0033598956 scopus 로고    scopus 로고
    • Molecular analysis of system N suggests novel physiological roles in nitrogen metabolism and synaptic transmission
    • Chaudhry F.A., Reimer R.J., Krizaj D., Barber D., Storm-Mathisen J., Copenhagen D.R., Edwards R.H. Molecular analysis of system N suggests novel physiological roles in nitrogen metabolism and synaptic transmission. Cell. 99:1999;769-780.
    • (1999) Cell , vol.99 , pp. 769-780
    • Chaudhry, F.A.1    Reimer, R.J.2    Krizaj, D.3    Barber, D.4    Storm-Mathisen, J.5    Copenhagen, D.R.6    Edwards, R.H.7
  • 180
    • 0032530566 scopus 로고    scopus 로고
    • Transgenic mice for interleukin 3 develop motor neuron degeneration associated with autoimmune reaction against spinal cord motor neurons
    • Chavany C., Vicarioabejon C., Miller G., Jendoubi M. Transgenic mice for interleukin 3 develop motor neuron degeneration associated with autoimmune reaction against spinal cord motor neurons. Proc. Natl. Acad. Sci. USA.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11354-11359
    • Chavany, C.1    Vicarioabejon, C.2    Miller, G.3    Jendoubi, M.4
  • 181
    • 0032914455 scopus 로고    scopus 로고
    • Antagonists selective for NMDA receptors containing the NR2b subunit
    • Chenard B.L., Menniti F.S. Antagonists selective for NMDA receptors containing the NR2b subunit. Curr. Pharm. Des. 5:1999;381-404.
    • (1999) Curr. Pharm. Des. , vol.5 , pp. 381-404
    • Chenard, B.L.1    Menniti, F.S.2
  • 182
    • 0032191207 scopus 로고    scopus 로고
    • Micromolar L-glutamate induces extensive apoptosis in an apoptotic-necrotic continuum of insult-dependent, excitotoxic injury in cultured cortical neurones
    • Cheung N.S., Pascoe C.J., Giardina S.F., John C.A., Beart P.M. Micromolar L-glutamate induces extensive apoptosis in an apoptotic-necrotic continuum of insult-dependent, excitotoxic injury in cultured cortical neurones. Neuropharmacology. 37:1998;1419-1429.
    • (1998) Neuropharmacology , vol.37 , pp. 1419-1429
    • Cheung, N.S.1    Pascoe, C.J.2    Giardina, S.F.3    John, C.A.4    Beart, P.M.5
  • 183
    • 0026778684 scopus 로고
    • Three-dimensional analysis of the structure and composition of CA3 branched dendritic spines and their synaptic relationships with mossy fiber boutons in the rat hippocampus
    • Chicurel M.E., Harris K.M. Three-dimensional analysis of the structure and composition of CA3 branched dendritic spines and their synaptic relationships with mossy fiber boutons in the rat hippocampus. J. Comp. Neurol. 325:1992;169-182.
    • (1992) J. Comp. Neurol. , vol.325 , pp. 169-182
    • Chicurel, M.E.1    Harris, K.M.2
  • 185
    • 0025570260 scopus 로고
    • Uptake of glutamate and cystine in C-6 glioma cells and cultured astrocytes
    • Cho Y., Bannai S. Uptake of glutamate and cystine in C-6 glioma cells and cultured astrocytes. J. Neurochem. 55:1990;2091-2097.
    • (1990) J. Neurochem. , vol.55 , pp. 2091-2097
    • Cho, Y.1    Bannai, S.2
  • 186
    • 0019461431 scopus 로고
    • Radial glia of developing human fetal spinal cord: Golgi, immunohistochemical and electron microscopic study
    • Choi B.H. Radial glia of developing human fetal spinal cord: Golgi, immunohistochemical and electron microscopic study. Brain Res. 227:1981;249-267.
    • (1981) Brain Res. , vol.227 , pp. 249-267
    • Choi, B.H.1
  • 187
    • 0026497926 scopus 로고
    • Excitotoxic cell death
    • Choi D.W. Excitotoxic cell death. J. Neurobiol. 23:1992;1261-1276.
    • (1992) J. Neurobiol. , vol.23 , pp. 1261-1276
    • Choi, D.W.1
  • 188
    • 0025265926 scopus 로고
    • The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death
    • Choi D.W., Rothman S.M. The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death. Annu. Rev. Neurosci. 13:1990;171-182.
    • (1990) Annu. Rev. Neurosci. , vol.13 , pp. 171-182
    • Choi, D.W.1    Rothman, S.M.2
  • 189
    • 8544230662 scopus 로고    scopus 로고
    • Expression of high-affinity neuronal and glial glutamate transporters in the rat optic nerve
    • Choi I., Chiu S.Y. Expression of high-affinity neuronal and glial glutamate transporters in the rat optic nerve. Glia. 20:1997;184-192.
    • (1997) Glia , vol.20 , pp. 184-192
    • Choi, I.1    Chiu, S.Y.2
  • 190
    • 0034068876 scopus 로고    scopus 로고
    • Postfusional regulation of cleft glutamate concentration during LTP at 'silent synapses'
    • Choi S., Klingauf J., Tsien R.W. Postfusional regulation of cleft glutamate concentration during LTP at 'silent synapses'. Nat. Neurosci. 3:2000;330-336.
    • (2000) Nat. Neurosci. , vol.3 , pp. 330-336
    • Choi, S.1    Klingauf, J.2    Tsien, R.W.3
  • 191
    • 0026548762 scopus 로고
    • Amino acid nutrition across the placenta
    • Christensen H.N. Amino acid nutrition across the placenta. Nutr. Rev. 50:1992;13-15.
    • (1992) Nutr. Rev. , vol.50 , pp. 13-15
    • Christensen, H.N.1
  • 192
    • 0026632904 scopus 로고
    • The ontogeny of the uptake systems for glutamate, GABA, and glycine in synaptic vesicles isolated from rat brain
    • Christensen H., Fonnum F. The ontogeny of the uptake systems for glutamate, GABA, and glycine in synaptic vesicles isolated from rat brain. Neurochem. Res. 17:1992;457-462.
    • (1992) Neurochem. Res. , vol.17 , pp. 457-462
    • Christensen, H.1    Fonnum, F.2
  • 193
    • 0029876527 scopus 로고    scopus 로고
    • Transmitter timecourse in the synaptic cleft: Its role in central synaptic function
    • Clements J.D. Transmitter timecourse in the synaptic cleft: its role in central synaptic function. Trends Neurosci. 19:1996;163-171.
    • (1996) Trends Neurosci. , vol.19 , pp. 163-171
    • Clements, J.D.1
  • 195
    • 0030788009 scopus 로고    scopus 로고
    • Sodium-dependent proline and glutamate uptake by hippocampal synaptosomes during postnatal development
    • Cohen S.M., Nadler J.V. Sodium-dependent proline and glutamate uptake by hippocampal synaptosomes during postnatal development. Dev. Brain Res. 100:1997;230-233.
    • (1997) Dev. Brain Res. , vol.100 , pp. 230-233
    • Cohen, S.M.1    Nadler, J.V.2
  • 196
    • 0027392187 scopus 로고
    • Changes in synaptosomal glutamate release during postnatal development in the rat hippocampus and cortex
    • Collard K.J., Edwards R., Liu Y. Changes in synaptosomal glutamate release during postnatal development in the rat hippocampus and cortex. Dev. Brain Res. 71:1993;37-43.
    • (1993) Dev. Brain Res. , vol.71 , pp. 37-43
    • Collard, K.J.1    Edwards, R.2    Liu, Y.3
  • 197
    • 0024829451 scopus 로고
    • Excitatory amino acid receptors in the vertebrate central nervous system
    • Collingridge G.L., Lester R.A.J. Excitatory amino acid receptors in the vertebrate central nervous system. Pharmacol. Rev. 40:1989;143-210.
    • (1989) Pharmacol. Rev. , vol.40 , pp. 143-210
    • Collingridge, G.L.1    Lester, R.A.J.2
  • 198
    • 0030995878 scopus 로고    scopus 로고
    • Pharmacology and functions of metabotropic glutamate receptors
    • Conn P.J., Pin J.P. Pharmacology and functions of metabotropic glutamate receptors. Annu. Rev. Pharmacol. Toxicol. 37:1997;205-237.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 205-237
    • Conn, P.J.1    Pin, J.P.2
  • 199
    • 0028846037 scopus 로고
    • +-dependent glutamate transporter GLAST-1 by site-directed mutagenesis
    • +-dependent glutamate transporter GLAST-1 by site-directed mutagenesis. J. Biol. Chem. 270:1995;25207-25212.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25207-25212
    • Conradt, M.1    Stoffel, W.2
  • 200
    • 0031017893 scopus 로고    scopus 로고
    • Inhibition of the high-affinity brain glutamate transporter GLAST-1 via direct phosphorylation
    • Conradt M., Stoffel W. Inhibition of the high-affinity brain glutamate transporter GLAST-1 via direct phosphorylation. J. Neurochem. 68:1997;1244-1251.
    • (1997) J. Neurochem. , vol.68 , pp. 1244-1251
    • Conradt, M.1    Stoffel, W.2
  • 201
    • 85047690143 scopus 로고
    • Localization of N-glycosylation sites and functional role of the carbohydrate units of GLAST-1, a cloned rat brain L-glutamate/L-aspartate transporter
    • Conradt M., Storck T., Stoffel W. Localization of N-glycosylation sites and functional role of the carbohydrate units of GLAST-1, a cloned rat brain L-glutamate/L-aspartate transporter. Eur. J. Biochem. 229:1995;682-687.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 682-687
    • Conradt, M.1    Storck, T.2    Stoffel, W.3
  • 202
    • 0031918486 scopus 로고    scopus 로고
    • EAAC1, a high-affinity glutamate transporter, is localized to astrocytes and GABAergic neurons besides pyramidal cells in the rat cerebral cortex
    • Conti F., DeBiasi S., Minelli A., Rothstein J.D., Melone M. EAAC1, a high-affinity glutamate transporter, is localized to astrocytes and GABAergic neurons besides pyramidal cells in the rat cerebral cortex. Cereb. Cortex. 8:1998;108-116.
    • (1998) Cereb. Cortex , vol.8 , pp. 108-116
    • Conti, F.1    Debiasi, S.2    Minelli, A.3    Rothstein, J.D.4    Melone, M.5
  • 203
    • 0032914177 scopus 로고    scopus 로고
    • Neuronal and glial localization of NR1 and NR2a/b subunits of the NMDA receptor in the human cerebral cortex
    • Conti F., Barbaresi P., Melone M., Ducati A. Neuronal and glial localization of NR1 and NR2a/b subunits of the NMDA receptor in the human cerebral cortex. Cereb. Cortex. 9:1999;110-120.
    • (1999) Cereb. Cortex , vol.9 , pp. 110-120
    • Conti, F.1    Barbaresi, P.2    Melone, M.3    Ducati, A.4
  • 204
    • 0032949602 scopus 로고    scopus 로고
    • Oxidative stress and motor neurone disease
    • Cookson M.R., Shaw P.J. Oxidative stress and motor neurone disease. Brain Pathol. 9:1999;165-186.
    • (1999) Brain Pathol. , vol.9 , pp. 165-186
    • Cookson, M.R.1    Shaw, P.J.2
  • 205
    • 0030792637 scopus 로고    scopus 로고
    • Multiple roles of glutathione in the central nervous system
    • Cooper A.J.L., Kristal B.S. Multiple roles of glutathione in the central nervous system. Biol. Chem. 378:1997;793-802.
    • (1997) Biol. Chem. , vol.378 , pp. 793-802
    • Cooper, A.J.L.1    Kristal, B.S.2
  • 207
    • 0028334675 scopus 로고
    • Protein kinase C modulates the activity of a cloned gamma-aminobutyric acid transporter expressed in Xenopus oocytes via regulated subcellular redistribution of the transporter
    • Corey J.L., Davidson N., Lester H.A., Brecha N., Quick M.W. Protein kinase C modulates the activity of a cloned gamma-aminobutyric acid transporter expressed in Xenopus oocytes via regulated subcellular redistribution of the transporter. J. Biol. Chem. 269:1994;14759-14767.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14759-14767
    • Corey, J.L.1    Davidson, N.2    Lester, H.A.3    Brecha, N.4    Quick, M.W.5
  • 208
    • 0027397195 scopus 로고
    • Cell culture evidence for neuronal degeneration in amyotrophic lateral sclerosis being linked to glutamate AMPA/kainate receptors
    • Couratier P., Hugon J., Sindou P., Vallat J.M., Dumas M. Cell culture evidence for neuronal degeneration in amyotrophic lateral sclerosis being linked to glutamate AMPA/kainate receptors. Lancet. 341:1993;265-268.
    • (1993) Lancet , vol.341 , pp. 265-268
    • Couratier, P.1    Hugon, J.2    Sindou, P.3    Vallat, J.M.4    Dumas, M.5
  • 209
    • 0032734205 scopus 로고    scopus 로고
    • Mechanisms of synaptic vesicle recycling illuminated by fluorescent dyes
    • Cousin M.A., Robinson P.J. Mechanisms of synaptic vesicle recycling illuminated by fluorescent dyes. J. Neurochem. 73:1999;2227-2239.
    • (1999) J. Neurochem. , vol.73 , pp. 2227-2239
    • Cousin, M.A.1    Robinson, P.J.2
  • 210
    • 0023838104 scopus 로고
    • Presynaptic and postsynaptic glutamatergic function in Alzheimer's disease
    • Cowburn R., Hardy J., Roberts P., Briggs R. Presynaptic and postsynaptic glutamatergic function in Alzheimer's disease. Neurosci. Lett. 86:1988;109-113.
    • (1988) Neurosci. Lett. , vol.86 , pp. 109-113
    • Cowburn, R.1    Hardy, J.2    Roberts, P.3    Briggs, R.4
  • 211
    • 0017740014 scopus 로고
    • Actions of L- And D-homocysteate in rat CNS: A correlation between low-affinity uptake and the time courses of excitation by microelectrophoretically applied L-glutamate analogues
    • Cox D.W.G., Headley M.H., Watkins J.C. Actions of L- and D-homocysteate in rat CNS: A correlation between low-affinity uptake and the time courses of excitation by microelectrophoretically applied L-glutamate analogues. J. Neurochem. 29:1977;579-588.
    • (1977) J. Neurochem. , vol.29 , pp. 579-588
    • Cox, D.W.G.1    Headley, M.H.2    Watkins, J.C.3
  • 213
    • 0033216120 scopus 로고    scopus 로고
    • Heteromeric kainate receptors formed by the coassembly of GluR5, GluR6, and GluR7
    • Cui C.H., Mayer M.L. Heteromeric kainate receptors formed by the coassembly of GluR5, GluR6, and GluR7. J. Neurosci. 19:1999;8281-8291.
    • (1999) J. Neurosci. , vol.19 , pp. 8281-8291
    • Cui, C.H.1    Mayer, M.L.2
  • 214
    • 33748643743 scopus 로고
    • Chemical excitation of spinal neurons
    • Curtis D.R., Phillis J.W., Watkins J.C. Chemical excitation of spinal neurons. Nature. 183:1959;611.
    • (1959) Nature , vol.183 , pp. 611
    • Curtis, D.R.1    Phillis, J.W.2    Watkins, J.C.3
  • 215
    • 70449549640 scopus 로고
    • The chemical excitation of spinal neurons by certain acidic amino acids
    • Curtis D.R., Phillis J.W., Watkins J.C. The chemical excitation of spinal neurons by certain acidic amino acids. J. Physiol. 150:1960;656-682.
    • (1960) J. Physiol. , vol.150 , pp. 656-682
    • Curtis, D.R.1    Phillis, J.W.2    Watkins, J.C.3
  • 216
    • 0027423261 scopus 로고
    • D-Aspartate binding to the glutamate uptake site in human brain tissue - Effects of leucotomy
    • Cutts A.J., Reynolds G.P. D-Aspartate binding to the glutamate uptake site in human brain tissue - effects of leucotomy. J. Neural Transm. 94:1993;147-152.
    • (1993) J. Neural Transm. , vol.94 , pp. 147-152
    • Cutts, A.J.1    Reynolds, G.P.2
  • 218
    • 0028143148 scopus 로고
    • The high affinity uptake system for excitatory amino acids in the brain
    • Danbolt N.C. The high affinity uptake system for excitatory amino acids in the brain. Prog. Neurobiol. 44:1994;377-396.
    • (1994) Prog. Neurobiol. , vol.44 , pp. 377-396
    • Danbolt, N.C.1
  • 219
    • 0001616532 scopus 로고    scopus 로고
    • Sodium- And potassium-dependent excitatory amino acid transporters in brain plasma membranes
    • O.P. Ottersen, & J. Storm-Mathisen. Amsterdam: Elsevier
    • Danbolt N.C. Sodium- and potassium-dependent excitatory amino acid transporters in brain plasma membranes. Ottersen O.P., Storm-Mathisen J. Glutamate. 2000;231-254 Elsevier, Amsterdam.
    • (2000) Glutamate , pp. 231-254
    • Danbolt, N.C.1
  • 220
    • 0022507258 scopus 로고
    • +-dependent D-aspartate uptake into brain membrane saccules
    • +-dependent D-aspartate uptake into brain membrane saccules. J. Neurochem. 47:1986;825-830.
    • (1986) J. Neurochem. , vol.47 , pp. 825-830
    • Danbolt, N.C.1    Storm-Mathisen, J.2
  • 221
    • 0022529283 scopus 로고
    • +-dependent 'binding' of D-aspartate in brain membranes is largely due to uptake into membrane bounded saccules
    • +-dependent 'binding' of D-aspartate in brain membranes is largely due to uptake into membrane bounded saccules. J. Neurochem. 47:1986;819-824.
    • (1986) J. Neurochem. , vol.47 , pp. 819-824
    • Danbolt, N.C.1    Storm-Mathisen, J.2
  • 222
    • 0025316950 scopus 로고
    • Purification and reconstitution of the sodium- And potassium-coupled glutamate transport glycoprotein from rat brain
    • Danbolt N.C., Pines G., Kanner B.I. Purification and reconstitution of the sodium- and potassium-coupled glutamate transport glycoprotein from rat brain. Biochemistry. 29:1990;6734-6740.
    • (1990) Biochemistry , vol.29 , pp. 6734-6740
    • Danbolt, N.C.1    Pines, G.2    Kanner, B.I.3
  • 223
    • 0026539793 scopus 로고
    • +]coupled L-glutamate transporter purified from rat brain is located in glial cell processes
    • +]coupled L-glutamate transporter purified from rat brain is located in glial cell processes. Neuroscience. 51:1992;295-310.
    • (1992) Neuroscience , vol.51 , pp. 295-310
    • Danbolt, N.C.1    Storm-Mathisen, J.2    Kanner, B.I.3
  • 226
    • 0033544844 scopus 로고    scopus 로고
    • Regulated trafficking of the human dopamine transporter
    • Daniels G.M., Amara S.G. Regulated trafficking of the human dopamine transporter. J. Biol. Chem. 274:1999;35794-35801.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35794-35801
    • Daniels, G.M.1    Amara, S.G.2
  • 227
    • 0032868626 scopus 로고    scopus 로고
    • Reversible activation of glutamate transport in rat brain glia by protein kinase C and an okadaic acid-sensitive phosphoprotein phosphatase
    • Daniels K.K., Vickroy T.W. Reversible activation of glutamate transport in rat brain glia by protein kinase C and an okadaic acid-sensitive phosphoprotein phosphatase. Neurochem. Res. 24:1999;1017-1025.
    • (1999) Neurochem. Res. , vol.24 , pp. 1017-1025
    • Daniels, K.K.1    Vickroy, T.W.2
  • 228
    • 0028606987 scopus 로고
    • Astrocytes as mediators of methylmercury neurotoxicity: Effects on D-aspartate and serotonin uptake
    • Dave V., Mullaney K.J., Goderie S., Kimelberg H.K., Aschner M. Astrocytes as mediators of methylmercury neurotoxicity: effects on D-aspartate and serotonin uptake. Dev. Neurosci. 16:1994;222-231.
    • (1994) Dev. Neurosci. , vol.16 , pp. 222-231
    • Dave, V.1    Mullaney, K.J.2    Goderie, S.3    Kimelberg, H.K.4    Aschner, M.5
  • 229
    • 0017238147 scopus 로고
    • Uptake and release of D- And L-aspartate by rat brain slices
    • Davies L.P., Johnston G.A.R. Uptake and release of D- and L-aspartate by rat brain slices. J. Neurochem. 26:1976;1007-1014.
    • (1976) J. Neurochem. , vol.26 , pp. 1007-1014
    • Davies, L.P.1    Johnston, G.A.R.2
  • 230
    • 0032053985 scopus 로고    scopus 로고
    • Multiple signaling pathways regulate cell surface expression and activity of the excitatory amino acid carrier 1 subtype of Glu transporter in C6 glioma
    • Davis K.E., Straff D.J., Weinstein E.A., Bannerman P.G., Correale D.M., Rothstein J.D., Robinson M.B. Multiple signaling pathways regulate cell surface expression and activity of the excitatory amino acid carrier 1 subtype of Glu transporter in C6 glioma. J. Neurosci. 18:1998;2475-2485.
    • (1998) J. Neurosci. , vol.18 , pp. 2475-2485
    • Davis, K.E.1    Straff, D.J.2    Weinstein, E.A.3    Bannerman, P.G.4    Correale, D.M.5    Rothstein, J.D.6    Robinson, M.B.7
  • 231
    • 0030065474 scopus 로고    scopus 로고
    • Free radicals and neuronal cell death
    • Dawson V.L., Dawson T.M. Free radicals and neuronal cell death. Cell Death Differ. 3:1996;71-78.
    • (1996) Cell Death Differ. , vol.3 , pp. 71-78
    • Dawson, V.L.1    Dawson, T.M.2
  • 232
    • 0033428885 scopus 로고    scopus 로고
    • A mouse model of familial amyotrophic lateral sclerosis expressing a mutant superoxide dismutase 1 shows evidence of disordered transport in the vasopressin hypothalamo-neurohypophysial axis
    • de Aguilar J.L., Gordon J.W., Rene F., Lutz-Bucher B., Kienlen-Campard P., Loeffler J.P. A mouse model of familial amyotrophic lateral sclerosis expressing a mutant superoxide dismutase 1 shows evidence of disordered transport in the vasopressin hypothalamo-neurohypophysial axis. Eur. J. Neurosci. 11:1999;4179-4187.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 4179-4187
    • De Aguilar, J.L.1    Gordon, J.W.2    Rene, F.3    Lutz-Bucher, B.4    Kienlen-Campard, P.5    Loeffler, J.P.6
  • 234
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S.L., Stocker R., Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324:1997;1-18.
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.L.2    Stocker, R.3    Davies, M.J.4
  • 235
    • 0023215742 scopus 로고
    • High-affinity transport of gamma-aminobutyric acid, glycine, taurine, L-aspartic acid, and L-glutamic acid in synaptosomal (P2) tissue: A kinetic and substrate specificity analysis
    • Debler E.A., Lajtha A. High-affinity transport of gamma-aminobutyric acid, glycine, taurine, L-aspartic acid, and L-glutamic acid in synaptosomal (P2) tissue: a kinetic and substrate specificity analysis. J. Neurochem. 48:1987;1851-1856.
    • (1987) J. Neurochem. , vol.48 , pp. 1851-1856
    • Debler, E.A.1    Lajtha, A.2
  • 236
    • 0032525096 scopus 로고    scopus 로고
    • The glutamate transporter EAAT4 in rat cerebellar Purkinje cells: A glutamate-gated chloride channel concentrated near the synapse in parts of the dendritic membrane facing astroglia
    • Dehnes Y., Chaudhry F.A., Ullensvang K., Lehre K.P., Storm-Mathisen J., Danbolt N.C. The glutamate transporter EAAT4 in rat cerebellar Purkinje cells: a glutamate-gated chloride channel concentrated near the synapse in parts of the dendritic membrane facing astroglia. J. Neurosci. 18:1998;3606-3619.
    • (1998) J. Neurosci. , vol.18 , pp. 3606-3619
    • Dehnes, Y.1    Chaudhry, F.A.2    Ullensvang, K.3    Lehre, K.P.4    Storm-Mathisen, J.5    Danbolt, N.C.6
  • 237
    • 0033807807 scopus 로고    scopus 로고
    • Transport rates of GABA transporters: Regulation by the N-terminal domain and syntaxin 1A
    • Deken S.L., Beckman M.L., Boos L., Quick M.W. Transport rates of GABA transporters: regulation by the N-terminal domain and syntaxin 1A. Nat. Neurosci. 3:2000;998-1003.
    • (2000) Nat. Neurosci. , vol.3 , pp. 998-1003
    • Deken, S.L.1    Beckman, M.L.2    Boos, L.3    Quick, M.W.4
  • 238
    • 0031843207 scopus 로고    scopus 로고
    • Glutamate receptor subunits GluR1 and GluR2/3 distribution shows reorganization in the human epileptogenic hippocampus
    • de Lanerolle, N.C., Eid, T., von Campe, G., Kovacs, I., Spencer, D.D., Brines, M., 1998. Glutamate receptor subunits GluR1 and GluR2/3 distribution shows reorganization in the human epileptogenic hippocampus. Eur. J. Neurosci. 10, 1687-1703.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1687-1703
    • De Lanerolle, N.C.1    Eid, T.2    Von Campe, G.3    Kovacs, I.4    Spencer, D.D.5    Brines, M.6
  • 239
    • 0031719445 scopus 로고    scopus 로고
    • Oxidative injury in the nervous system
    • Delanty N., Dichter M.A. Oxidative injury in the nervous system. Acta Neurol. Scand. 98:1998;145-153.
    • (1998) Acta Neurol. Scand. , vol.98 , pp. 145-153
    • Delanty, N.1    Dichter, M.A.2
  • 241
    • 0017143028 scopus 로고
    • Glutamate metabolism and transport in rat brain mitochondria
    • Dennis S.C., Land J.M., Clark J.B. Glutamate metabolism and transport in rat brain mitochondria. Biochem. J. 156:1976;323-331.
    • (1976) Biochem. J. , vol.156 , pp. 323-331
    • Dennis, S.C.1    Land, J.M.2    Clark, J.B.3
  • 242
    • 0030300223 scopus 로고    scopus 로고
    • Possible role of the Muller cell in uptake and metabolism of glutamate in the mammalian outer retina
    • Derouiche A. Possible role of the Muller cell in uptake and metabolism of glutamate in the mammalian outer retina. Vision Res. 36:1996;3875-3878.
    • (1996) Vision Res. , vol.36 , pp. 3875-3878
    • Derouiche, A.1
  • 243
    • 0029120602 scopus 로고
    • Coincidence of L-glutamate/L-aspartate transporter (GLAST) and glutamine synthetase (GS) immunoreactions in retinal glia: Evidence for coupling of GLAST and GS in transmitter clearance
    • Derouiche A., Rauen T. Coincidence of L-glutamate/L-aspartate transporter (GLAST) and glutamine synthetase (GS) immunoreactions in retinal glia: evidence for coupling of GLAST and GS in transmitter clearance. J. Neurosci. Res. 42:1995;131-143.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 131-143
    • Derouiche, A.1    Rauen, T.2
  • 244
    • 0031724201 scopus 로고    scopus 로고
    • Neurodevelopmental consequences of early exposure to phencyclidine and related drugs
    • Deutsch S.I., Mastropaolo J., Rosse R.B. Neurodevelopmental consequences of early exposure to phencyclidine and related drugs. Clin. Neuropharmacol. 21:1998;320-332.
    • (1998) Clin. Neuropharmacol. , vol.21 , pp. 320-332
    • Deutsch, S.I.1    Mastropaolo, J.2    Rosse, R.B.3
  • 247
    • 0030947654 scopus 로고    scopus 로고
    • Transporters buffer synaptically released glutamate on a submillisecond time scale
    • Diamond J.S., Jahr C.E. Transporters buffer synaptically released glutamate on a submillisecond time scale. J. Neurosci. 17:1997;4672-4687.
    • (1997) J. Neurosci. , vol.17 , pp. 4672-4687
    • Diamond, J.S.1    Jahr, C.E.2
  • 249
    • 0029993314 scopus 로고    scopus 로고
    • Transport and metabolism of L-glutamate during oxygenation, anoxia, and reoxygenation of rat cardiac myocytes
    • Dinkelborg L.M., Kinne R.K.H., Grieshaber M.K. Transport and metabolism of L-glutamate during oxygenation, anoxia, and reoxygenation of rat cardiac myocytes. Am. J. Physiol. 39:1996;H1825-H1832.
    • (1996) Am. J. Physiol. , vol.39 , pp. 1825-H1832
    • Dinkelborg, L.M.1    Kinne, R.K.H.2    Grieshaber, M.K.3
  • 250
    • 0033199996 scopus 로고    scopus 로고
    • Pathobiology of ischaemic stroke: An integrated view
    • Dirnagl U., Iadecola C., Moskowitz M.A. Pathobiology of ischaemic stroke: an integrated view. Trends Neurosci. 22:1999;391-397.
    • (1999) Trends Neurosci. , vol.22 , pp. 391-397
    • Dirnagl, U.1    Iadecola, C.2    Moskowitz, M.A.3
  • 252
    • 0017339785 scopus 로고
    • High affinity uptake of glutamate in terminals of corticostriatal axons
    • Divac I., Fonnum F., Storm-Mathisen J. High affinity uptake of glutamate in terminals of corticostriatal axons. Nature. 266:1977;377-378.
    • (1977) Nature , vol.266 , pp. 377-378
    • Divac, I.1    Fonnum, F.2    Storm-Mathisen, J.3
  • 253
    • 0033586654 scopus 로고    scopus 로고
    • Expression of glutamate transporters in the adult bovine corpus callosum
    • Domercq M., Matute C. Expression of glutamate transporters in the adult bovine corpus callosum. Mol. Brain Res. 67:1999;296-302.
    • (1999) Mol. Brain Res. , vol.67 , pp. 296-302
    • Domercq, M.1    Matute, C.2
  • 254
    • 0033008079 scopus 로고    scopus 로고
    • Expression of glutamate transporters in rat optic nerve oligodendrocytes
    • Domercq M., Sanchez-Gomez M.V., Areso P., Matute C. Expression of glutamate transporters in rat optic nerve oligodendrocytes. Eur. J. Neurosci. 11:1999;2226-2236.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 2226-2236
    • Domercq, M.1    Sanchez-Gomez, M.V.2    Areso, P.3    Matute, C.4
  • 255
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong H.L., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P. GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature. 386:1997;279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.L.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.5
  • 257
    • 0034112837 scopus 로고    scopus 로고
    • Substrate-stereoselectivity of a high-affinity glutamate transporter cloned from the CNS of the cockroach Diploptera punctata
    • Donly C., Jevnikar J., McLean H., Caveney S. Substrate-stereoselectivity of a high-affinity glutamate transporter cloned from the CNS of the cockroach Diploptera punctata. Insect Biochem. Mol. Biol. 30:2000;369-376.
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 369-376
    • Donly, C.1    Jevnikar, J.2    McLean, H.3    Caveney, S.4
  • 258
    • 0031987319 scopus 로고    scopus 로고
    • Venom phospholipase A2-induced impairment of glutamate uptake: An indirect and nonselective effect related to phospholipid hydrolysis
    • Dorandeu F., Antier D., Pernot-Marino I., Lapeyre P., Lallement G. Venom phospholipase A2-induced impairment of glutamate uptake: an indirect and nonselective effect related to phospholipid hydrolysis. J. Neurosci. Res. 51:1998;349-359.
    • (1998) J. Neurosci. Res. , vol.51 , pp. 349-359
    • Dorandeu, F.1    Antier, D.2    Pernot-Marino, I.3    Lapeyre, P.4    Lallement, G.5
  • 259
    • 0030036982 scopus 로고    scopus 로고
    • +-dependent L-glutamate transport activity in C6 glioma cells by phorbol ester
    • +-dependent L-glutamate transport activity in C6 glioma cells by phorbol ester. J. Neurochem. 67:1996;508-516.
    • (1996) J. Neurochem. , vol.67 , pp. 508-516
    • Dowd, L.A.1    Robinson, M.B.2
  • 260
    • 0029921679 scopus 로고    scopus 로고
    • +-dependent glutamate transport activity in synaptosomes, C6 glioma, and Xenopus oocytes expressing excitatory amino acid carrier 1 (EAAC1)
    • +-dependent glutamate transport activity in synaptosomes, C6 glioma, and Xenopus oocytes expressing excitatory amino acid carrier 1 (EAAC1). Mol. Pharmacol. 49:1996;465-473.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 465-473
    • Dowd, L.A.1    Coyle, A.J.2    Rothstein, J.D.3    Pritchett, D.B.4    Robinson, M.B.5
  • 261
    • 0019992714 scopus 로고
    • Characterization of L-glutamate uptake into and release from astrocytes and neurons cultured from different brain regions
    • Drejer J., Larsson O.M., Schousboe A. Characterization of L-glutamate uptake into and release from astrocytes and neurons cultured from different brain regions. Exp. Brain Res. 47:1982;259-269.
    • (1982) Exp. Brain Res. , vol.47 , pp. 259-269
    • Drejer, J.1    Larsson, O.M.2    Schousboe, A.3
  • 262
    • 0020574199 scopus 로고
    • Novel neuron-related regulatory mechanisms for astrocytic glutamate and GABA high affinity uptake
    • Drejer J., Meier E., Schousboe A. Novel neuron-related regulatory mechanisms for astrocytic glutamate and GABA high affinity uptake. Neurosci. Lett. 37:1983;301-306.
    • (1983) Neurosci. Lett. , vol.37 , pp. 301-306
    • Drejer, J.1    Meier, E.2    Schousboe, A.3
  • 263
    • 0021829328 scopus 로고
    • Cellular origin of ischemia-induced glutamate release from brain tissue in vivo and in vitro
    • Drejer J., Benveniste H., Diemer N.H., Schousboe A. Cellular origin of ischemia-induced glutamate release from brain tissue in vivo and in vitro. J. Neurochem. 45:1985;145-151.
    • (1985) J. Neurochem. , vol.45 , pp. 145-151
    • Drejer, J.1    Benveniste, H.2    Diemer, N.H.3    Schousboe, A.4
  • 264
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • Dringen R. Metabolism and functions of glutathione in brain. Prog. Neurobiol. 62:2000;649-671.
    • (2000) Prog. Neurobiol. , vol.62 , pp. 649-671
    • Dringen, R.1
  • 265
    • 0033501641 scopus 로고    scopus 로고
    • Glutamate induces rapid upregulation of astrocyte glutamate transport and cell-surface expression of GLAST
    • Duan S.M., Anderson C.M., Stein B.A., Swanson R.A. Glutamate induces rapid upregulation of astrocyte glutamate transport and cell-surface expression of GLAST. J. Neurosci. 19:1999;10193-10200.
    • (1999) J. Neurosci. , vol.19 , pp. 10193-10200
    • Duan, S.M.1    Anderson, C.M.2    Stein, B.A.3    Swanson, R.A.4
  • 266
    • 0023797159 scopus 로고
    • NMDA receptors activate the arachidonic acid cascade system in striatal neurons
    • Dumuis A., Sebben M., Haynes L., Pin J.-P., Bockaert J. NMDA receptors activate the arachidonic acid cascade system in striatal neurons. Nature. 336:1988;68-70.
    • (1988) Nature , vol.336 , pp. 68-70
    • Dumuis, A.1    Sebben, M.2    Haynes, L.3    Pin, J.-P.4    Bockaert, J.5
  • 267
    • 0032950134 scopus 로고    scopus 로고
    • An integrated view of pathophysiological models of schizophrenia
    • Duncan G.E., Sheitman B.B., Lieberman J.A. An integrated view of pathophysiological models of schizophrenia. Brain Res. Rev. 29:1999;250-264.
    • (1999) Brain Res. Rev. , vol.29 , pp. 250-264
    • Duncan, G.E.1    Sheitman, B.B.2    Lieberman, J.A.3
  • 268
    • 0032748509 scopus 로고    scopus 로고
    • Inducible expression and pharmacology of the human excitatory amino acid transporter 2 subtype of L-glutamate transporter
    • Dunlop J., Lou Z., Zhang Y., McIlvain H.B. Inducible expression and pharmacology of the human excitatory amino acid transporter 2 subtype of L-glutamate transporter. Br. J. Pharmacol. 128:1999;1485-1490.
    • (1999) Br. J. Pharmacol. , vol.128 , pp. 1485-1490
    • Dunlop, J.1    Lou, Z.2    Zhang, Y.3    McIlvain, H.B.4
  • 269
    • 0029921194 scopus 로고    scopus 로고
    • Long-term potentiation and functional synapse induction in developing hippocampus
    • Durand G.M., Kovalchuk Y., Konnerth A. Long-term potentiation and functional synapse induction in developing hippocampus. Nature. 381:1996;71-75.
    • (1996) Nature , vol.381 , pp. 71-75
    • Durand, G.M.1    Kovalchuk, Y.2    Konnerth, A.3
  • 270
    • 0027262604 scopus 로고
    • Extracellular hippocampal glutamate and spontaneous seizure in the conscious human brain
    • During M.J., Spencer D.D. Extracellular hippocampal glutamate and spontaneous seizure in the conscious human brain. Lancet. 341:1993;1607-1610.
    • (1993) Lancet , vol.341 , pp. 1607-1610
    • During, M.J.1    Spencer, D.D.2
  • 271
    • 0033168351 scopus 로고    scopus 로고
    • The concentration of synaptically released glutamate outside of the climbing fiber-Purkinje cell synaptic cleft
    • Dzubay J.A., Jahr C.E. The concentration of synaptically released glutamate outside of the climbing fiber-Purkinje cell synaptic cleft. J. Neurosci. 19:1999;5265-5274.
    • (1999) J. Neurosci. , vol.19 , pp. 5265-5274
    • Dzubay, J.A.1    Jahr, C.E.2
  • 273
    • 0033581830 scopus 로고    scopus 로고
    • Synapse structure: Glutamate receptors connected by the shanks
    • Ehlers M.D. Synapse structure: glutamate receptors connected by the shanks. Curr. Biol. 9:1999;R848-R850.
    • (1999) Curr. Biol. , vol.9 , pp. 848-R850
    • Ehlers, M.D.1
  • 274
    • 0026337224 scopus 로고
    • Glutamate uptake in primary cultures of biliary epithelial cells from normal rat liver
    • Eisenmann-Tappe I., Wizigmann S., Gebhardt R. Glutamate uptake in primary cultures of biliary epithelial cells from normal rat liver. Cell Biol. Toxicol. 7:1991;315-325.
    • (1991) Cell Biol. Toxicol. , vol.7 , pp. 315-325
    • Eisenmann-Tappe, I.1    Wizigmann, S.2    Gebhardt, R.3
  • 275
    • 0027392599 scopus 로고
    • Characterization of the glutamate transporter in retinal cones of the tiger salamander
    • Eliasof S., Werblin F. Characterization of the glutamate transporter in retinal cones of the tiger salamander. J. Neurosci. 13:1993;402-411.
    • (1993) J. Neurosci. , vol.13 , pp. 402-411
    • Eliasof, S.1    Werblin, F.2
  • 276
    • 0031972667 scopus 로고    scopus 로고
    • Excitatory amino acid transporters of the salamander retina: Identification, localization, and function
    • Eliasof S., Arriza J.L., Leighton B.H., Kavanaugh M.P., Amara S.G. Excitatory amino acid transporters of the salamander retina: identification, localization, and function. J. Neurosci. 18:1998;698-712.
    • (1998) J. Neurosci. , vol.18 , pp. 698-712
    • Eliasof, S.1    Arriza, J.L.2    Leighton, B.H.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 277
    • 0032078972 scopus 로고    scopus 로고
    • Localization and function of five glutamate transporters cloned from the salamander retina
    • Eliasof S., Arriza J.L., Leighton B.H., Amara S.G., Kavanaugh M.P. Localization and function of five glutamate transporters cloned from the salamander retina. Vision Res. 38:1998;1443-1454.
    • (1998) Vision Res. , vol.38 , pp. 1443-1454
    • Eliasof, S.1    Arriza, J.L.2    Leighton, B.H.3    Amara, S.G.4    Kavanaugh, M.P.5
  • 278
    • 0031555365 scopus 로고    scopus 로고
    • Expression of glutamate uptake transporters after dibutyryl cyclic AMP differentiation and traumatic injury in cultured astrocytes
    • Eng D.L., Lee Y.L., Lal P.G. Expression of glutamate uptake transporters after dibutyryl cyclic AMP differentiation and traumatic injury in cultured astrocytes. Brain Res. 778:1997;215-221.
    • (1997) Brain Res. , vol.778 , pp. 215-221
    • Eng, D.L.1    Lee, Y.L.2    Lal, P.G.3
  • 279
    • 0024742522 scopus 로고
    • Identification and sequence analysis of the Rhizobium meliloti DctA gene encoding the C4-dicarboxylate carrier
    • Engelke T., Jording D., Kapp D., Puhler A. Identification and sequence analysis of the Rhizobium meliloti DctA gene encoding the C4-dicarboxylate carrier. J. Bacteriol. 171:1989;5551-5560.
    • (1989) J. Bacteriol. , vol.171 , pp. 5551-5560
    • Engelke, T.1    Jording, D.2    Kapp, D.3    Puhler, A.4
  • 280
    • 0025275656 scopus 로고
    • Postnatal development of the excitatory amino acid system in visual cortex of the rat - Changes in uptake and levels of aspartate and glutamate
    • Erdö S.L., Wolff J.R. Postnatal development of the excitatory amino acid system in visual cortex of the rat - changes in uptake and levels of aspartate and glutamate. Int. J. Dev. Neurosci. 8:1990;205-208.
    • (1990) Int. J. Dev. Neurosci. , vol.8 , pp. 205-208
    • Erdö, S.L.1    Wolff, J.R.2
  • 281
    • 0020528956 scopus 로고
    • Aspartate transport in synaptosomes from rat brain
    • Erecinska M., Wantorsky D., Wilson D.F. Aspartate transport in synaptosomes from rat brain. J. Biol. Chem. 258:1983;9069-9077.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9069-9077
    • Erecinska, M.1    Wantorsky, D.2    Wilson, D.F.3
  • 282
    • 0023123012 scopus 로고
    • Amino acid neurotransmitters in the CNS. Relationships between net uptake and exchange in rat brain synaptosomes
    • Erecinska M., Nelson D. Amino acid neurotransmitters in the CNS. Relationships between net uptake and exchange in rat brain synaptosomes. FEBS Lett. 213:1987;61-66.
    • (1987) FEBS Lett. , vol.213 , pp. 61-66
    • Erecinska, M.1    Nelson, D.2
  • 283
    • 0029912099 scopus 로고    scopus 로고
    • Metabolic and energetic properties of isolated nerve ending particles (synaptosomes)
    • Erecinska, M., Nelson, D., Silver, I.A., 1996. Metabolic and energetic properties of isolated nerve ending particles (synaptosomes). Biochim. Biophys. Acta. 1277, 13-34.
    • (1996) Biochim. Biophys. Acta. , vol.1277 , pp. 13-34
    • Erecinska, M.1    Nelson, D.2    Silver, I.A.3
  • 284
    • 0025196959 scopus 로고
    • Metabolism and role of glutamate in mammalian brain
    • Erecinska M., Silver I.A. Metabolism and role of glutamate in mammalian brain. Prog. Neurobiol. 35:1990;245-296.
    • (1990) Prog. Neurobiol. , vol.35 , pp. 245-296
    • Erecinska, M.1    Silver, I.A.2
  • 285
    • 0026458380 scopus 로고
    • Expression cloning of a reserpine-sensitive vesicular monoamine transporter
    • Erickson J.D., Eiden L.E., Hoffman B.J. Expression cloning of a reserpine-sensitive vesicular monoamine transporter. Proc. Natl. Acad. Sci. USA. 89:1992;10993-10997.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10993-10997
    • Erickson, J.D.1    Eiden, L.E.2    Hoffman, B.J.3
  • 287
    • 0028785264 scopus 로고
    • Regional expression and dietary regulation of rat small intestinal peptide and amino acid transporter mRNAs
    • Erickson R.H., Gum J.R. Jr, Lindstrom M.M., McKean D., Kim Y.S. Regional expression and dietary regulation of rat small intestinal peptide and amino acid transporter mRNAs. Biochem. Biophys. Res. Commun. 216:1995;249-257.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 249-257
    • Erickson, R.H.1    Gum J.R., Jr.2    Lindstrom, M.M.3    McKean, D.4    Kim, Y.S.5
  • 291
    • 0028806645 scopus 로고
    • Immunocytochemical identification of cone bipolar cells in the rat retina
    • Euler T., Wassle H. Immunocytochemical identification of cone bipolar cells in the rat retina. J. Comp. Neurol. 361:1995;461-478.
    • (1995) J. Comp. Neurol. , vol.361 , pp. 461-478
    • Euler, T.1    Wassle, H.2
  • 292
    • 0031688235 scopus 로고    scopus 로고
    • Chronic ethanol consumption: From neuroadaptation to neurodegeneration
    • Fadda F., Rossetti Z.L. Chronic ethanol consumption: from neuroadaptation to neurodegeneration. Prog. Neurobiol. 56:1998;385-431.
    • (1998) Prog. Neurobiol. , vol.56 , pp. 385-431
    • Fadda, F.1    Rossetti, Z.L.2
  • 293
    • 0026540898 scopus 로고
    • Pharmacological strategies in CNS trauma
    • Faden A.I., Salzman S. Pharmacological strategies in CNS trauma. Trends Pharmacol. Sci. 13:1992;29-35.
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 29-35
    • Faden, A.I.1    Salzman, S.2
  • 294
    • 0024365739 scopus 로고
    • The role of excitatory amino acids and NMDA receptors in traumatic brain injury
    • Faden A.I., Demediuk P., Panter S.S., Vink R. The role of excitatory amino acids and NMDA receptors in traumatic brain injury. Science. 244:1989;798-800.
    • (1989) Science , vol.244 , pp. 798-800
    • Faden, A.I.1    Demediuk, P.2    Panter, S.S.3    Vink, R.4
  • 295
    • 0027565856 scopus 로고
    • Receptor subtype involved and mechanism of norepinephrine-induced stimulation of glutamate uptake into primary cultures of rat brain astrocytes
    • Fahrig T. Receptor subtype involved and mechanism of norepinephrine-induced stimulation of glutamate uptake into primary cultures of rat brain astrocytes. Glia. 7:1993;212-218.
    • (1993) Glia , vol.7 , pp. 212-218
    • Fahrig, T.1
  • 296
    • 0032479880 scopus 로고    scopus 로고
    • Ethanol and neurotransmitter interactions - From molecular to integrative effects
    • Faingold C.L., N'Gouemo P., Riaz A. Ethanol and neurotransmitter interactions - from molecular to integrative effects. Prog. Neurobiol. 55:1998;509-535.
    • (1998) Prog. Neurobiol. , vol.55 , pp. 509-535
    • Faingold, C.L.1    N'Gouemo, P.2    Riaz, A.3
  • 297
    • 0032699070 scopus 로고    scopus 로고
    • Functional diversity of excitatory amino acid transporters: Ion channel and transport modes
    • Fairman W.A., Amara S.G. Functional diversity of excitatory amino acid transporters: ion channel and transport modes. Am. J. Physiol. 277:1999;F481-F486.
    • (1999) Am. J. Physiol. , vol.277 , pp. 481-F486
    • Fairman, W.A.1    Amara, S.G.2
  • 298
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • Fairman W.A., Vandenberg R.J., Arriza J.L., Kavanaugh M.P., Amara S.G. An excitatory amino-acid transporter with properties of a ligand-gated chloride channel. Nature. 375:1995;599-603.
    • (1995) Nature , vol.375 , pp. 599-603
    • Fairman, W.A.1    Vandenberg, R.J.2    Arriza, J.L.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 299
    • 33644664236 scopus 로고    scopus 로고
    • Arachidonic acid elicits a substrate-gated proton current associated with the glutamate transporter EAAT4
    • Fairman W.A., Sonders M.S., Murdoch G.H., Amara S.G. Arachidonic acid elicits a substrate-gated proton current associated with the glutamate transporter EAAT4. Nat. Neurosci. 1:1998;105-113.
    • (1998) Nat. Neurosci. , vol.1 , pp. 105-113
    • Fairman, W.A.1    Sonders, M.S.2    Murdoch, G.H.3    Amara, S.G.4
  • 300
    • 0033165990 scopus 로고    scopus 로고
    • Experience-dependent development of NMDAR1 subunit expression in the lateral geniculate nucleus
    • Fava M.A., Duffy K.R., Murphy K.M. Experience-dependent development of NMDAR1 subunit expression in the lateral geniculate nucleus. Vis. Neurosci. 16:1999;781-789.
    • (1999) Vis. Neurosci. , vol.16 , pp. 781-789
    • Fava, M.A.1    Duffy, K.R.2    Murphy, K.M.3
  • 302
    • 0023007123 scopus 로고
    • Heterogeneity of sodium-dependent excitatory amino acid uptake mechanisms in rat brain
    • Ferkany J., Coyle J.T. Heterogeneity of sodium-dependent excitatory amino acid uptake mechanisms in rat brain. J. Neurosci. Res. 16:1986;491-503.
    • (1986) J. Neurosci. Res. , vol.16 , pp. 491-503
    • Ferkany, J.1    Coyle, J.T.2
  • 303
    • 0342471747 scopus 로고    scopus 로고
    • Rapid ischemic cell death in immature oligodendrocytes: A fatal glutamate release feedback loop
    • Fern R., Möller T. Rapid ischemic cell death in immature oligodendrocytes: a fatal glutamate release feedback loop. J. Neurosci. 20:2000;34-42.
    • (2000) J. Neurosci. , vol.20 , pp. 34-42
    • Fern, R.1    Möller, T.2
  • 306
    • 0022083950 scopus 로고
    • A possible mechanism of morphometric changes in dendritic spines induced by stimulation
    • Fifkova E. A possible mechanism of morphometric changes in dendritic spines induced by stimulation. Cell. Mol. Neurobiol. 5:1985;47-63.
    • (1985) Cell. Mol. Neurobiol. , vol.5 , pp. 47-63
    • Fifkova, E.1
  • 307
    • 0034657768 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide (PACAP), a neuron-derived peptide regulating glial glutamate transport and metabolism
    • Figiel M., Engele J. Pituitary adenylate cyclase-activating polypeptide (PACAP), a neuron-derived peptide regulating glial glutamate transport and metabolism. J. Neurosci. 20:2000;3596-3605.
    • (2000) J. Neurosci. , vol.20 , pp. 3596-3605
    • Figiel, M.1    Engele, J.2
  • 308
    • 0029943301 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha inhibits glutamate uptake by primary human astrocytes - Implications for pathogenesis of HIV-1 dementia
    • Fine S.M., Angel R.A., Perry S.W., Epstein L.G., Rothstein J.D., Dewhurst S., Gelbard H.A. Tumor necrosis factor alpha inhibits glutamate uptake by primary human astrocytes - implications for pathogenesis of HIV-1 dementia. J. Biol. Chem. 271:1996;15303-15306.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15303-15306
    • Fine, S.M.1    Angel, R.A.2    Perry, S.W.3    Epstein, L.G.4    Rothstein, J.D.5    Dewhurst, S.6    Gelbard, H.A.7
  • 309
    • 0022555698 scopus 로고
    • 3H]aspartate loaded gel particles permits restricted uptake sites for transmitter-selective axonal transport
    • 3H]aspartate loaded gel particles permits restricted uptake sites for transmitter-selective axonal transport. Exp. Brain Res. 63:1986;620-626.
    • (1986) Exp. Brain Res. , vol.63 , pp. 620-626
    • Fischer, B.O.1    Ottersen, O.P.2    Storm-Mathisen, J.3
  • 310
    • 0032078861 scopus 로고    scopus 로고
    • Rapid actin-based plasticity in dendritic spines
    • Fischer M., Kaech S., Knutti D., Matus A. Rapid actin-based plasticity in dendritic spines. Neuron. 20:1998;847-854.
    • (1998) Neuron , vol.20 , pp. 847-854
    • Fischer, M.1    Kaech, S.2    Knutti, D.3    Matus, A.4
  • 312
    • 0026331512 scopus 로고
    • Regional heterogeneity of L-glutamate and L-aspartate high-affinity uptake systems in the rat CNS
    • Fletcher E.J., Johnston G.A.R. Regional heterogeneity of L-glutamate and L-aspartate high-affinity uptake systems in the rat CNS. J. Neurochem. 57:1991;911-914.
    • (1991) J. Neurochem. , vol.57 , pp. 911-914
    • Fletcher, E.J.1    Johnston, G.A.R.2
  • 313
    • 0033982706 scopus 로고    scopus 로고
    • 35S]cystine transport into rat brain synaptosomes
    • 35S]cystine transport into rat brain synaptosomes. Neurochem. Int. 36:2000;513-521.
    • (2000) Neurochem. Int. , vol.36 , pp. 513-521
    • Flynn, J.1    McBean, G.J.2
  • 315
    • 0029901605 scopus 로고    scopus 로고
    • Chronic ethanol-mediated up-regulation of the N-methyl-D-aspartate receptor polypeptide subunits in mouse cortical neurons in culture
    • Follesa P., Ticku M.K. Chronic ethanol-mediated up-regulation of the N-methyl-D-aspartate receptor polypeptide subunits in mouse cortical neurons in culture. J. Biol. Chem. 271:1996;13297-13299.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13297-13299
    • Follesa, P.1    Ticku, M.K.2
  • 316
    • 0021330769 scopus 로고
    • Glutamate: A neurotransmitter in mammalian brain
    • Fonnum F. Glutamate: a neurotransmitter in mammalian brain. J. Neurochem. 42:1984;1-11.
    • (1984) J. Neurochem. , vol.42 , pp. 1-11
    • Fonnum, F.1
  • 317
    • 0027355540 scopus 로고
    • Regulation of the synthesis of the transmitter glutamate pool
    • Fonnum F. Regulation of the synthesis of the transmitter glutamate pool. Prog. Biophys. Mol. Biol. 60:1993;47-57.
    • (1993) Prog. Biophys. Mol. Biol. , vol.60 , pp. 47-57
    • Fonnum, F.1
  • 318
    • 0019434631 scopus 로고
    • Biochemical evidence for glutamate as neurotransmitter in corticostriatal and corticothalamic fibres in rat brain
    • Fonnum F., Storm-Mathisen J., Divac I. Biochemical evidence for glutamate as neurotransmitter in corticostriatal and corticothalamic fibres in rat brain. Neuroscience. 6:1981;863-873.
    • (1981) Neuroscience , vol.6 , pp. 863-873
    • Fonnum, F.1    Storm-Mathisen, J.2    Divac, I.3
  • 319
    • 0031172242 scopus 로고    scopus 로고
    • Synaptic transmission: Well-placed modulators
    • Forsythe I.D., Barnes-Davies M. Synaptic transmission: well-placed modulators. Curr. Biol. 7:1997;R362-R365.
    • (1997) Curr. Biol. , vol.7 , pp. 362-R365
    • Forsythe, I.D.1    Barnes-Davies, M.2
  • 320
    • 0021434352 scopus 로고
    • Acidic amino acid binding sites in mammalian neuronal membranes: Their characteristics and relationship to synaptic receptors
    • Foster A.C., Fagg G.E. Acidic amino acid binding sites in mammalian neuronal membranes: their characteristics and relationship to synaptic receptors. Brain Res. Rev. 7:1984;103-164.
    • (1984) Brain Res. Rev. , vol.7 , pp. 103-164
    • Foster, A.C.1    Fagg, G.E.2
  • 321
    • 0029927127 scopus 로고    scopus 로고
    • Glutamate receptor blockade at cortical synapses disrupts development of thalamocortical and columnar organization in somatosensory cortex
    • Fox K., Schlaggar B.L., Glazewski S., O'Leary D.D.M. Glutamate receptor blockade at cortical synapses disrupts development of thalamocortical and columnar organization in somatosensory cortex. Proc. Natl. Acad. Sci. USA. 93:1996;5584-5589.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5584-5589
    • Fox, K.1    Schlaggar, B.L.2    Glazewski, S.3    O'Leary, D.D.M.4
  • 322
    • 0025269014 scopus 로고
    • Development of excitatory amino acid induced cytotoxicity in cultured neurons
    • Frandsen A., Schousboe A. Development of excitatory amino acid induced cytotoxicity in cultured neurons. Int. J. Dev. Neurosci. 8:1990;209-216.
    • (1990) Int. J. Dev. Neurosci. , vol.8 , pp. 209-216
    • Frandsen, A.1    Schousboe, A.2
  • 323
    • 0031879593 scopus 로고    scopus 로고
    • The expression of the glial glutamate transporter protein EAAT2 in motor neuron disease: An immunohistochemical study
    • Fray A.E., Ince P.G., Banner S.J., Milton L.D., Usher P.A., Cookson M.R., Shaw P.J. The expression of the glial glutamate transporter protein EAAT2 in motor neuron disease: an immunohistochemical study. Eur. J. Neurosci. 10:1998;2481-2489.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2481-2489
    • Fray, A.E.1    Ince, P.G.2    Banner, S.J.3    Milton, L.D.4    Usher, P.A.5    Cookson, M.R.6    Shaw, P.J.7
  • 324
    • 0026035179 scopus 로고
    • Electrogenic uptake contributes a major component of the depolarizing action of L-glutamate in rat hippocampal slices
    • Frenguelli B.G., Blake J.F., Brown M.W., Collingridge G.L. Electrogenic uptake contributes a major component of the depolarizing action of L-glutamate in rat hippocampal slices. Br. J. Pharmacol. 102:1991;355-362.
    • (1991) Br. J. Pharmacol. , vol.102 , pp. 355-362
    • Frenguelli, B.G.1    Blake, J.F.2    Brown, M.W.3    Collingridge, G.L.4
  • 325
    • 0030806863 scopus 로고    scopus 로고
    • 2 radical anion), superoxide dismutases, and related matters
    • 2 radical anion), superoxide dismutases, and related matters. J. Biol. Chem. 272:1997;18515-18517.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 326
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst T.R., Niles E.G., Studier W., Moss B. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA. 83:1986;8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, W.3    Moss, B.4
  • 327
    • 0029112782 scopus 로고
    • Na-dependent glutamate transport in high K and high glutathione (HK/HG) and high K and low glutathione (HK/LG) dog red blood cells
    • Fujise H., Hamada Y., Mori M., Ochiai H. Na-dependent glutamate transport in high K and high glutathione (HK/HG) and high K and low glutathione (HK/LG) dog red blood cells. Biochim. Biophys. Acta. 1239:1995;22-26.
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 22-26
    • Fujise, H.1    Hamada, Y.2    Mori, M.3    Ochiai, H.4
  • 328
    • 0030929239 scopus 로고    scopus 로고
    • Immunocytochemical localization of a high-affinity glutamate-aspartate transporter, GLAST, in the rat and guinea-pig cochlea
    • Furness D.N., Lehre K.P. Immunocytochemical localization of a high-affinity glutamate-aspartate transporter, GLAST, in the rat and guinea-pig cochlea. Eur. J. Neurosci. 9:1997;1961-1969.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1961-1969
    • Furness, D.N.1    Lehre, K.P.2
  • 329
    • 0018844260 scopus 로고
    • Types of nerves in the enteric nervous system
    • Furness J.B., Costa M. Types of nerves in the enteric nervous system. Neuroscience. 5:1980;1-20.
    • (1980) Neuroscience , vol.5 , pp. 1-20
    • Furness, J.B.1    Costa, M.2
  • 330
    • 0031563761 scopus 로고    scopus 로고
    • Cellular and synaptic localization of the neuronal glutamate transporters excitatory amino acid transporter 3 and 4
    • Furuta A., Martin L.J., Lin C.L.G., Dykes-Hoberg M., Rothstein J.D. Cellular and synaptic localization of the neuronal glutamate transporters excitatory amino acid transporter 3 and 4. Neuroscience. 81:1997;1031-1042.
    • (1997) Neuroscience , vol.81 , pp. 1031-1042
    • Furuta, A.1    Martin, L.J.2    Lin, C.L.G.3    Dykes-Hoberg, M.4    Rothstein, J.D.5
  • 331
    • 0030782403 scopus 로고    scopus 로고
    • Glutamate transporter protein subtypes are expressed differentially during rat CNS development
    • Furuta A., Rothstein J.D., Martin L.J. Glutamate transporter protein subtypes are expressed differentially during rat CNS development. J. Neurosci. 17:1997;8363-8375.
    • (1997) J. Neurosci. , vol.17 , pp. 8363-8375
    • Furuta, A.1    Rothstein, J.D.2    Martin, L.J.3
  • 332
    • 0025352932 scopus 로고
    • Acromelic acid-C - A new toxic constituent of Clitocybe acromelalga - An efficient isolation of acromelic acids
    • Fushiya S., Sato S., Kanazawa T., Kusano G., Nozoe S. Acromelic acid-C - a new toxic constituent of Clitocybe acromelalga - an efficient isolation of acromelic acids. Tetrahedron Lett. 31:1990;3901-3904.
    • (1990) Tetrahedron Lett. , vol.31 , pp. 3901-3904
    • Fushiya, S.1    Sato, S.2    Kanazawa, T.3    Kusano, G.4    Nozoe, S.5
  • 333
    • 0029801022 scopus 로고    scopus 로고
    • Amino acid neurotransmission: Dynamics of vesicular uptake
    • Fykse E.M., Fonnum F. Amino acid neurotransmission: dynamics of vesicular uptake. Neurochem. Res. 21:1996;1053-1060.
    • (1996) Neurochem. Res. , vol.21 , pp. 1053-1060
    • Fykse, E.M.1    Fonnum, F.2
  • 334
    • 0026518395 scopus 로고
    • Inhibition of L-glutamate uptake into synaptic vesicles
    • Fykse E.M., Iversen E.G., Fonnum F. Inhibition of L-glutamate uptake into synaptic vesicles. Neurosci. Lett. 135:1992;125-128.
    • (1992) Neurosci. Lett. , vol.135 , pp. 125-128
    • Fykse, E.M.1    Iversen, E.G.2    Fonnum, F.3
  • 335
    • 0029743048 scopus 로고    scopus 로고
    • Norepinephrine transporters have channel modes of conduction
    • Galli A., Blakely R.D., Defelice L.J. Norepinephrine transporters have channel modes of conduction. Proc. Natl. Acad. Sci. USA. 93:1996;8671-8676.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8671-8676
    • Galli, A.1    Blakely, R.D.2    Defelice, L.J.3
  • 336
    • 0030982172 scopus 로고    scopus 로고
    • Drosophila serotonin transporters have voltage-dependent uptake coupled to a serotonin-gated ion channel
    • Galli A., Petersen C.I., Deblaquiere M., Blakely R.D., Defelice L.J. Drosophila serotonin transporters have voltage-dependent uptake coupled to a serotonin-gated ion channel. J. Neurosci. 17:1997;3401-3411.
    • (1997) J. Neurosci. , vol.17 , pp. 3401-3411
    • Galli, A.1    Petersen, C.I.2    Deblaquiere, M.3    Blakely, R.D.4    Defelice, L.J.5
  • 337
    • 0033179038 scopus 로고    scopus 로고
    • L-Proline and L-pipecolate induce enkephalin-sensitive currents in human embryonic kidney 293 cells transfected with the high-affinity mammalian brain L-proline transporter
    • Galli A., Jayanthi L.D., Ramsey I.S., Miller J.W., Fremeau R.T., Defelice L.J. L-Proline and L-pipecolate induce enkephalin-sensitive currents in human embryonic kidney 293 cells transfected with the high-affinity mammalian brain L-proline transporter. J. Neurosci. 19:1999;6290-6297.
    • (1999) J. Neurosci. , vol.19 , pp. 6290-6297
    • Galli, A.1    Jayanthi, L.D.2    Ramsey, I.S.3    Miller, J.W.4    Fremeau, R.T.5    Defelice, L.J.6
  • 339
    • 0031953107 scopus 로고    scopus 로고
    • Modulation of human glutamate transporter activity by phorbol ester
    • Ganel R., Crosson C.E. Modulation of human glutamate transporter activity by phorbol ester. J. Neurochem. 70:1998;993-1000.
    • (1998) J. Neurochem. , vol.70 , pp. 993-1000
    • Ganel, R.1    Crosson, C.E.2
  • 341
    • 0022270623 scopus 로고
    • 3H]aspartate accumulation in mouse cerebellar slices
    • 3H]aspartate accumulation in mouse cerebellar slices. Brain Res. 343:1985;129-136.
    • (1985) Brain Res. , vol.343 , pp. 129-136
    • Garthwaite, G.1    Garthwaite, J.2
  • 342
    • 0023856209 scopus 로고
    • 3H]aspartate uptake sites in mouse cerebellar slices shows poor labeling of mossy fibre terminals
    • 3H]aspartate uptake sites in mouse cerebellar slices shows poor labeling of mossy fibre terminals. Brain Res. 440:1988;162-166.
    • (1988) Brain Res. , vol.440 , pp. 162-166
    • Garthwaite, G.1    Garthwaite, J.2
  • 343
    • 0026562002 scopus 로고
    • Glutamate toxicity - An experimental and theoretical analysis
    • Garthwaite G., Williams G.D., Garthwaite J. Glutamate toxicity - an experimental and theoretical analysis. Eur. J. Neurosci. 4:1992;353-360.
    • (1992) Eur. J. Neurosci. , vol.4 , pp. 353-360
    • Garthwaite, G.1    Williams, G.D.2    Garthwaite, J.3
  • 344
    • 0343340425 scopus 로고    scopus 로고
    • Characterization of the interactions between the glycine transporters GLYT1 and GLYT2 and the SNARE protein syntaxin 1A
    • Geerlings A., Lopez-Corcuera B., Aragon C. Characterization of the interactions between the glycine transporters GLYT1 and GLYT2 and the SNARE protein syntaxin 1A. FEBS Lett. 470:2000;51-54.
    • (2000) FEBS Lett. , vol.470 , pp. 51-54
    • Geerlings, A.1    Lopez-Corcuera, B.2    Aragon, C.3
  • 345
    • 0030840881 scopus 로고    scopus 로고
    • High affinity glutamate transporters: Regulation of expression and activity
    • Gegelashvili G., Schousboe A. High affinity glutamate transporters: regulation of expression and activity. Mol. Pharmacol. 52:1997;6-15.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 6-15
    • Gegelashvili, G.1    Schousboe, A.2
  • 346
    • 0032006244 scopus 로고    scopus 로고
    • Cellular distribution and kinetic properties of high-affinity glutamate transporters
    • Gegelashvili G., Schousboe A. Cellular distribution and kinetic properties of high-affinity glutamate transporters. Brain Res. Bull. 45:1998;233-238.
    • (1998) Brain Res. Bull. , vol.45 , pp. 233-238
    • Gegelashvili, G.1    Schousboe, A.2
  • 348
    • 0030657941 scopus 로고    scopus 로고
    • Neuronal soluble factors differentially regulate the expression of the GLT1 and GLAST glutamate transporters in cultured astroglia
    • Gegelashvili G., Danbolt N.C., Schousboe A. Neuronal soluble factors differentially regulate the expression of the GLT1 and GLAST glutamate transporters in cultured astroglia. J. Neurochem. 69:1997;2612-2615.
    • (1997) J. Neurochem. , vol.69 , pp. 2612-2615
    • Gegelashvili, G.1    Danbolt, N.C.2    Schousboe, A.3
  • 349
    • 0034257164 scopus 로고    scopus 로고
    • The high-affinity glutamate transporters GLT1, GLAST and EAAT4 are regulated via different signalling mechanisms
    • Gegelashvili G., Dehnes Y., Danbolt N.C., Schousboe A. The high-affinity glutamate transporters GLT1, GLAST and EAAT4 are regulated via different signalling mechanisms. Neurochem. Int. 37:2000;163-170.
    • (2000) Neurochem. Int. , vol.37 , pp. 163-170
    • Gegelashvili, G.1    Dehnes, Y.2    Danbolt, N.C.3    Schousboe, A.4
  • 350
    • 0028054064 scopus 로고
    • Glutamate efflux via the reversal of the sodium-dependent glutamate transporter caused by glycolytic inhibition in rat cultured astrocytes
    • Gemba T., Oshima T., Ninomiya M. Glutamate efflux via the reversal of the sodium-dependent glutamate transporter caused by glycolytic inhibition in rat cultured astrocytes. Neuroscience. 63:1994;789-795.
    • (1994) Neuroscience , vol.63 , pp. 789-795
    • Gemba, T.1    Oshima, T.2    Ninomiya, M.3
  • 352
    • 0025071511 scopus 로고
    • Region-selective stress-induced increase of glutamate uptake and release in rat forebrain
    • Gilad G.M., Gilad V.H., Wyatt R.J., Tizabi Y. Region-selective stress-induced increase of glutamate uptake and release in rat forebrain. Brain Res. 525:1990;335-338.
    • (1990) Brain Res. , vol.525 , pp. 335-338
    • Gilad, G.M.1    Gilad, V.H.2    Wyatt, R.J.3    Tizabi, Y.4
  • 353
    • 0028822475 scopus 로고
    • Regional deafferentation down-regulates subtypes of glutamate transporter proteins
    • Ginsberg S.D., Martin L.J., Rothstein J.D. Regional deafferentation down-regulates subtypes of glutamate transporter proteins. J. Neurochem. 65:1995;2800-2803.
    • (1995) J. Neurochem. , vol.65 , pp. 2800-2803
    • Ginsberg, S.D.1    Martin, L.J.2    Rothstein, J.D.3
  • 354
    • 0029795954 scopus 로고    scopus 로고
    • Fimbria-fornix transections selectively down-regulate subtypes of glutamate transporter and glutamate receptor proteins in septum and hippocampus
    • Ginsberg S.D., Rothstein J.D., Price D.L., Martin L.J. Fimbria-fornix transections selectively down-regulate subtypes of glutamate transporter and glutamate receptor proteins in septum and hippocampus. J. Neurochem. 67:1996;1208-1216.
    • (1996) J. Neurochem. , vol.67 , pp. 1208-1216
    • Ginsberg, S.D.1    Rothstein, J.D.2    Price, D.L.3    Martin, L.J.4
  • 355
    • 0015372802 scopus 로고
    • The free amino acids in human cerebrospinal fluid
    • Gjessing L.R., Gjesdahl P., Sjaastad O. The free amino acids in human cerebrospinal fluid. J. Neurochem. 19:1972;1807-1808.
    • (1972) J. Neurochem. , vol.19 , pp. 1807-1808
    • Gjessing, L.R.1    Gjesdahl, P.2    Sjaastad, O.3
  • 356
    • 0034010338 scopus 로고    scopus 로고
    • Differential effects of BDNF, ADNF9, and TNF alpha on levels of NMDA receptor subunits, calcium homeostasis, and neuronal vulnerability to excitotoxicity
    • Glazner G.W., Mattson M.P. Differential effects of BDNF, ADNF9, and TNF alpha on levels of NMDA receptor subunits, calcium homeostasis, and neuronal vulnerability to excitotoxicity. Exp. Neurol. 161:2000;442-452.
    • (2000) Exp. Neurol. , vol.161 , pp. 442-452
    • Glazner, G.W.1    Mattson, M.P.2
  • 357
    • 0029112937 scopus 로고
    • Detection of free radical activity during transient global ischemia and recirculation: Effects of intraischemic brain temperature modulation
    • Globus M.Y., Busto R., Lin B., Schnippering H., Ginsberg M.D. Detection of free radical activity during transient global ischemia and recirculation: effects of intraischemic brain temperature modulation. J. Neurochem. 65:1995;1250-1256.
    • (1995) J. Neurochem. , vol.65 , pp. 1250-1256
    • Globus, M.Y.1    Busto, R.2    Lin, B.3    Schnippering, H.4    Ginsberg, M.D.5
  • 358
    • 0032912997 scopus 로고    scopus 로고
    • The consequences of traumatic brain injury on cerebral blood flow and autoregulation: A review
    • Golding E.M., Robertson C.S., Bryan R.M. The consequences of traumatic brain injury on cerebral blood flow and autoregulation: a review. Clin. Exp. Hypertens. 21:1999;299-332.
    • (1999) Clin. Exp. Hypertens. , vol.21 , pp. 299-332
    • Golding, E.M.1    Robertson, C.S.2    Bryan, R.M.3
  • 359
    • 0028917854 scopus 로고
    • Regulation by phorbol esters of the glycine transporter (GLYT1) in glioblastoma cells
    • Gomeza J., Zafra F., Olivares L., Gimenez C., Aragón C. Regulation by phorbol esters of the glycine transporter (GLYT1) in glioblastoma cells. Biochim. Biophys. Acta. 1233:1995;41-46.
    • (1995) Biochim. Biophys. Acta , vol.1233 , pp. 41-46
    • Gomeza, J.1    Zafra, F.2    Olivares, L.3    Gimenez, C.4    Aragón, C.5
  • 360
    • 0032408313 scopus 로고    scopus 로고
    • Postsynaptically silent synapses in single neuron cultures
    • Gomperts S.N., Rao A., Craig A.M., Malenka R.C., Nicoll R.A. Postsynaptically silent synapses in single neuron cultures. Neuron. 21:1998;1443-1451.
    • (1998) Neuron , vol.21 , pp. 1443-1451
    • Gomperts, S.N.1    Rao, A.2    Craig, A.M.3    Malenka, R.C.4    Nicoll, R.A.5
  • 361
    • 1842329222 scopus 로고    scopus 로고
    • +-dependent high affinity glutamate/aspartate transporter in cultured Bergmann glia by phorbol esters
    • +-dependent high affinity glutamate/aspartate transporter in cultured Bergmann glia by phorbol esters. J. Neurosci. Res. 50:1997;585-590.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 585-590
    • Gonzalez, M.I.1    Ortega, A.2
  • 362
    • 0345535774 scopus 로고    scopus 로고
    • Sodium-dependent glutamate transport in Müller glial cells: Regulation by phorbol esters
    • Gonzalez M.I., Lopez-Colome A.M., Ortega A. Sodium-dependent glutamate transport in Müller glial cells: regulation by phorbol esters. Brain Res. 831:1999;140-145.
    • (1999) Brain Res. , vol.831 , pp. 140-145
    • Gonzalez, M.I.1    Lopez-Colome, A.M.2    Ortega, A.3
  • 363
    • 0023730911 scopus 로고
    • Partial purification of the sodium- And potassium-coupled L-glutamate transport glycoprotein from rat brain
    • Gordon A.M., Kanner B.I. Partial purification of the sodium- and potassium-coupled L-glutamate transport glycoprotein from rat brain. Biochim. Biophys. Acta. 944:1988;90-96.
    • (1988) Biochim. Biophys. Acta , vol.944 , pp. 90-96
    • Gordon, A.M.1    Kanner, B.I.2
  • 364
    • 0027937548 scopus 로고
    • Oxidative stress: Free radical production in neural degeneration
    • Gotz M.E., Kunig G., Riederer P., Youdim M.B.H. Oxidative stress: free radical production in neural degeneration. Pharmacol. Ther. 63:1994;37-122.
    • (1994) Pharmacol. Ther. , vol.63 , pp. 37-122
    • Gotz, M.E.1    Kunig, G.2    Riederer, P.3    Youdim, M.B.H.4
  • 365
    • 0025268505 scopus 로고
    • Sodium-dependent D-aspartate 'binding' is not a measure of presynaptic neuronal uptake sites in an autoradiographic assay
    • Greenamyre J.T., Higgins D.S., Young A.B. Sodium-dependent D-aspartate 'binding' is not a measure of presynaptic neuronal uptake sites in an autoradiographic assay. Brain Res. 511:1990;310-318.
    • (1990) Brain Res. , vol.511 , pp. 310-318
    • Greenamyre, J.T.1    Higgins, D.S.2    Young, A.B.3
  • 366
    • 0029992108 scopus 로고    scopus 로고
    • Bioenergetics and glutamate excitotoxicity
    • Greene J.G., Greenamyre J.T. Bioenergetics and glutamate excitotoxicity. Prog. Neurobiol. 48:1996;613.
    • (1996) Prog. Neurobiol. , vol.48 , pp. 613
    • Greene, J.G.1    Greenamyre, J.T.2
  • 368
    • 0034662861 scopus 로고    scopus 로고
    • Glutamate translocation of the neuronal glutamate transporter EAAC1 occurs within milliseconds
    • Grewer C., Watzke N., Wiessner M., Rauen T. Glutamate translocation of the neuronal glutamate transporter EAAC1 occurs within milliseconds. Proc. Natl. Acad. Sci. USA. 97:2000;9706-9711.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9706-9711
    • Grewer, C.1    Watzke, N.2    Wiessner, M.3    Rauen, T.4
  • 369
    • 0024314299 scopus 로고
    • Inhibition by excitatory sulphur amino acids of the high-affinity L-glutamate transporter in synaptosomes and in primary cultures of cortical astrocytes and cerebellar neurons
    • Griffiths R., Grieve A., Dunlop J., Damgaard I., Fosmark H., Schousboe A. Inhibition by excitatory sulphur amino acids of the high-affinity L-glutamate transporter in synaptosomes and in primary cultures of cortical astrocytes and cerebellar neurons. Neurochem. Res. 14:1989;333-343.
    • (1989) Neurochem. Res. , vol.14 , pp. 333-343
    • Griffiths, R.1    Grieve, A.2    Dunlop, J.3    Damgaard, I.4    Fosmark, H.5    Schousboe, A.6
  • 370
    • 0028144230 scopus 로고
    • L-trans-pyrrolidine-2,4-dicarboxylate and cis-1-aminocyclobutane-1,3-dicarboxylate behave as transportable, competitive inhibitors of the high-affinity glutamate transporters
    • Griffiths R., Dunlop J., Gorman A., Senior J., Grieve A. L-trans-pyrrolidine-2,4-dicarboxylate and cis-1-aminocyclobutane-1,3-dicarboxylate behave as transportable, competitive inhibitors of the high-affinity glutamate transporters. Biochem. Pharmacol. 47:1994;267-274.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 267-274
    • Griffiths, R.1    Dunlop, J.2    Gorman, A.3    Senior, J.4    Grieve, A.5
  • 371
    • 0025308689 scopus 로고
    • Relationship between domoic acid levels in the blue mussel (Mytilus edulis) and toxicity in mice
    • Grimmelt B., Nijjar M.S., Brown J., Macnair N., Wagner S., Johnson G.R., Amend J.F. Relationship between domoic acid levels in the blue mussel (Mytilus edulis) and toxicity in mice. Toxicon. 28:1990;501-508.
    • (1990) Toxicon , vol.28 , pp. 501-508
    • Grimmelt, B.1    Nijjar, M.S.2    Brown, J.3    Macnair, N.4    Wagner, S.5    Johnson, G.R.6    Amend, J.F.7
  • 372
    • 0029041792 scopus 로고
    • Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states
    • Grunewald M., Kanner B. Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states. J. Biol. Chem. 270:1995;17017-17024.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17017-17024
    • Grunewald, M.1    Kanner, B.2
  • 373
    • 0034737622 scopus 로고    scopus 로고
    • The accessibility of a novel reentrant loop of the glutamate transporter GLT-1 is restricted by its substrate
    • Grunewald M., Kanner B.I. The accessibility of a novel reentrant loop of the glutamate transporter GLT-1 is restricted by its substrate. J. Biol. Chem. 275:2000;9684-9689.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9684-9689
    • Grunewald, M.1    Kanner, B.I.2
  • 374
    • 0032169137 scopus 로고    scopus 로고
    • Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology
    • Grunewald M., Bendahan A., Kanner B.I. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Neuron. 21:1998;623-632.
    • (1998) Neuron , vol.21 , pp. 623-632
    • Grunewald, M.1    Bendahan, A.2    Kanner, B.I.3
  • 375
    • 0027483125 scopus 로고
    • Ascorbic acid in the brain
    • Grunewald R.A. Ascorbic acid in the brain. Brain Res. Rev. 18:1993;123-133.
    • (1993) Brain Res. Rev. , vol.18 , pp. 123-133
    • Grunewald, R.A.1
  • 376
    • 0034724370 scopus 로고    scopus 로고
    • Identification and characterization of an amino acid transporter expressed differentially in liver
    • Gu S.M., Roderick H.L., Camacho P., Jiang J.X. Identification and characterization of an amino acid transporter expressed differentially in liver. Proc. Natl. Acad. Sci. USA. 97:2000;3230-3235.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3230-3235
    • Gu, S.M.1    Roderick, H.L.2    Camacho, P.3    Jiang, J.X.4
  • 379
    • 70350335822 scopus 로고    scopus 로고
    • Aspartate - Neurochemical evidence for a transmitter role
    • O.P. Ottersen, & J. Storm-Mathisen. Amsterdam: Elsevier
    • Gundersen V., Storm-Mathisen J. Aspartate - Neurochemical evidence for a transmitter role. Ottersen O.P., Storm-Mathisen J. Glutamate. 2000;45-62 Elsevier, Amsterdam.
    • (2000) Glutamate , pp. 45-62
    • Gundersen, V.1    Storm-Mathisen, J.2
  • 380
    • 0027363753 scopus 로고
    • Demonstration of glutamate/aspartate uptake activity in nerve endings by use of antibodies recognizing exogenous D-aspartate
    • Gundersen V., Danbolt N.C., Ottersen O.P., Storm-Mathisen J. Demonstration of glutamate/aspartate uptake activity in nerve endings by use of antibodies recognizing exogenous D-aspartate. Neuroscience. 57:1993;97-111.
    • (1993) Neuroscience , vol.57 , pp. 97-111
    • Gundersen, V.1    Danbolt, N.C.2    Ottersen, O.P.3    Storm-Mathisen, J.4
  • 381
    • 0029966433 scopus 로고    scopus 로고
    • Selective excitatory amino acid uptake in glutamatergic nerve terminals and in glia in the rat striatum: Quantitative electron microscopic immunocytochemistry of exogenous D-aspartate and endogenous glutamate and GABA
    • Gundersen V., Ottersen O.P., Storm-Mathisen J. Selective excitatory amino acid uptake in glutamatergic nerve terminals and in glia in the rat striatum: quantitative electron microscopic immunocytochemistry of exogenous D-aspartate and endogenous glutamate and GABA. Eur. J. Neurosci. 8:1996;758-765.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 758-765
    • Gundersen, V.1    Ottersen, O.P.2    Storm-Mathisen, J.3
  • 382
    • 0032529722 scopus 로고    scopus 로고
    • Synaptic vesicular localization and exocytosis of L-aspartate in excitatory nerve terminals: A quantitative immunogold analysis in rat hippocampus
    • Gundersen V., Chaudhry F.A., Bjaalie J.G., Fonnum F., Ottersen O.P., Storm-Mathisen J. Synaptic vesicular localization and exocytosis of L-aspartate in excitatory nerve terminals: a quantitative immunogold analysis in rat hippocampus. J. Neurosci. 18:1998;6059-6070.
    • (1998) J. Neurosci. , vol.18 , pp. 6059-6070
    • Gundersen, V.1    Chaudhry, F.A.2    Bjaalie, J.G.3    Fonnum, F.4    Ottersen, O.P.5    Storm-Mathisen, J.6
  • 383
    • 0002639306 scopus 로고    scopus 로고
    • Neurotrophic factors protect cortical synaptic terminals against amyloid- And oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function
    • Guo Z.H., Mattson M.P. Neurotrophic factors protect cortical synaptic terminals against amyloid- and oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function. Cereb. Cortex. 10:2000;50-57.
    • (2000) Cereb. Cortex , vol.10 , pp. 50-57
    • Guo, Z.H.1    Mattson, M.P.2
  • 384
    • 0034116190 scopus 로고    scopus 로고
    • ALS-linked Cu/Zn-SOD mutation impairs cerebral synaptic glucose and glutamate transport and exacerbates ischemic brain injury
    • Guo Z., Kindy M.S., Kruman I., Mattson M.P. ALS-linked Cu/Zn-SOD mutation impairs cerebral synaptic glucose and glutamate transport and exacerbates ischemic brain injury. J. Cereb. Blood Flow Metab. 20:2000;463-468.
    • (2000) J. Cereb. Blood Flow Metab. , vol.20 , pp. 463-468
    • Guo, Z.1    Kindy, M.S.2    Kruman, I.3    Mattson, M.P.4
  • 385
    • 0034116190 scopus 로고    scopus 로고
    • ALS-linked Cu/Zn-SOD mutation impairs cerebral synaptic glucose and glutamate transport and exacerbates ischemic brain injury
    • Guo Z.H., Kindy M.S., Kruman I., Mattson M.P. ALS-linked Cu/Zn-SOD mutation impairs cerebral synaptic glucose and glutamate transport and exacerbates ischemic brain injury. J. Cereb. Blood Flow Metab. 20:2000;463-468.
    • (2000) J. Cereb. Blood Flow Metab. , vol.20 , pp. 463-468
    • Guo, Z.H.1    Kindy, M.S.2    Kruman, I.3    Mattson, M.P.4
  • 386
    • 0027340070 scopus 로고
    • 2 deprivation in the central nervous system: On mechanisms of neuronal response, differential sensitivity and injury
    • 2 deprivation in the central nervous system: on mechanisms of neuronal response, differential sensitivity and injury. Prog. Neurobiol. 40:1993;277-318.
    • (1993) Prog. Neurobiol. , vol.40 , pp. 277-318
    • Haddad, G.G.1    Jiang, C.2
  • 387
    • 0030014686 scopus 로고    scopus 로고
    • Genomic organization, promoter analysis, and chromosomal localization of the gene for the mouse glial high-affinity glutamate transporter Slc1a3
    • Hagiwara T., Tanaka K., Takai S., Maenohikichi Y., Mukainaka Y., Wada K. Genomic organization, promoter analysis, and chromosomal localization of the gene for the mouse glial high-affinity glutamate transporter Slc1a3. Genomics. 33:1996;508-515.
    • (1996) Genomics , vol.33 , pp. 508-515
    • Hagiwara, T.1    Tanaka, K.2    Takai, S.3    Maenohikichi, Y.4    Mukainaka, Y.5    Wada, K.6
  • 388
    • 0034554777 scopus 로고    scopus 로고
    • Exacerbation of noise-induced hearing loss in mice lacking the glutamate transporter GLAST
    • Hakuba N., Koga K., Gyo K., Usami S.I., Tanaka K. Exacerbation of noise-induced hearing loss in mice lacking the glutamate transporter GLAST. J. Neurosci. 20:2000;8750-8753.
    • (2000) J. Neurosci. , vol.20 , pp. 8750-8753
    • Hakuba, N.1    Koga, K.2    Gyo, K.3    Usami, S.I.4    Tanaka, K.5
  • 389
    • 0033569442 scopus 로고    scopus 로고
    • The proton-linked monocarboxylate transporter (MCT) family: Structure, function and regulation
    • Halestrap A.P., Price N.T. The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation. Biochem. J. 343:(2):1999;281-299.
    • (1999) Biochem. J. , vol.343 , Issue.2 , pp. 281-299
    • Halestrap, A.P.1    Price, N.T.2
  • 390
    • 0031048975 scopus 로고    scopus 로고
    • Differential surface expression and phosphorylation of the N-methyl-D-aspartate receptor subunits NR1 and NR2 in cultured hippocampal neurons
    • Hall R.A., Soderling T.R. Differential surface expression and phosphorylation of the N-methyl-D-aspartate receptor subunits NR1 and NR2 in cultured hippocampal neurons. J. Biol. Chem. 272:1997;4135-4140.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4135-4140
    • Hall, R.A.1    Soderling, T.R.2
  • 391
    • 0032805574 scopus 로고    scopus 로고
    • Spatial correspondence between tactile projection patterns and the distribution of the antigenic Purkinje cell markers anti-zebrin I and anti-zebrin II in the cerebellar folium crus IIa of the rat
    • Hallem J.S., Thompson J.H., Gundappa-Sulur G., Hawkes R., Bjaalie J.G., Bower J.M. Spatial correspondence between tactile projection patterns and the distribution of the antigenic Purkinje cell markers anti-zebrin I and anti-zebrin II in the cerebellar folium crus IIa of the rat. Neuroscience. 93:1999;1083-1094.
    • (1999) Neuroscience , vol.93 , pp. 1083-1094
    • Hallem, J.S.1    Thompson, J.H.2    Gundappa-Sulur, G.3    Hawkes, R.4    Bjaalie, J.G.5    Bower, J.M.6
  • 392
    • 0021173149 scopus 로고
    • Extra- And intracellular amino acids in the hippocampus during development of hepatic encephalopathy
    • Hamberger A., Nyström B. Extra- and intracellular amino acids in the hippocampus during development of hepatic encephalopathy. Neurochem. Res. 9:1984;1181-1192.
    • (1984) Neurochem. Res. , vol.9 , pp. 1181-1192
    • Hamberger, A.1    Nyström, B.2
  • 393
    • 0018392519 scopus 로고
    • Glutamate as a CNS transmitter. I. Evaluation of glucose and glutamine as precursors for the synthesis of preferentially released glutamate
    • Hamberger A.C., Chiang G.H., Nylén E.S., Scheff S.W., Cotman C.W. Glutamate as a CNS transmitter. I. Evaluation of glucose and glutamine as precursors for the synthesis of preferentially released glutamate. Brain Res. 168:1979;513-530.
    • (1979) Brain Res. , vol.168 , pp. 513-530
    • Hamberger, A.C.1    Chiang, G.H.2    Nylén, E.S.3    Scheff, S.W.4    Cotman, C.W.5
  • 394
    • 0000966525 scopus 로고
    • Extracellular GABA, glutamate and glutamine in vivo - Perfusion-dialysis of rabbit hippocampus
    • Hamberger A., Berthold C.-H., Karlsson B., Lehmann A., Nystrom B. Extracellular GABA, glutamate and glutamine in vivo - perfusion-dialysis of rabbit hippocampus. Neurol. Neurobiol. 7:1983;473-492.
    • (1983) Neurol. Neurobiol. , vol.7 , pp. 473-492
    • Hamberger, A.1    Berthold, C.-H.2    Karlsson, B.3    Lehmann, A.4    Nystrom, B.5
  • 395
    • 0026749354 scopus 로고
    • Interaction of domoic acid and several derivatives with kainic acid and AMPA binding sites in rat brain
    • Hampson D.R., Huang X.P., Wells J.W., Walter J.A., Wright J.L.C. Interaction of domoic acid and several derivatives with kainic acid and AMPA binding sites in rat brain. Eur. J. Pharmacol. 218:1992;1-8.
    • (1992) Eur. J. Pharmacol. , vol.218 , pp. 1-8
    • Hampson, D.R.1    Huang, X.P.2    Wells, J.W.3    Walter, J.A.4    Wright, J.L.C.5
  • 396
    • 0002626143 scopus 로고    scopus 로고
    • Activity-dependent wiring of the developing hippocampal neuronal circuit
    • Hanse E., Durand G.M., Garaschuk O., Konnerth A. Activity-dependent wiring of the developing hippocampal neuronal circuit. Semin. Cell Dev. Biol. 8:1997;35-42.
    • (1997) Semin. Cell Dev. Biol. , vol.8 , pp. 35-42
    • Hanse, E.1    Durand, G.M.2    Garaschuk, O.3    Konnerth, A.4
  • 397
    • 0025190479 scopus 로고
    • Structural, conformational, and stereochemical requirements of central exitatory amino acid receptors
    • Hansen J.J., Krogsgaard-Larsen P. Structural, conformational, and stereochemical requirements of central exitatory amino acid receptors. Med. Res. Rev. 10:1990;55-94.
    • (1990) Med. Res. Rev. , vol.10 , pp. 55-94
    • Hansen, J.J.1    Krogsgaard-Larsen, P.2
  • 398
    • 0033178296 scopus 로고    scopus 로고
    • Group I metabotropic glutamate receptors at GABAergic synapses in monkeys
    • Hanson J.E., Smith Y. Group I metabotropic glutamate receptors at GABAergic synapses in monkeys. J. Neurosci. 19:1999;6488-6496.
    • (1999) J. Neurosci. , vol.19 , pp. 6488-6496
    • Hanson, J.E.1    Smith, Y.2
  • 399
    • 0024498337 scopus 로고
    • Regulation of glutamate and GABA transport by adrenoceptors in primary astroglial cell cultures
    • Hansson E., Rönnbäck L. Regulation of glutamate and GABA transport by adrenoceptors in primary astroglial cell cultures. Life Sci. 44:1989;27-37.
    • (1989) Life Sci. , vol.44 , pp. 27-37
    • Hansson, E.1    Rönnbäck, L.2
  • 400
    • 0025847589 scopus 로고
    • Receptor regulation of the glutamate, GABA and taurine high-affinity uptake into astrocytes in primary culture
    • Hansson E., Rönnbäck L. Receptor regulation of the glutamate, GABA and taurine high-affinity uptake into astrocytes in primary culture. Brain Res. 548:1991;215-221.
    • (1991) Brain Res. , vol.548 , pp. 215-221
    • Hansson, E.1    Rönnbäck, L.2
  • 404
    • 0033607224 scopus 로고    scopus 로고
    • Calcium from internal stores modifies dendritic spine shape
    • Harris K.M. Calcium from internal stores modifies dendritic spine shape. Proc. Natl. Acad. Sci. USA. 96:1999;12213-12215.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12213-12215
    • Harris, K.M.1
  • 405
    • 0028858391 scopus 로고
    • Variation in the number, location and size of synaptic vesicles provides an anatomical basis for the nonuniform probability of release at hippocampal CA1 synapses
    • Harris K.M., Sultan P. Variation in the number, location and size of synaptic vesicles provides an anatomical basis for the nonuniform probability of release at hippocampal CA1 synapses. Neuropharmacology. 34:1995;1387-1395.
    • (1995) Neuropharmacology , vol.34 , pp. 1387-1395
    • Harris, K.M.1    Sultan, P.2
  • 408
    • 0032746874 scopus 로고    scopus 로고
    • Ethanol actions on multiple ion channels: Which are important?
    • Harris R.A. Ethanol actions on multiple ion channels: which are important? Alcohol Clin. Exp. Res. 23:1999;1563-1570.
    • (1999) Alcohol Clin. Exp. Res. , vol.23 , pp. 1563-1570
    • Harris, R.A.1
  • 409
    • 0025784559 scopus 로고
    • Quantitative studies on the mammalian cerebellum
    • Harvey R.J., Napper R.M. Quantitative studies on the mammalian cerebellum. Prog. Neurobiol. 36:1991;437-463.
    • (1991) Prog. Neurobiol. , vol.36 , pp. 437-463
    • Harvey, R.J.1    Napper, R.M.2
  • 410
    • 0030850891 scopus 로고    scopus 로고
    • Free D-aspartate and D-serine in the mammalian brain and periphery
    • Hashimoto A., Oka T. Free D-aspartate and D-serine in the mammalian brain and periphery. Prog. Neurobiol. 52:1997;325-353.
    • (1997) Prog. Neurobiol. , vol.52 , pp. 325-353
    • Hashimoto, A.1    Oka, T.2
  • 411
    • 0028802388 scopus 로고
    • Glial formation of pyruvate and lactate from TCA cycle intermediates: Implications for the inactivation of transmitter amino acids?
    • Hassel B., Sonnewald U. Glial formation of pyruvate and lactate from TCA cycle intermediates: implications for the inactivation of transmitter amino acids? J. Neurochem. 65:1995;2227-2234.
    • (1995) J. Neurochem. , vol.65 , pp. 2227-2234
    • Hassel, B.1    Sonnewald, U.2
  • 412
    • 0033969656 scopus 로고    scopus 로고
    • Cerebral metabolism of lactate in vivo: Evidence for neuronal pyruvate carboxylation
    • Hassel B., Bråthe A. Cerebral metabolism of lactate in vivo: evidence for neuronal pyruvate carboxylation. J. Cereb. Blood Flow Metab. 20:2000;327-336.
    • (2000) J. Cereb. Blood Flow Metab. , vol.20 , pp. 327-336
    • Hassel, B.1    Bråthe, A.2
  • 413
    • 0342906183 scopus 로고    scopus 로고
    • Neuronal pyruvate carboxylation supports formation of transmitter glutamate
    • Hassel B., Bråthe A. Neuronal pyruvate carboxylation supports formation of transmitter glutamate. J. Neurosci. 20:2000;1342-1347.
    • (2000) J. Neurosci. , vol.20 , pp. 1342-1347
    • Hassel, B.1    Bråthe, A.2
  • 417
    • 0030921484 scopus 로고    scopus 로고
    • An anatomical model of cerebellar modules
    • Hawkes R. An anatomical model of cerebellar modules. Prog. Brain Res. 114:1997;39-52.
    • (1997) Prog. Brain Res. , vol.114 , pp. 39-52
    • Hawkes, R.1
  • 418
    • 85007947085 scopus 로고
    • Effects of sodium glutamate on the nervous system
    • Hayashi T. Effects of sodium glutamate on the nervous system. Keio J. Med. 3:1954;183-192.
    • (1954) Keio J. Med. , vol.3 , pp. 183-192
    • Hayashi, T.1
  • 419
    • 0033961498 scopus 로고    scopus 로고
    • Differential synaptic localization of the glutamate transporter EAAC1 and glutamate receptor subunit GluR2 in the rat hippocampus
    • He, Y., Janssen, W.G.M., Rothstein, J.D., Morrison, J.H., 2000. Differential synaptic localization of the glutamate transporter EAAC1 and glutamate receptor subunit GluR2 in the rat hippocampus. J. Comp. Neurol. 418, 255-269.
    • (2000) J. Comp. Neurol. , vol.418 , pp. 255-269
    • He, Y.1    Janssen, W.G.M.2    Rothstein, J.D.3    Morrison, J.H.4
  • 420
    • 0025277960 scopus 로고
    • Excitatory amino acids and synaptic transmission: The evidence for a physiological function
    • Headley P.M., Grillner S. Excitatory amino acids and synaptic transmission: the evidence for a physiological function. Trends Pharmacol. Sci. 11:1990;205-211.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 205-211
    • Headley, P.M.1    Grillner, S.2
  • 421
    • 0027082962 scopus 로고
    • Glucose transporter oligomeric structure determines transporter function
    • Hebert D.N., Carruthers A. Glucose transporter oligomeric structure determines transporter function. J. Biol. Chem. 267:1992;23829-23838.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23829-23838
    • Hebert, D.N.1    Carruthers, A.2
  • 422
    • 0032749353 scopus 로고    scopus 로고
    • Glutamate transporters in kidney and brain
    • Hediger M.A. Glutamate transporters in kidney and brain. Am. J. Physiol. 277:1999;F487-F492.
    • (1999) Am. J. Physiol. , vol.277 , pp. 487-F492
    • Hediger, M.A.1
  • 424
    • 0016719683 scopus 로고
    • Glial contamination of synaptosomal fractions
    • Henn F.A., Anderson D.J., Rustad D.G. Glial contamination of synaptosomal fractions. Brain Res. 101:1976;341-344.
    • (1976) Brain Res. , vol.101 , pp. 341-344
    • Henn, F.A.1    Anderson, D.J.2    Rustad, D.G.3
  • 425
    • 0031694652 scopus 로고    scopus 로고
    • Noncovalent and covalent labeling of vesicular monoamine transporter with tetrabenazine and ketanserin derivatives; Purification of photolabeled protein
    • Henry J.P., Sagné C., Isambert M.F., Gasnier B. Noncovalent and covalent labeling of vesicular monoamine transporter with tetrabenazine and ketanserin derivatives; purification of photolabeled protein. Methods Enzymol. 296:1998;73-83.
    • (1998) Methods Enzymol. , vol.296 , pp. 73-83
    • Henry, J.P.1    Sagné, C.2    Isambert, M.F.3    Gasnier, B.4
  • 426
    • 0032033189 scopus 로고    scopus 로고
    • The vesicular monoamine transporter: From chromaffin granule to brain
    • Henry J.P., Sagné C., Bedet C., Gasnier B. The vesicular monoamine transporter: from chromaffin granule to brain. Neurochem. Int. 32:1998;227-246.
    • (1998) Neurochem. Int. , vol.32 , pp. 227-246
    • Henry, J.P.1    Sagné, C.2    Bedet, C.3    Gasnier, B.4
  • 427
    • 0018204962 scopus 로고
    • GFA content, glutamate uptake and activity of glutamate metabolizing enzymes in differentiating mouse astrocytes
    • Hertz L., Bock E., Schousboe A. GFA content, glutamate uptake and activity of glutamate metabolizing enzymes in differentiating mouse astrocytes. Dev. Neurosci. 1:1978;226-238.
    • (1978) Dev. Neurosci. , vol.1 , pp. 226-238
    • Hertz, L.1    Bock, E.2    Schousboe, A.3
  • 428
    • 0025178979 scopus 로고
    • Mechanisms generating the time course of dual component excitatory synaptic currents recorded in hippocampal slices
    • Hestrin S., Sah P., Nicoll R.A. Mechanisms generating the time course of dual component excitatory synaptic currents recorded in hippocampal slices. Neuron. 5:1990;247-253.
    • (1990) Neuron , vol.5 , pp. 247-253
    • Hestrin, S.1    Sah, P.2    Nicoll, R.A.3
  • 429
    • 0034007509 scopus 로고    scopus 로고
    • Clustering of delta glutamate receptors is regulated by the actin cytoskeleton in the dendritic spines of cultured rat Purkinje cells
    • Hirai H. Clustering of delta glutamate receptors is regulated by the actin cytoskeleton in the dendritic spines of cultured rat Purkinje cells. Eur. J. Neurosci. 12:2000;563-570.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 563-570
    • Hirai, H.1
  • 430
    • 0019082582 scopus 로고
    • A nondenaturating zwitterionic detergent for membrane biochemistry: Design and synthesis
    • Hjelmeland L.M. A nondenaturating zwitterionic detergent for membrane biochemistry: design and synthesis. Proc. Natl. Acad. Sci. USA. 77:1980;6368-6370.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 6368-6370
    • Hjelmeland, L.M.1
  • 431
    • 0025346334 scopus 로고
    • Anionic amino acid transport systems in isolated basal plasma membrane of human placenta
    • Hoeltzli S.D., Kelley L.K., Moe A.J., Smith C.H. Anionic amino acid transport systems in isolated basal plasma membrane of human placenta. Am. J. Physiol. 259:1990;C47-C55.
    • (1990) Am. J. Physiol. , vol.259 , pp. 47-C55
    • Hoeltzli, S.D.1    Kelley, L.K.2    Moe, A.J.3    Smith, C.H.4
  • 432
    • 0029828966 scopus 로고    scopus 로고
    • The in vivo effect of bilirubin on the N-methyl-D-aspartate receptor/ion channel complex in the brains of newborn piglets
    • Hoffman D.J., Zanelli S.A., Kubin J., Mishra O.P., Delivoria-Papadopoulos M. The in vivo effect of bilirubin on the N-methyl-D-aspartate receptor/ion channel complex in the brains of newborn piglets. Pediatr. Res. 40:1996;804-808.
    • (1996) Pediatr. Res. , vol.40 , pp. 804-808
    • Hoffman, D.J.1    Zanelli, S.A.2    Kubin, J.3    Mishra, O.P.4    Delivoria-Papadopoulos, M.5
  • 433
    • 0028151384 scopus 로고
    • Human neutral amino acid transporter ASCT1: Structure of the gene (SLC1a4) and localization to chromosome 2p13-p15
    • Hofmann K., Duker M., Fink T., Lichter P., Stoffel W. Human neutral amino acid transporter ASCT1: structure of the gene (SLC1a4) and localization to chromosome 2p13-p15. Genomics. 24:1994;20-26.
    • (1994) Genomics , vol.24 , pp. 20-26
    • Hofmann, K.1    Duker, M.2    Fink, T.3    Lichter, P.4    Stoffel, W.5
  • 435
    • 0028840270 scopus 로고
    • Modeling the effect of glutamate diffusion and uptake on NMDA and non-NMDA receptor saturation
    • Holmes W.R. Modeling the effect of glutamate diffusion and uptake on NMDA and non-NMDA receptor saturation. Biophys. J. 69:1995;1734-1747.
    • (1995) Biophys. J. , vol.69 , pp. 1734-1747
    • Holmes, W.R.1
  • 436
    • 0034711151 scopus 로고    scopus 로고
    • Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls
    • Honig L.S., Chambliss D.D., Bigio E.H., Carroll S.L., Elliott J.L. Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls. Neurology. 55:2000;1082-1088.
    • (2000) Neurology , vol.55 , pp. 1082-1088
    • Honig, L.S.1    Chambliss, D.D.2    Bigio, E.H.3    Carroll, S.L.4    Elliott, J.L.5
  • 437
    • 0027518458 scopus 로고
    • Receptors for neurotransmitters on astrocytes in the mammalian central nervous system
    • Hösli E., Hösli L. Receptors for neurotransmitters on astrocytes in the mammalian central nervous system. Prog. Neurobiol. 40:1993;477-506.
    • (1993) Prog. Neurobiol. , vol.40 , pp. 477-506
    • Hösli, E.1    Hösli, L.2
  • 439
    • 0021189956 scopus 로고
    • The glutamate analog L-amino adipic acid is taken up by astrocytes before exerting its gliotoxic effect in vitro
    • Huck S., Grass F., Hortnagl H. The glutamate analog L-amino adipic acid is taken up by astrocytes before exerting its gliotoxic effect in vitro. J. Neurosci. 4:1984;2650-2657.
    • (1984) J. Neurosci. , vol.4 , pp. 2650-2657
    • Huck, S.1    Grass, F.2    Hortnagl, H.3
  • 440
    • 0034680749 scopus 로고    scopus 로고
    • +-dependent glutamate transporter GLAST-1 is expressed in bone and a splice variant of this molecule is expressed in bone and brain
    • +-dependent glutamate transporter GLAST-1 is expressed in bone and a splice variant of this molecule is expressed in bone and brain. FEBS Lett. 485:2000;13-18.
    • (2000) FEBS Lett. , vol.485 , pp. 13-18
    • Huggett, J.1    Vaughan-Thomas, A.2    Mason, D.3
  • 441
    • 33751263661 scopus 로고    scopus 로고
    • Alkalemia reduces recovery from global cerebral ischemia by NMDA receptor-mediated mechanism
    • Hurn P.D., Koehler R.C., Traystman R.J. Alkalemia reduces recovery from global cerebral ischemia by NMDA receptor-mediated mechanism. Am. J. Physiol. 41:1997;H2557-H2562.
    • (1997) Am. J. Physiol. , vol.41 , pp. 2557-H2562
    • Hurn, P.D.1    Koehler, R.C.2    Traystman, R.J.3
  • 442
    • 0029793450 scopus 로고    scopus 로고
    • New mutations and phenotypes associated with glutamate and aspartate transport in chinese hamster ovary (CHO-k1) cells
    • Igo R.P., Ash J.F. New mutations and phenotypes associated with glutamate and aspartate transport in chinese hamster ovary (CHO-k1) cells. Somat. Cell Mol. Genet. 22:1996;87-103.
    • (1996) Somat. Cell Mol. Genet. , vol.22 , pp. 87-103
    • Igo, R.P.1    Ash, J.F.2
  • 443
    • 0029871310 scopus 로고    scopus 로고
    • Nuclear disintegration as a leading step of glutamate excitotoxicity in brain neurons
    • Ikeda J., Terakawa S., Murota S., Morita I., Hirakawa K. Nuclear disintegration as a leading step of glutamate excitotoxicity in brain neurons. J. Neurosci. Res. 43:1996;613-622.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 613-622
    • Ikeda, J.1    Terakawa, S.2    Murota, S.3    Morita, I.4    Hirakawa, K.5
  • 444
    • 0024342862 scopus 로고
    • Sensitivity of the developing rat brain to hypobaric ischemic damage parallels sensitivity to N-methyl-aspartate neurotoxicity
    • Ikonomidou C., Mosinger J.L., Salles K.S., Labruyere J., Olney J.W. Sensitivity of the developing rat brain to hypobaric ischemic damage parallels sensitivity to N-methyl-aspartate neurotoxicity. J. Neurosci. 9:1989;2809-2818.
    • (1989) J. Neurosci. , vol.9 , pp. 2809-2818
    • Ikonomidou, C.1    Mosinger, J.L.2    Salles, K.S.3    Labruyere, J.4    Olney, J.W.5
  • 446
    • 0031777828 scopus 로고    scopus 로고
    • Expression of two glutamate transporters, GLAST and EAAT4, in the human cerebellum: Their correlation in development and neonatal hypoxic-ischemic damage
    • Inage Y.W., Itoh M., Wada K., Takashima S. Expression of two glutamate transporters, GLAST and EAAT4, in the human cerebellum: their correlation in development and neonatal hypoxic-ischemic damage. J. Neuropathol. Exp. Neurol. 57:1998;554-562.
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 554-562
    • Inage, Y.W.1    Itoh, M.2    Wada, K.3    Takashima, S.4
  • 447
    • 0034651097 scopus 로고    scopus 로고
    • Arachidonic acid stimulates a novel cocaine-sensitive cation conductance associated with the human dopamine transporter
    • Ingram S.L., Amara S.G. Arachidonic acid stimulates a novel cocaine-sensitive cation conductance associated with the human dopamine transporter. J. Neurosci. 20:2000;550-557.
    • (2000) J. Neurosci. , vol.20 , pp. 550-557
    • Ingram, S.L.1    Amara, S.G.2
  • 448
    • 0034161522 scopus 로고    scopus 로고
    • Imaging extracellular waves of glutamate during calcium signaling in cultured astrocytes
    • Innocenti B., Parpura V., Haydon P.G. Imaging extracellular waves of glutamate during calcium signaling in cultured astrocytes. J. Neurosci. 20:2000;1800-1808.
    • (2000) J. Neurosci. , vol.20 , pp. 1800-1808
    • Innocenti, B.1    Parpura, V.2    Haydon, P.G.3
  • 449
    • 0028794524 scopus 로고
    • Cloning and expression of a bovine glutamate transporter
    • Inoue K., Sakaitani M., Shimada S., Tohyama M. Cloning and expression of a bovine glutamate transporter. Mol. Brain Res. 28:1995;343-348.
    • (1995) Mol. Brain Res. , vol.28 , pp. 343-348
    • Inoue, K.1    Sakaitani, M.2    Shimada, S.3    Tohyama, M.4
  • 450
    • 0033151664 scopus 로고    scopus 로고
    • Glutamate spillover mediates excitatory transmission in the rat olfactory bulb
    • Isaacson J.S. Glutamate spillover mediates excitatory transmission in the rat olfactory bulb. Neuron. 23:1999;377-384.
    • (1999) Neuron , vol.23 , pp. 377-384
    • Isaacson, J.S.1
  • 451
    • 0027369524 scopus 로고
    • The uptake inhibitor L-trans-PDC enhances responses to glutamate but fails to alter the kinetics of excitatory synaptic currents in the hippocampus
    • Isaacson J.S., Nicoll R.A. The uptake inhibitor L-trans-PDC enhances responses to glutamate but fails to alter the kinetics of excitatory synaptic currents in the hippocampus. J. Neurophysiol. 70:1993;2187-2191.
    • (1993) J. Neurophysiol. , vol.70 , pp. 2187-2191
    • Isaacson, J.S.1    Nicoll, R.A.2
  • 452
    • 0026696845 scopus 로고
    • Characterization and purification of the monoamine transporter of bovine chromaffin granules
    • Isambert M.F., Gasnier B., Botton D., Henry J.P. Characterization and purification of the monoamine transporter of bovine chromaffin granules. Biochemistry. 31:1992;1980-1986.
    • (1992) Biochemistry , vol.31 , pp. 1980-1986
    • Isambert, M.F.1    Gasnier, B.2    Botton, D.3    Henry, J.P.4
  • 453
    • 0031034790 scopus 로고    scopus 로고
    • The glutamate hypothesis of schizophrenia: Therapeutic implications
    • Ishimaru M.J., Toru M. The glutamate hypothesis of schizophrenia: therapeutic implications. CNS Drugs. 7:1997;47-67.
    • (1997) CNS Drugs , vol.7 , pp. 47-67
    • Ishimaru, M.J.1    Toru, M.2
  • 455
    • 0030828931 scopus 로고    scopus 로고
    • Expression of a glutamate transporter subtype, EAAT4, in the developing human cerebellum
    • Itoh M., Watanabe Y., Watanabe M., Tanaka K., Wada K., Takashima S. Expression of a glutamate transporter subtype, EAAT4, in the developing human cerebellum. Brain Res. 767:1997;265-271.
    • (1997) Brain Res. , vol.767 , pp. 265-271
    • Itoh, M.1    Watanabe, Y.2    Watanabe, M.3    Tanaka, K.4    Wada, K.5    Takashima, S.6
  • 456
    • 0034607082 scopus 로고    scopus 로고
    • Specific antagonists of NMDA receptors prevent osteoclast sealing zone formation required for bone resorption
    • Itzstein C., Espinosa L., Delmas P.D., Chenu C. Specific antagonists of NMDA receptors prevent osteoclast sealing zone formation required for bone resorption. Biochem. Biophys. Res. Commun. 268:2000;201-209.
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 201-209
    • Itzstein, C.1    Espinosa, L.2    Delmas, P.D.3    Chenu, C.4
  • 457
    • 0024424845 scopus 로고
    • Domoic acid poisoning and mussel-associated intoxication - Preliminary investigations into the response of mice and rats to toxic mussel extract
    • Iverson F., Truelove J., Nera E., Tryphonas L., Campbell J., Lok E. Domoic acid poisoning and mussel-associated intoxication - preliminary investigations into the response of mice and rats to toxic mussel extract. Food Chem. Toxicol. 27:1989;377.
    • (1989) Food Chem. Toxicol. , vol.27 , pp. 377
    • Iverson, F.1    Truelove, J.2    Nera, E.3    Tryphonas, L.4    Campbell, J.5    Lok, E.6
  • 458
    • 0026586123 scopus 로고
    • Plasma amino acid levels in patients with amyotrophic lateral sclerosis
    • Iwasaki Y., Ikeda K., Kinoshita M. Plasma amino acid levels in patients with amyotrophic lateral sclerosis. J. Neurol. Sci. 107:1992;219-222.
    • (1992) J. Neurol. Sci. , vol.107 , pp. 219-222
    • Iwasaki, Y.1    Ikeda, K.2    Kinoshita, M.3
  • 462
    • 0033397263 scopus 로고    scopus 로고
    • Polymorphisms in the glutamate transporter gene EAAT2 in European ALS patients
    • Jackson M., Steers G., Leigh P.N., Morrison K.E. Polymorphisms in the glutamate transporter gene EAAT2 in European ALS patients. J. Neurol. 246:1999;1140-1144.
    • (1999) J. Neurol. , vol.246 , pp. 1140-1144
    • Jackson, M.1    Steers, G.2    Leigh, P.N.3    Morrison, K.E.4
  • 463
    • 0024274598 scopus 로고
    • Quantitative morphology and synaptology of cerebellar glomeroli in the rat
    • Jakab R.L., Hámori J. Quantitative morphology and synaptology of cerebellar glomeroli in the rat. J. Comp. Neurol. 179:1988;81-88.
    • (1988) J. Comp. Neurol. , vol.179 , pp. 81-88
    • Jakab, R.L.1    Hámori, J.2
  • 464
    • 0029044061 scopus 로고
    • In situ hybridization analysis of AMPA receptor subunit gene expression in the developing rat spinal cord
    • Jakowec M.W., Yen L., Kalb R.G. In situ hybridization analysis of AMPA receptor subunit gene expression in the developing rat spinal cord. Neuroscience. 67:1995;909-920.
    • (1995) Neuroscience , vol.67 , pp. 909-920
    • Jakowec, M.W.1    Yen, L.2    Kalb, R.G.3
  • 466
  • 467
    • 0032903301 scopus 로고    scopus 로고
    • The neuropsychopharmacology of phencyclidine: From NMDA receptor hypofunction to the dopamine hypothesis of schizophrenia
    • Jentsch J.D., Roth R.H. The neuropsychopharmacology of phencyclidine: from NMDA receptor hypofunction to the dopamine hypothesis of schizophrenia. Neuropsychopharmacology. 20:1999;201-225.
    • (1999) Neuropsychopharmacology , vol.20 , pp. 201-225
    • Jentsch, J.D.1    Roth, R.H.2
  • 468
    • 0030599201 scopus 로고    scopus 로고
    • The membrane-bound rat serotonin transporter, SERT1, is an oligomeric protein
    • Jess U., Betz H., Schloss P. The membrane-bound rat serotonin transporter, SERT1, is an oligomeric protein. FEBS Lett. 394:1996;44-46.
    • (1996) FEBS Lett. , vol.394 , pp. 44-46
    • Jess, U.1    Betz, H.2    Schloss, P.3
  • 469
    • 0025779755 scopus 로고
    • An electron microscopic, immunogold analysis of glutamate and glutamine in terminals of rat spinocerebellar fibres
    • Ji Z., Aas J.-E., Laake J., Walberg F., Ottersen O.P. An electron microscopic, immunogold analysis of glutamate and glutamine in terminals of rat spinocerebellar fibres. J. Comp. Neurol. 307:1991;296-310.
    • (1991) J. Comp. Neurol. , vol.307 , pp. 296-310
    • Ji, Z.1    Aas, J.-E.2    Laake, J.3    Walberg, F.4    Ottersen, O.P.5
  • 470
    • 0019153446 scopus 로고
    • Permeability and vascularity of the developing brain: Cerebellum vs cerebral cortex
    • Johanson C.E. Permeability and vascularity of the developing brain: cerebellum vs cerebral cortex. Brain Res. 190:1980;3-16.
    • (1980) Brain Res. , vol.190 , pp. 3-16
    • Johanson, C.E.1
  • 471
    • 0002614673 scopus 로고
    • Glutamate uptake and its possible role in neurotransmitter inactivation
    • P.J. Roberts, J. Storm-Mathisen, & G.A.R. Johnston. Chichester, UK: Wiley
    • Johnston G.A.R. Glutamate uptake and its possible role in neurotransmitter inactivation. Roberts P.J., Storm-Mathisen J., Johnston G.A.R. Glutamate: Transmitter in the Central Nervous System. 1981;77-87 Wiley, Chichester, UK.
    • (1981) Glutamate: Transmitter in the Central Nervous System , pp. 77-87
    • Johnston, G.A.R.1
  • 472
    • 0018741941 scopus 로고
    • Action of the neurotoxin kainic acid on high affinity uptake of L-glutamic acid in rat brain slices
    • Johnston G.A.R., Kennedy S.M.F., Twitchin B. Action of the neurotoxin kainic acid on high affinity uptake of L-glutamic acid in rat brain slices. J. Neurochem. 32:1979;121-127.
    • (1979) J. Neurochem. , vol.32 , pp. 121-127
    • Johnston, G.A.R.1    Kennedy, S.M.F.2    Twitchin, B.3
  • 473
    • 0018866120 scopus 로고
    • Potentation of L-glutamate and L-aspartate excitation of cat spinal neurones by the stereoisomers of threo-3-hydroxyaspartate
    • Johnston G.A.R., Lodge D., Bornstein J.C., Curtis D.R. Potentation of L-glutamate and L-aspartate excitation of cat spinal neurones by the stereoisomers of threo-3-hydroxyaspartate. J. Neurochem. 34:1980;241-243.
    • (1980) J. Neurochem. , vol.34 , pp. 241-243
    • Johnston, G.A.R.1    Lodge, D.2    Bornstein, J.C.3    Curtis, D.R.4
  • 474
    • 0028874967 scopus 로고
    • Neurotransmitters and vulnerability of the developing brain
    • Johnston M.V. Neurotransmitters and vulnerability of the developing brain. Brain Dev. 17:1995;301-306.
    • (1995) Brain Dev. , vol.17 , pp. 301-306
    • Johnston, M.V.1
  • 475
    • 0030915589 scopus 로고    scopus 로고
    • Neurofilaments and motor neuron disease
    • Julien J.P. Neurofilaments and motor neuron disease. Trends Cell Biol. 7:1997;243-249.
    • (1997) Trends Cell Biol. , vol.7 , pp. 243-249
    • Julien, J.P.1
  • 476
    • 0032589511 scopus 로고    scopus 로고
    • Heterodimerization of a functional GABA(b) receptor is mediated by parallel coiled-coil alpha-helices
    • Kammerer R.A., Frank S., Schulthess T., Landwehr R., Lustig A., Engel J. Heterodimerization of a functional GABA(b) receptor is mediated by parallel coiled-coil alpha-helices. Biochemistry. 38:1999;13263-13269.
    • (1999) Biochemistry , vol.38 , pp. 13263-13269
    • Kammerer, R.A.1    Frank, S.2    Schulthess, T.3    Landwehr, R.4    Lustig, A.5    Engel, J.6
  • 477
    • 0026458124 scopus 로고
    • Primary structure and functional characterization of a high-affinity glutamate transporter
    • Kanai Y., Hediger M.A. Primary structure and functional characterization of a high-affinity glutamate transporter. Nature. 360:1992;467-471.
    • (1992) Nature , vol.360 , pp. 467-471
    • Kanai, Y.1    Hediger, M.A.2
  • 478
    • 0027136017 scopus 로고
    • A new family of neurotransmitter transporters - The high-affinity glutamate transporters
    • Kanai Y., Smith C.P., Hediger M.A. A new family of neurotransmitter transporters - the high-affinity glutamate transporters. FASEB J. 7:1993;1450-1459.
    • (1993) FASEB J. , vol.7 , pp. 1450-1459
    • Kanai, Y.1    Smith, C.P.2    Hediger, M.A.3
  • 479
    • 0028124811 scopus 로고
    • The neuronal and epithelial human high affinity glutamate transporter - Insights into structure and mechanism of transport
    • Kanai Y., Stelzner M., Nussberger S., Khawaja S., Hebert S.C., Smith C.P., Hediger M.A. The neuronal and epithelial human high affinity glutamate transporter - insights into structure and mechanism of transport. J. Biol. Chem. 269:1994;20599-20606.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20599-20606
    • Kanai, Y.1    Stelzner, M.2    Nussberger, S.3    Khawaja, S.4    Hebert, S.C.5    Smith, C.P.6    Hediger, M.A.7
  • 480
    • 0029586025 scopus 로고
    • Neuronal high-affinity glutamate transport in the rat central nervous system
    • Kanai Y., Bhide P.G., DiFiglia M., Hediger M.A. Neuronal high-affinity glutamate transport in the rat central nervous system. Neuroreport. 6:1995;2357-2362.
    • (1995) Neuroreport , vol.6 , pp. 2357-2362
    • Kanai, Y.1    Bhide, P.G.2    Difiglia, M.3    Hediger, M.A.4
  • 482
    • 0032508585 scopus 로고    scopus 로고
    • Expression cloning and characterization of a transporter for large neutral amino acids activated by the heavy chain of 4F2 antigen (CD98)
    • Kanai Y., Segawa H., Miyamoto K., Uchino H., Takeda E., Endou H. Expression cloning and characterization of a transporter for large neutral amino acids activated by the heavy chain of 4F2 antigen (CD98). J. Biol. Chem. 273:1998;23629-23632.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23629-23632
    • Kanai, Y.1    Segawa, H.2    Miyamoto, K.3    Uchino, H.4    Takeda, E.5    Endou, H.6
  • 483
    • 0018138165 scopus 로고
    • Active transport of gamma-aminobutyric acid by membrane vesicles isolated from rat brain
    • Kanner B.I. Active transport of gamma-aminobutyric acid by membrane vesicles isolated from rat brain. Biochemistry. 17:1978;1207-1211.
    • (1978) Biochemistry , vol.17 , pp. 1207-1211
    • Kanner, B.I.1
  • 484
    • 0018103479 scopus 로고
    • Solubilization and reconstitution of the gamma-aminobutyric acid transporter from rat brain
    • Kanner B.I. Solubilization and reconstitution of the gamma-aminobutyric acid transporter from rat brain. FEBS Lett. 89:1978;47-50.
    • (1978) FEBS Lett. , vol.89 , pp. 47-50
    • Kanner, B.I.1
  • 485
    • 0021067890 scopus 로고
    • Bioenergetics of neurotransmitter transport
    • Kanner B.I. Bioenergetics of neurotransmitter transport. Biochim. Biophys. Acta. 726:1983;293-316.
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 293-316
    • Kanner, B.I.1
  • 486
    • 0020448447 scopus 로고
    • Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain
    • Kanner B.I., Bendahan A. Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain. Biochemistry. 21:1982;6327-6330.
    • (1982) Biochemistry , vol.21 , pp. 6327-6330
    • Kanner, B.I.1    Bendahan, A.2
  • 487
    • 0019950576 scopus 로고
    • Efflux of L-glutamate by synaptic plasma membrane vesicles isolated from rat brain
    • Kanner B.I., Marva E. Efflux of L-glutamate by synaptic plasma membrane vesicles isolated from rat brain. Biochemistry. 21:1982;3143-3147.
    • (1982) Biochemistry , vol.21 , pp. 3143-3147
    • Kanner, B.I.1    Marva, E.2
  • 488
    • 0023074631 scopus 로고
    • Mechanism of transport and storage of neurotransmitters
    • Kanner B.I., Schuldiner S. Mechanism of transport and storage of neurotransmitters. CRC Crit. Rev. Biochem. 22:1987;1-38.
    • (1987) CRC Crit. Rev. Biochem. , vol.22 , pp. 1-38
    • Kanner, B.I.1    Schuldiner, S.2
  • 489
    • 0018132541 scopus 로고
    • Active transport of L-glutamate by membrane vesicles isolated from rat brain
    • Kanner B.I., Sharon I. Active transport of L-glutamate by membrane vesicles isolated from rat brain. Biochemistry. 17:1978;3949-3953.
    • (1978) Biochemistry , vol.17 , pp. 3949-3953
    • Kanner, B.I.1    Sharon, I.2
  • 490
    • 0018090051 scopus 로고
    • Solubilization and reconstitution of the L-glutamic acid transporter from rat brain
    • Kanner B.I., Sharon I. Solubilization and reconstitution of the L-glutamic acid transporter from rat brain. FEBS Lett. 94:1978;245-248.
    • (1978) FEBS Lett. , vol.94 , pp. 245-248
    • Kanner, B.I.1    Sharon, I.2
  • 491
    • 0033971937 scopus 로고    scopus 로고
    • Viral hide-and-seek in sporadic ALS: A new challenge
    • Karpati G., Dalakas M.C. Viral hide-and-seek in sporadic ALS: a new challenge. Neurology. 54:2000;6-7.
    • (2000) Neurology , vol.54 , pp. 6-7
    • Karpati, G.1    Dalakas, M.C.2
  • 492
    • 0030766256 scopus 로고    scopus 로고
    • A postsynaptic excitatory amino acid transporter with chloride conductance functionally regulated by neuronal activity in cerebellar Purkinje cells
    • Kataoka Y., Morii H., Watanabe Y., Ohmori H. A postsynaptic excitatory amino acid transporter with chloride conductance functionally regulated by neuronal activity in cerebellar Purkinje cells. J. Neurosci. 17:1997;7017-7024.
    • (1997) J. Neurosci. , vol.17 , pp. 7017-7024
    • Kataoka, Y.1    Morii, H.2    Watanabe, Y.3    Ohmori, H.4
  • 493
    • 0025242563 scopus 로고
    • Massive increases in extracellular potassium and the indiscriminate release of glutamate following concussive brain injury
    • Katayama Y., Becker D.P., Tamura T., Hovda D.A. Massive increases in extracellular potassium and the indiscriminate release of glutamate following concussive brain injury. J. Neurosurg. 73:1990;889-900.
    • (1990) J. Neurosurg. , vol.73 , pp. 889-900
    • Katayama, Y.1    Becker, D.P.2    Tamura, T.3    Hovda, D.A.4
  • 494
    • 0028879714 scopus 로고
    • Role of excitatory amino acid-mediated ionic fluxes in traumatic brain injury
    • Katayama Y., Maeda T., Koshinaga M., Kawamata T., Tsubokawa T. Role of excitatory amino acid-mediated ionic fluxes in traumatic brain injury. Brain Pathol. 5:1995;427-435.
    • (1995) Brain Pathol. , vol.5 , pp. 427-435
    • Katayama, Y.1    Maeda, T.2    Koshinaga, M.3    Kawamata, T.4    Tsubokawa, T.5
  • 495
    • 0027290747 scopus 로고
    • Early anoxia-induced vesicular glutamate release results from mobilization of calcium from intracellular stores
    • Katchman A.N., Hershkowitz N. Early anoxia-induced vesicular glutamate release results from mobilization of calcium from intracellular stores. J. Neurophysiol. 70:1993;1-7.
    • (1993) J. Neurophysiol. , vol.70 , pp. 1-7
    • Katchman, A.N.1    Hershkowitz, N.2
  • 496
    • 0026637624 scopus 로고
    • A mechanism for glutamate toxicity in the C6 glioma cells involving inhibition of cystine uptake leading to glutathione depletion
    • Kato S., Negishi K., Mawatari K., Kuo C.H. A mechanism for glutamate toxicity in the C6 glioma cells involving inhibition of cystine uptake leading to glutathione depletion. Neuroscience. 48:1992;903-914.
    • (1992) Neuroscience , vol.48 , pp. 903-914
    • Kato, S.1    Negishi, K.2    Mawatari, K.3    Kuo, C.H.4
  • 497
    • 0023823059 scopus 로고
    • 2+ concentration in isolated nerve terminals following metabolic inhibition: Possible relevance to hypoglycaemia and anoxia
    • 2+ concentration in isolated nerve terminals following metabolic inhibition: possible relevance to hypoglycaemia and anoxia. Neuroscience. 27:1988;175-182.
    • (1988) Neuroscience , vol.27 , pp. 175-182
    • Kauppinen, R.A.1    McMahon, H.T.2    Nicholls, D.G.3
  • 498
    • 0032573098 scopus 로고    scopus 로고
    • Neurotransmitter transport: Models in flux
    • Kavanaugh M.P. Neurotransmitter transport: models in flux. Proc. Natl. Acad. Sci. USA. 95:1998;12737-12738.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12737-12738
    • Kavanaugh, M.P.1
  • 499
    • 24444443617 scopus 로고    scopus 로고
    • Glutamate transporters in brain: New complexities in structure and function
    • Kavanaugh M.P. Glutamate transporters in brain: new complexities in structure and function. J. Neurochem. 73:1999;S7B.
    • (1999) J. Neurochem. , vol.73
    • Kavanaugh, M.P.1
  • 500
    • 0031028206 scopus 로고    scopus 로고
    • Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GET-1 induces obligate exchange
    • Kavanaugh M.P., Bendahan A., Zerangue N., Zhang Y.M., Kanner B.I. Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GET-1 induces obligate exchange. J. Biol. Chem. 272:1997;1703-1708.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1703-1708
    • Kavanaugh, M.P.1    Bendahan, A.2    Zerangue, N.3    Zhang, Y.M.4    Kanner, B.I.5
  • 502
    • 0026504549 scopus 로고
    • Administration of excitatory amino acid antagonists via microdialysis attenuates the increase in glucose utilization seen following concussive brain injury
    • Kawamata T., Katayama Y., Hovda D.A., Yoshino A., Becker D.P. Administration of excitatory amino acid antagonists via microdialysis attenuates the increase in glucose utilization seen following concussive brain injury. J. Cereb. Blood Flow Metab. 12:1992;12-24.
    • (1992) J. Cereb. Blood Flow Metab. , vol.12 , pp. 12-24
    • Kawamata, T.1    Katayama, Y.2    Hovda, D.A.3    Yoshino, A.4    Becker, D.P.5
  • 503
    • 0030581635 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA for the glutamate transporter of the nematode Caenorhabditis elegans
    • Kawano T., Takuwa K., Nakajima T. Molecular cloning of a cDNA for the glutamate transporter of the nematode Caenorhabditis elegans. Biochem. Biophys. Res. Commun. 228:1996;415-420.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 415-420
    • Kawano, T.1    Takuwa, K.2    Nakajima, T.3
  • 504
    • 0031147785 scopus 로고    scopus 로고
    • Structure and activity of a new form of the glutamate transporter of the nematode Caenorhabditis elegans
    • Kawano T., Takuwa K., Nakajima T. Structure and activity of a new form of the glutamate transporter of the nematode Caenorhabditis elegans. Biosci. Biotechnol. Biochem. 61:1997;927-929.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 927-929
    • Kawano, T.1    Takuwa, K.2    Nakajima, T.3
  • 506
    • 0033613212 scopus 로고    scopus 로고
    • Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells
    • Kazantsev A., Preisinger E., Dranovsky A., Goldgaber D., Housman D. Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells. Proc. Natl. Acad. Sci. USA. 96:1999;11404-11409.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11404-11409
    • Kazantsev, A.1    Preisinger, E.2    Dranovsky, A.3    Goldgaber, D.4    Housman, D.5
  • 507
    • 0027252497 scopus 로고
    • Modification of hypoxia-induced injury in cultured rat astrocytes by high levels of glucose
    • Kelleher J.A., Chan P.H., Chan T.Y.Y., Gregory G.A. Modification of hypoxia-induced injury in cultured rat astrocytes by high levels of glucose. Stroke. 24:1993;855-863.
    • (1993) Stroke , vol.24 , pp. 855-863
    • Kelleher, J.A.1    Chan, P.H.2    Chan, T.Y.Y.3    Gregory, G.A.4
  • 508
    • 0030608841 scopus 로고    scopus 로고
    • +-ATPase activity, glucose transport, and glutamate transport induced by amyloid beta-peptide and iron
    • +-ATPase activity, glucose transport, and glutamate transport induced by amyloid beta-peptide and iron. J. Neurosci. Res. 50:1997;522-530.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 522-530
    • Keller, J.N.1    Germeyer, A.2    Begley, J.G.3    Mattson, M.P.4
  • 509
    • 0030754962 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, an aldehydic product of membrane lipid peroxidation, impairs glutamate transport and mitochondrial function in synaptosomes
    • Keller J.N., Mark R.J., Bruce A.J., Blanc E., Rothstein J.D., Uchida K., Waeg G., Mattson M.P. 4-Hydroxynonenal, an aldehydic product of membrane lipid peroxidation, impairs glutamate transport and mitochondrial function in synaptosomes. Neuroscience. 80:1997;685-696.
    • (1997) Neuroscience , vol.80 , pp. 685-696
    • Keller, J.N.1    Mark, R.J.2    Bruce, A.J.3    Blanc, E.4    Rothstein, J.D.5    Uchida, K.6    Waeg, G.7    Mattson, M.P.8
  • 510
    • 0030966546 scopus 로고    scopus 로고
    • Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: Role of the lipid peroxidation product 4-hydroxynonenal
    • Keller J.N., Pang Z., Geddes J.W., Begley J.G., Germeyer A., Waeg G., Mattson M.P. Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid beta-peptide: role of the lipid peroxidation product 4-hydroxynonenal. J. Neurochem. 69:1997;273-284.
    • (1997) J. Neurochem. , vol.69 , pp. 273-284
    • Keller, J.N.1    Pang, Z.2    Geddes, J.W.3    Begley, J.G.4    Germeyer, A.5    Waeg, G.6    Mattson, M.P.7
  • 511
    • 0032077680 scopus 로고    scopus 로고
    • Signal transduction molecules at the glutamatergic postsynaptic membrane
    • Kennedy M.B. Signal transduction molecules at the glutamatergic postsynaptic membrane. Brain Res. Brain Res. Rev. 26:1998;243-257.
    • (1998) Brain Res. Brain Res. Rev. , vol.26 , pp. 243-257
    • Kennedy, M.B.1
  • 512
    • 0020822339 scopus 로고
    • Topographic changes in high-affinity glutamate uptake in the cat red nucleus, substantia nigra, thalamus, and caudate nucleus after lesions of sensorimotor cortical areas
    • Kerkerian L., Nieoullon A., Dusticier N. Topographic changes in high-affinity glutamate uptake in the cat red nucleus, substantia nigra, thalamus, and caudate nucleus after lesions of sensorimotor cortical areas. Exp. Neurol. 81:1983;598-612.
    • (1983) Exp. Neurol. , vol.81 , pp. 598-612
    • Kerkerian, L.1    Nieoullon, A.2    Dusticier, N.3
  • 513
    • 0023502208 scopus 로고
    • Modulatory effect of dopamine on high-affinity glutamate uptake in rat striatum
    • Kerkerian L., Dusticier N., Nieoullon A. Modulatory effect of dopamine on high-affinity glutamate uptake in rat striatum. J. Neurochem. 48:1987;1301-1306.
    • (1987) J. Neurochem. , vol.48 , pp. 1301-1306
    • Kerkerian, L.1    Dusticier, N.2    Nieoullon, A.3
  • 514
    • 0029029066 scopus 로고
    • Arachidonic acid and free fatty acids as second messengers and the role of protein kinase C
    • Khan W.A., Blobe G.C., Hannun Y.A. Arachidonic acid and free fatty acids as second messengers and the role of protein kinase C. Cell Signal. 7:1995;171-184.
    • (1995) Cell Signal , vol.7 , pp. 171-184
    • Khan, W.A.1    Blobe, G.C.2    Hannun, Y.A.3
  • 515
    • 0030604018 scopus 로고    scopus 로고
    • Autoradiographic studies indicate regional variations in the characteristics of L-glutamate transporters in the rat brain
    • Killinger S., Blume G.L., Bohart L., Bested A., Dias L.S., Cooper B., Allan R.D., Balcar V.J. Autoradiographic studies indicate regional variations in the characteristics of L-glutamate transporters in the rat brain. Neurosci. Lett. 216:1996;101-104.
    • (1996) Neurosci. Lett. , vol.216 , pp. 101-104
    • Killinger, S.1    Blume, G.L.2    Bohart, L.3    Bested, A.4    Dias, L.S.5    Cooper, B.6    Allan, R.D.7    Balcar, V.J.8
  • 516
    • 0029588463 scopus 로고
    • Current concepts of brain edema - Review of laboratory investigations
    • Kimelberg H.K. Current concepts of brain edema - review of laboratory investigations. J. Neurosurg. 83:1995;1051-1059.
    • (1995) J. Neurosurg. , vol.83 , pp. 1051-1059
    • Kimelberg, H.K.1
  • 517
    • 0032252630 scopus 로고    scopus 로고
    • Swelling-activated release of excitatory amino acids in the brain: Relevance for pathophysiology
    • Kimelberg H.K., Mongin A.A. Swelling-activated release of excitatory amino acids in the brain: relevance for pathophysiology. Contrib. Nephrol. 123:1998;240-257.
    • (1998) Contrib. Nephrol. , vol.123 , pp. 240-257
    • Kimelberg, H.K.1    Mongin, A.A.2
  • 518
    • 0025425558 scopus 로고
    • Swelling-induced release of glutamate, aspartate, and taurine from astrocyte cultures
    • Kimelberg H.K., Goderie S.K., Higman S., Pang S., Waniewski R.A. Swelling-induced release of glutamate, aspartate, and taurine from astrocyte cultures. J. Neurosci. 10:1990;1583-1591.
    • (1990) J. Neurosci. , vol.10 , pp. 1583-1591
    • Kimelberg, H.K.1    Goderie, S.K.2    Higman, S.3    Pang, S.4    Waniewski, R.A.5
  • 519
    • 0030759961 scopus 로고    scopus 로고
    • Prolonged physiological entrapment of glutamate in the synaptic cleft of cerebellar unipolar brush cells
    • Kinney G.A., Overstreet L.S., Slater N.T. Prolonged physiological entrapment of glutamate in the synaptic cleft of cerebellar unipolar brush cells. J. Neurophysiol. 78:1997;1320-1333.
    • (1997) J. Neurophysiol. , vol.78 , pp. 1320-1333
    • Kinney, G.A.1    Overstreet, L.S.2    Slater, N.T.3
  • 520
    • 0033560905 scopus 로고    scopus 로고
    • Slices have more synapses than perfusion-fixed hippocampus from both young and mature rats
    • Kirov S.A., Sorra K.E., Harris K.M. Slices have more synapses than perfusion-fixed hippocampus from both young and mature rats. J. Neurosci. 19:1999;2876-2886.
    • (1999) J. Neurosci. , vol.19 , pp. 2876-2886
    • Kirov, S.A.1    Sorra, K.E.2    Harris, K.M.3
  • 521
    • 0027965106 scopus 로고
    • The mouse and human excitatory amino acid transporter gene (EAAT1) maps to mouse chromosome 15 and a region of syntenic homology on human chromosome 5
    • Kirschner M.A., Arriza J.L., Copeland N.G., Gilbert D.J., Jenkins N.A., Magenis E., Amara S.G. The mouse and human excitatory amino acid transporter gene (EAAT1) maps to mouse chromosome 15 and a region of syntenic homology on human chromosome 5. Genomics. 22:1994;631-633.
    • (1994) Genomics , vol.22 , pp. 631-633
    • Kirschner, M.A.1    Arriza, J.L.2    Copeland, N.G.3    Gilbert, D.J.4    Jenkins, N.A.5    Magenis, E.6    Amara, S.G.7
  • 522
    • 0028607643 scopus 로고
    • Mouse excitatory amino acid transporter EAAT2: Isolation, characterization, and proximity to neuroexcitability loci on mouse chromosome 2
    • Kirschner M.A., Copeland N.G., Gilbert D.J., Jenkins N.A., Amara S.G. Mouse excitatory amino acid transporter EAAT2: isolation, characterization, and proximity to neuroexcitability loci on mouse chromosome 2. Genomics. 24:1994;218-224.
    • (1994) Genomics , vol.24 , pp. 218-224
    • Kirschner, M.A.1    Copeland, N.G.2    Gilbert, D.J.3    Jenkins, N.A.4    Amara, S.G.5
  • 523
    • 13344275855 scopus 로고
    • Nerve injury enhances rat neuronal glutamate transporter expression: Identification by differential display PCR
    • Kiryu S., Yao G.L., Morita N., Kato H., Kiyama H. Nerve injury enhances rat neuronal glutamate transporter expression: identification by differential display PCR. J. Neurosci. 15:1995;7872-7878.
    • (1995) J. Neurosci. , vol.15 , pp. 7872-7878
    • Kiryu, S.1    Yao, G.L.2    Morita, N.3    Kato, H.4    Kiyama, H.5
  • 524
    • 0024492914 scopus 로고
    • Ontogeny of glutamate accumulating activity in rat brain synaptic vesicles
    • Kish P.E., Kim S.Y., Ueda T. Ontogeny of glutamate accumulating activity in rat brain synaptic vesicles. Neurosci. Lett. 97:1989;185-190.
    • (1989) Neurosci. Lett. , vol.97 , pp. 185-190
    • Kish, P.E.1    Kim, S.Y.2    Ueda, T.3
  • 525
    • 0024549407 scopus 로고
    • Interlaminar and lateral excitatory amino acid connections in the striate cortex of monkey
    • Kisvarday Z.F., Cowey A., Smith A.D., Somogyi P. Interlaminar and lateral excitatory amino acid connections in the striate cortex of monkey. J. Neurosci. 9:1989;667-682.
    • (1989) J. Neurosci. , vol.9 , pp. 667-682
    • Kisvarday, Z.F.1    Cowey, A.2    Smith, A.D.3    Somogyi, P.4
  • 526
    • 0029973626 scopus 로고    scopus 로고
    • Transmitter concentration profiles in the synaptic cleft: An analytical model of release and diffusion
    • Kleinle J., Vogt K., Lüscher H.R., Müller L., Senn W., Wyler K., Streit J. Transmitter concentration profiles in the synaptic cleft: an analytical model of release and diffusion. Biophys. J. 71:1996;2413-2426.
    • (1996) Biophys. J. , vol.71 , pp. 2413-2426
    • Kleinle, J.1    Vogt, K.2    Lüscher, H.R.3    Müller, L.4    Senn, W.5    Wyler, K.6    Streit, J.7
  • 527
    • 0029160417 scopus 로고
    • Astrocytic volume fluctuates in the hippocampal CA1 region across the estrous cycle
    • Klintsova A., Levy W.B., Desmond N.L. Astrocytic volume fluctuates in the hippocampal CA1 region across the estrous cycle. Brain Res. 690:1995;269-274.
    • (1995) Brain Res. , vol.690 , pp. 269-274
    • Klintsova, A.1    Levy, W.B.2    Desmond, N.L.3
  • 528
    • 0027165152 scopus 로고
    • Electrogenic L-glutamate uptake in Xenopus laevis oocytes expressing a cloned rat brain L-glutamate/L-aspartate transporter (GLAST-1)
    • Klöckner U., Storck T., Conradt M., Stoffel W. Electrogenic L-glutamate uptake in Xenopus laevis oocytes expressing a cloned rat brain L-glutamate/L-aspartate transporter (GLAST-1). J. Biol. Chem. 268:1993;14594-14596.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14594-14596
    • Klöckner, U.1    Storck, T.2    Conradt, M.3    Stoffel, W.4
  • 529
    • 0030789808 scopus 로고    scopus 로고
    • Decreased glutamate transporter (GLT-1) expression in frontal cortex of rats with acute liver failure
    • Knecht K., Michalak A., Rose C., Rothstein J.D., Butterworth R.F. Decreased glutamate transporter (GLT-1) expression in frontal cortex of rats with acute liver failure. Neurosci. Lett. 229:1997;201-203.
    • (1997) Neurosci. Lett. , vol.229 , pp. 201-203
    • Knecht, K.1    Michalak, A.2    Rose, C.3    Rothstein, J.D.4    Butterworth, R.F.5
  • 530
    • 0033973460 scopus 로고    scopus 로고
    • Tight junctions of the blood-brain barrier
    • Kniesel U., Wolburg H. Tight junctions of the blood-brain barrier. Cell. Mol. Neurobiol. 20:2000;57-76.
    • (2000) Cell. Mol. Neurobiol. , vol.20 , pp. 57-76
    • Kniesel, U.1    Wolburg, H.2
  • 532
    • 0032976901 scopus 로고    scopus 로고
    • Nontransportable inhibitors attenuate reversal of glutamate uptake in synaptosomes following a metabolic insult
    • Koch H.P., Chamberlin A.R., Bridges R.J. Nontransportable inhibitors attenuate reversal of glutamate uptake in synaptosomes following a metabolic insult. Mol. Pharmacol. 55:1999;1044-1048.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 1044-1048
    • Koch, H.P.1    Chamberlin, A.R.2    Bridges, R.J.3
  • 533
    • 0031587404 scopus 로고    scopus 로고
    • Insulin-like growth factor binding proteins-3 and -5 form sodium dodecyl sulfate-stable multimers
    • Koedam J.A., Hoogerbrugge C.M., Vanbuuloffers S.C. Insulin-like growth factor binding proteins-3 and -5 form sodium dodecyl sulfate-stable multimers. Biochem. Biophys. Res. Commun. 240:1997;707-714.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 707-714
    • Koedam, J.A.1    Hoogerbrugge, C.M.2    Vanbuuloffers, S.C.3
  • 535
    • 0027905017 scopus 로고
    • Modulation of neuronal migration by NMDA receptors
    • Komuro H., Rakic P. Modulation of neuronal migration by NMDA receptors. Science. 260:1993;95-97.
    • (1993) Science , vol.260 , pp. 95-97
    • Komuro, H.1    Rakic, P.2
  • 537
    • 0032171425 scopus 로고    scopus 로고
    • The basic chemistry of nitrogen monoxide and peroxynitrite
    • Koppenol W.H. The basic chemistry of nitrogen monoxide and peroxynitrite. Free Radic. Biol. Med. 25:1998;385-391.
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 385-391
    • Koppenol, W.H.1
  • 538
    • 0033538998 scopus 로고    scopus 로고
    • Bidirectional regulation of dendritic spine dimensions by glutamate receptors
    • Korkotian E., Segal M. Bidirectional regulation of dendritic spine dimensions by glutamate receptors. Neuroreport. 10:1999;2875-2877.
    • (1999) Neuroreport , vol.10 , pp. 2875-2877
    • Korkotian, E.1    Segal, M.2
  • 540
    • 0033008557 scopus 로고    scopus 로고
    • Confirmation of domoic acid production of pseudo-Nitzschia multiseries isolated from Ofunato bay, Japan
    • Kotaki Y., Koike K., Sato S., Ogata T., Fukuyo Y., Kodama M. Confirmation of domoic acid production of pseudo-Nitzschia multiseries isolated from Ofunato bay, Japan. Toxicon. 37:1999;677-682.
    • (1999) Toxicon , vol.37 , pp. 677-682
    • Kotaki, Y.1    Koike, K.2    Sato, S.3    Ogata, T.4    Fukuyo, Y.5    Kodama, M.6
  • 542
    • 0021246341 scopus 로고
    • 3H]glutamate binding to rat hippocampal membranes
    • 3H]glutamate binding to rat hippocampal membranes. Eur. J. Pharmacol. 102:1984;155-158.
    • (1984) Eur. J. Pharmacol. , vol.102 , pp. 155-158
    • Kramer, K.1    Baudry, M.2
  • 543
    • 0022855762 scopus 로고
    • Functional reconstitution of carrier proteins by removal of detergent with a hydrophobic ion exchange column
    • Kramer R., Heberger C. Functional reconstitution of carrier proteins by removal of detergent with a hydrophobic ion exchange column. Biochim. Biophys. Acta. 863:1986;289-296.
    • (1986) Biochim. Biophys. Acta , vol.863 , pp. 289-296
    • Kramer, R.1    Heberger, C.2
  • 544
    • 0024558293 scopus 로고
    • Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria
    • Kramer R., Palmieri F. Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria. Biochim. Biophys. Acta. 974:1989;1-23.
    • (1989) Biochim. Biophys. Acta , vol.974 , pp. 1-23
    • Kramer, R.1    Palmieri, F.2
  • 545
    • 0001062019 scopus 로고
    • Metabolism of amino acids. IV. Synthesis of glutamine from glutamic acid
    • Krebs H.A. Metabolism of amino acids. IV. Synthesis of glutamine from glutamic acid and ammonia, and the enzymatic hydrolysis of glutamine in animal tissue. Biochem. J. 29:1935;1951-1969.
    • (1935) Biochem. J. , vol.29 , pp. 1951-1969
    • Krebs, H.A.1
  • 546
    • 0026676888 scopus 로고
    • Naturally-occurring excitatory amino acids as neurotoxins and leads in drug design
    • Krogsgaard-Larsen P., Hansen J.J. Naturally-occurring excitatory amino acids as neurotoxins and leads in drug design. Toxicol. Lett. 64-65:1992;409-416.
    • (1992) Toxicol. Lett. , vol.6465 , pp. 409-416
    • Krogsgaard-Larsen, P.1    Hansen, J.J.2
  • 547
    • 0033959288 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of a cDNA encoding a glutamate transporter in the honeybee brain
    • Kucharski R., Ball E.E., Hayward D.C., Maleszka R. Molecular cloning and expression analysis of a cDNA encoding a glutamate transporter in the honeybee brain. Gene. 242:2000;399-405.
    • (2000) Gene , vol.242 , pp. 399-405
    • Kucharski, R.1    Ball, E.E.2    Hayward, D.C.3    Maleszka, R.4
  • 548
    • 0033178904 scopus 로고    scopus 로고
    • Glutamate transporter EAAC1 is expressed in neurons and glial cells in the rat nervous system
    • Kugler P., Schmitt A. Glutamate transporter EAAC1 is expressed in neurons and glial cells in the rat nervous system. Glia. 27:1999;129-142.
    • (1999) Glia , vol.27 , pp. 129-142
    • Kugler, P.1    Schmitt, A.2
  • 549
    • 0032970519 scopus 로고    scopus 로고
    • Synaptic and extrasynaptic roles of glutamate in the mammalian hippocampus
    • Kullmann D.M. Synaptic and extrasynaptic roles of glutamate in the mammalian hippocampus. Acta Physiol. Scand. 166:1999;79-83.
    • (1999) Acta Physiol. Scand. , vol.166 , pp. 79-83
    • Kullmann, D.M.1
  • 550
    • 0037830240 scopus 로고    scopus 로고
    • Extrasynaptic glutamate spillover in the hippocampus: Evidence and implications
    • Kullmann D.M., Asztely F. Extrasynaptic glutamate spillover in the hippocampus: evidence and implications. Trends Neurosci. 21:1998;8-14.
    • (1998) Trends Neurosci. , vol.21 , pp. 8-14
    • Kullmann, D.M.1    Asztely, F.2
  • 551
    • 0030248099 scopus 로고    scopus 로고
    • LTP of AMPA and NMDA receptor-mediated signals: Evidence for presynaptic expression and extrasynaptic glutamate spill-over
    • Kullmann D.M., Erdemli G., Asztely F. LTP of AMPA and NMDA receptor-mediated signals: evidence for presynaptic expression and extrasynaptic glutamate spill-over. Neuron. 17:1996;461-474.
    • (1996) Neuron , vol.17 , pp. 461-474
    • Kullmann, D.M.1    Erdemli, G.2    Asztely, F.3
  • 552
    • 0031950667 scopus 로고    scopus 로고
    • Ethanol and regulation of the NMDA receptor subunits in fetal cortical neurons
    • Kumari M., Ticku M.K. Ethanol and regulation of the NMDA receptor subunits in fetal cortical neurons. J. Neurochem. 70:1998;1467-1473.
    • (1998) J. Neurochem. , vol.70 , pp. 1467-1473
    • Kumari, M.1    Ticku, M.K.2
  • 553
    • 0031439985 scopus 로고    scopus 로고
    • Impaired parallel fiber→Purkinje cell synapse stabilization during cerebellar development of mutant mice lacking the glutamate receptor delta 2 subunit
    • Kurihara H., Hashimoto K., Kano M., Takayama C., Sakimura K., Mishina M., Inoue Y., Watanabe M. Impaired parallel fiber→Purkinje cell synapse stabilization during cerebellar development of mutant mice lacking the glutamate receptor delta 2 subunit. J. Neurosci. 17:1997;9613-9623.
    • (1997) J. Neurosci. , vol.17 , pp. 9613-9623
    • Kurihara, H.1    Hashimoto, K.2    Kano, M.3    Takayama, C.4    Sakimura, K.5    Mishina, M.6    Inoue, Y.7    Watanabe, M.8
  • 555
    • 0028871559 scopus 로고
    • Selective degeneration of inhibitory interneurons in the rat spinal cord induced by intrathecal infusion of acromelic acid
    • Kwak S., Nakamura R. Selective degeneration of inhibitory interneurons in the rat spinal cord induced by intrathecal infusion of acromelic acid. Brain Res. 702:1995;61-71.
    • (1995) Brain Res. , vol.702 , pp. 61-71
    • Kwak, S.1    Nakamura, R.2
  • 556
    • 0026625042 scopus 로고
    • Acromelic acid, a novel kainate analogue, induces long-lasting paraparesis with selective degeneration of interneurons in the rat spinal cord
    • Kwak S., Hitoshi A., Michiko I., Haruhiko S. Acromelic acid, a novel kainate analogue, induces long-lasting paraparesis with selective degeneration of interneurons in the rat spinal cord. Exp. Neurol. 116:1992;145-155.
    • (1992) Exp. Neurol. , vol.116 , pp. 145-155
    • Kwak, S.1    Hitoshi, A.2    Michiko, I.3    Haruhiko, S.4
  • 557
    • 0030911964 scopus 로고    scopus 로고
    • Increased CSF glutamate following injection of ALS immunoglobulins
    • La Bella V., Goodman J.C., Appel S.H. Increased CSF glutamate following injection of ALS immunoglobulins. Neurology. 48:1997;1270-1272.
    • (1997) Neurology , vol.48 , pp. 1270-1272
    • La Bella, V.1    Goodman, J.C.2    Appel, S.H.3
  • 558
    • 0029091514 scopus 로고
    • Glutamine from glial cells is essential for the maintenance of the nerve terminal pool of glutamate: Immunogold evidence from hippocampal slice cultures
    • Laake J.H., Slyngstad T.A., Haug F.M.S., Ottersen O.P. Glutamine from glial cells is essential for the maintenance of the nerve terminal pool of glutamate: immunogold evidence from hippocampal slice cultures. J. Neurochem. 65:1995;871-881.
    • (1995) J. Neurochem. , vol.65 , pp. 871-881
    • Laake, J.H.1    Slyngstad, T.A.2    Haug, F.M.S.3    Ottersen, O.P.4
  • 559
    • 0032890369 scopus 로고    scopus 로고
    • Postembedding immunogold labelling reveals subcellular localization and pathway-specific enrichment of phosphate activated glutaminase in rat cerebellum
    • Laake J.H., Takumi Y., Eidet J., Torgner I.A., Roberg B., Kvamme E., Ottersen O.P. Postembedding immunogold labelling reveals subcellular localization and pathway-specific enrichment of phosphate activated glutaminase in rat cerebellum. Neuroscience. 88:1999;1137-1151.
    • (1999) Neuroscience , vol.88 , pp. 1137-1151
    • Laake, J.H.1    Takumi, Y.2    Eidet, J.3    Torgner, I.A.4    Roberg, B.5    Kvamme, E.6    Ottersen, O.P.7
  • 560
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 561
    • 0027221998 scopus 로고
    • NMDA-dependent superoxide production and neurotoxicity
    • Lafon-Cazal M., Pietri S., Culcasi M., Bockaert J. NMDA-dependent superoxide production and neurotoxicity. Nature. 364:1993;535-537.
    • (1993) Nature , vol.364 , pp. 535-537
    • Lafon-Cazal, M.1    Pietri, S.2    Culcasi, M.3    Bockaert, J.4
  • 562
    • 0029617792 scopus 로고
    • The usual suspects: GABA and glutamate may regulate proliferation in the neocortex
    • LaMantia A.S. The usual suspects: GABA and glutamate may regulate proliferation in the neocortex. Neuron. 15:1995;1223-1225.
    • (1995) Neuron , vol.15 , pp. 1223-1225
    • Lamantia, A.S.1
  • 564
    • 0027535976 scopus 로고
    • High-affinity L-aspartate transporter in prostate epithelial cells that is regulated by testosterone
    • Lao L.X., Franklin R.B., Costello L.C. High-affinity L-aspartate transporter in prostate epithelial cells that is regulated by testosterone. Prostate. 22:1993;53-63.
    • (1993) Prostate , vol.22 , pp. 53-63
    • Lao, L.X.1    Franklin, R.B.2    Costello, L.C.3
  • 565
    • 0031034744 scopus 로고    scopus 로고
    • Isoflurane increases the uptake of glutamate in synaptosomes from rat cerebral cortex
    • Larsen M., Hegstad E., Berg-Johnsen J., Langmoen I.A. Isoflurane increases the uptake of glutamate in synaptosomes from rat cerebral cortex. Br. J. Anaesth. 78:1997;55-59.
    • (1997) Br. J. Anaesth. , vol.78 , pp. 55-59
    • Larsen, M.1    Hegstad, E.2    Berg-Johnsen, J.3    Langmoen, I.A.4
  • 566
    • 0031976583 scopus 로고    scopus 로고
    • Effect of isoflurane on release and uptake of gamma-aminobutyric acid from rat cortical synaptosomes
    • Larsen M., Haugstad T.S., Bergjohnsen J., Langmoen I.A. Effect of isoflurane on release and uptake of gamma-aminobutyric acid from rat cortical synaptosomes. Br. J. Anaesth. 80:1998;634-638.
    • (1998) Br. J. Anaesth. , vol.80 , pp. 634-638
    • Larsen, M.1    Haugstad, T.S.2    Bergjohnsen, J.3    Langmoen, I.A.4
  • 567
    • 0032523002 scopus 로고    scopus 로고
    • Evidence for a tetrameric structure of recombinant NMDA receptors
    • Laube B., Kuhse J., Betz H. Evidence for a tetrameric structure of recombinant NMDA receptors. J. Neurosci. 18:1998;2954-2961.
    • (1998) J. Neurosci. , vol.18 , pp. 2954-2961
    • Laube, B.1    Kuhse, J.2    Betz, H.3
  • 568
    • 0030808979 scopus 로고    scopus 로고
    • New beta-hydroxyaspartate derivatives are competitive blockers for the bovine glutamate/aspartate transporter
    • Lebrun B., Sakaitani M., Shimamoto K., Yasudakamatani Y., Nakajima T. New beta-hydroxyaspartate derivatives are competitive blockers for the bovine glutamate/aspartate transporter. J. Biol. Chem. 272:1997;20336-20339.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20336-20339
    • Lebrun, B.1    Sakaitani, M.2    Shimamoto, K.3    Yasudakamatani, Y.4    Nakajima, T.5
  • 569
    • 0029147583 scopus 로고
    • Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors
    • Lee R.K.K., Wurtman R.J., Cox A.J., Nitsch R.M. Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors. Proc. Natl. Acad. Sci. USA. 92:1995;8083-8087.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8083-8087
    • Lee, R.K.K.1    Wurtman, R.J.2    Cox, A.J.3    Nitsch, R.M.4
  • 570
    • 0020611267 scopus 로고
    • Effects of in vivo administration of kainic acid on the extracellular amino acid pool in the rabbit hippocampus
    • Lehmann A., Isacsson H., Hamberger A. Effects of in vivo administration of kainic acid on the extracellular amino acid pool in the rabbit hippocampus. J. Neurochem. 40:1983;1314-1320.
    • (1983) J. Neurochem. , vol.40 , pp. 1314-1320
    • Lehmann, A.1    Isacsson, H.2    Hamberger, A.3
  • 571
    • 0032194950 scopus 로고    scopus 로고
    • The number of glutamate transporter subtype molecules at glutamatergic synapses: Chemical and stereological quantification in young adult rat brain
    • Lehre K.P., Danbolt N.C. The number of glutamate transporter subtype molecules at glutamatergic synapses: chemical and stereological quantification in young adult rat brain. J. Neurosci. 18:1998;8751-8757.
    • (1998) J. Neurosci. , vol.18 , pp. 8751-8757
    • Lehre, K.P.1    Danbolt, N.C.2
  • 572
    • 0028958939 scopus 로고
    • Differential expression of two glial glutamate transporters in the rat brain: Quantitative and immunocytochemical observations
    • Lehre K.P., Levy L.M., Ottersen O.P., Storm-Mathisen J., Danbolt N.C. Differential expression of two glial glutamate transporters in the rat brain: quantitative and immunocytochemical observations. J. Neurosci. 15:1995;1835-1853.
    • (1995) J. Neurosci. , vol.15 , pp. 1835-1853
    • Lehre, K.P.1    Levy, L.M.2    Ottersen, O.P.3    Storm-Mathisen, J.4    Danbolt, N.C.5
  • 573
    • 0031032196 scopus 로고    scopus 로고
    • Localization of the glutamate transporter protein GLAST in rat retina
    • Lehre K.P., Davanger S., Danbolt N.C. Localization of the glutamate transporter protein GLAST in rat retina. Brain Res. 744:1997;129-137.
    • (1997) Brain Res. , vol.744 , pp. 129-137
    • Lehre, K.P.1    Davanger, S.2    Danbolt, N.C.3
  • 574
    • 0031057837 scopus 로고    scopus 로고
    • Exploring the etiology of Alzheimer disease using molecular genetics
    • Lendon C.L., Ashall F., Goate A.M. Exploring the etiology of Alzheimer disease using molecular genetics. JAMA. 277:1997;825-831.
    • (1997) JAMA , vol.277 , pp. 825-831
    • Lendon, C.L.1    Ashall, F.2    Goate, A.M.3
  • 575
    • 0024799178 scopus 로고
    • The effects of progressive formaldehyde fixation on the preservation of tissue antigens
    • Leong A.S.Y., Gilham P.N. The effects of progressive formaldehyde fixation on the preservation of tissue antigens. Pathology (Phila.). 21:1989;266-268.
    • (1989) Pathology (Phila.) , vol.21 , pp. 266-268
    • Leong, A.S.Y.1    Gilham, P.N.2
  • 576
    • 0023064885 scopus 로고
    • Acidic amino acid transport in animal cells and tissues
    • Lerner J. Acidic amino acid transport in animal cells and tissues. Comp. Biochem. Physiol. 87B:1987;443-457.
    • (1987) Comp. Biochem. Physiol. , vol.87 , pp. 443-457
    • Lerner, J.1
  • 577
    • 0034679877 scopus 로고    scopus 로고
    • Localization of glutamate and glutamate transporters in the sensory neurons of Aplysia
    • Levenson J., Sherry D.M., Dryer L., Chin J., Byrne J.H., Eskin A. Localization of glutamate and glutamate transporters in the sensory neurons of Aplysia. J. Comp. Neurol. 423:2000;121-131.
    • (2000) J. Comp. Neurol. , vol.423 , pp. 121-131
    • Levenson, J.1    Sherry, D.M.2    Dryer, L.3    Chin, J.4    Byrne, J.H.5    Eskin, A.6
  • 578
    • 0016907175 scopus 로고
    • Uptake and exchange of GABA and glutamate in isolated nerve endings
    • Levi G., Poce U., Raiteri M. Uptake and exchange of GABA and glutamate in isolated nerve endings. Adv. Exp. Med. Biol. 69:1976;273-289.
    • (1976) Adv. Exp. Med. Biol. , vol.69 , pp. 273-289
    • Levi, G.1    Poce, U.2    Raiteri, M.3
  • 579
    • 0027428320 scopus 로고
    • Carrier-mediated release of neurotransmitters
    • Levi G., Raiteri M. Carrier-mediated release of neurotransmitters. Trends Neurosci. 16:1993;415-419.
    • (1993) Trends Neurosci. , vol.16 , pp. 415-419
    • Levi, G.1    Raiteri, M.2
  • 580
    • 0032786820 scopus 로고    scopus 로고
    • Autoantibodies to the glutamate receptor kill neurons via activation of the receptor ion channel
    • Levite M., Fleidervish I.A., Schwarz A., Pelled D., Futerman A.H. Autoantibodies to the glutamate receptor kill neurons via activation of the receptor ion channel. J. Autoimmun. 13:1999;61-72.
    • (1999) J. Autoimmun. , vol.13 , pp. 61-72
    • Levite, M.1    Fleidervish, I.A.2    Schwarz, A.3    Pelled, D.4    Futerman, A.H.5
  • 581
    • 0011895977 scopus 로고
    • Down regulation of a glial glutamate transporter in striatum after destruction of the glutamatergic corticostriatal projection
    • Levy L.M., Lehre K.P., Walaas S.I., Storm-Mathisen J., Danbolt N.C. Down regulation of a glial glutamate transporter in striatum after destruction of the glutamatergic corticostriatal projection. J. Neurochem. 61:1993;S208.
    • (1993) J. Neurochem. , vol.61 , pp. 208
    • Levy, L.M.1    Lehre, K.P.2    Walaas, S.I.3    Storm-Mathisen, J.4    Danbolt, N.C.5
  • 582
    • 0027405648 scopus 로고
    • +]coupled L-glutamate transporter purified from rat brain confirms glial cell localization
    • +]coupled L-glutamate transporter purified from rat brain confirms glial cell localization. FEBS Lett. 317:1993;79-84.
    • (1993) FEBS Lett. , vol.317 , pp. 79-84
    • Levy, L.M.1    Lehre, K.P.2    Rolstad, B.3    Danbolt, N.C.4
  • 583
    • 0029119884 scopus 로고
    • Down-regulation of glial glutamate transporters after glutamatergic denervation in the rat brain
    • Levy L.M., Lehre K.P., Walaas S.I., Storm-Mathisen J., Danbolt N.C. Down-regulation of glial glutamate transporters after glutamatergic denervation in the rat brain. Eur. J. Neurosci. 7:1995;2036-2041.
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 2036-2041
    • Levy, L.M.1    Lehre, K.P.2    Walaas, S.I.3    Storm-Mathisen, J.4    Danbolt, N.C.5
  • 584
    • 0032488807 scopus 로고    scopus 로고
    • Inducible expression of the GLT-1 glutamate transporter in a CHO cell line selected for low endogenous glutamate uptake
    • Levy L.M., Attwell D., Hoover F., Ash J.F., Bjørås M., Danbolt N.C. Inducible expression of the GLT-1 glutamate transporter in a CHO cell line selected for low endogenous glutamate uptake. FEBS Lett. 422:1998;339-342.
    • (1998) FEBS Lett. , vol.422 , pp. 339-342
    • Levy, L.M.1    Attwell, D.2    Hoover, F.3    Ash, J.F.4    Bjørås, M.5    Danbolt, N.C.6
  • 586
    • 0030872412 scopus 로고    scopus 로고
    • Glutamate transporter alterations in Alzheimer disease are possibly associated with abnormal APP expression
    • Li S., Mallory M., Alford M., Tanaka S., Masliah E. Glutamate transporter alterations in Alzheimer disease are possibly associated with abnormal APP expression. J. Neuropathol. Exp. Neurol. 56:1997;901-911.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 901-911
    • Li, S.1    Mallory, M.2    Alford, M.3    Tanaka, S.4    Masliah, E.5
  • 587
    • 0028874843 scopus 로고
    • Assignment of the gene SLC1a2 coding for the human glutamate transporter EAAT2 to human chromosome 11 bands p13-p12
    • Li X., Francke U. Assignment of the gene SLC1a2 coding for the human glutamate transporter EAAT2 to human chromosome 11 bands p13-p12. Cytogenet. Cell Genet. 71:1995;212-213.
    • (1995) Cytogenet. Cell Genet. , vol.71 , pp. 212-213
    • Li, X.1    Francke, U.2
  • 588
    • 0028347852 scopus 로고
    • 3H]L-aspartate in thaw-mounted sections of rat forebrain
    • 3H]L-aspartate in thaw-mounted sections of rat forebrain. Exp. Brain Res. 97:1994;415-422.
    • (1994) Exp. Brain Res. , vol.97 , pp. 415-422
    • Li, Y.1    Balcar, V.J.2
  • 589
    • 0033963248 scopus 로고    scopus 로고
    • 3H]L-aspartate binding to L-glutamate transporters in rat brain: Structure-activity studies using L-trans-pyrrolidine-2,4-dicarboxylate (L-t-PDC) and 2-(carboxycyclopropyl)-glycine (CCG)
    • 3H]L-aspartate binding to L-glutamate transporters in rat brain: structure-activity studies using L-trans-pyrrolidine-2,4-dicarboxylate (L-t-PDC) and 2-(carboxycyclopropyl)-glycine (CCG). Neurochem. Int. 36:2000;319-327.
    • (2000) Neurochem. Int. , vol.36 , pp. 319-327
    • Lieb, I.1    Chebib, M.2    Cooper, B.3    Dias, L.S.4    Balcar, V.J.5
  • 590
    • 0342905443 scopus 로고    scopus 로고
    • Differential effects of corticostriatal and thalamostriatal deafferentation on expression of the glutamate transporter GLT1 in the rat striatum
    • Liévens J.C., Salin P., Had-Aissouni L., Mahy N., Kerkerian-Le Goff L. Differential effects of corticostriatal and thalamostriatal deafferentation on expression of the glutamate transporter GLT1 in the rat striatum. J. Neurochem. 74:2000;909-919.
    • (2000) J. Neurochem. , vol.74 , pp. 909-919
    • Liévens, J.C.1    Salin, P.2    Had-Aissouni, L.3    Mahy, N.4    Kerkerian-Le Goff, L.5
  • 591
    • 0035282612 scopus 로고    scopus 로고
    • Modulation of the neuronal glutamate transporter EAAC1 by the interacting protein GTRAP3-18
    • Lin, C.I., Orlov, I., Ruggiero, A.M., Dykes-Hoberg, M., Lee, A., Jackson, M., Rothstein, J.D., 2001. Modulation of the neuronal glutamate transporter EAAC1 by the interacting protein GTRAP3-18. Nature 410, 84-8.
    • (2001) Nature , vol.410 , pp. 84-88
    • Lin, C.I.1    Orlov, I.2    Ruggiero, A.M.3    Dykes-Hoberg, M.4    Lee, A.5    Jackson, M.6    Rothstein, J.D.7
  • 592
    • 0032032013 scopus 로고    scopus 로고
    • Aberrant RNA processing in a neurodegenerative disease: The cause for absent EAAT2 a glutamate transporter, in amyotrophic lateral sclerosis
    • Lin C.L.G., Bristol L.A., Jin L., Dykes-Hoberg M., Crawford T., Clawson L., Rothstein J.D. Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2 a glutamate transporter, in amyotrophic lateral sclerosis. Neuron. 20:1998;589-602.
    • (1998) Neuron , vol.20 , pp. 589-602
    • Lin, C.L.G.1    Bristol, L.A.2    Jin, L.3    Dykes-Hoberg, M.4    Crawford, T.5    Clawson, L.6    Rothstein, J.D.7
  • 594
    • 0032845121 scopus 로고    scopus 로고
    • Ischemic cell death in brain neurons
    • Lipton P. Ischemic cell death in brain neurons. Physiol. Rev. 79:1999;1431-1568.
    • (1999) Physiol. Rev. , vol.79 , pp. 1431-1568
    • Lipton, P.1
  • 596
    • 0025907224 scopus 로고
    • Excitatory amino acids rise to toxic levels upon impact injury to the rat spinal cord
    • Liu D., Thangnipon W., McAdoo D.J. Excitatory amino acids rise to toxic levels upon impact injury to the rat spinal cord. Brain Res. 547:1991;344-348.
    • (1991) Brain Res. , vol.547 , pp. 344-348
    • Liu, D.1    Thangnipon, W.2    McAdoo, D.J.3
  • 597
    • 0030924715 scopus 로고    scopus 로고
    • Localization of glutamate receptor subunits of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) type in the pancreas of newborn guinea pigs
    • Liu H.P., Tay S.S.W., Leong S.K. Localization of glutamate receptor subunits of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) type in the pancreas of newborn guinea pigs. Pancreas. 14:1997;360-368.
    • (1997) Pancreas , vol.14 , pp. 360-368
    • Liu, H.P.1    Tay, S.S.W.2    Leong, S.K.3
  • 599
    • 0033401861 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha attenuates N-methyl-D-aspartate-mediated neurotoxicity in neonatal rat hippocampus
    • Liu X.H., Xu H.Y., Barks J.D.E. Tumor necrosis factor-alpha attenuates N-methyl-D-aspartate-mediated neurotoxicity in neonatal rat hippocampus. Brain Res. 851:1999;94-104.
    • (1999) Brain Res. , vol.851 , pp. 94-104
    • Liu, X.H.1    Xu, H.Y.2    Barks, J.D.E.3
  • 600
    • 0031044233 scopus 로고    scopus 로고
    • The role of vesicular transport proteins in synaptic transmission and neural degeneration
    • Liu Y., Edwards R.H. The role of vesicular transport proteins in synaptic transmission and neural degeneration. Annu. Rev. Neurosci. 20:1997;125-156.
    • (1997) Annu. Rev. Neurosci. , vol.20 , pp. 125-156
    • Liu, Y.1    Edwards, R.H.2
  • 602
    • 0033198811 scopus 로고    scopus 로고
    • Membrane trafficking of neurotransmitter transporters in the regulation of synaptic transmission
    • Liu Y., Krantz D.E., Waites C., Edwards R.H. Membrane trafficking of neurotransmitter transporters in the regulation of synaptic transmission. Trends Cell. Biol. 9:1999;356-363.
    • (1999) Trends Cell. Biol. , vol.9 , pp. 356-363
    • Liu, Y.1    Krantz, D.E.2    Waites, C.3    Edwards, R.H.4
  • 603
    • 0015209755 scopus 로고
    • Unique high affinity uptake systems for glycine, glutamic and aspartic acids in central nervous tissue of the rat
    • Logan W.J., Snyder S.H. Unique high affinity uptake systems for glycine, glutamic and aspartic acids in central nervous tissue of the rat. Nature. 234:1971;297-299.
    • (1971) Nature , vol.234 , pp. 297-299
    • Logan, W.J.1    Snyder, S.H.2
  • 604
    • 0015517461 scopus 로고
    • High affinity uptake systems for glycine, glutamic and aspartic acids in synaptosomes of rat central nervous tissues
    • Logan W.J., Snyder S.H. High affinity uptake systems for glycine, glutamic and aspartic acids in synaptosomes of rat central nervous tissues. Brain Res. 42:1972;413-431.
    • (1972) Brain Res. , vol.42 , pp. 413-431
    • Logan, W.J.1    Snyder, S.H.2
  • 606
    • 0028020779 scopus 로고
    • 3H]glutamate by striatal synaptosomes
    • 3H]glutamate by striatal synaptosomes. J. Neurochem. 63:1994;2108-2117.
    • (1994) J. Neurochem. , vol.63 , pp. 2108-2117
    • Lonart, G.1    Johnson, K.M.2
  • 607
    • 0028896256 scopus 로고
    • Excitatory amino acid release from astrocytes during energy failure by reversal of sodium-dependent uptake
    • Longuemare M.C., Swanson R.A. Excitatory amino acid release from astrocytes during energy failure by reversal of sodium-dependent uptake. J. Neurosci. Res. 40:1995;379-386.
    • (1995) J. Neurosci. Res. , vol.40 , pp. 379-386
    • Longuemare, M.C.1    Swanson, R.A.2
  • 608
    • 0030851529 scopus 로고    scopus 로고
    • Net glutamate release from astrocytes is not induced by extracellular potassium concentrations attainable in brain
    • Longuemare M.C., Swanson R.A. Net glutamate release from astrocytes is not induced by extracellular potassium concentrations attainable in brain. J. Neurochem. 69:1997;879-882.
    • (1997) J. Neurochem. , vol.69 , pp. 879-882
    • Longuemare, M.C.1    Swanson, R.A.2
  • 610
    • 0024381168 scopus 로고
    • Reconstitution and partial purification of the sodium and chloride-coupled glycine transporter from rat spinal cord
    • López-Corcuera B., Kanner B.I., Aragón C. Reconstitution and partial purification of the sodium and chloride-coupled glycine transporter from rat spinal cord. Biochim. Biophys. Acta. 983:1989;247-252.
    • (1989) Biochim. Biophys. Acta , vol.983 , pp. 247-252
    • López-Corcuera, B.1    Kanner, B.I.2    Aragón, C.3
  • 611
    • 0026321612 scopus 로고
    • Purification of sodium- And chloride-coupled glycine transporter from central nervous system
    • López-Corcuera B., Vázquez J., Aragón C. Purification of sodium- and chloride-coupled glycine transporter from central nervous system. J. Biol. Chem. 266:1991;24809-24814.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24809-24814
    • López-Corcuera, B.1    Vázquez, J.2    Aragón, C.3
  • 612
    • 0027470691 scopus 로고
    • Hydrodynamic properties and immunological identification of the sodium-coupled and chloride-coupled glycine transporter
    • López-Corcuera B., Alcántara R., Vázquez J., Aragón C. Hydrodynamic properties and immunological identification of the sodium-coupled and chloride-coupled glycine transporter. J. Biol. Chem. 268:1993;2239-2243.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2239-2243
    • López-Corcuera, B.1    Alcántara, R.2    Vázquez, J.3    Aragón, C.4
  • 613
    • 0034728639 scopus 로고    scopus 로고
    • Glutamate transporter GLT-1 is highly expressed in activated microglia following facial nerve axotomy
    • Lopez-Redondo F., Nakajima K., Honda S., Kohsaka S. Glutamate transporter GLT-1 is highly expressed in activated microglia following facial nerve axotomy. Brain Res. Mol. Brain Res. 76:2000;429-435.
    • (2000) Brain Res. Mol. Brain Res. , vol.76 , pp. 429-435
    • Lopez-Redondo, F.1    Nakajima, K.2    Honda, S.3    Kohsaka, S.4
  • 614
    • 0033055937 scopus 로고    scopus 로고
    • Effects of PKA and PKC modulators on high affinity glutamate uptake in primary neuronal cell cultures from rat cerebral cortex
    • Lortet S., Samuel D., Had-Aissouni L., Masmejean F., Kerkerian-Le Goff L., Pisano P. Effects of PKA and PKC modulators on high affinity glutamate uptake in primary neuronal cell cultures from rat cerebral cortex. Neuropharmacology. 38:1999;395-402.
    • (1999) Neuropharmacology , vol.38 , pp. 395-402
    • Lortet, S.1    Samuel, D.2    Had-Aissouni, L.3    Masmejean, F.4    Kerkerian-Le Goff, L.5    Pisano, P.6
  • 615
    • 0024535962 scopus 로고
    • Ethanol inhibits NMDA-activated ion current in hippocampal neurons
    • Lovinger D.M., White G., Weight F.F. Ethanol inhibits NMDA-activated ion current in hippocampal neurons. Science. 243:1989;1721-1724.
    • (1989) Science , vol.243 , pp. 1721-1724
    • Lovinger, D.M.1    White, G.2    Weight, F.F.3
  • 616
    • 0031841676 scopus 로고    scopus 로고
    • Exocytosis: SNAREs drum up!
    • Ludger J., Galli T. Exocytosis: SNAREs drum up! Eur. J. Neurosci. 10:1998;415-422.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 415-422
    • Ludger, J.1    Galli, T.2
  • 617
    • 0344631768 scopus 로고    scopus 로고
    • Neurotoxic mechanisms of degeneration in motor neuron diseases
    • Ludolph A.C., Münch C. Neurotoxic mechanisms of degeneration in motor neuron diseases. Drug Metab. Rev. 31:1999;619-634.
    • (1999) Drug Metab. Rev. , vol.31 , pp. 619-634
    • Ludolph, A.C.1    Münch, C.2
  • 619
    • 0030704241 scopus 로고    scopus 로고
    • Differential plasma membrane distribution of metabotropic glutamate receptors mGluR1 alpha, mGluR2 and mGluR5, relative to neurotransmitter release sites
    • Luján R., Roberts J.D., Shigemoto R., Ohishi H., Somogyi P. Differential plasma membrane distribution of metabotropic glutamate receptors mGluR1 alpha, mGluR2 and mGluR5, relative to neurotransmitter release sites. J. Chem. Neuroanat. 13:1997;219-241.
    • (1997) J. Chem. Neuroanat. , vol.13 , pp. 219-241
    • Luján, R.1    Roberts, J.D.2    Shigemoto, R.3    Ohishi, H.4    Somogyi, P.5
  • 621
    • 0028158917 scopus 로고
    • The effect of arachidonic acid on glutamate uptake in cortical and hippocampal preparations
    • Lynch M.A., Jaquesberg W., Lawson P.R., Voss K.L., Bliss T.V.P. The effect of arachidonic acid on glutamate uptake in cortical and hippocampal preparations. Neurosci. Res. Commun. 14:1994;53-61.
    • (1994) Neurosci. Res. Commun. , vol.14 , pp. 53-61
    • Lynch, M.A.1    Jaquesberg, W.2    Lawson, P.R.3    Voss, K.L.4    Bliss, T.V.P.5
  • 622
    • 0034602141 scopus 로고    scopus 로고
    • Glutamate is not a messenger in insulin secretion
    • MacDonald M.J., Fahien L.A. Glutamate is not a messenger in insulin secretion. J. Biol. Chem. 275:2000;34025-34027.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34025-34027
    • MacDonald, M.J.1    Fahien, L.A.2
  • 623
    • 0031570787 scopus 로고    scopus 로고
    • Glutamate-treated rat cortical neuronal cultures die in a way different from the classical apoptosis induced by staurosporine
    • MacManus J.P., Rasquinha I., Black M.A., Laferriere N.B., Monette R., Walker T., Morley P. Glutamate-treated rat cortical neuronal cultures die in a way different from the classical apoptosis induced by staurosporine. Exp. Cell Res. 233:1997;310-320.
    • (1997) Exp. Cell Res. , vol.233 , pp. 310-320
    • MacManus, J.P.1    Rasquinha, I.2    Black, M.A.3    Laferriere, N.B.4    Monette, R.5    Walker, T.6    Morley, P.7
  • 624
    • 0027527251 scopus 로고
    • Adenosine triphosphate depletion reverses sodium-dependent, neuronal uptake of glutamate in rat hippocampal slices
    • Madl J.E., Burgesser K. Adenosine triphosphate depletion reverses sodium-dependent, neuronal uptake of glutamate in rat hippocampal slices. J. Neurosci. 13:1993;4429-4444.
    • (1993) J. Neurosci. , vol.13 , pp. 4429-4444
    • Madl, J.E.1    Burgesser, K.2
  • 625
    • 0033540037 scopus 로고    scopus 로고
    • Mitochondrial glutamate acts as a messenger in glucose-induced insulin exocytosis
    • Maechler P., Wollheim C.B. Mitochondrial glutamate acts as a messenger in glucose-induced insulin exocytosis. Nature. 402:1999;685-689.
    • (1999) Nature , vol.402 , pp. 685-689
    • Maechler, P.1    Wollheim, C.B.2
  • 628
    • 0027537292 scopus 로고
    • Steady states, charge movements, and rates for a cloned GABA transporter expressed in Xenopus oocytes
    • Mager S., Naeve J., Quick M., Labarca C., Davidson N., Lester H.A. Steady states, charge movements, and rates for a cloned GABA transporter expressed in Xenopus oocytes. Neuron. 10:1993;177-188.
    • (1993) Neuron , vol.10 , pp. 177-188
    • Mager, S.1    Naeve, J.2    Quick, M.3    Labarca, C.4    Davidson, N.5    Lester, H.A.6
  • 631
    • 0002731745 scopus 로고
    • Neonatal jaundice
    • G.B. Avery. Philadelphia, PA: J.B. Lippincott
    • Maisels M.J. Neonatal jaundice. Avery G.B. Neonatology. 1981;473-544 J.B. Lippincott, Philadelphia, PA.
    • (1981) Neonatology , pp. 473-544
    • Maisels, M.J.1
  • 632
    • 0032479813 scopus 로고    scopus 로고
    • Protein kinase C: A physiological mediator of enhanced transmitter output
    • Majewski H., Iannazzo L. Protein kinase C: a physiological mediator of enhanced transmitter output. Prog. Neurobiol. 55:1998;463-475.
    • (1998) Prog. Neurobiol. , vol.55 , pp. 463-475
    • Majewski, H.1    Iannazzo, L.2
  • 633
    • 0028051595 scopus 로고
    • The glutamate uptake inhibitor L-trans-pyrrolidine-2,4-dicarboxylate depresses excitatory synaptic transmission via a presynaptic mechanism in cultured hippocampal neurons
    • Maki R., Robinson M.B., Dichter M.A. The glutamate uptake inhibitor L-trans-pyrrolidine-2,4-dicarboxylate depresses excitatory synaptic transmission via a presynaptic mechanism in cultured hippocampal neurons. J. Neurosci. 14:1994;6754-6762.
    • (1994) J. Neurosci. , vol.14 , pp. 6754-6762
    • Maki, R.1    Robinson, M.B.2    Dichter, M.A.3
  • 634
    • 0029892792 scopus 로고    scopus 로고
    • Molecular biology of mammalian amino acid transporters
    • Malandro M.S., Kilberg M.S. Molecular biology of mammalian amino acid transporters. Annu. Rev. Biochem. 65:1996;305-336.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 305-336
    • Malandro, M.S.1    Kilberg, M.S.2
  • 635
    • 0028063217 scopus 로고
    • Cloning and characterization of a glutamate transporter cDNA from human brain and pancreas
    • Manfras B.J., Rudert W.A., Trucco M., Boehm B.O. Cloning and characterization of a glutamate transporter cDNA from human brain and pancreas. Biochim. Biophys. Acta. 1195:1994;185-188.
    • (1994) Biochim. Biophys. Acta , vol.1195 , pp. 185-188
    • Manfras, B.J.1    Rudert, W.A.2    Trucco, M.3    Boehm, B.O.4
  • 636
    • 0019522428 scopus 로고
    • The human platelet as a model for the glutamatergic neuron: Platelet uptake of L-glutamate
    • Mangano, R.M., Schwarcz, R., 1981a. The human platelet as a model for the glutamatergic neuron: platelet uptake of L-glutamate. J. Neurochem. 36, 1067-1076.
    • (1981) J. Neurochem. , vol.36 , pp. 1067-1076
    • Mangano, R.M.1    Schwarcz, R.2
  • 637
    • 0019855489 scopus 로고
    • Platelet glutamate and aspartate uptake in Huntington's disease
    • Mangano, R.M., Schwarcz, R., 1981b. Platelet glutamate and aspartate uptake in Huntington's disease. J. Neurochem. 37, 1072-1074.
    • (1981) J. Neurochem. , vol.37 , pp. 1072-1074
    • Mangano, R.M.1    Schwarcz, R.2
  • 638
    • 0030976939 scopus 로고    scopus 로고
    • 3H-glutamate uptake with different potencies in rodent central nervous system regions expressing different transporter subtypes
    • 3H-glutamate uptake with different potencies in rodent central nervous system regions expressing different transporter subtypes. Pharmacol. Res. 35:1997;149-151.
    • (1997) Pharmacol. Res. , vol.35 , pp. 149-151
    • Manzoni, C.1    Mennini, T.2
  • 639
    • 0033569524 scopus 로고    scopus 로고
    • C-terminal interactions modulate the affinity of GLAST glutamate transporters in salamander retinal glial cells
    • Marie H., Attwell D. C-terminal interactions modulate the affinity of GLAST glutamate transporters in salamander retinal glial cells. J. Physiol. (Lond.). 520:1999;393-397.
    • (1999) J. Physiol. (Lond.) , vol.520 , pp. 393-397
    • Marie, H.1    Attwell, D.2
  • 640
    • 0343333753 scopus 로고    scopus 로고
    • Characterization of the interaction between the LIM protein Ajuba and the glial glutamate transporter GLT-1, in COS cells and bipolar cells in slices of rat retina
    • 61P
    • Marie, H., Billups, D., Bedford, F., Attwell, D., Moss, S., 2000. Characterization of the interaction between the LIM protein Ajuba and the glial glutamate transporter GLT-1, in COS cells and bipolar cells in slices of rat retina. J. Physiol. 525, 61P.
    • (2000) J. Physiol. , vol.525
    • Marie, H.1    Billups, D.2    Bedford, F.3    Attwell, D.4    Moss, S.5
  • 641
    • 0033870901 scopus 로고    scopus 로고
    • Sodium-dependent neutral amino acid transporter type 1 is an auxiliary receptor for baboon endogenous retrovirus
    • Marin M., Tailor C.S., Nouri A., Kabat D. Sodium-dependent neutral amino acid transporter type 1 is an auxiliary receptor for baboon endogenous retrovirus. J. Virol. 74:2000;8085-8093.
    • (2000) J. Virol. , vol.74 , pp. 8085-8093
    • Marin, M.1    Tailor, C.S.2    Nouri, A.3    Kabat, D.4
  • 642
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery W.R., Carney J.M. Oxidative alterations in Alzheimer's disease. Brain Pathol. 9:1999;133-146.
    • (1999) Brain Pathol. , vol.9 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 644
    • 0017579832 scopus 로고
    • Glutamine synthetase: Glial localization in brain
    • Martinez-Hernandez A., Bell K.P., Norenberg M.D. Glutamine synthetase: glial localization in brain. Science. 195:1977;1356-1358.
    • (1977) Science , vol.195 , pp. 1356-1358
    • Martinez-Hernandez, A.1    Bell, K.P.2    Norenberg, M.D.3
  • 645
    • 0032466380 scopus 로고    scopus 로고
    • The L-glutamate transporters GLAST (EAAT1) and GLT-1 (EAAT2): Expression and regulation in rat lactating mammary gland
    • Martinez-López I., García C., Barber T., Viña J.R., Miralles V.J. The L-glutamate transporters GLAST (EAAT1) and GLT-1 (EAAT2): expression and regulation in rat lactating mammary gland. Mol. Membr. Biol. 15:1998;237-242.
    • (1998) Mol. Membr. Biol. , vol.15 , pp. 237-242
    • Martinez-López, I.1    García, C.2    Barber, T.3    Viña, J.R.4    Miralles, V.J.5
  • 646
    • 0019821465 scopus 로고
    • L-Aspartate transport into plasma membrane vesicles derived from rat brain synaptosomes
    • Marvizón J.G., Mayor F.J.r., Aragón M.C., Giménez C., Valdivieso F. L-Aspartate transport into plasma membrane vesicles derived from rat brain synaptosomes. J. Neurochem. 37:1981;1401-1406.
    • (1981) J. Neurochem. , vol.37 , pp. 1401-1406
    • Marvizón, J.G.1    Mayor, F.J.R.2    Aragón, M.C.3    Giménez, C.4    Valdivieso, F.5
  • 647
    • 0029811226 scopus 로고    scopus 로고
    • Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease
    • Masliah E., Alford M., Deteresa R., Mallory M., Hansen L. Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease. Ann. Neurol. 40:1996;759-766.
    • (1996) Ann. Neurol. , vol.40 , pp. 759-766
    • Masliah, E.1    Alford, M.2    Deteresa, R.3    Mallory, M.4    Hansen, L.5
  • 648
    • 0032524290 scopus 로고    scopus 로고
    • Amyloid protein precursor stimulates excitatory amino acid transport - Implications for roles in neuroprotection and pathogenesis
    • Masliah E., Raber J., Alford M., Mallory M., Mattson M.P., Yang D.S., Wong D.R., Mucke L. Amyloid protein precursor stimulates excitatory amino acid transport - implications for roles in neuroprotection and pathogenesis. J. Biol. Chem. 273:1998;12548-12554.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12548-12554
    • Masliah, E.1    Raber, J.2    Alford, M.3    Mallory, M.4    Mattson, M.P.5    Yang, D.S.6    Wong, D.R.7    Mucke, L.8
  • 649
    • 0034042926 scopus 로고    scopus 로고
    • Abnormal glutamate transport function in mutant amyloid precursor protein transgenic mice
    • Masliah E., Alford M., Mallory M., Rockenstein E., Moechars D., Vanleuven F. Abnormal glutamate transport function in mutant amyloid precursor protein transgenic mice. Exp. Neurol. 163:2000;381-387.
    • (2000) Exp. Neurol. , vol.163 , pp. 381-387
    • Masliah, E.1    Alford, M.2    Mallory, M.3    Rockenstein, E.4    Moechars, D.5    Vanleuven, F.6
  • 650
    • 0030948207 scopus 로고    scopus 로고
    • Mechanically regulated expression of a neural glutamate transporter in bone: A role for excitatory amino acids as osteotropic agents?
    • Mason D.J., Suva L.J., Genever P.G., Patton A.J., Steuckle S., Hillam R.A., Skerry T.M. Mechanically regulated expression of a neural glutamate transporter in bone: a role for excitatory amino acids as osteotropic agents? Bone. 20:1997;199-205.
    • (1997) Bone , vol.20 , pp. 199-205
    • Mason, D.J.1    Suva, L.J.2    Genever, P.G.3    Patton, A.J.4    Steuckle, S.5    Hillam, R.A.6    Skerry, T.M.7
  • 651
    • 0035847639 scopus 로고    scopus 로고
    • Expression of the high-affinity glutamate transporter EAAT4 in mammalian cerebral cortex
    • Massie, A., Vandesande, F., Arckens, L., 2001. Expression of the high-affinity glutamate transporter EAAT4 in mammalian cerebral cortex. Neuroreport 12, 393-397.
    • (2001) Neuroreport , vol.12 , pp. 393-397
    • Massie, A.1    Vandesande, F.2    Arckens, L.3
  • 652
    • 0032852641 scopus 로고    scopus 로고
    • Neurotransmitter transporters in the central nervous system
    • Masson J., Sagné C., Hamon M., El Mestikawy S. Neurotransmitter transporters in the central nervous system. Pharmacol. Rev. 51:1999;439-464.
    • (1999) Pharmacol. Rev. , vol.51 , pp. 439-464
    • Masson, J.1    Sagné, C.2    Hamon, M.3    El Mestikawy, S.4
  • 655
    • 0033072841 scopus 로고    scopus 로고
    • Identification of truncated human glutamate transporter
    • Matsumoto Y., Enomoto T., Masuko T. Identification of truncated human glutamate transporter. Tohoku J. Exp. Med. 187:1999;173-182.
    • (1999) Tohoku J. Exp. Med. , vol.187 , pp. 173-182
    • Matsumoto, Y.1    Enomoto, T.2    Masuko, T.3
  • 656
    • 0033998946 scopus 로고    scopus 로고
    • Real-time monitoring of glutamate following fluid percussion brain injury with hypoxia in the rat
    • Matsushita Y., Shima K., Nawashiro H., Wada K. Real-time monitoring of glutamate following fluid percussion brain injury with hypoxia in the rat. J. Neurotrauma. 17:2000;143-153.
    • (2000) J. Neurotrauma , vol.17 , pp. 143-153
    • Matsushita, Y.1    Shima, K.2    Nawashiro, H.3    Wada, K.4
  • 658
    • 0030758647 scopus 로고    scopus 로고
    • Mother's legacy: Mitochondrial DNA mutations and Alzheimer's disease
    • Mattson M.P. Mother's legacy: mitochondrial DNA mutations and Alzheimer's disease. Trends Neurosci. 20:1997;373-375.
    • (1997) Trends Neurosci. , vol.20 , pp. 373-375
    • Mattson, M.P.1
  • 659
    • 0344483869 scopus 로고    scopus 로고
    • Secreted form of amyloid precursor protein enhances basal glucose and glutamate transport and protects against oxidative impairment of glucose and glutamate transport in synaptosomes by a cyclic GMP-mediated mechanism
    • Mattson M.P., Guo Z.H., Geiger J.D. Secreted form of amyloid precursor protein enhances basal glucose and glutamate transport and protects against oxidative impairment of glucose and glutamate transport in synaptosomes by a cyclic GMP-mediated mechanism. J. Neurochem. 73:1999;532-537.
    • (1999) J. Neurochem. , vol.73 , pp. 532-537
    • Mattson, M.P.1    Guo, Z.H.2    Geiger, J.D.3
  • 660
    • 0027291920 scopus 로고
    • Ultrastructural evidence that mercuric chloride lowers the threshold for glutamate neurotoxicity in an organotypic culture of rat cerebellum
    • Matyja E., Albrecht J. Ultrastructural evidence that mercuric chloride lowers the threshold for glutamate neurotoxicity in an organotypic culture of rat cerebellum. Neurosci. Lett. 158:1993;155-158.
    • (1993) Neurosci. Lett. , vol.158 , pp. 155-158
    • Matyja, E.1    Albrecht, J.2
  • 661
    • 0029904205 scopus 로고    scopus 로고
    • Reactive oxygen species involved in the glutamate toxicity of C6 glioma cells via x(c)over-bar antiporter system
    • Mawatari C., Yasui Y., Sugitani K., Takadera T., Kato S. Reactive oxygen species involved in the glutamate toxicity of C6 glioma cells via x(c)over-bar antiporter system. Neuroscience. 73:1996;201-208.
    • (1996) Neuroscience , vol.73 , pp. 201-208
    • Mawatari, C.1    Yasui, Y.2    Sugitani, K.3    Takadera, T.4    Kato, S.5
  • 662
    • 0028927274 scopus 로고
    • Immunoprecipitation, immunoblotting, and immunocytochemistry studies suggest that glutamate receptor delta subunits form novel postsynaptic receptor complexes
    • Mayat E., Petralia R.S., Wang Y.X., Wenthold R.J. Immunoprecipitation, immunoblotting, and immunocytochemistry studies suggest that glutamate receptor delta subunits form novel postsynaptic receptor complexes. J. Neurosci. 15:1995;2533-2546.
    • (1995) J. Neurosci. , vol.15 , pp. 2533-2546
    • Mayat, E.1    Petralia, R.S.2    Wang, Y.X.3    Wenthold, R.J.4
  • 664
    • 0023125256 scopus 로고
    • The physiology of excitatory amino acids in the vertebrate central nervous system
    • Mayer M.L., Westbrook G.L. The physiology of excitatory amino acids in the vertebrate central nervous system. Prog. Neurobiol. 28:1987;197-276.
    • (1987) Prog. Neurobiol. , vol.28 , pp. 197-276
    • Mayer, M.L.1    Westbrook, G.L.2
  • 665
    • 0025002972 scopus 로고
    • Regional variation of extracellular space in the hippocampus
    • McBain C.J., Traynelis S.F., Dingledine R. Regional variation of extracellular space in the hippocampus. Science. 249:1990;674-677.
    • (1990) Science , vol.249 , pp. 674-677
    • McBain, C.J.1    Traynelis, S.F.2    Dingledine, R.3
  • 666
    • 0021924355 scopus 로고
    • Neurotoxicity of L-glutamate and DL-threo-3-hydroxyaspartate in the rat striatum
    • McBean G.J., Roberts P.J. Neurotoxicity of L-glutamate and DL-threo-3-hydroxyaspartate in the rat striatum. J. Neurochem. 44:1985;247-254.
    • (1985) J. Neurochem. , vol.44 , pp. 247-254
    • McBean, G.J.1    Roberts, P.J.2
  • 667
    • 0025257513 scopus 로고
    • Physiological and pathophysiological roles of excitatory amino acids during central nervous system development
    • McDonald J.W., Johnston M.V. Physiological and pathophysiological roles of excitatory amino acids during central nervous system development. Brain Res. Rev. 15:1990;41-70.
    • (1990) Brain Res. Rev. , vol.15 , pp. 41-70
    • McDonald, J.W.1    Johnston, M.V.2
  • 668
    • 0031952612 scopus 로고    scopus 로고
    • Oligodendrocytes from forebrain are highly vulnerable to AMPA/kainate receptor-mediated excitotoxicity
    • McDonald J.W., Althomsons S.P., Hyrc K.L., Choi D.W., Goldberg M.P. Oligodendrocytes from forebrain are highly vulnerable to AMPA/kainate receptor-mediated excitotoxicity. Nat. Med. 4:1998;291-297.
    • (1998) Nat. Med. , vol.4 , pp. 291-297
    • McDonald, J.W.1    Althomsons, S.P.2    Hyrc, K.L.3    Choi, D.W.4    Goldberg, M.P.5
  • 669
    • 0032032683 scopus 로고    scopus 로고
    • Role of glutamate receptor-mediated excitotoxicity in bilirubin-induced brain injury in the Gunn rat model
    • McDonald J.W., Shapiro S.M., Silverstein F.S., Johnston M.V. Role of glutamate receptor-mediated excitotoxicity in bilirubin-induced brain injury in the Gunn rat model. Exp. Neurol. 150:1998;21-29.
    • (1998) Exp. Neurol. , vol.150 , pp. 21-29
    • McDonald, J.W.1    Shapiro, S.M.2    Silverstein, F.S.3    Johnston, M.V.4
  • 670
    • 0023183896 scopus 로고
    • Sodium-dependent glutamate binding in senile dementia
    • McGeer E.G., Singh E.A., McGeer P.L. Sodium-dependent glutamate binding in senile dementia. Neurobiol. Aging. 8:1987;219-223.
    • (1987) Neurobiol. Aging , vol.8 , pp. 219-223
    • McGeer, E.G.1    Singh, E.A.2    McGeer, P.L.3
  • 672
  • 673
    • 0027377278 scopus 로고
    • Novel pharmacologic therapies in the treatment of experimental traumatic brain injury - A review
    • McIntosh T.K. Novel pharmacologic therapies in the treatment of experimental traumatic brain injury - a review. J. Neurotrauma. 10:1993;215-261.
    • (1993) J. Neurotrauma , vol.10 , pp. 215-261
    • McIntosh, T.K.1
  • 674
    • 0031766138 scopus 로고    scopus 로고
    • Novel pharmacologic strategies in the treatment of experimental traumatic brain injury: 1998
    • McIntosh T.K., Juhler M., Wieloch T. Novel pharmacologic strategies in the treatment of experimental traumatic brain injury: 1998. J. Neurotrauma. 15:1998;731-769.
    • (1998) J. Neurotrauma , vol.15 , pp. 731-769
    • McIntosh, T.K.1    Juhler, M.2    Wieloch, T.3
  • 675
    • 0030061356 scopus 로고    scopus 로고
    • Exogenous glutamate concentration regulates the metabolic fate of glutamate in astrocytes
    • McKenna M.C., Sonnewald U., Huang X., Stevenson J., Zielke H.R. Exogenous glutamate concentration regulates the metabolic fate of glutamate in astrocytes. J. Neurochem. 66:1996;386-393.
    • (1996) J. Neurochem. , vol.66 , pp. 386-393
    • McKenna, M.C.1    Sonnewald, U.2    Huang, X.3    Stevenson, J.4    Zielke, H.R.5
  • 676
    • 0034256931 scopus 로고    scopus 로고
    • Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals
    • McKenna M.C., Stevenson J.H., Huang X., Hopkins I.B. Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals. Neurochem. Int. 37:2000;229-241.
    • (2000) Neurochem. Int. , vol.37 , pp. 229-241
    • McKenna, M.C.1    Stevenson, J.H.2    Huang, X.3    Hopkins, I.B.4
  • 677
    • 0017199245 scopus 로고
    • 3H]glutamate in rat brain tissue
    • 3H]glutamate in rat brain tissue. Brain Res. 115:1976;139-144.
    • (1976) Brain Res. , vol.115 , pp. 139-144
    • McLennan, H.1
  • 678
    • 0024374743 scopus 로고
    • Glutamate release from guinea-pig synaptosomes - Stimulation by reuptake-induced depolarization
    • McMahon H.T., Barrie A.P., Lowe M., Nicholls D.G. Glutamate release from guinea-pig synaptosomes - stimulation by reuptake-induced depolarization. J. Neurochem. 53:1989;71-79.
    • (1989) J. Neurochem. , vol.53 , pp. 71-79
    • McMahon, H.T.1    Barrie, A.P.2    Lowe, M.3    Nicholls, D.G.4
  • 679
    • 0027461725 scopus 로고
    • Did radicals strike Lou Gehrig?
    • McNamara J.O., Fridovich I. Did radicals strike Lou Gehrig? Nature. 362:1993;20-21.
    • (1993) Nature , vol.362 , pp. 20-21
    • McNamara, J.O.1    Fridovich, I.2
  • 680
    • 0032401003 scopus 로고    scopus 로고
    • Glutamate transport in cultures from developing avian cerebellum: Presence of GLT-1 immunoreactivity in Purkinje neurons
    • Meaney J.A., Balcar V.J., Rothstein J.D., Jeffrey P.L. Glutamate transport in cultures from developing avian cerebellum: presence of GLT-1 immunoreactivity in Purkinje neurons. J. Neurosci. Res. 54:1998;595-603.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 595-603
    • Meaney, J.A.1    Balcar, V.J.2    Rothstein, J.D.3    Jeffrey, P.L.4
  • 681
  • 682
    • 0027165858 scopus 로고
    • Amino acids as dietary excitotoxins - A contribution to understanding neurodegenerative disorders
    • Meldrum B. Amino acids as dietary excitotoxins - a contribution to understanding neurodegenerative disorders. Brain Res. Rev. 18:1993;293-314.
    • (1993) Brain Res. Rev. , vol.18 , pp. 293-314
    • Meldrum, B.1
  • 683
    • 0028535070 scopus 로고
    • The role of glutamate in epilepsy and other CNS disorders
    • Meldrum B.S. The role of glutamate in epilepsy and other CNS disorders. Neurology. 44:1994;S14-S23.
    • (1994) Neurology , vol.44 , pp. 14-S23
    • Meldrum, B.S.1
  • 684
    • 0025063609 scopus 로고
    • Excitatory amino acid neurotoxicity and neurodegenerative disease
    • Meldrum B., Garthwaite J. Excitatory amino acid neurotoxicity and neurodegenerative disease. Trends Pharmacol. Sci. 11:1990;379-387.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 379-387
    • Meldrum, B.1    Garthwaite, J.2
  • 685
    • 0033568870 scopus 로고    scopus 로고
    • Membrane trafficking regulates the activity of the human dopamine transporter
    • Melikian H.E., Buckley K.M. Membrane trafficking regulates the activity of the human dopamine transporter. J. Neurosci. 19:1999;7699-7710.
    • (1999) J. Neurosci. , vol.19 , pp. 7699-7710
    • Melikian, H.E.1    Buckley, K.M.2
  • 686
    • 0021912735 scopus 로고
    • Cations differentially affect subpopulations of L-glutamate receptors in rat synaptic plasma membranes
    • Mena E.E., Monaghan D.T., Whittemore S.R., Cotman C.W. Cations differentially affect subpopulations of L-glutamate receptors in rat synaptic plasma membranes. Brain Res. 329:1985;319-322.
    • (1985) Brain Res. , vol.329 , pp. 319-322
    • Mena, E.E.1    Monaghan, D.T.2    Whittemore, S.R.3    Cotman, C.W.4
  • 687
    • 0028349645 scopus 로고
    • Glial contributions to excitatory neurotransmission in cultured hippocampal cells
    • Mennerick S., Zorumski C.F. Glial contributions to excitatory neurotransmission in cultured hippocampal cells. Nature. 368:1994;59-62.
    • (1994) Nature , vol.368 , pp. 59-62
    • Mennerick, S.1    Zorumski, C.F.2
  • 688
    • 0028903332 scopus 로고
    • Presynaptic influence on the time course of fast excitatory synaptic currents in cultured hippocampal cells
    • Mennerick S., Zorumski C.F. Presynaptic influence on the time course of fast excitatory synaptic currents in cultured hippocampal cells. J. Neurosci. 15:1995;3178-3192.
    • (1995) J. Neurosci. , vol.15 , pp. 3178-3192
    • Mennerick, S.1    Zorumski, C.F.2
  • 689
    • 0031718931 scopus 로고    scopus 로고
    • Measurement of glial transport currents in microcultures: Application to excitatory neurotransmission
    • Mennerick S., Zorumski C.F. Measurement of glial transport currents in microcultures: application to excitatory neurotransmission. Methods Enzymol. 296:1998;632-645.
    • (1998) Methods Enzymol. , vol.296 , pp. 632-645
    • Mennerick, S.1    Zorumski, C.F.2
  • 690
    • 0030033083 scopus 로고    scopus 로고
    • Components of glial responses to exogenous and synaptic glutamate in rat hippocampal microcultures
    • Mennerick S., Benz A., Zorumski C.F. Components of glial responses to exogenous and synaptic glutamate in rat hippocampal microcultures. J. Neurosci. 16:1996;55-64.
    • (1996) J. Neurosci. , vol.16 , pp. 55-64
    • Mennerick, S.1    Benz, A.2    Zorumski, C.F.3
  • 693
    • 0029019529 scopus 로고
    • Studies of the coding region of the neuronal glutamate transporter gene in amyotrophic lateral sclerosis
    • Meyer T., Lenk U., Küther G., Weindl A., Speer A., Ludolph A.C. Studies of the coding region of the neuronal glutamate transporter gene in amyotrophic lateral sclerosis. Ann. Neurol. 37:1995;817-839.
    • (1995) Ann. Neurol. , vol.37 , pp. 817-839
    • Meyer, T.1    Lenk, U.2    Küther, G.3    Weindl, A.4    Speer, A.5    Ludolph, A.C.6
  • 694
    • 0030889711 scopus 로고    scopus 로고
    • Genomic organization of the human excitatory amino acid transporter gene GLT-1
    • Meyer T., Ludolph A.C., Morkel M., Hagemeier C., Speer A. Genomic organization of the human excitatory amino acid transporter gene GLT-1. Neuroreport. 8:1997;775-777.
    • (1997) Neuroreport , vol.8 , pp. 775-777
    • Meyer, T.1    Ludolph, A.C.2    Morkel, M.3    Hagemeier, C.4    Speer, A.5
  • 696
    • 0031755870 scopus 로고    scopus 로고
    • The EAAT2 (GLT-1) gene in motor neuron disease: Absence of mutations in amyotrophic lateral sclerosis and a point mutation in patients with hereditary spastic paraplegia
    • Meyer T., Münch C., Völkel H., Booms P., Ludolph A.C. The EAAT2 (GLT-1) gene in motor neuron disease: absence of mutations in amyotrophic lateral sclerosis and a point mutation in patients with hereditary spastic paraplegia. J. Neurol. Neurosurg. Psychiatry. 65:1998;594-596.
    • (1998) J. Neurol. Neurosurg. Psychiatry , vol.65 , pp. 594-596
    • Meyer, T.1    Münch, C.2    Völkel, H.3    Booms, P.4    Ludolph, A.C.5
  • 699
    • 0033432654 scopus 로고    scopus 로고
    • Neuropharmacologic aspects of apoptosis: Significance for neurodegenerative diseases
    • Michel P.P., Lambeng N., Ruberg M. Neuropharmacologic aspects of apoptosis: significance for neurodegenerative diseases. Clin. Neuropharmacol. 22:1999;137-150.
    • (1999) Clin. Neuropharmacol. , vol.22 , pp. 137-150
    • Michel, P.P.1    Lambeng, N.2    Ruberg, M.3
  • 700
    • 0030939042 scopus 로고    scopus 로고
    • Alterations in glutamate transporter protein levels in kindling-induced epilepsy
    • Miller H.P., Levey A.I., Rothstein J.D., Tzingounis A.V., Conn P.J. Alterations in glutamate transporter protein levels in kindling-induced epilepsy. J. Neurochem. 68:1997;1564-1570.
    • (1997) J. Neurochem. , vol.68 , pp. 1564-1570
    • Miller, H.P.1    Levey, A.I.2    Rothstein, J.D.3    Tzingounis, A.V.4    Conn, P.J.5
  • 701
    • 0027586243 scopus 로고
    • Induction of astrocyte glutamine synthetase activity by the Lathyrus toxin beta-N-oxalyl-L-alfa,beta-diaminoproprionic acid (beta-L-ODAP)
    • Miller S., Nunn P.B., Bridges R.J. Induction of astrocyte glutamine synthetase activity by the Lathyrus toxin beta-N-oxalyl-L-alfa,beta-diaminoproprionic acid (beta-L-ODAP). Glia. 7:1993;329-336.
    • (1993) Glia , vol.7 , pp. 329-336
    • Miller, S.1    Nunn, P.B.2    Bridges, R.J.3
  • 703
    • 0032168174 scopus 로고    scopus 로고
    • Activation of AMPA, kainate, and metabotropic receptors at hippocampal mossy fiber synapses: Role of glutamate diffusion
    • Min M.Y., Rusakov D.A., Kullmann D.M. Activation of AMPA, kainate, and metabotropic receptors at hippocampal mossy fiber synapses: role of glutamate diffusion. Neuron. 21:1998;561-570.
    • (1998) Neuron , vol.21 , pp. 561-570
    • Min, M.Y.1    Rusakov, D.A.2    Kullmann, D.M.3
  • 704
    • 0029133369 scopus 로고
    • The expression of two splice variants of metabotropic glutamate receptor subtype 5 in the rat brain and neuronal cells during development
    • Minakami R., Iida K., Hirakawa N., Sugiyama H. The expression of two splice variants of metabotropic glutamate receptor subtype 5 in the rat brain and neuronal cells during development. J. Neurochem. 65:1995;1536-1542.
    • (1995) J. Neurochem. , vol.65 , pp. 1536-1542
    • Minakami, R.1    Iida, K.2    Hirakawa, N.3    Sugiyama, H.4
  • 705
    • 0017553878 scopus 로고
    • Kinetic study of glutamate transport in rat brain mitochondria
    • Minn A., Gayet T. Kinetic study of glutamate transport in rat brain mitochondria. J. Neurochem. 29:1977;873-881.
    • (1977) J. Neurochem. , vol.29 , pp. 873-881
    • Minn, A.1    Gayet, T.2
  • 706
    • 0034732122 scopus 로고    scopus 로고
    • Glutamate spillover suppresses inhibition by activating presynaptic mGluRs
    • Mitchell S.J., Silver R.A. Glutamate spillover suppresses inhibition by activating presynaptic mGluRs. Nature. 404:2000;498-502.
    • (2000) Nature , vol.404 , pp. 498-502
    • Mitchell, S.J.1    Silver, R.A.2
  • 707
    • 0032511029 scopus 로고    scopus 로고
    • Identification of functional domains of the human glutamate transporters EAAT1 and EAAT2
    • Mitrovic A.D., Amara S.G., Johnston G.A.R., Vandenberg R.J. Identification of functional domains of the human glutamate transporters EAAT1 and EAAT2. J. Biol. Chem. 273:1998;14698-14706.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14698-14706
    • Mitrovic, A.D.1    Amara, S.G.2    Johnston, G.A.R.3    Vandenberg, R.J.4
  • 708
    • 0033051857 scopus 로고    scopus 로고
    • Influence of the oestrous cycle on L-glutamate and L-aspartate transport in rat brain synaptosomes
    • Mitrovic A.D., Maddison J.E., Johnston G.A.R. Influence of the oestrous cycle on L-glutamate and L-aspartate transport in rat brain synaptosomes. Neurochem. Int. 34:1999;101-108.
    • (1999) Neurochem. Int. , vol.34 , pp. 101-108
    • Mitrovic, A.D.1    Maddison, J.E.2    Johnston, G.A.R.3
  • 709
    • 0026605725 scopus 로고
    • Cystine uptake and glutathione level in endothelial cells exposed to oxidative stress
    • Miura K., Ishii T., Sugita Y., Bannai S. Cystine uptake and glutathione level in endothelial cells exposed to oxidative stress. Am. J. Physiol. 262:1992;C50-C58.
    • (1992) Am. J. Physiol. , vol.262 , pp. 50-C58
    • Miura, K.1    Ishii, T.2    Sugita, Y.3    Bannai, S.4
  • 710
    • 0030952381 scopus 로고    scopus 로고
    • Increase of glutamate uptake in astrocytes: A possible mechanism of action of volatile anesthetics
    • Miyazaki H., Nakamura Y., Arai T., Kataoka K. Increase of glutamate uptake in astrocytes: a possible mechanism of action of volatile anesthetics. Anesthesiology. 86:1997;1359-1366.
    • (1997) Anesthesiology , vol.86 , pp. 1359-1366
    • Miyazaki, H.1    Nakamura, Y.2    Arai, T.3    Kataoka, K.4
  • 711
    • 0028796853 scopus 로고
    • Placental amino acid transport
    • Moe A.J. Placental amino acid transport. Am. J. Physiol. 37:1995;C1321-C1331.
    • (1995) Am. J. Physiol. , vol.37 , pp. 1321-C1331
    • Moe, A.J.1
  • 712
    • 0024760404 scopus 로고
    • Anionic amino acid uptake by microvillous membrane vesicles from human placenta
    • Moe A.J., Smith C.H. Anionic amino acid uptake by microvillous membrane vesicles from human placenta. Am. J. Physiol. 257:1989;C1005-C1011.
    • (1989) Am. J. Physiol. , vol.257 , pp. 1005-C1011
    • Moe, A.J.1    Smith, C.H.2
  • 713
    • 0027231058 scopus 로고
    • Stress preferentially increases extraneuronal levels of excitatory amino acids in the prefrontal cortex: Comparison to hippocampus and basal ganglia
    • Moghaddam B. Stress preferentially increases extraneuronal levels of excitatory amino acids in the prefrontal cortex: comparison to hippocampus and basal ganglia. J. Neurochem. 60:1993;1650-1657.
    • (1993) J. Neurochem. , vol.60 , pp. 1650-1657
    • Moghaddam, B.1
  • 714
    • 0028027113 scopus 로고
    • Glucocorticoids mediate the stress-induced extracellular accumulation of glutamate
    • Moghaddam B., Bolinao M.L., Steinbehrens B., Sapolsky R. Glucocorticoids mediate the stress-induced extracellular accumulation of glutamate. Brain Res. 655:1994;251-254.
    • (1994) Brain Res. , vol.655 , pp. 251-254
    • Moghaddam, B.1    Bolinao, M.L.2    Steinbehrens, B.3    Sapolsky, R.4
  • 715
    • 0029116537 scopus 로고
    • Identification of functional ionotropic glutamate receptor proteins in pancreatic beta-cells and in islets of Langerhans
    • Molnár E., Varadi A., McIlhinney R.A.J., Ashcroft S.J.H. Identification of functional ionotropic glutamate receptor proteins in pancreatic beta-cells and in islets of Langerhans. FEBS Lett. 371:1995;253-257.
    • (1995) FEBS Lett. , vol.371 , pp. 253-257
    • Molnár, E.1    Varadi, A.2    McIlhinney, R.A.J.3    Ashcroft, S.J.H.4
  • 716
    • 0024596865 scopus 로고
    • The excitatory amino acid receptors: Their classes, pharmacology, and distinct properties in the function of the central nervous system
    • Monaghan D.T., Bridges R.J., Cotman C.W. The excitatory amino acid receptors: their classes, pharmacology, and distinct properties in the function of the central nervous system. Annu. Rev. Pharmacol. Toxicol. 29:1989;365-402.
    • (1989) Annu. Rev. Pharmacol. Toxicol. , vol.29 , pp. 365-402
    • Monaghan, D.T.1    Bridges, R.J.2    Cotman, C.W.3
  • 717
    • 0028810883 scopus 로고
    • Structure and function of the NMDA receptor channel
    • Mori H., Mishina M. Structure and function of the NMDA receptor channel. Neuropharmacology. 34:1995;1219-1237.
    • (1995) Neuropharmacology , vol.34 , pp. 1219-1237
    • Mori, H.1    Mishina, M.2
  • 718
    • 0032400783 scopus 로고    scopus 로고
    • Attenuation of focal ischemic brain injury in mice deficient in the epsilon 1 (NR2a) subunit of NMDA receptor
    • Morikawa E., Mori H., Kiyama Y., Mishina M., Asano T., Kirino T. Attenuation of focal ischemic brain injury in mice deficient in the epsilon 1 (NR2a) subunit of NMDA receptor. J. Neurosci. 18:1998;9727-9732.
    • (1998) J. Neurosci. , vol.18 , pp. 9727-9732
    • Morikawa, E.1    Mori, H.2    Kiyama, Y.3    Mishina, M.4    Asano, T.5    Kirino, T.6
  • 719
    • 0029020844 scopus 로고
    • Microvesicles isolated from bovine pineal gland specifically accumulate L-glutamate
    • Moriyama Y., Yamamoto A. Microvesicles isolated from bovine pineal gland specifically accumulate L-glutamate. FEBS Lett. 367:1995;233-236.
    • (1995) FEBS Lett. , vol.367 , pp. 233-236
    • Moriyama, Y.1    Yamamoto, A.2
  • 721
    • 0033981087 scopus 로고    scopus 로고
    • Synaptic-like microvesicles, synaptic vesicle counterparts in endocrine cells, are involved in a novel regulatory mechanism for the synthesis and secretion of hormones
    • Moriyama Y., Hayashi M., Yamada H., Yatsushiro S., Ishio S., Yamamoto A. Synaptic-like microvesicles, synaptic vesicle counterparts in endocrine cells, are involved in a novel regulatory mechanism for the synthesis and secretion of hormones. J. Exp. Biol. 203:2000;117-125.
    • (2000) J. Exp. Biol. , vol.203 , pp. 117-125
    • Moriyama, Y.1    Hayashi, M.2    Yamada, H.3    Yatsushiro, S.4    Ishio, S.5    Yamamoto, A.6
  • 722
    • 0034046898 scopus 로고    scopus 로고
    • Pharmacological and molecular characterization of glutamate receptors in the MIN6 pancreatic beta-cell line
    • Morley P., Maclean S., Gendron T.F., Small D.L., Tremblay R., Durkin J.P., Mealing G. Pharmacological and molecular characterization of glutamate receptors in the MIN6 pancreatic beta-cell line. Neurol. Res. 22:2000;379-385.
    • (2000) Neurol. Res. , vol.22 , pp. 379-385
    • Morley, P.1    Maclean, S.2    Gendron, T.F.3    Small, D.L.4    Tremblay, R.5    Durkin, J.P.6    Mealing, G.7
  • 723
    • 0032908774 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: A putative mechanism of degeneration
    • Morrison B.M., Morrison J.H. Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: a putative mechanism of degeneration. Brain Res. Rev. 29:1999;121-135.
    • (1999) Brain Res. Rev. , vol.29 , pp. 121-135
    • Morrison, B.M.1    Morrison, J.H.2
  • 724
    • 0034905891 scopus 로고    scopus 로고
    • The effect of ammonia on glutamate transport in glial cells isolated from the salamander retina
    • in press
    • Mort, D., Marcaggi, P., Grant, J., Attwell, D., 2001. The effect of ammonia on glutamate transport in glial cells isolated from the salamander retina. J. Neurophysiol., in press.
    • (2001) J. Neurophysiol.
    • Mort, D.1    Marcaggi, P.2    Grant, J.3    Attwell, D.4
  • 725
    • 0030973404 scopus 로고    scopus 로고
    • The unipolar brush cells of the mammalian cerebellum and cochlear nucleus: Cytology and microcircuitry
    • Mugnaini E., Dino M.R., Jaarsma D. The unipolar brush cells of the mammalian cerebellum and cochlear nucleus: cytology and microcircuitry. Prog. Brain Res. 114:1997;131-150.
    • (1997) Prog. Brain Res. , vol.114 , pp. 131-150
    • Mugnaini, E.1    Dino, M.R.2    Jaarsma, D.3
  • 726
    • 0029060825 scopus 로고
    • Molecular cloning of two glutamate transporter subtypes from mouse brain
    • Mukainaka Y., Tanaka K., Hagiwara T., Wada K. Molecular cloning of two glutamate transporter subtypes from mouse brain. Biochim. Biophys. Acta. 1244:1995;233-237.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 233-237
    • Mukainaka, Y.1    Tanaka, K.2    Hagiwara, T.3    Wada, K.4
  • 727
    • 0027448568 scopus 로고
    • Stimulation of D-aspartate efflux by mercuric chloride from rat primary astrocyte cultures
    • Mullaney K.J., Vitarella D., Albrecht J., Kimelberg H.K., Aschner M. Stimulation of D-aspartate efflux by mercuric chloride from rat primary astrocyte cultures. Dev. Brain Res. 75:1993;261-268.
    • (1993) Dev. Brain Res. , vol.75 , pp. 261-268
    • Mullaney, K.J.1    Vitarella, D.2    Albrecht, J.3    Kimelberg, H.K.4    Aschner, M.5
  • 728
    • 0032033864 scopus 로고    scopus 로고
    • Free radicals and glutamate uptake in the retina
    • Muller A., Maurin L., Bonne C. Free radicals and glutamate uptake in the retina. Gen. Pharmacol. 30:1998;315-318.
    • (1998) Gen. Pharmacol. , vol.30 , pp. 315-318
    • Muller, A.1    Maurin, L.2    Bonne, C.3
  • 731
    • 0023087077 scopus 로고
    • Effects of dihydrokainic acid on extracellular amino acids and neuronal excitability in the in vivo rat hippocampus
    • Munoz M.D., Herreras O., Herranz A.S., Solis J.M., Martin del Rio R., Lerma J. Effects of dihydrokainic acid on extracellular amino acids and neuronal excitability in the in vivo rat hippocampus. Neuropharmacology. 26:1987;1-8.
    • (1987) Neuropharmacology , vol.26 , pp. 1-8
    • Munoz, M.D.1    Herreras, O.2    Herranz, A.S.3    Solis, J.M.4    Martin Del Rio, R.5    Lerma, J.6
  • 732
    • 0032833772 scopus 로고    scopus 로고
    • Parkinsonism-dementia complex on Guam - Overview of clinical aspects
    • Murakami N. Parkinsonism-dementia complex on Guam - overview of clinical aspects. J. Neurol. 246:1999;16-18.
    • (1999) J. Neurol. , vol.246 , pp. 16-18
    • Murakami, N.1
  • 733
    • 0024678458 scopus 로고
    • Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress
    • Murphy T.H., Miyamoto M., Sastre A., Schnaar R.L., Coyle J.T. Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress. Neuron. 2:1989;1547-1558.
    • (1989) Neuron , vol.2 , pp. 1547-1558
    • Murphy, T.H.1    Miyamoto, M.2    Sastre, A.3    Schnaar, R.L.4    Coyle, J.T.5
  • 734
    • 0025355933 scopus 로고
    • Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake
    • Murphy T.H., Schnaar R.L., Coyle J.T. Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake. FASEB J. 4:1990;1624-1633.
    • (1990) FASEB J. , vol.4 , pp. 1624-1633
    • Murphy, T.H.1    Schnaar, R.L.2    Coyle, J.T.3
  • 735
    • 0034728677 scopus 로고    scopus 로고
    • Alternative splicing of the NMDAR1 glutamate receptor subunit in human temporal lobe epilepsy
    • Musshoff, U., Schünke, U., Köhling, R., Speckmann, E.J., 2000. Alternative splicing of the NMDAR1 glutamate receptor subunit in human temporal lobe epilepsy. Molecular Brain Research 76, 377-384.
    • (2000) Molecular Brain Research , vol.76 , pp. 377-384
    • Musshoff, U.1    Schünke, U.2    Köhling, R.3    Speckmann, E.J.4
  • 736
    • 0345267170 scopus 로고    scopus 로고
    • Adverse psychological impact, glutamatergic dysfunction, and risk factors for Alzheimer's disease
    • Myhrer T. Adverse psychological impact, glutamatergic dysfunction, and risk factors for Alzheimer's disease. Neurosci. Biobehav. Rev. 23:1998;131-139.
    • (1998) Neurosci. Biobehav. Rev. , vol.23 , pp. 131-139
    • Myhrer, T.1
  • 737
    • 0032549709 scopus 로고    scopus 로고
    • Identification of alternative splicing forms of GLT-1 mRNA in the spinal cord of amyotrophic lateral sclerosis patients
    • Nagai M., Abe K., Okamoto K., Itoyama Y. Identification of alternative splicing forms of GLT-1 mRNA in the spinal cord of amyotrophic lateral sclerosis patients. Neurosci. Lett. 244:1998;165-168.
    • (1998) Neurosci. Lett. , vol.244 , pp. 165-168
    • Nagai, M.1    Abe, K.2    Okamoto, K.3    Itoyama, Y.4
  • 738
    • 0032498946 scopus 로고    scopus 로고
    • 3H]gamma-aminobutyric acid, in taste buds of the mudpuppy, Necturus maculosus
    • 3H]gamma-aminobutyric acid, in taste buds of the mudpuppy, Necturus maculosus. J. Comp. Neurol. 392:1998;199-208.
    • (1998) J. Comp. Neurol. , vol.392 , pp. 199-208
    • Nagai, T.1    Delay, R.J.2    Welton, J.3    Roper, S.D.4
  • 739
    • 0030993144 scopus 로고    scopus 로고
    • EAAT4, a glutamate transporter with properties of a chloride channel, is predominantly localized in Purkinje cell dendrites, and forms parasagittal compartments in rat cerebellum
    • Nagao S., Kwak S., Kanazawa I. EAAT4, a glutamate transporter with properties of a chloride channel, is predominantly localized in Purkinje cell dendrites, and forms parasagittal compartments in rat cerebellum. Neuroscience. 78:1997;929-933.
    • (1997) Neuroscience , vol.78 , pp. 929-933
    • Nagao, S.1    Kwak, S.2    Kanazawa, I.3
  • 740
    • 0029852988 scopus 로고    scopus 로고
    • Mercuric chloride uncouples glutamate uptake from the countertransport of hydroxyl equivalents
    • Nagaraja T.N., Brookes N. Mercuric chloride uncouples glutamate uptake from the countertransport of hydroxyl equivalents. Am. J. Physiol. 40:1996;C1487-C1493.
    • (1996) Am. J. Physiol. , vol.40 , pp. 1487-C1493
    • Nagaraja, T.N.1    Brookes, N.2
  • 741
    • 0020691267 scopus 로고
    • Adenosine triphosphate-dependent uptake of glutamate into protein I-associated synaptic vesicles
    • Naito S., Ueda T. Adenosine triphosphate-dependent uptake of glutamate into protein I-associated synaptic vesicles. J. Biol. Chem. 258:1983;696-699.
    • (1983) J. Biol. Chem. , vol.258 , pp. 696-699
    • Naito, S.1    Ueda, T.2
  • 742
    • 0021965984 scopus 로고
    • Characterization of glutamate uptake into synaptic vesicles
    • Naito S., Ueda T. Characterization of glutamate uptake into synaptic vesicles. J. Neurochem. 44:1985;99-109.
    • (1985) J. Neurochem. , vol.44 , pp. 99-109
    • Naito, S.1    Ueda, T.2
  • 743
    • 0027216795 scopus 로고
    • (2s,3s,4r)-2-(carboxycyclopropyl)glycine, a potent and competitive inhibitor of both glial and neuronal uptake of glutamate
    • Nakamura Y., Kataoka K., Ishida M., Shinozaki H. (2s,3s,4r)-2-(carboxycyclopropyl)glycine, a potent and competitive inhibitor of both glial and neuronal uptake of glutamate. Neuropharmacology. 32:1993;833-837.
    • (1993) Neuropharmacology , vol.32 , pp. 833-837
    • Nakamura, Y.1    Kataoka, K.2    Ishida, M.3    Shinozaki, H.4
  • 744
    • 0027669806 scopus 로고
    • Glial plasmalemmal vesicles: A subcellular fraction from rat hippocampal homogenate distinct from synaptosomes
    • Nakamura Y., Iga K., Shibata T., Shudo M., Kataoka K. Glial plasmalemmal vesicles: a subcellular fraction from rat hippocampal homogenate distinct from synaptosomes. Glia. 9:1993;48-56.
    • (1993) Glia , vol.9 , pp. 48-56
    • Nakamura, Y.1    Iga, K.2    Shibata, T.3    Shudo, M.4    Kataoka, K.5
  • 746
    • 0030027044 scopus 로고    scopus 로고
    • Expression of three glutamate transporter subtype mRNAs in human brain regions and peripheral tissues
    • Nakayama T., Kawakami H., Tanaka K., Nakamura S. Expression of three glutamate transporter subtype mRNAs in human brain regions and peripheral tissues. Mol. Brain Res. 36:1996;189-192.
    • (1996) Mol. Brain Res. , vol.36 , pp. 189-192
    • Nakayama, T.1    Kawakami, H.2    Tanaka, K.3    Nakamura, S.4
  • 747
    • 0028281952 scopus 로고
    • Longitudinal analysis of amyotrophic lateral sclerosis mortality in Norway, 1966-1989 - Evidence for a susceptible subpopulation
    • Neilson S., Robinson I., Nymoen E.H. Longitudinal analysis of amyotrophic lateral sclerosis mortality in Norway, 1966-1989 - evidence for a susceptible subpopulation. J. Neurol. Sci. 122:1994;148-154.
    • (1994) J. Neurol. Sci. , vol.122 , pp. 148-154
    • Neilson, S.1    Robinson, I.2    Nymoen, E.H.3
  • 748
    • 0031753789 scopus 로고    scopus 로고
    • - neurotransmitter transporters
    • - neurotransmitter transporters. J. Neurochem. 71:1998;1785-1803.
    • (1998) J. Neurochem. , vol.71 , pp. 1785-1803
    • Nelson, N.1
  • 749
    • 0029057338 scopus 로고
    • Neurotransmitter and neuromodulatory mechanisms involved in alcohol abuse and alcoholism
    • Nevo I., Hamon M. Neurotransmitter and neuromodulatory mechanisms involved in alcohol abuse and alcoholism. Neurochem. Int. 26:1995;305-336.
    • (1995) Neurochem. Int. , vol.26 , pp. 305-336
    • Nevo, I.1    Hamon, M.2
  • 750
    • 0030893024 scopus 로고    scopus 로고
    • Increased production of extracellular glutamate by the mitochondrial glutaminase following neuronal death
    • Newcomb R., Sun X.Y., Taylor L., Curthoys N., Giffard R.G. Increased production of extracellular glutamate by the mitochondrial glutaminase following neuronal death. J. Biol. Chem. 272:1997;11276-11282.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11276-11282
    • Newcomb, R.1    Sun, X.Y.2    Taylor, L.3    Curthoys, N.4    Giffard, R.G.5
  • 753
    • 0027418419 scopus 로고
    • The glutamatergic nerve terminal
    • Nicholls D.G. The glutamatergic nerve terminal. Eur. J. Biochem. 212:1993;613-631.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 613-631
    • Nicholls, D.G.1
  • 754
    • 0012118616 scopus 로고    scopus 로고
    • Protein kinase C and synaptic transmission
    • In: Parker, P.J., Dekker, L.V. (Eds.) R.G. Landes Company
    • Nicholls, D.G., 1997. Protein kinase C and synaptic transmission. In: Parker, P.J., Dekker, L.V. (Eds.), Protein Kinase C. R.G. Landes Company, pp. 167-178.
    • (1997) Protein Kinase C , pp. 167-178
    • Nicholls, D.G.1
  • 755
    • 0025052336 scopus 로고
    • The release and uptake of excitatory amino acids
    • Nicholls D., Attwell D. The release and uptake of excitatory amino acids. Trends Pharmacol. Sci. 11:1990;462-468.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 462-468
    • Nicholls, D.1    Attwell, D.2
  • 756
    • 0032504708 scopus 로고    scopus 로고
    • Mitochondria and neuronal glutamate excitotoxicity
    • Nicholls D.G., Budd S.L. Mitochondria and neuronal glutamate excitotoxicity. Biochim. Biophys. Acta. 1366:1998;97-112.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 97-112
    • Nicholls, D.G.1    Budd, S.L.2
  • 757
    • 0029842263 scopus 로고    scopus 로고
    • Induction of high affinity glutamate transport activity by amino acid deprivation is dependent on cellular glutamate concentrations in renal epithelial cells does not involve an increase in the amount of transporter protein
    • Nicholson B., McGivan J.D. Induction of high affinity glutamate transport activity by amino acid deprivation is dependent on cellular glutamate concentrations in renal epithelial cells does not involve an increase in the amount of transporter protein. Biochem. Soc. Trans. 24:1996;S481.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 481
    • Nicholson, B.1    McGivan, J.D.2
  • 758
    • 0032079334 scopus 로고    scopus 로고
    • Extracellular space structure revealed by diffusion analysis
    • Nicholson C., Syková E. Extracellular space structure revealed by diffusion analysis. Trends Neurosci. 21:1998;207-215.
    • (1998) Trends Neurosci. , vol.21 , pp. 207-215
    • Nicholson, C.1    Syková, E.2
  • 759
    • 0028033893 scopus 로고
    • 3H]glutamate into rat cerebrocortical and cerebellar synaptosomes. Effects of anaesthetic agents
    • 3H]glutamate into rat cerebrocortical and cerebellar synaptosomes. Effects of anaesthetic agents. Biochem. Soc. Trans. 22:1994;S410.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 410
    • Nicol, B.1    Rowbotham, D.J.2    Lambert, D.G.3
  • 760
    • 0029019186 scopus 로고
    • Glutamate uptake is not a major target site for anaesthetic agents
    • Nicol B., Rowbotham D.J., Lambert D.G. Glutamate uptake is not a major target site for anaesthetic agents. Br. J. Anaesth. 75:1995;61-65.
    • (1995) Br. J. Anaesth. , vol.75 , pp. 61-65
    • Nicol, B.1    Rowbotham, D.J.2    Lambert, D.G.3
  • 761
    • 0021071836 scopus 로고
    • Presynaptic dopaminergic control of high affinity glutamate uptake in the striatum
    • Nieoullon A., Kerkerian L., Dusticier N. Presynaptic dopaminergic control of high affinity glutamate uptake in the striatum. Neurosci. Lett. 43:1983;191-196.
    • (1983) Neurosci. Lett. , vol.43 , pp. 191-196
    • Nieoullon, A.1    Kerkerian, L.2    Dusticier, N.3
  • 762
    • 0026442514 scopus 로고
    • A procedure for large-scale purification of domoic acid from toxic blue mussels (Mytilus-edulis)
    • Nijjar M.S., MacKenzie P.M., Brown J.A. A procedure for large-scale purification of domoic acid from toxic blue mussels (Mytilus-edulis). Mol. Cell. Biochem. 115:1992;213-217.
    • (1992) Mol. Cell. Biochem. , vol.115 , pp. 213-217
    • Nijjar, M.S.1    MacKenzie, P.M.2    Brown, J.A.3
  • 763
    • 0025182940 scopus 로고
    • Changes in cortical extracellular levels of energy-related metabolites and amino acids following concussive brain injury in rats
    • Nilsson P., Hillered L., Ponten U., Ungerstedt U. Changes in cortical extracellular levels of energy-related metabolites and amino acids following concussive brain injury in rats. J. Cereb. Blood Flow Metab. 10:1990;631-637.
    • (1990) J. Cereb. Blood Flow Metab. , vol.10 , pp. 631-637
    • Nilsson, P.1    Hillered, L.2    Ponten, U.3    Ungerstedt, U.4
  • 764
    • 0027023998 scopus 로고
    • Purification and characterization of an astrocyte GABA-carrier inducing protein (GABA-CIP) released from cerebellar granule cells in culture
    • Nissen J., Schousboe A., Halkier T., Schousboe I. Purification and characterization of an astrocyte GABA-carrier inducing protein (GABA-CIP) released from cerebellar granule cells in culture. Glia. 6:1992;236-243.
    • (1992) Glia , vol.6 , pp. 236-243
    • Nissen, J.1    Schousboe, A.2    Halkier, T.3    Schousboe, I.4
  • 765
    • 0031238547 scopus 로고    scopus 로고
    • The glial glutamate transporter in hyperammonemia and hepatic encephalopathy: Relation to energy metabolism and glutamatergic neurotransmission
    • Norenberg M.D., Huo Z.F., Neary J.T., Roigcantesano A. The glial glutamate transporter in hyperammonemia and hepatic encephalopathy: relation to energy metabolism and glutamatergic neurotransmission. Glia. 21:1997;124-133.
    • (1997) Glia , vol.21 , pp. 124-133
    • Norenberg, M.D.1    Huo, Z.F.2    Neary, J.T.3    Roigcantesano, A.4
  • 766
    • 0032144778 scopus 로고    scopus 로고
    • Regional and cellular expression of glial (GLT1) and neuronal (EAAC1) glutamate transporter proteins in ovine fetal brain
    • Northington F.J., Traystman R.J., Koehler R.C., Rothstein J.D., Martin L.J. Regional and cellular expression of glial (GLT1) and neuronal (EAAC1) glutamate transporter proteins in ovine fetal brain. Neuroscience. 85:1998;1183-1193.
    • (1998) Neuroscience , vol.85 , pp. 1183-1193
    • Northington, F.J.1    Traystman, R.J.2    Koehler, R.C.3    Rothstein, J.D.4    Martin, L.J.5
  • 767
    • 0033564453 scopus 로고    scopus 로고
    • GLT1, glial glutamate transporter, is transiently expressed in neurons and develops astrocyte specificity only after midgestation in the ovine fetal brain
    • Northington F.J., Traystman R.J., Koehler R.C., Martin L.J. GLT1, glial glutamate transporter, is transiently expressed in neurons and develops astrocyte specificity only after midgestation in the ovine fetal brain. J. Neurobiol. 39:1999;515-526.
    • (1999) J. Neurobiol. , vol.39 , pp. 515-526
    • Northington, F.J.1    Traystman, R.J.2    Koehler, R.C.3    Martin, L.J.4
  • 768
    • 0022887764 scopus 로고
    • Differential sensitivity of neural cells to bilirubin toxicity
    • Notter M.F.D., Kendig J.W. Differential sensitivity of neural cells to bilirubin toxicity. Exp. Neurol. 94:1986;670-682.
    • (1986) Exp. Neurol. , vol.94 , pp. 670-682
    • Notter, M.F.D.1    Kendig, J.W.2
  • 769
    • 0023895734 scopus 로고
    • Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced
    • Novelli A., Reilly J.A., Lysko P.G., Henneberry R.C. Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced. Brain Res. 451:1988;205-212.
    • (1988) Brain Res. , vol.451 , pp. 205-212
    • Novelli, A.1    Reilly, J.A.2    Lysko, P.G.3    Henneberry, R.C.4
  • 770
    • 0034064724 scopus 로고    scopus 로고
    • Differential effects of ethanol on glycine uptake mediated by the recombinant GLYT1 and GLYT2 glycine transporters
    • Núnez E., López-Corcuera B., Martínez-Maza R., Aragón C. Differential effects of ethanol on glycine uptake mediated by the recombinant GLYT1 and GLYT2 glycine transporters. Br. J. Pharmacol. 129:2000;802-810.
    • (2000) Br. J. Pharmacol. , vol.129 , pp. 802-810
    • Núnez, E.1    López-Corcuera, B.2    Martínez-Maza, R.3    Aragón, C.4
  • 771
    • 0032167980 scopus 로고    scopus 로고
    • Cell type and pathway dependence of synaptic AMPA receptor number and variability in the hippocampus
    • Nusser Z., Lujan R., Laube G., Roberts J.D., Molnar E., Somogyi P. Cell type and pathway dependence of synaptic AMPA receptor number and variability in the hippocampus. Neuron. 21:1998;545-559.
    • (1998) Neuron , vol.21 , pp. 545-559
    • Nusser, Z.1    Lujan, R.2    Laube, G.3    Roberts, J.D.4    Molnar, E.5    Somogyi, P.6
  • 772
    • 0022364119 scopus 로고
    • Cerebellar hypoplasia in the Gunn rat is associated with changes in neurotypic and gliotypic proteins
    • O'Callaghan J.P., Miller D.B. Cerebellar hypoplasia in the Gunn rat is associated with changes in neurotypic and gliotypic proteins. J. Pharmacol. Exp. Ther. 234:1985;522-533.
    • (1985) J. Pharmacol. Exp. Ther. , vol.234 , pp. 522-533
    • O'Callaghan, J.P.1    Miller, D.B.2
  • 773
    • 0024459205 scopus 로고
    • Methylmercury-induced movement and postural disorders in developing rat - High-affinity uptake of choline, glutamate and gamma-aminobutyric acid in the cerebral cortex and caudate putamen
    • O'Kusky J.R., McGeer E.G. Methylmercury-induced movement and postural disorders in developing rat - high-affinity uptake of choline, glutamate and gamma-aminobutyric acid in the cerebral cortex and caudate putamen. J. Neurochem. 53:1989;999-1006.
    • (1989) J. Neurochem. , vol.53 , pp. 999-1006
    • O'Kusky, J.R.1    McGeer, E.G.2
  • 775
    • 0031049236 scopus 로고    scopus 로고
    • Altered glutamatergic transmission in neurological disorders: From high extracellular glutamate to excessive synaptic efficacy
    • Obrenovitch T.P., Urenjak J. Altered glutamatergic transmission in neurological disorders: from high extracellular glutamate to excessive synaptic efficacy. Prog. Neurobiol. 51:1997;39-87.
    • (1997) Prog. Neurobiol. , vol.51 , pp. 39-87
    • Obrenovitch, T.P.1    Urenjak, J.2
  • 776
    • 0030670737 scopus 로고    scopus 로고
    • Is high extracellular glutamate the key to excitotoxicity in traumatic brain injury?
    • Obrenovitch T.P., Urenjak J. Is high extracellular glutamate the key to excitotoxicity in traumatic brain injury? J. Neurotrauma. 14:1997;677-698.
    • (1997) J. Neurotrauma , vol.14 , pp. 677-698
    • Obrenovitch, T.P.1    Urenjak, J.2
  • 777
    • 0031841655 scopus 로고    scopus 로고
    • Lysine and glutamate transport in the erythrocytes of common brushtail possum, tammar wallaby and eastern grey kangaroo
    • Ogawa E., Kuchel P.W., Agar N.S. Lysine and glutamate transport in the erythrocytes of common brushtail possum, tammar wallaby and eastern grey kangaroo. Comp. Biochem. Physiol. Mol. Integr. Physiol. 119:1998;951-956.
    • (1998) Comp. Biochem. Physiol. Mol. Integr. Physiol. , vol.119 , pp. 951-956
    • Ogawa, E.1    Kuchel, P.W.2    Agar, N.S.3
  • 778
    • 0023028965 scopus 로고
    • 3H]glutamate in synaptic membranes from rat brain
    • 3H]glutamate in synaptic membranes from rat brain. Brain Res. 397:1986;137-144.
    • (1986) Brain Res. , vol.397 , pp. 137-144
    • Ogita, K.1    Yoneda, Y.2
  • 779
    • 0010457889 scopus 로고
    • L-2-(carboxycyclopropyl)glycines - Conformationally constrained L-glutamate analogues
    • New York: Raven Press
    • Ohfune Y., Shinozaki H. L-2-(carboxycyclopropyl)glycines - conformationally constrained L-glutamate analogues. Drug Design for Neuroscience. 1993;261-283 Raven Press, New York.
    • (1993) Drug Design for Neuroscience , pp. 261-283
    • Ohfune, Y.1    Shinozaki, H.2
  • 780
    • 0027534340 scopus 로고
    • Synthesis of L-2-(2,3-dicarboxycyclopropyl)glycines - Novel conformationally restricted glutamate analogues
    • Ohfune Y., Shimamoto K., Ishida M., Shinozaki H. Synthesis of L-2-(2,3-dicarboxycyclopropyl)glycines - novel conformationally restricted glutamate analogues. Bioorg. Med. Chem. Lett. 3:1993;15-18.
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 15-18
    • Ohfune, Y.1    Shimamoto, K.2    Ishida, M.3    Shinozaki, H.4
  • 781
    • 0032078391 scopus 로고    scopus 로고
    • Expression of the human excitatory amino acid transporter 2 and metabotropic glutamate receptors 3 and 5 in the prefrontal cortex from normal individuals and patients with schizophrenia
    • Ohnuma T., Augood S.J., Arai H., Mckenna P.J., Emson P.C. Expression of the human excitatory amino acid transporter 2 and metabotropic glutamate receptors 3 and 5 in the prefrontal cortex from normal individuals and patients with schizophrenia. Mol. Brain Res. 56:1998;207-217.
    • (1998) Mol. Brain Res. , vol.56 , pp. 207-217
    • Ohnuma, T.1    Augood, S.J.2    Arai, H.3    McKenna, P.J.4    Emson, P.C.5
  • 782
    • 0023680343 scopus 로고
    • Oxidative stresses induced the cystine transport activity in human erythrocytes
    • Ohtsuka Y., Kondo T., Kawakami Y. Oxidative stresses induced the cystine transport activity in human erythrocytes. Biochem. Biophys. Res. Commun. 155:1988;160-166.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 160-166
    • Ohtsuka, Y.1    Kondo, T.2    Kawakami, Y.3
  • 783
    • 0027468201 scopus 로고
    • Vulnerability of oligodendroglia to glutamate - Pharmacology, mechanisms, and prevention
    • Oka A., Belliveau M.J., Rosenberg P.A., Volpe J.J. Vulnerability of oligodendroglia to glutamate - pharmacology, mechanisms, and prevention. J. Neurosci. 13:1993;1441-1453.
    • (1993) J. Neurosci. , vol.13 , pp. 1441-1453
    • Oka, A.1    Belliveau, M.J.2    Rosenberg, P.A.3    Volpe, J.J.4
  • 784
    • 0033568842 scopus 로고    scopus 로고
    • Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit
    • Okabe S., Miwa A., Okado H. Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit. J. Neurosci. 19:1999;7781-7792.
    • (1999) J. Neurosci. , vol.19 , pp. 7781-7792
    • Okabe, S.1    Miwa, A.2    Okado, H.3
  • 785
    • 0014668762 scopus 로고
    • Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate
    • Olney J.W. Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate. Science. 164:1969;719-721.
    • (1969) Science , vol.164 , pp. 719-721
    • Olney, J.W.1
  • 786
    • 0024399770 scopus 로고
    • Excitatory amino acids and neuropsychiatric disorders
    • Olney J.W. Excitatory amino acids and neuropsychiatric disorders. Biol. Psychiatry. 26:1989;505-525.
    • (1989) Biol. Psychiatry , vol.26 , pp. 505-525
    • Olney, J.W.1
  • 787
    • 0025304789 scopus 로고
    • Excitotoxic amino acids and neuropsychiatric disorders
    • Olney J.W. Excitotoxic amino acids and neuropsychiatric disorders. Annu. Rev. Pharmacol. Toxicol. 30:1990;47-71.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 47-71
    • Olney, J.W.1
  • 788
    • 0014937190 scopus 로고
    • Brain damage in infant mice following oral intake of glutamate, aspartate or cysteine
    • Olney J.W., Ho O.L. Brain damage in infant mice following oral intake of glutamate, aspartate or cysteine. Nature. 227:1970;609-611.
    • (1970) Nature , vol.227 , pp. 609-611
    • Olney, J.W.1    Ho, O.L.2
  • 789
    • 0026649002 scopus 로고
    • Amyotrophic lateral sclerosis - Increased solubility of skin collagen
    • Ono S., Yamauchi M. Amyotrophic lateral sclerosis - increased solubility of skin collagen. Neurology. 42:1992;1535-1539.
    • (1992) Neurology , vol.42 , pp. 1535-1539
    • Ono, S.1    Yamauchi, M.2
  • 791
    • 0032531028 scopus 로고    scopus 로고
    • Anion currents and predicted glutamate flux through a neuronal glutamate transporter
    • Otis T.S., Jahr C.E. Anion currents and predicted glutamate flux through a neuronal glutamate transporter. J. Neurosci. 18:1998;7099-7110.
    • (1998) J. Neurosci. , vol.18 , pp. 7099-7110
    • Otis, T.S.1    Jahr, C.E.2
  • 792
    • 0034655871 scopus 로고    scopus 로고
    • Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2
    • Otis T.S., Kavanaugh M.P. Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2. J. Neurosci. 20:2000;2749-2757.
    • (2000) J. Neurosci. , vol.20 , pp. 2749-2757
    • Otis, T.S.1    Kavanaugh, M.P.2
  • 793
    • 0029915273 scopus 로고    scopus 로고
    • Delayed clearance of transmitter and the role of glutamate transporters at synapses with multiple release sites
    • Otis T.S., Wu Y.C., Trussell L.O. Delayed clearance of transmitter and the role of glutamate transporters at synapses with multiple release sites. J. Neurosci. 16:1996;1634-1644.
    • (1996) J. Neurosci. , vol.16 , pp. 1634-1644
    • Otis, T.S.1    Wu, Y.C.2    Trussell, L.O.3
  • 794
    • 0030761115 scopus 로고    scopus 로고
    • Postsynaptic glutamate transport at the climbing fiber Purkinje cell synapse
    • Otis T.S., Kavanaugh M.P., Jahr C.E. Postsynaptic glutamate transport at the climbing fiber Purkinje cell synapse. Science. 277:1997;1515-1518.
    • (1997) Science , vol.277 , pp. 1515-1518
    • Otis, T.S.1    Kavanaugh, M.P.2    Jahr, C.E.3
  • 795
    • 0028079925 scopus 로고
    • Marked increase in glutamate-aspartate transporter (GLAST/glut-1) mRNA following transient retinal ischemia
    • Otori Y., Shimada S., Tanaka K., Ishimoto I., Tano Y., Tohyama M. Marked increase in glutamate-aspartate transporter (GLAST/glut-1) mRNA following transient retinal ischemia. Mol. Brain Res. 27:1994;310-314.
    • (1994) Mol. Brain Res. , vol.27 , pp. 310-314
    • Otori, Y.1    Shimada, S.2    Tanaka, K.3    Ishimoto, I.4    Tano, Y.5    Tohyama, M.6
  • 796
    • 0024605419 scopus 로고
    • Postembedding immunogold labelling of fixed glutamate: An electron microscopic analysis of the relationship between gold particle density and antigen concentration
    • Ottersen O.P. Postembedding immunogold labelling of fixed glutamate: an electron microscopic analysis of the relationship between gold particle density and antigen concentration. J. Chem. Neuroanat. 2:1989;57-66.
    • (1989) J. Chem. Neuroanat. , vol.2 , pp. 57-66
    • Ottersen, O.P.1
  • 797
    • 0024393209 scopus 로고
    • Quantitative electron microscopic immunocytochemistry of neuroactive amino acids
    • Ottersen O.P. Quantitative electron microscopic immunocytochemistry of neuroactive amino acids. Anat. Embryol. 180:1989;1-15.
    • (1989) Anat. Embryol. , vol.180 , pp. 1-15
    • Ottersen, O.P.1
  • 798
    • 0001749575 scopus 로고
    • Neurons containing or accumulating transmitter amino acids
    • In: Björklund, A., Hökfelt, T., Kuhar, M.J. (Eds.), Handbook of Chemical Neuroanatomy Elsevier, Amsterdam
    • Ottersen, O.P., Storm-Mathisen, J., 1984. Neurons containing or accumulating transmitter amino acids. In: Björklund, A., Hökfelt, T., Kuhar, M.J. (Eds.), Handbook of Chemical Neuroanatomy. In: Classical Transmitters and Transmitter Receptors in the CNS, Vol. 3, Part II. Elsevier, Amsterdam, pp. 141-246.
    • (1984) In: Classical Transmitters and Transmitter Receptors in the CNS , vol.3 , Issue.2 PART , pp. 141-246
    • Ottersen, O.P.1    Storm-Mathisen, J.2
  • 799
    • 0023202178 scopus 로고
    • Localization of amino acid neurotransmitters by immunocytochemistry
    • Ottersen O.P., Storm-Mathisen J. Localization of amino acid neurotransmitters by immunocytochemistry. Trends Neurosci. 10:1987;250-255.
    • (1987) Trends Neurosci. , vol.10 , pp. 250-255
    • Ottersen, O.P.1    Storm-Mathisen, J.2
  • 800
    • 0026544324 scopus 로고
    • Metabolic compartmentation of glutamate and glutamine: Morphological evidence obtained by quantitative immunocytochemistry in rat cerebellum
    • Ottersen O.P., Zhang N., Walberg F. Metabolic compartmentation of glutamate and glutamine: morphological evidence obtained by quantitative immunocytochemistry in rat cerebellum. Neuroscience. 46:1992;519-534.
    • (1992) Neuroscience , vol.46 , pp. 519-534
    • Ottersen, O.P.1    Zhang, N.2    Walberg, F.3
  • 801
    • 0030293629 scopus 로고    scopus 로고
    • Ischemic disruption of glutamate homeostasis in brain: Quantitative immunocytochemical analysis
    • Ottersen O.P., Laake J.H., Reichelt W., Haug F.M., Torp R. Ischemic disruption of glutamate homeostasis in brain: quantitative immunocytochemical analysis. J. Chem. Neuroanat. 12:1996;1-14.
    • (1996) J. Chem. Neuroanat. , vol.12 , pp. 1-14
    • Ottersen, O.P.1    Laake, J.H.2    Reichelt, W.3    Haug, F.M.4    Torp, R.5
  • 802
    • 0032008180 scopus 로고    scopus 로고
    • Molecular organization of a type of peripheral glutamate synapse: The afferent synapses of hair cells in the inner ear
    • Ottersen O.P., Takumi Y., Matsubara A., Landsend A.S., Laake J.H., Usami S. Molecular organization of a type of peripheral glutamate synapse: the afferent synapses of hair cells in the inner ear. Prog. Neurobiol. 54:1998;127-148.
    • (1998) Prog. Neurobiol. , vol.54 , pp. 127-148
    • Ottersen, O.P.1    Takumi, Y.2    Matsubara, A.3    Landsend, A.S.4    Laake, J.H.5    Usami, S.6
  • 803
    • 0033232782 scopus 로고    scopus 로고
    • Glutamate transporters contribute to the time course of synaptic transmission in cerebellar granule cells
    • Overstreet L.S., Kinney G.A., Liu Y.B., Billups D., Slater N.T. Glutamate transporters contribute to the time course of synaptic transmission in cerebellar granule cells. J. Neurosci. 19:1999;9663-9673.
    • (1999) J. Neurosci. , vol.19 , pp. 9663-9673
    • Overstreet, L.S.1    Kinney, G.A.2    Liu, Y.B.3    Billups, D.4    Slater, N.T.5
  • 804
    • 0032834820 scopus 로고    scopus 로고
    • Neuropathology of parkinsonism-dementia complex and amyotrophic lateral sclerosis of Guam: An update
    • Oyanagi K., Wada M. Neuropathology of parkinsonism-dementia complex and amyotrophic lateral sclerosis of Guam: an update. J. Neurol. 246:1999;19-27.
    • (1999) J. Neurol. , vol.246 , pp. 19-27
    • Oyanagi, K.1    Wada, M.2
  • 805
    • 0031912995 scopus 로고    scopus 로고
    • Glutamate receptors in the mammalian central nervous system
    • Ozawa S., Kamiya H., Tsuzuki K. Glutamate receptors in the mammalian central nervous system. Prog. Neurobiol. 54:1998;581-618.
    • (1998) Prog. Neurobiol. , vol.54 , pp. 581-618
    • Ozawa, S.1    Kamiya, H.2    Tsuzuki, K.3
  • 806
    • 0031798539 scopus 로고    scopus 로고
    • Glutamate transport and storage in synaptic vesicles
    • Õzkan E.D., Ueda T. Glutamate transport and storage in synaptic vesicles. Jpn. J. Pharmacol. 77:1998;1-10.
    • (1998) Jpn. J. Pharmacol. , vol.77 , pp. 1-10
    • Õzkan, E.D.1    Ueda, T.2
  • 807
    • 0029968824 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a sodium-dicarboxylate cotransporter from human kidney
    • Pajor A.M. Molecular cloning and functional expression of a sodium-dicarboxylate cotransporter from human kidney. Am. J. Physiol. 270:1996;F642-F648.
    • (1996) Am. J. Physiol. , vol.270 , pp. 642-F648
    • Pajor, A.M.1
  • 810
    • 0028586835 scopus 로고
    • Increased transmitter amino acid concentration in human ventricular CSF after brain trauma
    • Palmer A.M., Marion D.W., Botscheller M.L., Bowen D.M., Dekosky S.T. Increased transmitter amino acid concentration in human ventricular CSF after brain trauma. Neuroreport. 6:1994;153-156.
    • (1994) Neuroreport , vol.6 , pp. 153-156
    • Palmer, A.M.1    Marion, D.W.2    Botscheller, M.L.3    Bowen, D.M.4    Dekosky, S.T.5
  • 812
    • 0029984610 scopus 로고    scopus 로고
    • Rat C6 and human astrocytic tumor cells express a neuronal type of glutamate transporter
    • Palos T.P., Ramachandran B., Boado R., Howard B.D. Rat C6 and human astrocytic tumor cells express a neuronal type of glutamate transporter. Mol. Brain Res. 37:1996;297-303.
    • (1996) Mol. Brain Res. , vol.37 , pp. 297-303
    • Palos, T.P.1    Ramachandran, B.2    Boado, R.3    Howard, B.D.4
  • 813
    • 0032818544 scopus 로고    scopus 로고
    • Wnt signaling induces GLT-1 expression in rat C6 glioma cells
    • Palos T.P., Zheng S., Howard B.D. Wnt signaling induces GLT-1 expression in rat C6 glioma cells. J. Neurochem. 73:1999;1012-1023.
    • (1999) J. Neurochem. , vol.73 , pp. 1012-1023
    • Palos, T.P.1    Zheng, S.2    Howard, B.D.3
  • 814
    • 0031940166 scopus 로고    scopus 로고
    • HIV decreases glutamate transport in SK-n-MC neuroblastoma cells
    • Pappas T.C., Alagarsamy S., Pollard R.B., Nokta M. HIV decreases glutamate transport in SK-n-MC neuroblastoma cells. J. Neurovirol. 4:1998;69-79.
    • (1998) J. Neurovirol. , vol.4 , pp. 69-79
    • Pappas, T.C.1    Alagarsamy, S.2    Pollard, R.B.3    Nokta, M.4
  • 815
    • 0034710306 scopus 로고    scopus 로고
    • Presynaptic NMDA receptor subunit immunoreactivity in GABAergic terminals in rat brain
    • Paquet M., Smith Y. Presynaptic NMDA receptor subunit immunoreactivity in GABAergic terminals in rat brain. J. Comp. Neurol. 423:2000;330-347.
    • (2000) J. Comp. Neurol. , vol.423 , pp. 330-347
    • Paquet, M.1    Smith, Y.2
  • 816
    • 0030894036 scopus 로고    scopus 로고
    • The inhibitory effects of beta-amyloid on glutamate and glucose uptakes by cultured astrocytes
    • Parpura-Gill A., Beitz D., Uemura E. The inhibitory effects of beta-amyloid on glutamate and glucose uptakes by cultured astrocytes. Brain Res. 754:1997;65-71.
    • (1997) Brain Res. , vol.754 , pp. 65-71
    • Parpura-Gill, A.1    Beitz, D.2    Uemura, E.3
  • 819
    • 0031579422 scopus 로고    scopus 로고
    • Developmental changes of RNA editing of glutamate receptor subunits GluR5 and GluR6: In vivo versus in vitro
    • Paschen W., Schmitt J., Gissel C., Dux E. Developmental changes of RNA editing of glutamate receptor subunits GluR5 and GluR6: In vivo versus in vitro. Dev. Brain Res. 98:1997;271-280.
    • (1997) Dev. Brain Res. , vol.98 , pp. 271-280
    • Paschen, W.1    Schmitt, J.2    Gissel, C.3    Dux, E.4
  • 820
    • 0025456905 scopus 로고
    • Structure-activity relationships for amino acid transmitter candidates acting at N-methyl-D-aspartate and quisqualate receptors
    • Patneau D.K., Mayer M.L. Structure-activity relationships for amino acid transmitter candidates acting at N-methyl-D-aspartate and quisqualate receptors. J. Neurosci. 10:1990;2385-2399.
    • (1990) J. Neurosci. , vol.10 , pp. 2385-2399
    • Patneau, D.K.1    Mayer, M.L.2
  • 821
    • 0023659710 scopus 로고
    • Glutamate acting on NMDA receptors stimulates neurite outgrowth from cerebellar granule cells
    • Pearce I.A., Cambray-Deakin M.A., Burgoyne R.D. Glutamate acting on NMDA receptors stimulates neurite outgrowth from cerebellar granule cells. FEBS Lett. 233:1987;143-147.
    • (1987) FEBS Lett. , vol.233 , pp. 143-147
    • Pearce, I.A.1    Cambray-Deakin, M.A.2    Burgoyne, R.D.3
  • 822
    • 0031768026 scopus 로고    scopus 로고
    • Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients
    • Pedersen W.A., Fu W.M., Keller J.N., Markesbery W.R., Appel S., Smith R.G., Kasarskis E., Mattson M.P. Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients. Ann. Neurol. 44:1998;819-824.
    • (1998) Ann. Neurol. , vol.44 , pp. 819-824
    • Pedersen, W.A.1    Fu, W.M.2    Keller, J.N.3    Markesbery, W.R.4    Appel, S.5    Smith, R.G.6    Kasarskis, E.7    Mattson, M.P.8
  • 823
    • 0033004618 scopus 로고    scopus 로고
    • The lipid peroxidation product 4-hydroxynonenal impairs glutamate and glucose transport and choline acetyltransferase activity in NSC-19 motor neuron cells
    • Pedersen W.A., Cashman N.R., Mattson M.P. The lipid peroxidation product 4-hydroxynonenal impairs glutamate and glucose transport and choline acetyltransferase activity in NSC-19 motor neuron cells. Exp. Neurol. 155:1999;1-10.
    • (1999) Exp. Neurol. , vol.155 , pp. 1-10
    • Pedersen, W.A.1    Cashman, N.R.2    Mattson, M.P.3
  • 824
    • 0030976929 scopus 로고    scopus 로고
    • Glutamate transporter EAAC-1-deficient mice develop dicarboxylic aminoaciduria and behavioral abnormalities but no neurodegeneration
    • Peghini P., Janzen J., Stoffel W. Glutamate transporter EAAC-1-deficient mice develop dicarboxylic aminoaciduria and behavioral abnormalities but no neurodegeneration. EMBO J. 16:1997;3822-3832.
    • (1997) EMBO J. , vol.16 , pp. 3822-3832
    • Peghini, P.1    Janzen, J.2    Stoffel, W.3
  • 825
    • 0028080101 scopus 로고
    • Glutamate uptake into astrocytes stimulates aerobic glycolysis: A mechanism coupling neuronal activity to glucose utilization
    • Pellerin L., Magistretti P.J. Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization. Proc. Natl. Acad. Sci. USA. 91:1994;10625-10629.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10625-10629
    • Pellerin, L.1    Magistretti, P.J.2
  • 826
    • 0030870286 scopus 로고    scopus 로고
    • +-ATPase activity in astrocytes via activation of a distinct subunit highly sensitive to ouabain
    • +-ATPase activity in astrocytes via activation of a distinct subunit highly sensitive to ouabain. J. Neurochem. 69:1997;2132-2137.
    • (1997) J. Neurochem. , vol.69 , pp. 2132-2137
    • Pellerin, L.1    Magistretti, P.J.2
  • 827
    • 0033522488 scopus 로고    scopus 로고
    • PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells
    • Perego C., Vanoni C., Villa A., Longhi R., Kaech S.M., Frohli E., Hajnal A., Kim S.K., Pietrini G. PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells. EMBO J. 18:1999;2384-2393.
    • (1999) EMBO J. , vol.18 , pp. 2384-2393
    • Perego, C.1    Vanoni, C.2    Villa, A.3    Longhi, R.4    Kaech, S.M.5    Frohli, E.6    Hajnal, A.7    Kim, S.K.8    Pietrini, G.9
  • 828
    • 0033840578 scopus 로고    scopus 로고
    • The GLT-1 and GLAST glutamate transporters are expressed on morphologically distinct astrocytes and regulated by neuronal activity in primary hippocampal cocultures
    • Perego C., Vanoni C., Bossi M., Massari S., Basudev H., Longhi R., Pietrini G. The GLT-1 and GLAST glutamate transporters are expressed on morphologically distinct astrocytes and regulated by neuronal activity in primary hippocampal cocultures. J. Neurochem. 75:2000;1076-1084.
    • (2000) J. Neurochem. , vol.75 , pp. 1076-1084
    • Perego, C.1    Vanoni, C.2    Bossi, M.3    Massari, S.4    Basudev, H.5    Longhi, R.6    Pietrini, G.7
  • 829
    • 0030757990 scopus 로고    scopus 로고
    • Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress
    • Pereira C.M.F., Oliveira C.R. Glutamate toxicity on a PC12 cell line involves glutathione (GSH) depletion and oxidative stress. Free Radic. Biol. Med. 23:1997;637-647.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 637-647
    • Pereira, C.M.F.1    Oliveira, C.R.2
  • 830
    • 0025366777 scopus 로고
    • An outbreak of toxic encephalopathy caused by eating mussels contaminated with domoic acid
    • Perl T.M., Bedard L., Kosatsky T., Hockin J.C., Todd E.C.D., Remis R.S. An outbreak of toxic encephalopathy caused by eating mussels contaminated with domoic acid. N. Engl. J. Med. 322:1990;1775-1780.
    • (1990) N. Engl. J. Med. , vol.322 , pp. 1775-1780
    • Perl, T.M.1    Bedard, L.2    Kosatsky, T.3    Hockin, J.C.4    Todd, E.C.D.5    Remis, R.S.6
  • 831
    • 0025337382 scopus 로고
    • Amyotrophic lateral sclerosis - Amino acid levels in plasma and cerebrospinal fluid
    • Perry T.L., Krieger C., Hansen S., Eisen A. Amyotrophic lateral sclerosis - amino acid levels in plasma and cerebrospinal fluid. Ann. Neurol. 28:1990;12-17.
    • (1990) Ann. Neurol. , vol.28 , pp. 12-17
    • Perry, T.L.1    Krieger, C.2    Hansen, S.3    Eisen, A.4
  • 832
    • 0033613830 scopus 로고    scopus 로고
    • Molecular basis of insulin-stimulated GLUT4 vesicle trafficking - Location! location! location!
    • Pessin J.E., Thurmond D.C., Elmendorf J.S., Coker K.J., Okada S. Molecular basis of insulin-stimulated GLUT4 vesicle trafficking - location! location! location! J. Biol. Chem. 274:1999;2593-2596.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2593-2596
    • Pessin, J.E.1    Thurmond, D.C.2    Elmendorf, J.S.3    Coker, K.J.4    Okada, S.5
  • 833
    • 0026560573 scopus 로고
    • Light and electron immunocytochemical localization of AMPA-selective glutamate receptors in the rat brain
    • Petralia R.S., Wenthold R.J. Light and electron immunocytochemical localization of AMPA-selective glutamate receptors in the rat brain. J. Comp. Neurol. 318:1992;329-354.
    • (1992) J. Comp. Neurol. , vol.318 , pp. 329-354
    • Petralia, R.S.1    Wenthold, R.J.2
  • 835
    • 0000876580 scopus 로고    scopus 로고
    • Cellular and subcellular distribution of glutamate receptors
    • P. Jonas, & H. Monyer. Berlin: Springer
    • Petralia R.S., Rubio M.E., Wenthold R.J. Cellular and subcellular distribution of glutamate receptors. Jonas P., Monyer H. Ionotropic Glutamate Receptors in the CNS. 1999;143-171 Springer, Berlin.
    • (1999) Ionotropic Glutamate Receptors in the CNS , pp. 143-171
    • Petralia, R.S.1    Rubio, M.E.2    Wenthold, R.J.3
  • 836
    • 0034674519 scopus 로고    scopus 로고
    • Transporter reversal as a mechanism of glutamate release from the ischemic rat cerebral cortex: Studies with DL-threo-beta-benzyloxyaspartate
    • Phillis J.W., Ren J., O'Regan M.H. Transporter reversal as a mechanism of glutamate release from the ischemic rat cerebral cortex: studies with DL-threo-beta-benzyloxyaspartate. Brain Res. 868:2000;105-112.
    • (2000) Brain Res. , vol.868 , pp. 105-112
    • Phillis, J.W.1    Ren, J.2    O'Regan, M.H.3
  • 837
    • 0028297676 scopus 로고
    • Involvement of the cystine transport system x(c)(-) macrophage-induced glutamate-dependent cytotoxicity to neurons
    • Piani D., Fontana A. Involvement of the cystine transport system x(c)(-) macrophage-induced glutamate-dependent cytotoxicity to neurons. J. Immunol. 152:1994;3578-3585.
    • (1994) J. Immunol. , vol.152 , pp. 3578-3585
    • Piani, D.1    Fontana, A.2
  • 838
    • 0027369531 scopus 로고
    • Glutamate uptake by astrocytes is inhibited by reactive oxygen intermediates but not by other macrophage-derived molecules including cytokines, leukotrienes or platelet-activating factor
    • Piani D., Frei K., Pfister H.W., Fontana A. Glutamate uptake by astrocytes is inhibited by reactive oxygen intermediates but not by other macrophage-derived molecules including cytokines, leukotrienes or platelet-activating factor. J. Neuroimmunol. 48:1993;99-104.
    • (1993) J. Neuroimmunol. , vol.48 , pp. 99-104
    • Piani, D.1    Frei, K.2    Pfister, H.W.3    Fontana, A.4
  • 839
    • 0021285831 scopus 로고
    • 3H]glutamate binding: A new receptor or a particular transport process?
    • 3H]glutamate binding: a new receptor or a particular transport process? FEBS Lett. 175:1984;31-36.
    • (1984) FEBS Lett. , vol.175 , pp. 31-36
    • Pin, J.P.1    Bockaert, J.2    Recasens, M.3
  • 840
    • 0025691629 scopus 로고
    • Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain
    • Pines G., Kanner B.I. Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain. Biochemistry. 29:1990;11209-11214.
    • (1990) Biochemistry , vol.29 , pp. 11209-11214
    • Pines, G.1    Kanner, B.I.2
  • 843
    • 0033551415 scopus 로고    scopus 로고
    • H-1-MRS evidence of neurodegeneration and excess glutamate plus glutamine in ALS medulla
    • Pioro E.P., Majors A.W., Mitsumoto H., Nelson D.R., Ng T.C. H-1-MRS evidence of neurodegeneration and excess glutamate plus glutamine in ALS medulla. Neurology. 53:1999;71-79.
    • (1999) Neurology , vol.53 , pp. 71-79
    • Pioro, E.P.1    Majors, A.W.2    Mitsumoto, H.3    Nelson, D.R.4    Ng, T.C.5
  • 844
    • 0030152063 scopus 로고    scopus 로고
    • Activation of the adenylate cyclase-dependent protein kinase pathway increases high affinity glutamate uptake into rat striatal synaptosomes
    • Pisano P., Samuel D., Nieoullon A., Kerkerian-Le Goff L. Activation of the adenylate cyclase-dependent protein kinase pathway increases high affinity glutamate uptake into rat striatal synaptosomes. Neuropharmacology. 35:1996;541-547.
    • (1996) Neuropharmacology , vol.35 , pp. 541-547
    • Pisano, P.1    Samuel, D.2    Nieoullon, A.3    Kerkerian-Le Goff, L.4
  • 845
    • 0034006904 scopus 로고    scopus 로고
    • Transient expression of the glial glutamate transporters GLAST and GLT in hippocampal neurons in primary culture
    • Plachez C., Danbolt N.C., Recasens M. Transient expression of the glial glutamate transporters GLAST and GLT in hippocampal neurons in primary culture. J. Neurosci. Res. 59:2000;587-593.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 587-593
    • Plachez, C.1    Danbolt, N.C.2    Recasens, M.3
  • 846
    • 0023617392 scopus 로고
    • Abnormal glutamate metabolism in amyotrophic lateral sclerosis
    • Plaitakis A., Caroscio J.T. Abnormal glutamate metabolism in amyotrophic lateral sclerosis. Ann. Neurol. 22:1987;575-579.
    • (1987) Ann. Neurol. , vol.22 , pp. 575-579
    • Plaitakis, A.1    Caroscio, J.T.2
  • 847
    • 0027367787 scopus 로고
    • Regulation of the glutamate transporter by amino acid deprivation and associated effects on the level of EAAC1 messenger RNA in the renal epithelial cell line NBL-1
    • Plakidou-Dymock S., McGivan J.D. Regulation of the glutamate transporter by amino acid deprivation and associated effects on the level of EAAC1 messenger RNA in the renal epithelial cell line NBL-1. Biochem. J. 295:1993;749-755.
    • (1993) Biochem. J. , vol.295 , pp. 749-755
    • Plakidou-Dymock, S.1    McGivan, J.D.2
  • 848
    • 0028651932 scopus 로고
    • Regulation of neurotransmitter reuptake by nitric oxide
    • Pogun S., Kuhar M.J. Regulation of neurotransmitter reuptake by nitric oxide. Ann. N. Y. Acad. Sci. 738:1994;305-315.
    • (1994) Ann. N. Y. Acad. Sci. , vol.738 , pp. 305-315
    • Pogun, S.1    Kuhar, M.J.2
  • 849
    • 0034602529 scopus 로고    scopus 로고
    • The rat hepatoma cell line H4-II-E-C3 expresses high activities of the high-affinity glutamate transporter GLT-1A
    • Pollard M., McGivan J. The rat hepatoma cell line H4-II-E-C3 expresses high activities of the high-affinity glutamate transporter GLT-1A. FEBS Lett. 484:2000;74-76.
    • (2000) FEBS Lett. , vol.484 , pp. 74-76
    • Pollard, M.1    McGivan, J.2
  • 850
    • 0023847643 scopus 로고
    • D-Aspartate uptake and release in the guinea pig spinal cord after partial ablation of the cerebral cortex
    • Potashner S.J., Dymczyk L., Deangelis M.M. D-Aspartate uptake and release in the guinea pig spinal cord after partial ablation of the cerebral cortex. J. Neurochem. 50:1988;103-111.
    • (1988) J. Neurochem. , vol.50 , pp. 103-111
    • Potashner, S.J.1    Dymczyk, L.2    Deangelis, M.M.3
  • 851
    • 0002264450 scopus 로고    scopus 로고
    • The structure and function of norepinephrine, dopamine, and serotonin transporters
    • M.E.A. Reith. Totowa, NJ: Humana Press Inc
    • Povlock S.L., Amara S.G. The structure and function of norepinephrine, dopamine, and serotonin transporters. Reith M.E.A. Neurotransmitter Transporters: Structure, Function, and Regulation. 1997;1-28 Humana Press Inc, Totowa, NJ.
    • (1997) Neurotransmitter Transporters: Structure, Function, and Regulation , pp. 1-28
    • Povlock, S.L.1    Amara, S.G.2
  • 852
    • 0033007878 scopus 로고    scopus 로고
    • Changing patterns of spatial buffering of glutamate in developing rat retinae are mediated by the Muller cell glutamate transporter GLAST
    • Pow D.V., Barnett N.L. Changing patterns of spatial buffering of glutamate in developing rat retinae are mediated by the Muller cell glutamate transporter GLAST. Cell Tissue Res. 297:1999;57-66.
    • (1999) Cell Tissue Res. , vol.297 , pp. 57-66
    • Pow, D.V.1    Barnett, N.L.2
  • 853
    • 0027234260 scopus 로고
    • Aspartate and glutamate transport in unfertilized pig oocytes and blastocysts
    • Prather R.S., Peters M.S., Vanwinkle L.J. Aspartate and glutamate transport in unfertilized pig oocytes and blastocysts. Mol. Reprod. Dev. 36:1993;49-52.
    • (1993) Mol. Reprod. Dev. , vol.36 , pp. 49-52
    • Prather, R.S.1    Peters, M.S.2    Vanwinkle, L.J.3
  • 855
    • 0031014266 scopus 로고    scopus 로고
    • Protein kinase C activation regulates human serotonin transporters in HEK-293 cells via altered cell surface expression
    • Qian Y., Galli A., Ramamoorthy S., Risso S., DeFelice L. Protein kinase C activation regulates human serotonin transporters in HEK-293 cells via altered cell surface expression. J. Neurosci. 17:1997;45-57.
    • (1997) J. Neurosci. , vol.17 , pp. 45-57
    • Qian, Y.1    Galli, A.2    Ramamoorthy, S.3    Risso, S.4    Defelice, L.5
  • 857
    • 0030964875 scopus 로고    scopus 로고
    • Second messengers, trafficking-related proteins, and amino acid residues that contribute to the functional regulation of the rat brain GABA transporter GAT1
    • Quick M.W., Corey J.L., Davidson N., Lester H.A. Second messengers, trafficking-related proteins, and amino acid residues that contribute to the functional regulation of the rat brain GABA transporter GAT1. J. Neurosci. 17:1997;2967-2979.
    • (1997) J. Neurosci. , vol.17 , pp. 2967-2979
    • Quick, M.W.1    Corey, J.L.2    Davidson, N.3    Lester, H.A.4
  • 858
    • 0033359937 scopus 로고    scopus 로고
    • Rapid, experience-dependent expression of synaptic NMDA receptors in visual cortex in vivo
    • Quinlan E.M., Philpot B.D., Huganir R.L., Bear M.F. Rapid, experience-dependent expression of synaptic NMDA receptors in visual cortex in vivo. Nat. Neurosci. 2:1999;352-357.
    • (1999) Nat. Neurosci. , vol.2 , pp. 352-357
    • Quinlan, E.M.1    Philpot, B.D.2    Huganir, R.L.3    Bear, M.F.4
  • 859
    • 0026719035 scopus 로고
    • Involvement of the N-methyl-D-aspartate (NMDA) receptor in synapse elimination during cerebellar development
    • Rabacchi S., Bailly Y., Delhaye-Bouchaud N., Mariani J. Involvement of the N-methyl-D-aspartate (NMDA) receptor in synapse elimination during cerebellar development. Science. 256:1992;1823-1825.
    • (1992) Science , vol.256 , pp. 1823-1825
    • Rabacchi, S.1    Bailly, Y.2    Delhaye-Bouchaud, N.3    Mariani, J.4
  • 860
    • 0022178608 scopus 로고
    • Reconstitution and purification of the sodium- And chloride-coupled gamma-aminobutyric acid transporter from rat brain
    • Radian R., Kanner B.I. Reconstitution and purification of the sodium- and chloride-coupled gamma-aminobutyric acid transporter from rat brain. J. Biol. Chem. 260:1985;11859-11865.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11859-11865
    • Radian, R.1    Kanner, B.I.2
  • 861
    • 0023002440 scopus 로고
    • Purification and identification of the functional sodium- And chloride-coupled gamma-aminobutyric acid transport glycoprotein from rat brain
    • Radian R., Bendahan A., Kanner B.I. Purification and identification of the functional sodium- and chloride-coupled gamma-aminobutyric acid transport glycoprotein from rat brain. J. Biol. Chem. 261:1986;15437-15441.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15437-15441
    • Radian, R.1    Bendahan, A.2    Kanner, B.I.3
  • 862
    • 0030222470 scopus 로고    scopus 로고
    • Cloning and characterization of cDNAs encoding putative glutamate transporters from Caenorhabditis elegans and Onchocerca volvulus
    • Radice A.D., Lustigman S. Cloning and characterization of cDNAs encoding putative glutamate transporters from Caenorhabditis elegans and Onchocerca volvulus. Mol. Biochem. Parasitol. 80:1996;41-53.
    • (1996) Mol. Biochem. Parasitol. , vol.80 , pp. 41-53
    • Radice, A.D.1    Lustigman, S.2
  • 863
    • 0020538298 scopus 로고
    • A glial progenitor cell that develops in vitro into an astrocyte or an oligodendrocyte depending on culture medium
    • Raff M.C., Miller R.H., Noble M. A glial progenitor cell that develops in vitro into an astrocyte or an oligodendrocyte depending on culture medium. Nature. 303:1983;390-396.
    • (1983) Nature , vol.303 , pp. 390-396
    • Raff, M.C.1    Miller, R.H.2    Noble, M.3
  • 864
    • 0032190087 scopus 로고    scopus 로고
    • Glutamate receptor activity is required for normal development of tectal cells dendrites in vivo
    • Rajan I., Cline H.T. Glutamate receptor activity is required for normal development of tectal cells dendrites in vivo. J. Neurosci. 18:1998;7836-7846.
    • (1998) J. Neurosci. , vol.18 , pp. 7836-7846
    • Rajan, I.1    Cline, H.T.2
  • 865
    • 0015244631 scopus 로고
    • Guidance of neurons migrating to the fetal monkey neocortex
    • Rakic P. Guidance of neurons migrating to the fetal monkey neocortex. Brain Res. 33:1971;471-476.
    • (1971) Brain Res. , vol.33 , pp. 471-476
    • Rakic, P.1
  • 866
    • 0027359597 scopus 로고
    • Differential expression of transporters for norepinephrine and glutamate in wild type, variant, and WNT1-expressing PC12 cells
    • Ramachandran B., Houben K., Rozenberg Y.Y., Haigh J.R., Varpetian A., Howard B.D. Differential expression of transporters for norepinephrine and glutamate in wild type, variant, and WNT1-expressing PC12 cells. J. Biol. Chem. 268:1993;23891-23897.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23891-23897
    • Ramachandran, B.1    Houben, K.2    Rozenberg, Y.Y.3    Haigh, J.R.4    Varpetian, A.5    Howard, B.D.6
  • 867
    • 0031915461 scopus 로고    scopus 로고
    • Phosphorylation and regulation of antidepressant-sensitive serotonin transporters
    • Ramamoorthy S., Giovanetti E., Qian Y., Blakely R.D. Phosphorylation and regulation of antidepressant-sensitive serotonin transporters. J. Biol. Chem. 273:1998;2458-2466.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2458-2466
    • Ramamoorthy, S.1    Giovanetti, E.2    Qian, Y.3    Blakely, R.D.4
  • 868
    • 0030819659 scopus 로고    scopus 로고
    • Activity regulates the synaptic localization of the NMDA receptor in hippocampal neurons
    • Rao A., Craig A.M. Activity regulates the synaptic localization of the NMDA receptor in hippocampal neurons. Neuron. 19:1997;801-812.
    • (1997) Neuron , vol.19 , pp. 801-812
    • Rao, A.1    Craig, A.M.2
  • 869
    • 2642709999 scopus 로고    scopus 로고
    • Traumatic brain injury down-regulates glial glutamate transporter (GLT-1 and GLAST) proteins in rat brain
    • Rao V.L.R., Baskaya M.K., Dogan A., Rothstein J.D., Dempsey R.J. Traumatic brain injury down-regulates glial glutamate transporter (GLT-1 and GLAST) proteins in rat brain. J. Neurochem. 70:1998;2020-2027.
    • (1998) J. Neurochem. , vol.70 , pp. 2020-2027
    • Rao, V.L.R.1    Baskaya, M.K.2    Dogan, A.3    Rothstein, J.D.4    Dempsey, R.J.5
  • 870
    • 0033969456 scopus 로고    scopus 로고
    • Glial glutamate transporter GLT-1 down-regulation precedes delayed neuronal death in gerbil hippocampus following transient global cerebral ischemia
    • Rao V.L.R., Rao A.M., Dogan A., Bowen K.K., Hatcher J., Rothstein J.D., Dempsey R.J. Glial glutamate transporter GLT-1 down-regulation precedes delayed neuronal death in gerbil hippocampus following transient global cerebral ischemia. Neurochem. Int. 36:2000;531-537.
    • (2000) Neurochem. Int. , vol.36 , pp. 531-537
    • Rao, V.L.R.1    Rao, A.M.2    Dogan, A.3    Bowen, K.K.4    Hatcher, J.5    Rothstein, J.D.6    Dempsey, R.J.7
  • 871
    • 0028176067 scopus 로고
    • Localization of the glutamate transporter GLT-1 in rat and macaque monkey retinae
    • Rauen T., Kanner B.I. Localization of the glutamate transporter GLT-1 in rat and macaque monkey retinae. Neurosci. Lett. 169:1994;137-140.
    • (1994) Neurosci. Lett. , vol.169 , pp. 137-140
    • Rauen, T.1    Kanner, B.I.2
  • 872
    • 0033801093 scopus 로고    scopus 로고
    • Diversity of glutamate transporter expression and function in the mammalian retina
    • Rauen T. Diversity of glutamate transporter expression and function in the mammalian retina. Amino Acids. 19:2000;53-62.
    • (2000) Amino Acids , vol.19 , pp. 53-62
    • Rauen, T.1
  • 873
    • 0342906189 scopus 로고    scopus 로고
    • Fine tuning of glutamate uptake and degradation in glial cells: Common transcriptional regulation of GLAST1 and GS
    • Rauen T., Wiessner M. Fine tuning of glutamate uptake and degradation in glial cells: common transcriptional regulation of GLAST1 and GS. Neurochem. Int. 37:2000;179-189.
    • (2000) Neurochem. Int. , vol.37 , pp. 179-189
    • Rauen, T.1    Wiessner, M.2
  • 874
    • 0026658477 scopus 로고
    • Comparative analysis of sodium-dependent L-glutamate transport of synaptosomal and astroglial membrane vesicles from mouse cortex
    • Rauen T., Jeserich G., Danbolt N.C., Kanner B.I. Comparative analysis of sodium-dependent L-glutamate transport of synaptosomal and astroglial membrane vesicles from mouse cortex. FEBS Lett. 312:1992;15-20.
    • (1992) FEBS Lett. , vol.312 , pp. 15-20
    • Rauen, T.1    Jeserich, G.2    Danbolt, N.C.3    Kanner, B.I.4
  • 875
    • 0029904836 scopus 로고    scopus 로고
    • Differential expression of three glutamate transporter subtypes in the rat retina
    • Rauen T., Rothstein J.D., Wassle H. Differential expression of three glutamate transporter subtypes in the rat retina. Cell Tissue Res. 286:1996;325-336.
    • (1996) Cell Tissue Res. , vol.286 , pp. 325-336
    • Rauen, T.1    Rothstein, J.D.2    Wassle, H.3
  • 876
    • 0031939889 scopus 로고    scopus 로고
    • High-affinity glutamate transporters in the rat retina: A major role of the glial glutamate transporter GLAST-1 in transmitter clearance
    • Rauen T., Taylor W.R., Kuhlbrodt K., Wiessner M. High-affinity glutamate transporters in the rat retina: a major role of the glial glutamate transporter GLAST-1 in transmitter clearance. Cell Tissue Res. 291:1998;19-31.
    • (1998) Cell Tissue Res. , vol.291 , pp. 19-31
    • Rauen, T.1    Taylor, W.R.2    Kuhlbrodt, K.3    Wiessner, M.4
  • 877
    • 0034465354 scopus 로고    scopus 로고
    • Glia-neuron interaction by high-affinity glutamate transporters in neurotransmission
    • Rauen T., Fischer F., Wiessner M. Glia-neuron interaction by high-affinity glutamate transporters in neurotransmission. Adv. Exp. Med. Biol. 468:1999;81-95.
    • (1999) Adv. Exp. Med. Biol. , vol.468 , pp. 81-95
    • Rauen, T.1    Fischer, F.2    Wiessner, M.3
  • 878
    • 0030669618 scopus 로고    scopus 로고
    • Moving GLUT4: The biogenesis and trafficking of GLUT4 storage vesicles
    • Rea S., James D.E. Moving GLUT4: the biogenesis and trafficking of GLUT4 storage vesicles. Diabetes. 46:1997;1667-1677.
    • (1997) Diabetes , vol.46 , pp. 1667-1677
    • Rea, S.1    James, D.E.2
  • 879
    • 0032104055 scopus 로고    scopus 로고
    • Vesicular neurotransmitter transport and the presynaptic regulation of quantal size
    • Reimer R.J., Fon E.A., Edwards R.H. Vesicular neurotransmitter transport and the presynaptic regulation of quantal size. Curr. Opin. Neurobiol. 8:1998;405-412.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 405-412
    • Reimer, R.J.1    Fon, E.A.2    Edwards, R.H.3
  • 880
    • 0034608866 scopus 로고    scopus 로고
    • Amino acid transport system A resembles system N in sequence, but differs in mechanism
    • Reimer R.J., Chaudhry F.A., Gray A.I., Edwards R.H. Amino acid transport system A resembles system N in sequence, but differs in mechanism. Proc. Natl. Acad. Sci. USA. 97:2000;7715-7720.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7715-7720
    • Reimer, R.J.1    Chaudhry, F.A.2    Gray, A.I.3    Edwards, R.H.4
  • 882
    • 0023847642 scopus 로고
    • Glutamate transport in large muscle fibres of balanus nubilus
    • Revest P.A., Baker P.F. Glutamate transport in large muscle fibres of balanus nubilus. J. Neurochem. 50:1988;94-102.
    • (1988) J. Neurochem. , vol.50 , pp. 94-102
    • Revest, P.A.1    Baker, P.F.2
  • 883
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds I.J., Hastings T.G. Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J. Neurosci. 15:1995;3318-3327.
    • (1995) J. Neurosci. , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.G.2
  • 884
    • 0020583966 scopus 로고
    • Modulation of membrane transport by free fatty acids: Inhibition of synaptosomal sodium-dependent amino acid uptake
    • Rhoads D.E., Ockner R.K., Peterson N.A., Raghupathy E. Modulation of membrane transport by free fatty acids: inhibition of synaptosomal sodium-dependent amino acid uptake. Biochemistry. 22:1983;1965-1970.
    • (1983) Biochemistry , vol.22 , pp. 1965-1970
    • Rhoads, D.E.1    Ockner, R.K.2    Peterson, N.A.3    Raghupathy, E.4
  • 886
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps M.E., Huntley G.W., Hof P.R., Morrison J.H., Gordon J.W. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA. 92:1995;689-693.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3    Morrison, J.H.4    Gordon, J.W.5
  • 887
    • 0023022617 scopus 로고
    • Glutamate in rat brain cortex synaptic vesicles: Influence of the vesicle isolation procedure
    • Riveros N., Fiedler J., Lagos N., Muñoz C., Orrego F. Glutamate in rat brain cortex synaptic vesicles: influence of the vesicle isolation procedure. Brain Res. 386:1986;405-408.
    • (1986) Brain Res. , vol.386 , pp. 405-408
    • Riveros, N.1    Fiedler, J.2    Lagos, N.3    Muñoz, C.4    Orrego, F.5
  • 888
    • 0034072769 scopus 로고    scopus 로고
    • Oxidative stress in amyotrophic lateral sclerosis
    • Robberecht W. Oxidative stress in amyotrophic lateral sclerosis. J. Neurol. 247:2000;1-6.
    • (2000) J. Neurol. , vol.247 , pp. 1-6
    • Robberecht, W.1
  • 889
    • 0016333024 scopus 로고
    • Glutamate receptors in the rat central nervous system
    • Roberts P.J. Glutamate receptors in the rat central nervous system. Nature. 252:1974;399-401.
    • (1974) Nature , vol.252 , pp. 399-401
    • Roberts, P.J.1
  • 890
    • 0016438450 scopus 로고
    • Structural requirements for the inhibition for L-glutamate uptake by glia and nerve endings
    • Roberts P.J., Watkins J.C. Structural requirements for the inhibition for L-glutamate uptake by glia and nerve endings. Brain Res. 85:1975;120-125.
    • (1975) Brain Res. , vol.85 , pp. 120-125
    • Roberts, P.J.1    Watkins, J.C.2
  • 892
    • 0031662117 scopus 로고    scopus 로고
    • Examination of glutamate transporter heterogeneity using synaptosomal preparations
    • Robinson M.B. Examination of glutamate transporter heterogeneity using synaptosomal preparations. Methods Enzymol. 296:1998;189-202.
    • (1998) Methods Enzymol. , vol.296 , pp. 189-202
    • Robinson, M.B.1
  • 893
    • 0011323738 scopus 로고    scopus 로고
    • Heterogeneity and functional properties of subtypes of sodium-dependent glutamate transporters in the mammalian central nervous system
    • Robinson M.B., Dowd L.A. Heterogeneity and functional properties of subtypes of sodium-dependent glutamate transporters in the mammalian central nervous system. Adv. Pharmacol. 37:1997;69-115.
    • (1997) Adv. Pharmacol. , vol.37 , pp. 69-115
    • Robinson, M.B.1    Dowd, L.A.2
  • 895
    • 0027441565 scopus 로고
    • 3H]glutamate transport activity - Pharmacologic specificity and regulation by sodium and potassium
    • 3H]glutamate transport activity - pharmacologic specificity and regulation by sodium and potassium. J. Neurochem. 60:1993;167-179.
    • (1993) J. Neurochem. , vol.60 , pp. 167-179
    • Robinson, M.B.1    Sinor, J.D.2    Dowd, L.A.3    Kerwin, J.F.4
  • 897
    • 0030561276 scopus 로고    scopus 로고
    • Mechanism of glutamate release from rat hippocampal slices during in vitro ischemia
    • Roettger V., Lipton P. Mechanism of glutamate release from rat hippocampal slices during in vitro ischemia. Neuroscience. 75:1996;677-685.
    • (1996) Neuroscience , vol.75 , pp. 677-685
    • Roettger, V.1    Lipton, P.2
  • 899
    • 0029872230 scopus 로고    scopus 로고
    • Enhanced early developmental expression of the metabotropic glutamate receptor mGluR5 in rat brain: Protein, mRNA splice variants, and regional distribution
    • Romano C., Vandenpol A.N., Omalley K.L. Enhanced early developmental expression of the metabotropic glutamate receptor mGluR5 in rat brain: protein, mRNA splice variants, and regional distribution. J. Comp. Neurol. 367:1996;403-412.
    • (1996) J. Comp. Neurol. , vol.367 , pp. 403-412
    • Romano, C.1    Vandenpol, A.N.2    Omalley, K.L.3
  • 900
    • 0029820948 scopus 로고    scopus 로고
    • + changes induced by glutamate, kainate, and D-aspartate in rat hippocampal astrocytes
    • + changes induced by glutamate, kainate, and D-aspartate in rat hippocampal astrocytes. J. Neurosci. 16:1996;5393-5404.
    • (1996) J. Neurosci. , vol.16 , pp. 5393-5404
    • Rose, C.R.1    Ransom, B.R.2
  • 902
    • 0026596688 scopus 로고
    • Glutamate uptake disguises neurotoxic potency of glutamate agonists in cerebral cortex in dissociated cell culture
    • Rosenberg P.A., Amin S., Leitner M. Glutamate uptake disguises neurotoxic potency of glutamate agonists in cerebral cortex in dissociated cell culture. J. Neurosci. 12:1992;56-61.
    • (1992) J. Neurosci. , vol.12 , pp. 56-61
    • Rosenberg, P.A.1    Amin, S.2    Leitner, M.3
  • 903
    • 0030175394 scopus 로고    scopus 로고
    • Definition of the readily releasable pool of vesicles at hippocampal synapses
    • Rosenmund C., Stevens C.F. Definition of the readily releasable pool of vesicles at hippocampal synapses. Neuron. 16:1996;1197-1207.
    • (1996) Neuron , vol.16 , pp. 1197-1207
    • Rosenmund, C.1    Stevens, C.F.2
  • 904
    • 0032486422 scopus 로고    scopus 로고
    • The tetrameric structure of a glutamate receptor channel
    • Rosenmund C., Sternbach Y., Stevens C.F. The tetrameric structure of a glutamate receptor channel. Science. 280:1998;1596-1599.
    • (1998) Science , vol.280 , pp. 1596-1599
    • Rosenmund, C.1    Sternbach, Y.2    Stevens, C.F.3
  • 905
    • 0018330345 scopus 로고
    • Net uptake of aspartate by high-affinity rat cortical synaptosomal transport system
    • Roskoski R. Jr. Net uptake of aspartate by high-affinity rat cortical synaptosomal transport system. Brain Res. 160:1979;85-93.
    • (1979) Brain Res. , vol.160 , pp. 85-93
    • Roskoski R., Jr.1
  • 906
    • 0019408152 scopus 로고
    • Glutamate, aspartate and gammaaminobutyrate transport by membrane vesicles prepared from rat brain
    • Roskoski R. Jr, Rauch N., Roskoski L.M. Glutamate, aspartate and gammaaminobutyrate transport by membrane vesicles prepared from rat brain. Arch. Biochem. Biophys. 207:1981;407-415.
    • (1981) Arch. Biochem. Biophys. , vol.207 , pp. 407-415
    • Roskoski R., Jr.1    Rauch, N.2    Roskoski, L.M.3
  • 907
    • 0024344673 scopus 로고
    • Beta-N-oxalylamino-L-alanine action on glutamate receptors
    • Ross S.M., Roy D.N., Spencer P.S. Beta-N-oxalylamino-L-alanine action on glutamate receptors. J. Neurochem. 53:1989;710-715.
    • (1989) J. Neurochem. , vol.53 , pp. 710-715
    • Ross, S.M.1    Roy, D.N.2    Spencer, P.S.3
  • 908
    • 0032773638 scopus 로고    scopus 로고
    • Glutamate-induced increase of extracellular glutamate through N-methyl-D-aspartate receptors in ethanol withdrawal
    • Rossetti Z.L., Carboni S., Fadda F. Glutamate-induced increase of extracellular glutamate through N-methyl-D-aspartate receptors in ethanol withdrawal. Neuroscience. 93:1999;1135-1140.
    • (1999) Neuroscience , vol.93 , pp. 1135-1140
    • Rossetti, Z.L.1    Carboni, S.2    Fadda, F.3
  • 909
    • 0035239239 scopus 로고    scopus 로고
    • Tetanus and botulinum neurotoxins: Turning bad guys into good by research
    • Rossetto O., Seveso M., Caccin P., Schiavo G., Montecucco C. Tetanus and botulinum neurotoxins: turning bad guys into good by research. Toxicon. 39:2001;27-41.
    • (2001) Toxicon , vol.39 , pp. 27-41
    • Rossetto, O.1    Seveso, M.2    Caccin, P.3    Schiavo, G.4    Montecucco, C.5
  • 910
    • 0027385331 scopus 로고
    • The developmental onset of NMDA receptor-channel activity during neuronal migration
    • Rossi D.J., Slater N.T. The developmental onset of NMDA receptor-channel activity during neuronal migration. Neuropharmacology. 32:1993;1239-1248.
    • (1993) Neuropharmacology , vol.32 , pp. 1239-1248
    • Rossi, D.J.1    Slater, N.T.2
  • 911
    • 0029093040 scopus 로고
    • Properties of transmission at a giant glutamatergic synapse in cerebellum: The mossy fiber-unipolar brush cell synapse
    • Rossi D.J., Alford S., Mugnaini E., Slater N.T. Properties of transmission at a giant glutamatergic synapse in cerebellum: the mossy fiber-unipolar brush cell synapse. J. Neurophysiol. 74:1995;24-42.
    • (1995) J. Neurophysiol. , vol.74 , pp. 24-42
    • Rossi, D.J.1    Alford, S.2    Mugnaini, E.3    Slater, N.T.4
  • 912
    • 0034688312 scopus 로고    scopus 로고
    • Glutamate release in severe brain ischaemia is mainly by reversed uptake
    • Rossi D.J., Oshima T., Attwell D. Glutamate release in severe brain ischaemia is mainly by reversed uptake. Nature. 403:2000;316-321.
    • (2000) Nature , vol.403 , pp. 316-321
    • Rossi, D.J.1    Oshima, T.2    Attwell, D.3
  • 913
    • 0022620257 scopus 로고
    • Glutamate and the pathophysiology of hypoxic-ischemic brain damage
    • Rothman S.M., Olney J.W. Glutamate and the pathophysiology of hypoxic-ischemic brain damage. Ann. Neurol. 19:1986;105-111.
    • (1986) Ann. Neurol. , vol.19 , pp. 105-111
    • Rothman, S.M.1    Olney, J.W.2
  • 915
    • 0026597010 scopus 로고
    • Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis
    • Rothstein J.D., Martin L.J., Kuncl R.W. Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis. N. Engl. J. Med. 326:1992;1464-1468.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1464-1468
    • Rothstein, J.D.1    Martin, L.J.2    Kuncl, R.W.3
  • 917
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein J.D., Van Kammen M., Levey A.I., Martin L.J., Kuncl R.W. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann. Neurol. 38:1995;73-84.
    • (1995) Ann. Neurol. , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3    Martin, L.J.4    Kuncl, R.W.5
  • 918
    • 0033757857 scopus 로고    scopus 로고
    • Neuronal and glial glycine transporters have different stoichiometries
    • Roux M.J., Supplisson S. Neuronal and glial glycine transporters have different stoichiometries. Neuron. 25:2000;373-383.
    • (2000) Neuron , vol.25 , pp. 373-383
    • Roux, M.J.1    Supplisson, S.2
  • 919
    • 0032402093 scopus 로고    scopus 로고
    • Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms
    • Roy J., Minotti S., Dong L.C., Figlewicz D.A., Durham H.D. Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms. J. Neurosci. 18:1998;9673-9684.
    • (1998) J. Neurosci. , vol.18 , pp. 9673-9684
    • Roy, J.1    Minotti, S.2    Dong, L.C.3    Figlewicz, D.A.4    Durham, H.D.5
  • 920
    • 0032936851 scopus 로고    scopus 로고
    • The cell biology of the blood-brain barrier
    • Rubin L.L., Staddon J.M. The cell biology of the blood-brain barrier. Annu. Rev. Neurosci. 22:1999;11-28.
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 11-28
    • Rubin, L.L.1    Staddon, J.M.2
  • 921
    • 0032079863 scopus 로고    scopus 로고
    • Extrasynaptic glutamate diffusion in the hippocampus: Ultrastructural constraints, uptake, and receptor activation
    • Rusakov D.A., Kullmann D.M. Extrasynaptic glutamate diffusion in the hippocampus: ultrastructural constraints, uptake, and receptor activation. J. Neurosci. 18:1998;3158-3170.
    • (1998) J. Neurosci. , vol.18 , pp. 3158-3170
    • Rusakov, D.A.1    Kullmann, D.M.2
  • 922
    • 0031780158 scopus 로고    scopus 로고
    • Synapses in hippocampus occupy only 1-2% of cell membranes and are spaced less than half-micron apart: A quantitative ultrastructural analysis with discussion of physiological implications
    • Rusakov D.A., Harrison E., Stewart M.G. Synapses in hippocampus occupy only 1-2% of cell membranes and are spaced less than half-micron apart: a quantitative ultrastructural analysis with discussion of physiological implications. Neuropharmacology. 37:1998;513-521.
    • (1998) Neuropharmacology , vol.37 , pp. 513-521
    • Rusakov, D.A.1    Harrison, E.2    Stewart, M.G.3
  • 923
    • 0033199358 scopus 로고    scopus 로고
    • Hippocampal synapses: Do they talk to their neighbours?
    • Rusakov D.A., Kullmann D.M., Stewart M.G. Hippocampal synapses: do they talk to their neighbours? Trends Neurosci. 22:1999;382-388.
    • (1999) Trends Neurosci. , vol.22 , pp. 382-388
    • Rusakov, D.A.1    Kullmann, D.M.2    Stewart, M.G.3
  • 924
    • 0027203938 scopus 로고
    • Expression of the metabotropic glutamate receptor mGluR1-alpha and the ionotropic glutamate receptor GluR1 in the brain during the postnatal development of normal mouse and in the cerebellum from mutant mice
    • Ryo Y., Miyawaki A., Furuichi T., Mikoshiba K. Expression of the metabotropic glutamate receptor mGluR1-alpha and the ionotropic glutamate receptor GluR1 in the brain during the postnatal development of normal mouse and in the cerebellum from mutant mice. J. Neurosci. Res. 36:1993;19-32.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 19-32
    • Ryo, Y.1    Miyawaki, A.2    Furuichi, T.3    Mikoshiba, K.4
  • 925
    • 0019866893 scopus 로고
    • Sodium gradient- And sodium plus potassium gradient-dependent L-glutamate uptake in renal basolateral membrane vesicles
    • Sacktor B., Rosenbloom I.L., Liang C.T., Cheng L. Sodium gradient- and sodium plus potassium gradient-dependent L-glutamate uptake in renal basolateral membrane vesicles. J. Membr. Biol. 60:1981;63-71.
    • (1981) J. Membr. Biol. , vol.60 , pp. 63-71
    • Sacktor, B.1    Rosenbloom, I.L.2    Liang, C.T.3    Cheng, L.4
  • 926
    • 0029818933 scopus 로고    scopus 로고
    • SDS-resistant aggregation of membrane proteins: Application to the purification of the vesicular monoamine transporter
    • Sagné C., Isambert M.F., Henry J.P., Gasnier B. SDS-resistant aggregation of membrane proteins: application to the purification of the vesicular monoamine transporter. Biochem. J. 316:1996;825-831.
    • (1996) Biochem. J. , vol.316 , pp. 825-831
    • Sagné, C.1    Isambert, M.F.2    Henry, J.P.3    Gasnier, B.4
  • 927
    • 0030840107 scopus 로고    scopus 로고
    • Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases
    • Sagné C., Elmestikawy S., Isambert M.F., Hamon M., Henry J.P., Giros B., Gasnier B. Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases. FEBS Lett. 417:1997;177-183.
    • (1997) FEBS Lett. , vol.417 , pp. 177-183
    • Sagné, C.1    Elmestikawy, S.2    Isambert, M.F.3    Hamon, M.4    Henry, J.P.5    Giros, B.6    Gasnier, B.7
  • 928
    • 0032902048 scopus 로고    scopus 로고
    • Eukaryotic transmembrane solute transport systems
    • Saier M.H. Eukaryotic transmembrane solute transport systems. Int. Rev. Cytol. 190:1999;61-136.
    • (1999) Int. Rev. Cytol. , vol.190 , pp. 61-136
    • Saier, M.H.1
  • 930
    • 0030580450 scopus 로고    scopus 로고
    • Involvement of the glutamatergic metabotropic receptors in the regulation of glutamate uptake and extracellular excitatory amino acid levels in the striatum of chloral hydrate-anesthetized rats
    • Samuel D., Pisano P., Forni C., Nieoullon A., Kerkerian-Le Goff L. Involvement of the glutamatergic metabotropic receptors in the regulation of glutamate uptake and extracellular excitatory amino acid levels in the striatum of chloral hydrate-anesthetized rats. Brain Res. 739:1996;156-162.
    • (1996) Brain Res. , vol.739 , pp. 156-162
    • Samuel, D.1    Pisano, P.2    Forni, C.3    Nieoullon, A.4    Kerkerian-Le Goff, L.5
  • 931
    • 0023819058 scopus 로고
    • 2+-independent release of glutamate during anoxia in isolated nerve terminals (synaptosomes)
    • 2+-independent release of glutamate during anoxia in isolated nerve terminals (synaptosomes). J. Neurochem. 50:1988;1322-1324.
    • (1988) J. Neurochem. , vol.50 , pp. 1322-1324
    • Sánchez-Prieto, J.1    González, P.2
  • 933
    • 0022485129 scopus 로고
    • Extracellular overflow of neuroactive amino acids during severe insulin-induced hypoglycemia: In vivo dialysis of the rat hippocampus
    • Sandberg M., Butcher S.P., Hagberg H. Extracellular overflow of neuroactive amino acids during severe insulin-induced hypoglycemia: in vivo dialysis of the rat hippocampus. J. Neurochem. 47:1986;178-184.
    • (1986) J. Neurochem. , vol.47 , pp. 178-184
    • Sandberg, M.1    Butcher, S.P.2    Hagberg, H.3
  • 934
    • 0025360371 scopus 로고
    • Glutamate uptake in mammalian retinal glia is voltage-dependent and potassium-dependent
    • Sarantis M., Attwell D. Glutamate uptake in mammalian retinal glia is voltage-dependent and potassium-dependent. Brain Res. 516:1990;322-325.
    • (1990) Brain Res. , vol.516 , pp. 322-325
    • Sarantis, M.1    Attwell, D.2
  • 935
    • 0023856913 scopus 로고
    • A presynaptic action of glutamate at the cone output synapse
    • Sarantis M., Everett K., Attwell D. A presynaptic action of glutamate at the cone output synapse. Nature. 332:1988;451-453.
    • (1988) Nature , vol.332 , pp. 451-453
    • Sarantis, M.1    Everett, K.2    Attwell, D.3
  • 936
    • 0027375540 scopus 로고
    • Glutamate uptake from the synaptic cleft does not shape the decay of the non-NMDA component of the synaptic current
    • Sarantis M., Ballerini L., Miller B., Silver R.A., Edwards M., Attwell D. Glutamate uptake from the synaptic cleft does not shape the decay of the non-NMDA component of the synaptic current. Neuron. 11:1993;541-549.
    • (1993) Neuron , vol.11 , pp. 541-549
    • Sarantis, M.1    Ballerini, L.2    Miller, B.3    Silver, R.A.4    Edwards, M.5    Attwell, D.6
  • 937
    • 0033607715 scopus 로고    scopus 로고
    • Deficits of NMDA receptors and glutamate uptake sites in the frontal cortex in AIDS
    • Sardar A.M., Hutson P.H., Reynolds G.P. Deficits of NMDA receptors and glutamate uptake sites in the frontal cortex in AIDS. Neuroreport. 10:1999;3513-3515.
    • (1999) Neuroreport , vol.10 , pp. 3513-3515
    • Sardar, A.M.1    Hutson, P.H.2    Reynolds, G.P.3
  • 938
    • 0033938202 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 1 and 2 immunoreactivity in the spinal cord in amyotrophic lateral sclerosis
    • Sasaki S., Komori T., Iwata M. Excitatory amino acid transporter 1 and 2 immunoreactivity in the spinal cord in amyotrophic lateral sclerosis. Acta Neuropathol. (Berl.). 100:2000;138-144.
    • (2000) Acta Neuropathol. (Berl.) , vol.100 , pp. 138-144
    • Sasaki, S.1    Komori, T.2    Iwata, M.3
  • 939
    • 0031854439 scopus 로고    scopus 로고
    • Neurotransmitters and their receptors in the islets of Langerhans of the pancreas - What messages do acetylcholine, glutamate, and GABA transmit
    • Satin L.S., Kinard T.A. Neurotransmitters and their receptors in the islets of Langerhans of the pancreas - what messages do acetylcholine, glutamate, and GABA transmit. Endocrine. 8:1998;213-223.
    • (1998) Endocrine , vol.8 , pp. 213-223
    • Satin, L.S.1    Kinard, T.A.2
  • 940
    • 0029057036 scopus 로고
    • Induction of cystine transport activity in mouse peritoneal macrophages by bacterial lipopolysaccharide
    • Sato H., Fujiwara K., Sagara J., Bannai S. Induction of cystine transport activity in mouse peritoneal macrophages by bacterial lipopolysaccharide. Biochem. J. 310:1995;547-551.
    • (1995) Biochem. J. , vol.310 , pp. 547-551
    • Sato, H.1    Fujiwara, K.2    Sagara, J.3    Bannai, S.4
  • 941
    • 0033597349 scopus 로고    scopus 로고
    • Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins
    • Sato H., Tamba M., Ishii T., Bannai S. Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins. J. Biol. Chem. 274:1999;11455-11458.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3    Bannai, S.4
  • 942
    • 0028818536 scopus 로고
    • Modulation of a recombinant glycine transporter (GLYT1b) by activation of protein kinase C
    • Sato K., Adams R., Betz H., Schloss P. Modulation of a recombinant glycine transporter (GLYT1b) by activation of protein kinase C. J. Neurochem. 65:1995;1967-1973.
    • (1995) J. Neurochem. , vol.65 , pp. 1967-1973
    • Sato, K.1    Adams, R.2    Betz, H.3    Schloss, P.4
  • 943
    • 0028793381 scopus 로고
    • The recombinant GABA transporter GAT1 is downregulated upon activation of protein kinase C
    • Sato K., Betz H., Schloss P. The recombinant GABA transporter GAT1 is downregulated upon activation of protein kinase C. FEBS Lett. 375:1995;99-102.
    • (1995) FEBS Lett. , vol.375 , pp. 99-102
    • Sato, K.1    Betz, H.2    Schloss, P.3
  • 944
    • 0034056041 scopus 로고    scopus 로고
    • Inherited defects of sodium-dependent glutamate transport mediated by glutamate/aspartate transporter in canine red cells due to a decreased level of transporter protein expression
    • Sato K., Inaba M., Suwa Y., Matsuu A., Hikasa Y., Ono K., Kagota K. Inherited defects of sodium-dependent glutamate transport mediated by glutamate/aspartate transporter in canine red cells due to a decreased level of transporter protein expression. J. Biol. Chem. 275:2000;6620-6627.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6620-6627
    • Sato, K.1    Inaba, M.2    Suwa, Y.3    Matsuu, A.4    Hikasa, Y.5    Ono, K.6    Kagota, K.7
  • 945
    • 0031884393 scopus 로고    scopus 로고
    • Apoptosis in neurological disease
    • Savitz S.I., Rosenbaum D.M. Apoptosis in neurological disease. Neurosurgery. 42:1998;555-572.
    • (1998) Neurosurgery , vol.42 , pp. 555-572
    • Savitz, S.I.1    Rosenbaum, D.M.2
  • 946
    • 17644448326 scopus 로고
    • Amplification of glutamate-induced oxidative stress
    • Savolainen K.M., Loikkanen J., Naarala J. Amplification of glutamate-induced oxidative stress. Toxicol. Lett. 82-83:1995;399-405.
    • (1995) Toxicol. Lett. , vol.8283 , pp. 399-405
    • Savolainen, K.M.1    Loikkanen, J.2    Naarala, J.3
  • 947
    • 0031036195 scopus 로고    scopus 로고
    • Use-dependent increases in glutamate concentration activate presynaptic metabotropic glutamate receptors
    • Scanziani M., Salin P.A., Vogt K.E., Malenka R.C., Nicoll R.A. Use-dependent increases in glutamate concentration activate presynaptic metabotropic glutamate receptors. Nature. 385:1997;630-634.
    • (1997) Nature , vol.385 , pp. 630-634
    • Scanziani, M.1    Salin, P.A.2    Vogt, K.E.3    Malenka, R.C.4    Nicoll, R.A.5
  • 948
    • 0030820683 scopus 로고    scopus 로고
    • Quantitative ultrastructural analysis of hippocampal excitatory synapses
    • Schikorski T., Stevens C.F. Quantitative ultrastructural analysis of hippocampal excitatory synapses. J. Neurosci. 17:1997;5858-5867.
    • (1997) J. Neurosci. , vol.17 , pp. 5858-5867
    • Schikorski, T.1    Stevens, C.F.2
  • 949
    • 0029810095 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a primary event in glutamate neurotoxicity
    • Schinder A.F., Olson E.C., Spitzer N.C., Montal M. Mitochondrial dysfunction is a primary event in glutamate neurotoxicity. J. Neurosci. 16:1996;6125-6133.
    • (1996) J. Neurosci. , vol.16 , pp. 6125-6133
    • Schinder, A.F.1    Olson, E.C.2    Spitzer, N.C.3    Montal, M.4
  • 951
    • 0023926959 scopus 로고
    • 3H]aspartate during postnatal development of the hippocampal formation: A quantitative autoradiographic study
    • 3H]aspartate during postnatal development of the hippocampal formation: a quantitative autoradiographic study. Exp. Brain Res. 70:1988;50-54.
    • (1988) Exp. Brain Res. , vol.70 , pp. 50-54
    • Schmidt, W.1    Wolf, G.2
  • 952
    • 0029880185 scopus 로고    scopus 로고
    • Expression of the glutamate transporter GLT1 in neural cells of the rat central nervous system: Non-radioactive in situ hybridization and comparative immunocytochemistry
    • Schmitt A., Asan E., Püschel B., Jöns T., Kugler P. Expression of the glutamate transporter GLT1 in neural cells of the rat central nervous system: non-radioactive in situ hybridization and comparative immunocytochemistry. Neuroscience. 71:1996;989-1004.
    • (1996) Neuroscience , vol.71 , pp. 989-1004
    • Schmitt, A.1    Asan, E.2    Püschel, B.3    Jöns, T.4    Kugler, P.5
  • 953
    • 0031024715 scopus 로고    scopus 로고
    • Cellular and regional distribution of the glutamate transporter GLAST in the CNS of rats: Nonradioactive in situ hybridization and comparative immunocytochemistry
    • Schmitt A., Asan E., Püschel B., Kugler P. Cellular and regional distribution of the glutamate transporter GLAST in the CNS of rats: nonradioactive in situ hybridization and comparative immunocytochemistry. J. Neurosci. 17:1997;1-10.
    • (1997) J. Neurosci. , vol.17 , pp. 1-10
    • Schmitt, A.1    Asan, E.2    Püschel, B.3    Kugler, P.4
  • 954
    • 0000210569 scopus 로고
    • Zur kenntnis des ikterus neonatorum
    • Schmorl G. Zur kenntnis des ikterus neonatorum. Verh. Dtsch. Pathol. Ges. 6:1904;109-115.
    • (1904) Verh. Dtsch. Pathol. Ges. , vol.6 , pp. 109-115
    • Schmorl, G.1
  • 955
    • 0019170323 scopus 로고
    • Sodium gradient-dependent L-glutamate transport in renal brush border membrane vesicles
    • Schneider E.G., Hammerman M.R., Sacktor B. Sodium gradient-dependent L-glutamate transport in renal brush border membrane vesicles. J. Biol. Chem. 255:1980;7650-7656.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7650-7656
    • Schneider, E.G.1    Hammerman, M.R.2    Sacktor, B.3
  • 957
    • 0032484645 scopus 로고    scopus 로고
    • Chronic neuroleptic treatment alters expression of glial glutamate transporter GLT-1 mRNA in the striatum
    • Schneider J.S., Wade T., Lidsky T.I. Chronic neuroleptic treatment alters expression of glial glutamate transporter GLT-1 mRNA in the striatum. Neuroreport. 9:1998;133-136.
    • (1998) Neuroreport , vol.9 , pp. 133-136
    • Schneider, J.S.1    Wade, T.2    Lidsky, T.I.3
  • 959
    • 0032834028 scopus 로고    scopus 로고
    • Pharmacological agents acting at subtypes of metabotropic glutamate receptors
    • Schoepp D.D., Jane D.E., Monn J.A. Pharmacological agents acting at subtypes of metabotropic glutamate receptors. Neuropharmacology. 38:1999;1431-1476.
    • (1999) Neuropharmacology , vol.38 , pp. 1431-1476
    • Schoepp, D.D.1    Jane, D.E.2    Monn, J.A.3
  • 960
    • 0019347565 scopus 로고
    • Transport and metabolism of glutamate and GABA in neurons and glial cells
    • Schousboe A. Transport and metabolism of glutamate and GABA in neurons and glial cells. Int. Rev. Neurobiol. 22:1981;1-45.
    • (1981) Int. Rev. Neurobiol. , vol.22 , pp. 1-45
    • Schousboe, A.1
  • 961
    • 0017233051 scopus 로고
    • Postnatal alterations in effects of potassium on uptake and release of glutamate and GABA in rat brain cortex slices
    • Schousboe A., Lisy V., Hertz L. Postnatal alterations in effects of potassium on uptake and release of glutamate and GABA in rat brain cortex slices. J. Neurochem. 26:1976;1023-1027.
    • (1976) J. Neurochem. , vol.26 , pp. 1023-1027
    • Schousboe, A.1    Lisy, V.2    Hertz, L.3
  • 962
    • 0028912433 scopus 로고
    • Vesicular neurotransmitter transporters: From bacteria to humans
    • Schuldiner S., Shirvan A., Linial M. Vesicular neurotransmitter transporters: from bacteria to humans. Physiol. Rev. 75:1995;369-392.
    • (1995) Physiol. Rev. , vol.75 , pp. 369-392
    • Schuldiner, S.1    Shirvan, A.2    Linial, M.3
  • 963
    • 0028849016 scopus 로고
    • UDP galactose:ceramide galactosyltransferase and glutamate aspartate transporter-copurification, separation and characterization of the two glycoproteins
    • Schulte S., Stoffel W. UDP galactose:ceramide galactosyltransferase and glutamate aspartate transporter-copurification, separation and characterization of the two glycoproteins. Eur. J. Biochem. 233:1995;947-953.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 947-953
    • Schulte, S.1    Stoffel, W.2
  • 964
    • 0030604659 scopus 로고    scopus 로고
    • Immunocytochemical localization of the high-affinity glutamate transporter, EAACl, in the retina of representative vertebrate species
    • Schultz K., Stell W.K. Immunocytochemical localization of the high-affinity glutamate transporter, EAACl, in the retina of representative vertebrate species. Neurosci. Lett. 211:1996;191-194.
    • (1996) Neurosci. Lett. , vol.211 , pp. 191-194
    • Schultz, K.1    Stell, W.K.2
  • 965
    • 0028961895 scopus 로고
    • Variant forms of neuronal glutamate transporter sites in Alzheimer's disease cerebral cortex
    • Scott H.L., Tannenberg A.E.G., Dodd P.R. Variant forms of neuronal glutamate transporter sites in Alzheimer's disease cerebral cortex. J. Neurochem. 64:1995;2193-2202.
    • (1995) J. Neurochem. , vol.64 , pp. 2193-2202
    • Scott, H.L.1    Tannenberg, A.E.G.2    Dodd, P.R.3
  • 966
    • 0032434691 scopus 로고    scopus 로고
    • A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation
    • Seal R.P., Amara S.G. A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation. Neuron. 21:1998;1487-1498.
    • (1998) Neuron , vol.21 , pp. 1487-1498
    • Seal, R.P.1    Amara, S.G.2
  • 967
    • 0032925862 scopus 로고    scopus 로고
    • Excitatory amino acid transporters: A family in flux
    • Seal R.P., Amara S.G. Excitatory amino acid transporters: a family in flux. Annu. Rev. Pharmacol. Toxicol. 39:1999;431-456.
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 431-456
    • Seal, R.P.1    Amara, S.G.2
  • 968
    • 0031815580 scopus 로고    scopus 로고
    • Identification and characterization of a cDNA encoding a neuronal glutamate transporter from Drosophila melanogaster
    • Seal R.P., Daniels G.M., Wolfgang W.J., Forte M.A., Amara S.G. Identification and characterization of a cDNA encoding a neuronal glutamate transporter from Drosophila melanogaster. Receptors Channels. 6:1998;51-64.
    • (1998) Receptors Channels , vol.6 , pp. 51-64
    • Seal, R.P.1    Daniels, G.M.2    Wolfgang, W.J.3    Forte, M.A.4    Amara, S.G.5
  • 969
    • 0033681163 scopus 로고    scopus 로고
    • A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines
    • Seal R.P., Leighton B.H., Amara S.G. A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines. Neuron. 25:2000;695-706.
    • (2000) Neuron , vol.25 , pp. 695-706
    • Seal, R.P.1    Leighton, B.H.2    Amara, S.G.3
  • 970
    • 0034649477 scopus 로고    scopus 로고
    • Increasing mortality from amyotrophic lateral sclerosis in Norway?
    • Seljeseth Y.M., Vollset S.E., Tysnes O.B. Increasing mortality from amyotrophic lateral sclerosis in Norway? Neurology. 55:2000;1262-1266.
    • (2000) Neurology , vol.55 , pp. 1262-1266
    • Seljeseth, Y.M.1    Vollset, S.E.2    Tysnes, O.B.3
  • 971
    • 0033710845 scopus 로고    scopus 로고
    • Modulation of GABAergic signaling among interneurons by metabotropic glutamate receptors
    • Semyanov A., Kullmann D.M. Modulation of GABAergic signaling among interneurons by metabotropic glutamate receptors. Neuron. 25:2000;663-672.
    • (2000) Neuron , vol.25 , pp. 663-672
    • Semyanov, A.1    Kullmann, D.M.2
  • 973
    • 0021907132 scopus 로고
    • Multiple synaptic receptors for neuroactive amino acid transmitters - New vistas
    • Sharif N.A. Multiple synaptic receptors for neuroactive amino acid transmitters - new vistas. Int. Rev. Neurobiol. 26:1985;85-150.
    • (1985) Int. Rev. Neurobiol. , vol.26 , pp. 85-150
    • Sharif, N.A.1
  • 974
    • 0027488129 scopus 로고
    • Cloning and characterization of a glutamate transporter cDNA from human cerebellum
    • Shashidharan P., Plaitakis A. Cloning and characterization of a glutamate transporter cDNA from human cerebellum. Biochim. Biophys. Acta. 1216:1993;161-164.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 161-164
    • Shashidharan, P.1    Plaitakis, A.2
  • 975
    • 0028234978 scopus 로고
    • Molecular cloning of human brain glutamate/aspartate transporter II
    • Shashidharan P., Wittenberg I., Plaitakis A. Molecular cloning of human brain glutamate/aspartate transporter II. Biochim. Biophys. Acta. 1191:1994;393-396.
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 393-396
    • Shashidharan, P.1    Wittenberg, I.2    Plaitakis, A.3
  • 976
    • 0028127303 scopus 로고
    • Neuron-specific human glutamate transporter: Molecular cloning, characterization and expression in human brain
    • Shashidharan P., Huntley G.W., Meyer T., Morrison J.H., Plaitakis A. Neuron-specific human glutamate transporter: molecular cloning, characterization and expression in human brain. Brain Res. 662:1994;245-250.
    • (1994) Brain Res. , vol.662 , pp. 245-250
    • Shashidharan, P.1    Huntley, G.W.2    Meyer, T.3    Morrison, J.H.4    Plaitakis, A.5
  • 977
    • 0030716444 scopus 로고    scopus 로고
    • Immunohistochemical localization of the neuron-specific glutamate transporter EAAC1 (EAAT3) in rat brain and spinal cord revealed by a novel monoclonal antibody
    • Shashidharan P., Huntley G.W., Murray J.M., Buku A., Moran T., Walsh M.J., Morrison J.H., Plaitakis A. Immunohistochemical localization of the neuron-specific glutamate transporter EAAC1 (EAAT3) in rat brain and spinal cord revealed by a novel monoclonal antibody. Brain Res. 773:1997;139-148.
    • (1997) Brain Res. , vol.773 , pp. 139-148
    • Shashidharan, P.1    Huntley, G.W.2    Murray, J.M.3    Buku, A.4    Moran, T.5    Walsh, M.J.6    Morrison, J.H.7    Plaitakis, A.8
  • 978
    • 0032709462 scopus 로고    scopus 로고
    • Calcium, glutamate, and amyotrophic lateral sclerosis: More evidence but no certainties
    • Shaw P.J. Calcium, glutamate, and amyotrophic lateral sclerosis: more evidence but no certainties. Ann. Neurol. 46:1999;803-805.
    • (1999) Ann. Neurol. , vol.46 , pp. 803-805
    • Shaw, P.J.1
  • 979
    • 0028168346 scopus 로고
    • 3H]D-Aspartate binding sites in the normal human spinal cord and changes in motor neuron disease: A quantitative autoradiographic study
    • 3H]D-Aspartate binding sites in the normal human spinal cord and changes in motor neuron disease: a quantitative autoradiographic study. Brain Res. 655:1994;195-201.
    • (1994) Brain Res. , vol.655 , pp. 195-201
    • Shaw, P.J.1    Chinnery, R.M.2    Ince, P.G.3
  • 980
    • 0029082389 scopus 로고
    • Oxidative damage to protein in sporadic motor neuron disease spinal cord
    • Shaw P.J., Ince P.G., Falkous G., Mantle D. Oxidative damage to protein in sporadic motor neuron disease spinal cord. Ann. Neurol. 38:1995;691-695.
    • (1995) Ann. Neurol. , vol.38 , pp. 691-695
    • Shaw, P.J.1    Ince, P.G.2    Falkous, G.3    Mantle, D.4
  • 982
    • 0033103308 scopus 로고    scopus 로고
    • Mature hippocampal astrocytes exhibit functional metabotropic and ionotropic glutamate receptors in situ
    • Shelton M.K., McCarthy K.D. Mature hippocampal astrocytes exhibit functional metabotropic and ionotropic glutamate receptors in situ. Glia. 26:1999;1-11.
    • (1999) Glia , vol.26 , pp. 1-11
    • Shelton, M.K.1    McCarthy, K.D.2
  • 983
    • 0024994811 scopus 로고
    • Increased glutamate uptake and glutamine synthetase activity in neuronal cell cultures surviving chronic hypoxia
    • Sher P.K., Hu S.X. Increased glutamate uptake and glutamine synthetase activity in neuronal cell cultures surviving chronic hypoxia. Glia. 3:1990;350-357.
    • (1990) Glia , vol.3 , pp. 350-357
    • Sher, P.K.1    Hu, S.X.2
  • 984
    • 0033546052 scopus 로고    scopus 로고
    • Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation
    • Shi S.H., Hayashi Y., Petralia R.S., Zaman S.H., Wenthold R.J., Svoboda K., Malinow R. Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation. Science. 284:1999;1811-1816.
    • (1999) Science , vol.284 , pp. 1811-1816
    • Shi, S.H.1    Hayashi, Y.2    Petralia, R.S.3    Zaman, S.H.4    Wenthold, R.J.5    Svoboda, K.6    Malinow, R.7
  • 985
    • 0029865144 scopus 로고    scopus 로고
    • Dynamic changes in expression of glutamate transporter mRNAs in developing brain
    • Shibata T., Watanabe M., Tanaka K., Wada K., Inoue Y. Dynamic changes in expression of glutamate transporter mRNAs in developing brain. Neuroreport. 7:1996;705-709.
    • (1996) Neuroreport , vol.7 , pp. 705-709
    • Shibata, T.1    Watanabe, M.2    Tanaka, K.3    Wada, K.4    Inoue, Y.5
  • 986
    • 0030724776 scopus 로고    scopus 로고
    • Glutamate transporter GLAST is expressed in the radial glia-astrocyte lineage of developing mouse spinal cord
    • Shibata T., Yamada K., Watanabe M., Ikenaka K., Wada K. Glutamate transporter GLAST is expressed in the radial glia-astrocyte lineage of developing mouse spinal cord. J. Neurosci. 17:1997;9212-9219.
    • (1997) J. Neurosci. , vol.17 , pp. 9212-9219
    • Shibata, T.1    Yamada, K.2    Watanabe, M.3    Ikenaka, K.4    Wada, K.5
  • 988
    • 0025797354 scopus 로고
    • Synthesis of four diastereomeric L-2-(carboxycyclopropyl)glycines. Conformationally constrained L-glutamate analogues
    • Shimamoto K., Ishida M., Shinozaki H., Ohfune Y. Synthesis of four diastereomeric L-2-(carboxycyclopropyl)glycines. Conformationally constrained L-glutamate analogues. J. Org. Chem. 56:1991;4167-4176.
    • (1991) J. Org. Chem. , vol.56 , pp. 4167-4176
    • Shimamoto, K.1    Ishida, M.2    Shinozaki, H.3    Ohfune, Y.4
  • 991
    • 0022838813 scopus 로고
    • Acromelic acid, a novel excitatory amino acid from a poisonous mushroom: Effects on the crayfish neuromuscular junction
    • Shinozaki H., Ishida M., Okamoto T. Acromelic acid, a novel excitatory amino acid from a poisonous mushroom: effects on the crayfish neuromuscular junction. Brain Res. 399:1986;395-398.
    • (1986) Brain Res. , vol.399 , pp. 395-398
    • Shinozaki, H.1    Ishida, M.2    Okamoto, T.3
  • 992
    • 0024843541 scopus 로고
    • Potent NMDA-like actions and potentiation of glutamate responses by conformational variants of a glutamate analogue in the rat spinal cord
    • Shinozaki H., Ishida M., Shimamoto K., Ohfune Y. Potent NMDA-like actions and potentiation of glutamate responses by conformational variants of a glutamate analogue in the rat spinal cord. Br. J. Pharmacol. 98:1989;1213-1224.
    • (1989) Br. J. Pharmacol. , vol.98 , pp. 1213-1224
    • Shinozaki, H.1    Ishida, M.2    Shimamoto, K.3    Ohfune, Y.4
  • 993
    • 0026746392 scopus 로고
    • Immunogold quantification of glutamate in two types of excitatory synapse with different firing patterns
    • Shupliakov O., Brodin L., Cullheim S., Ottersen O.P., Storm-Mathisen J. Immunogold quantification of glutamate in two types of excitatory synapse with different firing patterns. J. Neurosci. 12:1992;3789-3803.
    • (1992) J. Neurosci. , vol.12 , pp. 3789-3803
    • Shupliakov, O.1    Brodin, L.2    Cullheim, S.3    Ottersen, O.P.4    Storm-Mathisen, J.5
  • 995
    • 0029810307 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis
    • Siddique T., Deng H.X. Genetics of amyotrophic lateral sclerosis. Hum. Mol. Genet. 5:1996;1465-1470.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1465-1470
    • Siddique, T.1    Deng, H.X.2
  • 996
    • 0014138169 scopus 로고
    • The effects of unconjugated bilirubin and related pigments on cultures of rat cerebellum
    • Silberberg D.H., Schutta H.S. The effects of unconjugated bilirubin and related pigments on cultures of rat cerebellum. J. Neuropathol. Exp. Neurol. 26:1967;572-583.
    • (1967) J. Neuropathol. Exp. Neurol. , vol.26 , pp. 572-583
    • Silberberg, D.H.1    Schutta, H.S.2
  • 997
    • 0033547349 scopus 로고    scopus 로고
    • Inhibition of glutamate uptake by unconjugated bilirubin in cultured cortical rat astrocytes: Role of concentration and pH
    • Silva R., Mata L.R., Gulbenkian S., Brito M.A., Tiribelli C., Brites D. Inhibition of glutamate uptake by unconjugated bilirubin in cultured cortical rat astrocytes: role of concentration and pH. Biochem. Biophys. Res. Commun. 265:1999;67-72.
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 67-72
    • Silva, R.1    Mata, L.R.2    Gulbenkian, S.3    Brito, M.A.4    Tiribelli, C.5    Brites, D.6
  • 998
    • 0033582705 scopus 로고    scopus 로고
    • Changes in expression of neuronal and glial glutamate transporters in rat hippocampus following kainate-induced seizure activity
    • Simantov R., Crispino M., Hoc W., Broutman G., Tocco G., Rothstein J.D., Baudry M. Changes in expression of neuronal and glial glutamate transporters in rat hippocampus following kainate-induced seizure activity. Mol. Brain Res. 65:1999;112-123.
    • (1999) Mol. Brain Res. , vol.65 , pp. 112-123
    • Simantov, R.1    Crispino, M.2    Hoc, W.3    Broutman, G.4    Tocco, G.5    Rothstein, J.D.6    Baudry, M.7
  • 999
    • 0021743001 scopus 로고
    • Blockade of N-methyl-D-aspartate receptors may protect against ischemic damage in the brain
    • Simon R.P., Swan J.H., Griffiths T., Meldrum B.S. Blockade of N-methyl-D-aspartate receptors may protect against ischemic damage in the brain. Science. 226:1984;850-852.
    • (1984) Science , vol.226 , pp. 850-852
    • Simon, R.P.1    Swan, J.H.2    Griffiths, T.3    Meldrum, B.S.4
  • 1000
    • 0027289605 scopus 로고
    • Mitochondrial impairment reduces the threshold for in vivo NMDA-mediated neuronal death in the striatum
    • Simpson J.R., Isacson O. Mitochondrial impairment reduces the threshold for in vivo NMDA-mediated neuronal death in the striatum. Exp. Neurol. 121:1993;57-64.
    • (1993) Exp. Neurol. , vol.121 , pp. 57-64
    • Simpson, J.R.1    Isacson, O.2
  • 1002
    • 0032530782 scopus 로고    scopus 로고
    • Comparison of glutamate and gamma-aminobutyric acid uptake binding sites in frontal and temporal lobes in schizophrenia
    • Simpson M.D.C., Slater P., Deakin J.F.W. Comparison of glutamate and gamma-aminobutyric acid uptake binding sites in frontal and temporal lobes in schizophrenia. Biol. Psychiatry. 44:1998;423-427.
    • (1998) Biol. Psychiatry , vol.44 , pp. 423-427
    • Simpson, M.D.C.1    Slater, P.2    Deakin, J.F.W.3
  • 1003
    • 0032862658 scopus 로고    scopus 로고
    • Expression patterns and regulation of glutamate transporters in the developing and adult nervous system
    • Sims K.D., Robinson M.B. Expression patterns and regulation of glutamate transporters in the developing and adult nervous system. Crit. Rev. Neurobiol. 13:1999;169-197.
    • (1999) Crit. Rev. Neurobiol. , vol.13 , pp. 169-197
    • Sims, K.D.1    Robinson, M.B.2
  • 1004
    • 0034681452 scopus 로고    scopus 로고
    • Platelet-derived growth factor rapidly increases activity and cell surface expression of the EAAC1 subtype of glutamate transporter through activation of phosphatidylinositol 3-kinase
    • Sims K.D., Straff D.J., Robinson M.B. Platelet-derived growth factor rapidly increases activity and cell surface expression of the EAAC1 subtype of glutamate transporter through activation of phosphatidylinositol 3-kinase. J. Biol. Chem. 275:2000;5228-5237.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5228-5237
    • Sims, K.D.1    Straff, D.J.2    Robinson, M.B.3
  • 1005
    • 0020060041 scopus 로고
    • Transport of L-aspartate and L-glutamate in plasma-membrane vesicles from rat liver
    • Sips H.J., De Graaf P.A., van Dam K. Transport of L-aspartate and L-glutamate in plasma-membrane vesicles from rat liver. Eur. J. Biochem. 122:1982;259-264.
    • (1982) Eur. J. Biochem. , vol.122 , pp. 259-264
    • Sips, H.J.1    De Graaf, P.A.2    Van Dam, K.3
  • 1006
    • 0026568217 scopus 로고
    • Loss of excitatory amino acid transport sites after lesioning a glutamatergic pathway in rat brain
    • Slater P., Simpson M.D.C., Hunter A.J., Cross A.J. Loss of excitatory amino acid transport sites after lesioning a glutamatergic pathway in rat brain. Neurosci. Res. Commun. 10:1992;135-140.
    • (1992) Neurosci. Res. Commun. , vol.10 , pp. 135-140
    • Slater, P.1    Simpson, M.D.C.2    Hunter, A.J.3    Cross, A.J.4
  • 1007
    • 0029913959 scopus 로고    scopus 로고
    • Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family
    • Slotboom D.J., Lolkema J.S., Konings W.N. Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family. J. Biol. Chem. 271:1996;31317-31321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31317-31321
    • Slotboom, D.J.1    Lolkema, J.S.2    Konings, W.N.3
  • 1008
    • 0033431036 scopus 로고    scopus 로고
    • A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive reentrant loop
    • Slotboom D.J., Sobczak I., Konings W.N., Lolkema J.S. A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive reentrant loop. Proc. Natl. Acad. Sci. USA. 96:1999;14282-14287.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14282-14287
    • Slotboom, D.J.1    Sobczak, I.2    Konings, W.N.3    Lolkema, J.S.4
  • 1010
    • 0030330291 scopus 로고    scopus 로고
    • Mitochondrial metabolite carrier family, topology, structure and functional properties: An overview
    • Sluse F.E. Mitochondrial metabolite carrier family, topology, structure and functional properties: an overview. Acta Biochim. Pol. 43:1996;349-360.
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 349-360
    • Sluse, F.E.1
  • 1014
    • 0028217120 scopus 로고
    • Assignment of the gene coding for the human high-affinity glutamate transporter EAAC1 to 9p24-potential role in dicarboxylic aminoaciduria and neurodegenerative disorders - Brief report
    • Smith C.P., Weremowicz S., Kanai Y., Stelzner M., Morton C.C., Hediger M.A. Assignment of the gene coding for the human high-affinity glutamate transporter EAAC1 to 9p24-potential role in dicarboxylic aminoaciduria and neurodegenerative disorders - brief report. Genomics. 20:1994;335-336.
    • (1994) Genomics , vol.20 , pp. 335-336
    • Smith, C.P.1    Weremowicz, S.2    Kanai, Y.3    Stelzner, M.4    Morton, C.C.5    Hediger, M.A.6
  • 1015
    • 0026772797 scopus 로고
    • Cloning and expression of a glycine transporter reveal colocalization with NMDA receptors
    • Smith K.E., Borden L.A., Hartig P.R., Branchek T., Weinshank R.L. Cloning and expression of a glycine transporter reveal colocalization with NMDA receptors. Neuron. 8:1992;927-935.
    • (1992) Neuron , vol.8 , pp. 927-935
    • Smith, K.E.1    Borden, L.A.2    Hartig, P.R.3    Branchek, T.4    Weinshank, R.L.5
  • 1019
    • 0031567713 scopus 로고    scopus 로고
    • Regulation of glutamate uptake in astrocytes continuously exposed to ethanol
    • Smith T.L. Regulation of glutamate uptake in astrocytes continuously exposed to ethanol. Life Sci. 61:1997;2499-2505.
    • (1997) Life Sci. , vol.61 , pp. 2499-2505
    • Smith, T.L.1
  • 1020
    • 0033575504 scopus 로고    scopus 로고
    • Increased calcium calmodulin protein kinase activity in astrocytes chronically exposed to ethanol: Influences on glutamate transport
    • Smith T.L., Navratilova E. Increased calcium calmodulin protein kinase activity in astrocytes chronically exposed to ethanol: influences on glutamate transport. Neurosci. Lett. 269:1999;145-148.
    • (1999) Neurosci. Lett. , vol.269 , pp. 145-148
    • Smith, T.L.1    Navratilova, E.2
  • 1021
    • 0030297253 scopus 로고    scopus 로고
    • +-dependent high affinity uptake of glutamate in astrocytes chronically exposed to ethanol
    • +-dependent high affinity uptake of glutamate in astrocytes chronically exposed to ethanol. Neurosci. Lett. 218:1996;142-144.
    • (1996) Neurosci. Lett. , vol.218 , pp. 142-144
    • Smith, T.L.1    Zsigo, A.2
  • 1022
    • 0031470568 scopus 로고    scopus 로고
    • Chronic ethanol exposure leads to a selective enhancement of N-methyl-D-aspartate receptor function in cultured hippocampal neurons
    • Smothers C.T., Mrotek J.J., Lovinger D.M. Chronic ethanol exposure leads to a selective enhancement of N-methyl-D-aspartate receptor function in cultured hippocampal neurons. J. Pharmacol. Exp. Ther. 283:1997;1214-1222.
    • (1997) J. Pharmacol. Exp. Ther. , vol.283 , pp. 1214-1222
    • Smothers, C.T.1    Mrotek, J.J.2    Lovinger, D.M.3
  • 1024
    • 0031036030 scopus 로고    scopus 로고
    • Multiple ionic conductances of the human dopamine transporter: The actions of dopamine and psychostimulants
    • Sonders M.S., Zhu S.J., Zahniser N.R., Kavanaugh M.P., Amara S.G. Multiple ionic conductances of the human dopamine transporter: The actions of dopamine and psychostimulants. J. Neurosci. 17:1997;960-974.
    • (1997) J. Neurosci. , vol.17 , pp. 960-974
    • Sonders, M.S.1    Zhu, S.J.2    Zahniser, N.R.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 1025
    • 0030881783 scopus 로고    scopus 로고
    • Inhibition of astrocyte glutamate uptake by reactive oxygen species: Role of antioxidant enzymes
    • Sorg O., Horn T.F.W., Yu N.C., Gruol D.L., Bloom F.E. Inhibition of astrocyte glutamate uptake by reactive oxygen species: role of antioxidant enzymes. Mol. Med. 3:1997;431-440.
    • (1997) Mol. Med. , vol.3 , pp. 431-440
    • Sorg, O.1    Horn, T.F.W.2    Yu, N.C.3    Gruol, D.L.4    Bloom, F.E.5
  • 1026
    • 0021960807 scopus 로고
    • Three-dimensional analysis of dendritic spines. III. Glial sheath
    • Spacek J. Three-dimensional analysis of dendritic spines. III. Glial sheath. Anat. Embryol. 171:1985;245-252.
    • (1985) Anat. Embryol. , vol.171 , pp. 245-252
    • Spacek, J.1
  • 1027
    • 0032786968 scopus 로고    scopus 로고
    • Food toxins, AMPA receptors, and motor neuron diseases
    • Spencer P.S. Food toxins, AMPA receptors, and motor neuron diseases. Drug. Metab. Rev. 31:1999;561-587.
    • (1999) Drug. Metab. Rev. , vol.31 , pp. 561-587
    • Spencer, P.S.1
  • 1029
    • 0023181410 scopus 로고
    • Guam amyotrophic lateral sclerosis-parkinsonism-dementia linked to a plant excitant neurotoxin
    • Spencer P.S., Nunn P.B., Hugon J., Ludolph A.C., Ross S.M., Roy D.N., Robertson R.C. Guam amyotrophic lateral sclerosis-parkinsonism-dementia linked to a plant excitant neurotoxin. Science. 237:1987;517-522.
    • (1987) Science , vol.237 , pp. 517-522
    • Spencer, P.S.1    Nunn, P.B.2    Hugon, J.3    Ludolph, A.C.4    Ross, S.M.5    Roy, D.N.6    Robertson, R.C.7
  • 1030
    • 0030920387 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, a lipid peroxidation product, rapidly accumulates following traumatic spinal cord injury and inhibits glutamate uptake
    • Springer J.E., Azbill R.D., Mark R.J., Begley J.G., Waeg G., Mattson M.P. 4-Hydroxynonenal, a lipid peroxidation product, rapidly accumulates following traumatic spinal cord injury and inhibits glutamate uptake. J. Neurochem. 68:1997;2469-2476.
    • (1997) J. Neurochem. , vol.68 , pp. 2469-2476
    • Springer, J.E.1    Azbill, R.D.2    Mark, R.J.3    Begley, J.G.4    Waeg, G.5    Mattson, M.P.6
  • 1031
    • 0018769153 scopus 로고
    • Coupled transport of glutamate and sodium in a cerebellar nerve cell line
    • Stallcup W.B., Bulloch K., Baetge E.E. Coupled transport of glutamate and sodium in a cerebellar nerve cell line. J. Neurochem. 32:1979;57-65.
    • (1979) J. Neurochem. , vol.32 , pp. 57-65
    • Stallcup, W.B.1    Bulloch, K.2    Baetge, E.E.3
  • 1032
    • 0031081439 scopus 로고    scopus 로고
    • Stimulation of glutamate uptake and Na, K-ATPase activity in rat astrocytes exposed to ischemia-like insults
    • Stanimirovic D.B., Ball R., Durkin J.P. Stimulation of glutamate uptake and Na, K-ATPase activity in rat astrocytes exposed to ischemia-like insults. Glia. 19:1997;123-134.
    • (1997) Glia , vol.19 , pp. 123-134
    • Stanimirovic, D.B.1    Ball, R.2    Durkin, J.P.3
  • 1033
    • 0033053566 scopus 로고    scopus 로고
    • Developmental regulation of glutamate transporters and glutamine synthetase activity in astrocyte cultures differentiated in vitro
    • Stanimirovic D.B., Ball R., Small D.L., Muruganandam A. Developmental regulation of glutamate transporters and glutamine synthetase activity in astrocyte cultures differentiated in vitro. Int. J. Dev. Neurosci. 17:1999;173-184.
    • (1999) Int. J. Dev. Neurosci. , vol.17 , pp. 173-184
    • Stanimirovic, D.B.1    Ball, R.2    Small, D.L.3    Muruganandam, A.4
  • 1034
    • 0030984173 scopus 로고    scopus 로고
    • The dietary excitotoxins beta-n-methylamino-L-alanine and beta-N-oxalylamino-L-alanine induce necrotic- And apoptotic-like death of rat cerebellar granule cells
    • Staton P.C., Bristow D.R. The dietary excitotoxins beta-n-methylamino-L-alanine and beta-N-oxalylamino-L-alanine induce necrotic- and apoptotic-like death of rat cerebellar granule cells. J. Neurochem. 69:1997;1508-1518.
    • (1997) J. Neurochem. , vol.69 , pp. 1508-1518
    • Staton, P.C.1    Bristow, D.R.2
  • 1035
    • 0030221564 scopus 로고    scopus 로고
    • News on glutamate receptors in glial cells
    • Steinhauser C., Gallo V. News on glutamate receptors in glial cells. Trends Neurosci. 19:1996;339-345.
    • (1996) Trends Neurosci. , vol.19 , pp. 339-345
    • Steinhauser, C.1    Gallo, V.2
  • 1036
    • 0028009443 scopus 로고
    • Glutamate-evoked release of arachidonic acid from mouse brain astrocytes
    • Stella N., Tence M., Glowinski J., Premont D. Glutamate-evoked release of arachidonic acid from mouse brain astrocytes. J. Neurosci. 14:1994;568-575.
    • (1994) J. Neurosci. , vol.14 , pp. 568-575
    • Stella, N.1    Tence, M.2    Glowinski, J.3    Premont, D.4
  • 1037
    • 0025247884 scopus 로고
    • Identification and purification of a functional amine transporter from bovine chromaffin granules
    • Stern-Bach Y., Greenberg-Ofrath N., Flechner I., Schuldiner S. Identification and purification of a functional amine transporter from bovine chromaffin granules. J. Biol. Chem. 265:1990;3961-3966.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3961-3966
    • Stern-Bach, Y.1    Greenberg-Ofrath, N.2    Flechner, I.3    Schuldiner, S.4
  • 1038
    • 0000706619 scopus 로고
    • Accumulation of glutamic acid in isolated brain tissue
    • Stern J.R., Eggleston L.V., Hems R., Krebs H.A. Accumulation of glutamic acid in isolated brain tissue. Biochem. J. 44:1949;410-418.
    • (1949) Biochem. J. , vol.44 , pp. 410-418
    • Stern, J.R.1    Eggleston, L.V.2    Hems, R.3    Krebs, H.A.4
  • 1039
    • 0028878175 scopus 로고
    • Estimates for the pool size of releasable quanta at a single central synapse and for the time required to refill the pool
    • Stevens C.F., Tsujimoto T. Estimates for the pool size of releasable quanta at a single central synapse and for the time required to refill the pool. Proc. Natl. Acad. Sci. USA. 92:1995;846-849.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 846-849
    • Stevens, C.F.1    Tsujimoto, T.2
  • 1040
    • 0032143848 scopus 로고    scopus 로고
    • Activity-dependent modulation of the rate at which synaptic vesicles become available to undergo exocytosis
    • Stevens C.F., Wesseling J.F. Activity-dependent modulation of the rate at which synaptic vesicles become available to undergo exocytosis. Neuron. 21:1998;415-424.
    • (1998) Neuron , vol.21 , pp. 415-424
    • Stevens, C.F.1    Wesseling, J.F.2
  • 1041
    • 0025007340 scopus 로고
    • Domoic acid - A dementia-inducing excitotoxic food poison with kainic acid receptor specificity
    • Stewart G.R., Zorumski C.F., Price M.T., Olney J.W. Domoic acid - a dementia-inducing excitotoxic food poison with kainic acid receptor specificity. Exp. Neurol. 110:1990;127-138.
    • (1990) Exp. Neurol. , vol.110 , pp. 127-138
    • Stewart, G.R.1    Zorumski, C.F.2    Price, M.T.3    Olney, J.W.4
  • 1042
    • 0031308907 scopus 로고    scopus 로고
    • The penumbra zone of a traumatic cortical lesion: A microdialysis study of excitatory amino acid release
    • Stoffel M., Eriskat J., Plesnila M., Aggarwal N., Baethmann A. The penumbra zone of a traumatic cortical lesion: a microdialysis study of excitatory amino acid release. Acta Neurochir. Suppl. (Wien). 70:1997;91-93.
    • (1997) Acta Neurochir. Suppl. (Wien) , vol.70 , pp. 91-93
    • Stoffel, M.1    Eriskat, J.2    Plesnila, M.3    Aggarwal, N.4    Baethmann, A.5
  • 1043
    • 0030011331 scopus 로고    scopus 로고
    • +-dependent L-glutamate/L-aspartate transporter GLAST-1 (EAAT-1): Gene structure and localization to chromosome 5p11-p12
    • +-dependent L-glutamate/L-aspartate transporter GLAST-1 (EAAT-1): gene structure and localization to chromosome 5p11-p12. FEBS Lett. 386:1996;189-193.
    • (1996) FEBS Lett. , vol.386 , pp. 189-193
    • Stoffel, W.1    Sasse, J.2    Duker, M.3    Muller, R.4    Hofmann, K.5    Fink, T.6    Lichter, P.7
  • 1044
    • 0027236685 scopus 로고
    • Guam: Deadly disease dying out - A condition once thought to be an excellent model for diseases such as Alzheimer's and ALS may vanish before its causes can be fully understood
    • Stone R. Guam: deadly disease dying out - a condition once thought to be an excellent model for diseases such as Alzheimer's and ALS may vanish before its causes can be fully understood. Science. 261:1993;424-426.
    • (1993) Science , vol.261 , pp. 424-426
    • Stone, R.1
  • 1046
    • 0017614742 scopus 로고
    • Glutamic acid and excitatory nerve endings: Reduction of glutamic acid uptake after axotomy
    • Storm-Mathisen J. Glutamic acid and excitatory nerve endings: reduction of glutamic acid uptake after axotomy. Brain Res. 120:1977;379-386.
    • (1977) Brain Res. , vol.120 , pp. 379-386
    • Storm-Mathisen, J.1
  • 1047
    • 0017577453 scopus 로고
    • Localization of transmitter candidates in the brain: The hippocampal formation as a model
    • Storm-Mathisen J. Localization of transmitter candidates in the brain: the hippocampal formation as a model. Prog. Neurobiol. 8:1977;119-181.
    • (1977) Prog. Neurobiol. , vol.8 , pp. 119-181
    • Storm-Mathisen, J.1
  • 1048
    • 0002205716 scopus 로고
    • Autoradiographic and microchemical localization of high affinity glutamate uptake
    • P.J. Roberts, J. Storm-Mathisen, & G.A.R. Johnston. New York: Wiley
    • Storm-Mathisen J. Autoradiographic and microchemical localization of high affinity glutamate uptake. Roberts P.J., Storm-Mathisen J., Johnston G.A.R. Glutamate: Transmitter in the Central Nervous System. 1981;89-115 Wiley, New York.
    • (1981) Glutamate: Transmitter in the Central Nervous System , pp. 89-115
    • Storm-Mathisen, J.1
  • 1049
    • 0018656506 scopus 로고
    • 3H]glutamic acid in excitatory nerve endings: Light and electronmicroscopic observations in the hippocampal formation of the rat
    • 3H]glutamic acid in excitatory nerve endings: light and electronmicroscopic observations in the hippocampal formation of the rat. Neuroscience. 4:1979;1237-1253.
    • (1979) Neuroscience , vol.4 , pp. 1237-1253
    • Storm-Mathisen, J.1    Iversen, L.L.2
  • 1050
    • 0025015354 scopus 로고
    • Immunocytochemistry of glutamate at the synaptic level
    • Storm-Mathisen J., Ottersen O.P. Immunocytochemistry of glutamate at the synaptic level. J. Histochem. Cytochem. 38:1990;1733-1743.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1733-1743
    • Storm-Mathisen, J.1    Ottersen, O.P.2
  • 1053
    • 0026764215 scopus 로고
    • Electron microscopic localization of glutamate, glutamine and GABA at putative glutamatergic and GABA-ergic synapses
    • Storm-Mathisen J., Zhang N., Ottersen O.P. Electron microscopic localization of glutamate, glutamine and GABA at putative glutamatergic and GABA-ergic synapses. Mol. Neuropharmacol. 2:1992;7-13.
    • (1992) Mol. Neuropharmacol. , vol.2 , pp. 7-13
    • Storm-Mathisen, J.1    Zhang, N.2    Ottersen, O.P.3
  • 1055
    • 0029972423 scopus 로고    scopus 로고
    • Cellular and molecular physiology of volume-sensitive anion channels
    • Strange K., Emma F., Jackson P.S. Cellular and molecular physiology of volume-sensitive anion channels. Am. J. Physiol. 270:1996;C711-C730.
    • (1996) Am. J. Physiol. , vol.270 , pp. 711-C730
    • Strange, K.1    Emma, F.2    Jackson, P.S.3
  • 1056
    • 0018824712 scopus 로고
    • Selective retrograde labeling indicating the transmitter of neuronal pathways
    • Streit P. Selective retrograde labeling indicating the transmitter of neuronal pathways. J. Comp. Neurol. 191:1980;429-463.
    • (1980) J. Comp. Neurol. , vol.191 , pp. 429-463
    • Streit, P.1
  • 1057
    • 0034708716 scopus 로고    scopus 로고
    • Modulation of glutamate transporters (GLAST, GLT-1 and EAAC1) in the rat cerebellum following portocaval anastomosis
    • Suárez I., Bodega G., Fernández B. Modulation of glutamate transporters (GLAST, GLT-1 and EAAC1) in the rat cerebellum following portocaval anastomosis. Brain Res. 859:2000;293-302.
    • (2000) Brain Res. , vol.859 , pp. 293-302
    • Suárez, I.1    Bodega, G.2    Fernández, B.3
  • 1058
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof T.C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:1995;645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 1059
    • 0034595870 scopus 로고    scopus 로고
    • Cloning of an amino acid transporter with functional characteristics and tissue expression pattern identical to that of system A
    • Sugawara M., Nakanishi T., Fei Y.J., Huang W., Ganapathy M.E., Leibach F.H., Ganapathy V. Cloning of an amino acid transporter with functional characteristics and tissue expression pattern identical to that of system A. J. Biol. Chem. 275:2000;16473-16477.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16473-16477
    • Sugawara, M.1    Nakanishi, T.2    Fei, Y.J.3    Huang, W.4    Ganapathy, M.E.5    Leibach, F.H.6    Ganapathy, V.7
  • 1060
    • 0029092532 scopus 로고
    • Molecular characterization of a high-affinity mouse glutamate transporter
    • Sutherland M.L., Delaney T.A., Noebels J.L. Molecular characterization of a high-affinity mouse glutamate transporter. Gene. 162:1995;271-274.
    • (1995) Gene , vol.162 , pp. 271-274
    • Sutherland, M.L.1    Delaney, T.A.2    Noebels, J.L.3
  • 1061
    • 0029885882 scopus 로고    scopus 로고
    • Glutamate transporter mRNA expression in proliferative zones of the developing and adult murine CNS
    • Sutherland M.L., Delaney T.A., Noebels J.L. Glutamate transporter mRNA expression in proliferative zones of the developing and adult murine CNS. J. Neurosci. 16:1996;2191-2207.
    • (1996) J. Neurosci. , vol.16 , pp. 2191-2207
    • Sutherland, M.L.1    Delaney, T.A.2    Noebels, J.L.3
  • 1062
    • 0026482507 scopus 로고
    • Astrocyte glutamate uptake during chemical hypoxia in vitro
    • Swanson R.A. Astrocyte glutamate uptake during chemical hypoxia in vitro. Neurosci. Lett. 147:1992;143-146.
    • (1992) Neurosci. Lett. , vol.147 , pp. 143-146
    • Swanson, R.A.1
  • 1065
    • 0028024908 scopus 로고
    • Triggering and execution of neuronal death in brain ischaemia: Two phases of glutamate release by different mechanisms
    • Szatkowski M., Attwell D. Triggering and execution of neuronal death in brain ischaemia: two phases of glutamate release by different mechanisms. Trends Neurosci. 17:1994;359-365.
    • (1994) Trends Neurosci. , vol.17 , pp. 359-365
    • Szatkowski, M.1    Attwell, D.2
  • 1066
    • 0025251185 scopus 로고
    • Non-vesicular release of glutamate from glial cells by reversed electrogenic glutamate uptake
    • Szatkowski M., Barbour B., Attwell D. Non-vesicular release of glutamate from glial cells by reversed electrogenic glutamate uptake. Nature. 348:1990;443-446.
    • (1990) Nature , vol.348 , pp. 443-446
    • Szatkowski, M.1    Barbour, B.2    Attwell, D.3
  • 1067
    • 0025895791 scopus 로고
    • The potassium-dependence of excitatory amino acid transport - Resolution of a paradox
    • Szatkowski M., Barbour B., Attwell D. The potassium-dependence of excitatory amino acid transport - resolution of a paradox. Brain Res. 555:1991;343-345.
    • (1991) Brain Res. , vol.555 , pp. 343-345
    • Szatkowski, M.1    Barbour, B.2    Attwell, D.3
  • 1068
    • 0033945533 scopus 로고    scopus 로고
    • Human T-cell lymphotropic virus type 1-infected T lymphocytes impair catabolism and uptake of glutamate by astrocytes via tax-1 and tumor necrosis factor alpha
    • Szymocha R., Akaoka H., Dutuit M., Malcus C., Didier-Bazes M., Belin M.F., Giraudon P. Human T-cell lymphotropic virus type 1-infected T lymphocytes impair catabolism and uptake of glutamate by astrocytes via tax-1 and tumor necrosis factor alpha. J. Virol. 74:2000;6433-6441.
    • (2000) J. Virol. , vol.74 , pp. 6433-6441
    • Szymocha, R.1    Akaoka, H.2    Dutuit, M.3    Malcus, C.4    Didier-Bazes, M.5    Belin, M.F.6    Giraudon, P.7
  • 1069
    • 0026755199 scopus 로고
    • Glutamate transport into synaptic vesicles - Roles of membrane potential, pH gradient, and intravesicular pH
    • Tabb J.S., Kish P.E., Vandyke R., Ueda T. Glutamate transport into synaptic vesicles - roles of membrane potential, pH gradient, and intravesicular pH. J. Biol. Chem. 267:1992;15412-15418.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15412-15418
    • Tabb, J.S.1    Kish, P.E.2    Vandyke, R.3    Ueda, T.4
  • 1070
    • 0017096825 scopus 로고
    • Properties of the uptake and release of glutamic acid by synaptosomes from rat cerebral cortex
    • Takagaki G. Properties of the uptake and release of glutamic acid by synaptosomes from rat cerebral cortex. J. Neurochem. 27:1976;1417-1425.
    • (1976) J. Neurochem. , vol.27 , pp. 1417-1425
    • Takagaki, G.1
  • 1071
    • 0017838774 scopus 로고
    • Sodium and potassium ions and accumulation of labelled D-aspartate and GABA in crude synaptosomal fraction from rat cerebral cortex
    • Takagaki G. Sodium and potassium ions and accumulation of labelled D-aspartate and GABA in crude synaptosomal fraction from rat cerebral cortex. J. Neurochem. 30:1978;47-56.
    • (1978) J. Neurochem. , vol.30 , pp. 47-56
    • Takagaki, G.1
  • 1072
    • 0023472258 scopus 로고
    • The critical period of Purkinje cell degeneration and cerebellar hypoplasia due to bilirubin
    • Takagishi Y., Yamamura H. The critical period of Purkinje cell degeneration and cerebellar hypoplasia due to bilirubin. Acta Neuropathol. 75:1987;41-45.
    • (1987) Acta Neuropathol. , vol.75 , pp. 41-45
    • Takagishi, Y.1    Yamamura, H.2
  • 1073
    • 0029088203 scopus 로고
    • Pre- And postsynaptic determinants of EPSC waveform at cerebellar climbing fiber and parallel fiber to Purkinje cell synapses
    • Takahashi M., Kovalchuk Y., Attwell D. Pre- and postsynaptic determinants of EPSC waveform at cerebellar climbing fiber and parallel fiber to Purkinje cell synapses. J. Neurosci. 15:1995;5693-5702.
    • (1995) J. Neurosci. , vol.15 , pp. 5693-5702
    • Takahashi, M.1    Kovalchuk, Y.2    Attwell, D.3
  • 1074
    • 0029950359 scopus 로고    scopus 로고
    • Postsynaptic glutamate uptake in rat cerebellar Purkinje cells
    • Takahashi M., Sarantis M., Attwell D. Postsynaptic glutamate uptake in rat cerebellar Purkinje cells. J. Physiol. (Lond.). 497:1996;523-530.
    • (1996) J. Physiol. (Lond.) , vol.497 , pp. 523-530
    • Takahashi, M.1    Sarantis, M.2    Attwell, D.3
  • 1075
    • 0031682580 scopus 로고    scopus 로고
    • Glutamate uptake in Purkinje cells in rat cerebellar slices
    • Takahashi M., Sarantis M., Attwell D. Glutamate uptake in Purkinje cells in rat cerebellar slices. Methods Enzymol. 296:1998;608-617.
    • (1998) Methods Enzymol. , vol.296 , pp. 608-617
    • Takahashi, M.1    Sarantis, M.2    Attwell, D.3
  • 1076
    • 0028948773 scopus 로고
    • Localization of the gene (SLC1A3) encoding human glutamate transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
    • Takai S., Yamada K., Kawakami H., Tanaka K., Nakamura S. Localization of the gene (SLC1A3) encoding human glutamate transporter (GluT-1) to 5p13 by fluorescence in situ hybridization. Cytogenet. Cell Genet. 69:1995;209-210.
    • (1995) Cytogenet. Cell Genet. , vol.69 , pp. 209-210
    • Takai, S.1    Yamada, K.2    Kawakami, H.3    Tanaka, K.4    Nakamura, S.5
  • 1077
    • 0034648770 scopus 로고    scopus 로고
    • Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons
    • Takamori S., Rhee J.S., Rosenmund C., Jahn R. Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons. Nature. 407:2000;189-194.
    • (2000) Nature , vol.407 , pp. 189-194
    • Takamori, S.1    Rhee, J.S.2    Rosenmund, C.3    Jahn, R.4
  • 1078
    • 0032581422 scopus 로고    scopus 로고
    • D-Aspartate uptake into cultured rat pinealocytes and the concomitant effect on L-aspartate levels and melatonin secretion
    • Takigawa Y., Homma H., Lee J.A., Fukushima T., Santa T., Iwatsubo T., Imai K. D-Aspartate uptake into cultured rat pinealocytes and the concomitant effect on L-aspartate levels and melatonin secretion. Biochem. Biophys. Res. Commun. 248:1998;641-647.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 641-647
    • Takigawa, Y.1    Homma, H.2    Lee, J.A.3    Fukushima, T.4    Santa, T.5    Iwatsubo, T.6    Imai, K.7
  • 1079
    • 0032752054 scopus 로고    scopus 로고
    • Reduction of GluR2 RNA editing, a molecular change that increases calcium influx through AMPA receptors, selective in the spinal ventral gray of patients with amyotrophic lateral sclerosis
    • Takuma H., Kwak S., Yoshizawa T., Kanazawa I. Reduction of GluR2 RNA editing, a molecular change that increases calcium influx through AMPA receptors, selective in the spinal ventral gray of patients with amyotrophic lateral sclerosis. Ann. Neurol. 46:1999;806-815.
    • (1999) Ann. Neurol. , vol.46 , pp. 806-815
    • Takuma, H.1    Kwak, S.2    Yoshizawa, T.3    Kanazawa, I.4
  • 1080
    • 0030797406 scopus 로고    scopus 로고
    • Discrete cellular and subcellular localization of glutamine synthetase and the glutamate transporter GLAST in the rat vestibular end organ
    • Takumi Y., Matsubara A., Danbolt N.C., Laake J.H., Storm-Mathisen J., Usami S., Shinkawa H., Ottersen O.P. Discrete cellular and subcellular localization of glutamine synthetase and the glutamate transporter GLAST in the rat vestibular end organ. Neuroscience. 79:1997;1137-1144.
    • (1997) Neuroscience , vol.79 , pp. 1137-1144
    • Takumi, Y.1    Matsubara, A.2    Danbolt, N.C.3    Laake, J.H.4    Storm-Mathisen, J.5    Usami, S.6    Shinkawa, H.7    Ottersen, O.P.8
  • 1082
    • 0342375000 scopus 로고    scopus 로고
    • Different modes of expression of AMPA and NMDA receptors in hippocampal synapses
    • Takumi Y., Ramirez-Leon V., Laake P., Rinvik E., Ottersen O.P. Different modes of expression of AMPA and NMDA receptors in hippocampal synapses. Nat. Neurosci. 2:1999;618-624.
    • (1999) Nat. Neurosci. , vol.2 , pp. 618-624
    • Takumi, Y.1    Ramirez-Leon, V.2    Laake, P.3    Rinvik, E.4    Ottersen, O.P.5
  • 1083
    • 0031979134 scopus 로고    scopus 로고
    • Schizophrenia and glutamatergic transmission
    • Tamminga C.A. Schizophrenia and glutamatergic transmission. Crit. Rev. Neurobiol. 12:1998;21-36.
    • (1998) Crit. Rev. Neurobiol. , vol.12 , pp. 21-36
    • Tamminga, C.A.1
  • 1085
    • 0030872228 scopus 로고    scopus 로고
    • Extra-junctional localization of glutamate transporter EAAT4 at excitatory Purkinje cell synapses
    • Tanaka J., Ichikawa R., Watanabe M., Tanaka K., Inoue Y. Extra-junctional localization of glutamate transporter EAAT4 at excitatory Purkinje cell synapses. Neuroreport. 8:1997;2461-2464.
    • (1997) Neuroreport , vol.8 , pp. 2461-2464
    • Tanaka, J.1    Ichikawa, R.2    Watanabe, M.3    Tanaka, K.4    Inoue, Y.5
  • 1087
    • 0027328158 scopus 로고
    • Cloning and expression of a glutamate transporter from mouse brain
    • Tanaka K. Cloning and expression of a glutamate transporter from mouse brain. Neurosci. Lett. 159:1993;183-186.
    • (1993) Neurosci. Lett. , vol.159 , pp. 183-186
    • Tanaka, K.1
  • 1088
    • 0027483397 scopus 로고
    • Expression cloning of a rat glutamate transporter
    • Tanaka K. Expression cloning of a rat glutamate transporter. Neurosci. Res. 16:1993;149-153.
    • (1993) Neurosci. Res. , vol.16 , pp. 149-153
    • Tanaka, K.1
  • 1089
    • 0024580689 scopus 로고
    • Quisqualate activates a rapidly inactivating high conductance ionic channel in hippocampal neurons
    • Tang C.M., Dichter M., Morad M. Quisqualate activates a rapidly inactivating high conductance ionic channel in hippocampal neurons. Science. 243:1989;1474-1477.
    • (1989) Science , vol.243 , pp. 1474-1477
    • Tang, C.M.1    Dichter, M.2    Morad, M.3
  • 1090
    • 0028913759 scopus 로고
    • Dithiothreitol promotes a higher affinity state of the serotonin transporter for the tricyclic antidepressant, imipramine
    • Tarrant H.M., Williams D.C. Dithiothreitol promotes a higher affinity state of the serotonin transporter for the tricyclic antidepressant, imipramine. Biochem. Soc. Trans. 23:1995;S41.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 41
    • Tarrant, H.M.1    Williams, D.C.2
  • 1091
    • 0031029081 scopus 로고    scopus 로고
    • Inhibition of the electrogenic Na pump underlies delayed depolarization of cortical neurons after mechanical injury or glutamate
    • Tavalin S.J., Ellis E.F., Satin L.S. Inhibition of the electrogenic Na pump underlies delayed depolarization of cortical neurons after mechanical injury or glutamate. J. Neurophysiol. 77:1997;632-638.
    • (1997) J. Neurophysiol. , vol.77 , pp. 632-638
    • Tavalin, S.J.1    Ellis, E.F.2    Satin, L.S.3
  • 1093
    • 0021327983 scopus 로고
    • Uptake of D-aspartate and L-glutamate in excitatory axon terminals in hippocampus: Autoradiographic and biochemical comparison with gamma-aminobutyrate and other amino acids in normal rats and in rats with lesions
    • Taxt T., Storm-Mathisen J. Uptake of D-aspartate and L-glutamate in excitatory axon terminals in hippocampus: autoradiographic and biochemical comparison with gamma-aminobutyrate and other amino acids in normal rats and in rats with lesions. Neuroscience. 11:1984;79-100.
    • (1984) Neuroscience , vol.11 , pp. 79-100
    • Taxt, T.1    Storm-Mathisen, J.2
  • 1095
    • 0030007906 scopus 로고    scopus 로고
    • Activation of protein kinase C down-regulates glial but not neuronal taurine uptake
    • Tchoumkeu-Nzouessa G.C., Rebel G. Activation of protein kinase C down-regulates glial but not neuronal taurine uptake. Neurosci. Lett. 206:1996;61-64.
    • (1996) Neurosci. Lett. , vol.206 , pp. 61-64
    • Tchoumkeu-Nzouessa, G.C.1    Rebel, G.2
  • 1096
    • 0030043302 scopus 로고    scopus 로고
    • Characterization of taurine transport in human glioma GL15 cell line: Regulation by protein kinase C
    • Tchoumkeu-Nzouessa G.C., Rebel G. Characterization of taurine transport in human glioma GL15 cell line: regulation by protein kinase C. Neuropharmacology. 35:1996;37-44.
    • (1996) Neuropharmacology , vol.35 , pp. 37-44
    • Tchoumkeu-Nzouessa, G.C.1    Rebel, G.2
  • 1099
    • 0020613439 scopus 로고
    • The corticopontine projection: Axotomy-induced loss of high affinity L-glutamate and D-aspartate uptake, but not of gamma-aminobutyrate uptake, glutamate decarboxylase or choline acetyltransferase, in the pontine nuclei
    • Thangnipon W., Taxt T., Brodal P., Storm-Mathisen J. The corticopontine projection: axotomy-induced loss of high affinity L-glutamate and D-aspartate uptake, but not of gamma-aminobutyrate uptake, glutamate decarboxylase or choline acetyltransferase, in the pontine nuclei. Neuroscience. 8:1983;449-457.
    • (1983) Neuroscience , vol.8 , pp. 449-457
    • Thangnipon, W.1    Taxt, T.2    Brodal, P.3    Storm-Mathisen, J.4
  • 1100
    • 0030821363 scopus 로고    scopus 로고
    • MK-801 administration during ethanol withdrawal in neonatal rat pups attenuates ethanol-induced behavioral deficits
    • Thomas J.D., Weinert S.P., Sharif S., Riley E.P. MK-801 administration during ethanol withdrawal in neonatal rat pups attenuates ethanol-induced behavioral deficits. Alcohol Clin. Exp. Res. 21:1997;1218-1225.
    • (1997) Alcohol Clin. Exp. Res. , vol.21 , pp. 1218-1225
    • Thomas, J.D.1    Weinert, S.P.2    Sharif, S.3    Riley, E.P.4
  • 1101
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 1102
    • 0028076043 scopus 로고
    • L-glutamate uptake inhibitors may stimulate phosphoinositide hydrolysis in baby hamster kidney cells expressing mGluR1a via heteroexchange with L-glutamate without direct activation of mGluR1a
    • Thomsen C., Hansen L., Suzdak P.D. L-glutamate uptake inhibitors may stimulate phosphoinositide hydrolysis in baby hamster kidney cells expressing mGluR1a via heteroexchange with L-glutamate without direct activation of mGluR1a. J. Neurochem. 63:1994;2038-2047.
    • (1994) J. Neurochem. , vol.63 , pp. 2038-2047
    • Thomsen, C.1    Hansen, L.2    Suzdak, P.D.3
  • 1104
    • 0003206372 scopus 로고
    • Laboratory techniques in biochemistry and molecular biology
    • Amsterdam: Elsevier
    • Tijssen P. Laboratory techniques in biochemistry and molecular biology. Practice and Theory of Enzyme Immunoassays. 15:1985;Elsevier, Amsterdam.
    • (1985) Practice and Theory of Enzyme Immunoassays , vol.15
    • Tijssen, P.1
  • 1105
    • 0033009113 scopus 로고    scopus 로고
    • Remarkable increase in cerebrospinal fluid 3-nitrotyrosine in patients with sporadic amyotrophic lateral sclerosis
    • Tohgi H., Abe T., Yamazaki K., Murata T., Ishizaki E., Isobe C. Remarkable increase in cerebrospinal fluid 3-nitrotyrosine in patients with sporadic amyotrophic lateral sclerosis. Ann. Neurol. 46:1999;129-131.
    • (1999) Ann. Neurol. , vol.46 , pp. 129-131
    • Tohgi, H.1    Abe, T.2    Yamazaki, K.3    Murata, T.4    Ishizaki, E.5    Isobe, C.6
  • 1106
    • 0026602714 scopus 로고
    • Revised nucleotide sequence of the gltP gene, which encodes the proton-glutamate-aspartate transport protein of Escherichia coli K-12
    • Tolner B., Poolman B., Wallace B., Konings W.N. Revised nucleotide sequence of the gltP gene, which encodes the proton-glutamate-aspartate transport protein of Escherichia coli K-12. J. Bacteriol. 174:1992;2391-2393.
    • (1992) J. Bacteriol. , vol.174 , pp. 2391-2393
    • Tolner, B.1    Poolman, B.2    Wallace, B.3    Konings, W.N.4
  • 1107
    • 0028803285 scopus 로고
    • Cation-selectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: Dependence on the environment in which the proteins are expressed
    • Tolner B., Ubbink-Kok T., Poolman B., Konings W.N. Cation-selectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: dependence on the environment in which the proteins are expressed. Mol. Microbiol. 18:1995;123-133.
    • (1995) Mol. Microbiol. , vol.18 , pp. 123-133
    • Tolner, B.1    Ubbink-Kok, T.2    Poolman, B.3    Konings, W.N.4
  • 1108
    • 0028061339 scopus 로고
    • Block of glutamate transporters potentiates postsynaptic excitation
    • Tong G., Jahr C.E. Block of glutamate transporters potentiates postsynaptic excitation. Neuron. 13:1994;1195-1203.
    • (1994) Neuron , vol.13 , pp. 1195-1203
    • Tong, G.1    Jahr, C.E.2
  • 1109
    • 0025761431 scopus 로고
    • Cellular and subcellular redistribution of glutamate-, glutamine- And taurine-like immunoreactivities during forebrain ischemia: A semiquantitative electron microscopic study in rat hippocampus
    • Torp R., Andine P., Hagberg H., Karagulle T., Blackstad T.W., Ottersen O.P. Cellular and subcellular redistribution of glutamate-, glutamine- and taurine-like immunoreactivities during forebrain ischemia: a semiquantitative electron microscopic study in rat hippocampus. Neuroscience. 41:1991;433-447.
    • (1991) Neuroscience , vol.41 , pp. 433-447
    • Torp, R.1    Andine, P.2    Hagberg, H.3    Karagulle, T.4    Blackstad, T.W.5    Ottersen, O.P.6
  • 1110
    • 0027842804 scopus 로고
    • Effect of ischemia and reperfusion on the extra- And intracellular distribution of glutamate, glutamine, aspartate and GABA in the rat hippocampus, with a note on the effect of the sodium channel blocker BW1003C87
    • Torp R., Arvin B., Le Peillet E., Chapman A.G., Ottersen O.P., Meldrum B.S. Effect of ischemia and reperfusion on the extra- and intracellular distribution of glutamate, glutamine, aspartate and GABA in the rat hippocampus, with a note on the effect of the sodium channel blocker BW1003C87. Exp. Brain Res. 96:1993;365-376.
    • (1993) Exp. Brain Res. , vol.96 , pp. 365-376
    • Torp, R.1    Arvin, B.2    Le Peillet, E.3    Chapman, A.G.4    Ottersen, O.P.5    Meldrum, B.S.6
  • 1113
    • 0030902855 scopus 로고    scopus 로고
    • Differential distribution of the glutamate transporters GLT1 and rEAAC1 in rat cerebral cortex and thalamus: An in situ hybridization analysis
    • Torp R., Hoover F., Danbolt N.C., Storm-Mathisen J., Ottersen O.P. Differential distribution of the glutamate transporters GLT1 and rEAAC1 in rat cerebral cortex and thalamus: an in situ hybridization analysis. Anat. Embryol. 195:1997;317-326.
    • (1997) Anat. Embryol. , vol.195 , pp. 317-326
    • Torp, R.1    Hoover, F.2    Danbolt, N.C.3    Storm-Mathisen, J.4    Ottersen, O.P.5
  • 1115
    • 0032484216 scopus 로고    scopus 로고
    • Identification and characterization of a membrane protein (y+L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y+L. A candidate gene for lysinuric protein intolerance
    • Torrents D., Estévez R., Pineda M., Fernández E., Lloberas J., Shi Y.B., Zorzano A., Palacín M. Identification and characterization of a membrane protein (y+L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y+L. A candidate gene for lysinuric protein intolerance. J. Biol. Chem. 273:1998;32437-32445.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32437-32445
    • Torrents, D.1    Estévez, R.2    Pineda, M.3    Fernández, E.4    Lloberas, J.5    Shi, Y.B.6    Zorzano, A.7    Palacín, M.8
  • 1116
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 1117
    • 0033695016 scopus 로고    scopus 로고
    • Rasmussen's syndrome - Aetiology, clinical features and treatment options
    • Tran, T.X., Day, J.A., Eskin, T.A., Carney, P.R., Maria, B.L., 2000. Rasmussen's syndrome - Aetiology, clinical features and treatment options. CNS Drugs 14, 343-354.
    • (2000) CNS Drugs , vol.14 , pp. 343-354
    • Tran, T.X.1    Day, J.A.2    Eskin, T.A.3    Carney, P.R.4    Maria, B.L.5
  • 1118
    • 0025350861 scopus 로고
    • Proton inhibition of N-methyl-D-aspartate receptors in cerebellar neurons
    • Traynelis S.F., Cull-Candy S.G. Proton inhibition of N-methyl-D-aspartate receptors in cerebellar neurons. Nature. 345:1990;347-350.
    • (1990) Nature , vol.345 , pp. 347-350
    • Traynelis, S.F.1    Cull-Candy, S.G.2
  • 1119
    • 0028953410 scopus 로고
    • Arachidonic acid inhibits a purified and reconstituted glutamate transporter directly from the water phase and not via the phospholipid membrane
    • Trotti D., Volterra A., Lehre K.P., Rossi D., Gjesdal O., Racagni G., Danbolt N.C. Arachidonic acid inhibits a purified and reconstituted glutamate transporter directly from the water phase and not via the phospholipid membrane. J. Biol. Chem. 270:1995;9890-9895.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9890-9895
    • Trotti, D.1    Volterra, A.2    Lehre, K.P.3    Rossi, D.4    Gjesdal, O.5    Racagni, G.6    Danbolt, N.C.7
  • 1121
    • 0030690557 scopus 로고    scopus 로고
    • Differential modulation of the uptake currents by redox interconversion of cysteine residues in the human neuronal glutamate transporter EAAC1
    • Trotti D., Nussberger S., Volterra A., Hediger M.A. Differential modulation of the uptake currents by redox interconversion of cysteine residues in the human neuronal glutamate transporter EAAC1. Eur. J. Neurosci. 9:1997;2207-2212.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 2207-2212
    • Trotti, D.1    Nussberger, S.2    Volterra, A.3    Hediger, M.A.4
  • 1123
    • 0032145886 scopus 로고    scopus 로고
    • Glutamate transporters are oxidant-vulnerable: A molecular link between oxidative and excitotoxic neurodegeneration?
    • Trotti D., Danbolt N.C., Volterra A. Glutamate transporters are oxidant-vulnerable: a molecular link between oxidative and excitotoxic neurodegeneration? Trends Pharmacol. Sci. 19:1998;328-334.
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 328-334
    • Trotti, D.1    Danbolt, N.C.2    Volterra, A.3
  • 1124
    • 0033366461 scopus 로고    scopus 로고
    • SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter
    • Trotti D., Rolfs A., Danbolt N.C., Brown R.H.J.r., Hediger M.A. SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. Nat. Neurosci. 2:1999;427-433.
    • (1999) Nat. Neurosci. , vol.2 , pp. 427-433
    • Trotti, D.1    Rolfs, A.2    Danbolt, N.C.3    Brown, R.H.J.R.4    Hediger, M.A.5
  • 1125
  • 1126
    • 0024713443 scopus 로고
    • Glutamate receptor desensitization and its role in synaptic transmission
    • Trussell L.O., Fischbach G.D. Glutamate receptor desensitization and its role in synaptic transmission. Neuron. 3:1989;209-218.
    • (1989) Neuron , vol.3 , pp. 209-218
    • Trussell, L.O.1    Fischbach, G.D.2
  • 1127
    • 0027210626 scopus 로고
    • Desensitization of AMPA receptors upon multiquantal neurotransmitter release
    • Trussell L.O., Zhang S., Raman I.M. Desensitization of AMPA receptors upon multiquantal neurotransmitter release. Neuron. 10:1993;1185-1196.
    • (1993) Neuron , vol.10 , pp. 1185-1196
    • Trussell, L.O.1    Zhang, S.2    Raman, I.M.3
  • 1128
    • 0343341215 scopus 로고    scopus 로고
    • Control of synaptic depression by glutamate transporters
    • Turecek R., Trussell L.O. Control of synaptic depression by glutamate transporters. J. Neurosci. 20:2000;2054-2063.
    • (2000) J. Neurosci. , vol.20 , pp. 2054-2063
    • Turecek, R.1    Trussell, L.O.2
  • 1129
    • 0032504238 scopus 로고    scopus 로고
    • Arachidonic acid activates a proton current in the rat glutamate transporter EAAT4
    • Tzingounis A.V., Lin C.L., Rothstein J.D., Kavanaugh M.P. Arachidonic acid activates a proton current in the rat glutamate transporter EAAT4. J. Biol. Chem. 273:1998;17315-17317.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17315-17317
    • Tzingounis, A.V.1    Lin, C.L.2    Rothstein, J.D.3    Kavanaugh, M.P.4
  • 1130
    • 0034662017 scopus 로고    scopus 로고
    • Hippocampal gamma-aminobutyric acid transporter alterations following focal epileptogenesis induced in rat amygdala
    • Ueda Y., Willmore L.J. Hippocampal gamma-aminobutyric acid transporter alterations following focal epileptogenesis induced in rat amygdala. Brain Res. Bull. 52:2000;357-361.
    • (2000) Brain Res. Bull. , vol.52 , pp. 357-361
    • Ueda, Y.1    Willmore, L.J.2
  • 1131
    • 0033926889 scopus 로고    scopus 로고
    • Molecular regulation of glutamate and GABA transporter proteins by valproic acid in rat hippocampus during epileptogenesis
    • Ueda Y., Willmore L.J. Molecular regulation of glutamate and GABA transporter proteins by valproic acid in rat hippocampus during epileptogenesis. Exp. Brain Res. 133:2000;334-339.
    • (2000) Exp. Brain Res. , vol.133 , pp. 334-339
    • Ueda, Y.1    Willmore, L.J.2
  • 1133
    • 0030803577 scopus 로고    scopus 로고
    • Differential developmental expression of the two rat brain glutamate transporter proteins GLAST and GLT
    • Ullensvang K., Lehre K.P., Storm-Mathisen J., Danbolt N.C. Differential developmental expression of the two rat brain glutamate transporter proteins GLAST and GLT. Eur. J. Neurosci. 9:1997;1646-1655.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1646-1655
    • Ullensvang, K.1    Lehre, K.P.2    Storm-Mathisen, J.3    Danbolt, N.C.4
  • 1134
    • 0034254104 scopus 로고    scopus 로고
    • Update on the pathophysiology of the epilepsies
    • Ure., J.A., Perassolo, M., 2000. Update on the pathophysiology of the epilepsies. J. Neurol. Sci. 177, 1-17.
    • (2000) J. Neurol. Sci. , vol.177 , pp. 1-17
    • Ure, J.A.1    Perassolo, M.2
  • 1135
    • 0029906156 scopus 로고    scopus 로고
    • Molecular and clinical aspects of apoptosis
    • Uren A.G., Vaux D.L. Molecular and clinical aspects of apoptosis. Pharmacol. Ther. 72:1996;37-50.
    • (1996) Pharmacol. Ther. , vol.72 , pp. 37-50
    • Uren, A.G.1    Vaux, D.L.2
  • 1136
    • 0029763313 scopus 로고    scopus 로고
    • A mathematical description of miniature postsynaptic current generation at central nervous system synapses
    • Uteshev V.V., Pennefather P.S. A mathematical description of miniature postsynaptic current generation at central nervous system synapses. Biophys. J. 71:1996;1256-1266.
    • (1996) Biophys. J. , vol.71 , pp. 1256-1266
    • Uteshev, V.V.1    Pennefather, P.S.2
  • 1138
    • 0030716859 scopus 로고    scopus 로고
    • Tissue specific variants of glutamate transporter GLT-1
    • Utsunomiya-Tate N., Endou H., Kanai Y. Tissue specific variants of glutamate transporter GLT-1. FEBS Lett. 416:1997;312-316.
    • (1997) FEBS Lett. , vol.416 , pp. 312-316
    • Utsunomiya-Tate, N.1    Endou, H.2    Kanai, Y.3
  • 1139
    • 0032408210 scopus 로고    scopus 로고
    • Developmental aspects of NMDA receptor function
    • Vallano M.L. Developmental aspects of NMDA receptor function. Crit. Rev. Neurobiol. 12:1998;177-204.
    • (1998) Crit. Rev. Neurobiol. , vol.12 , pp. 177-204
    • Vallano, M.L.1
  • 1140
    • 0015071185 scopus 로고
    • A simulation study of brain compartments - Metabolism of glutamate and related substances in mouse brain
    • Van den Berg C.J., Garfinkel D. A simulation study of brain compartments - metabolism of glutamate and related substances in mouse brain. Biochem. J. 123:1971;211-218.
    • (1971) Biochem. J. , vol.123 , pp. 211-218
    • Van Den Berg, C.J.1    Garfinkel, D.2
  • 1142
    • 0025738016 scopus 로고
    • Freeze-substitution and Lowicryl HM20 embedding of fixed rat brain: Suitability for immunogold ultrastructural localization of neural antigens
    • van Lookeren Campagne M., Oestreicher A.B., van der Krift T.P., Gispen W.H., Verkleij A.J. Freeze-substitution and Lowicryl HM20 embedding of fixed rat brain: suitability for immunogold ultrastructural localization of neural antigens. J. Histochem. Cytochem. 39:1991;1267-1279.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1267-1279
    • Van Lookeren Campagne, M.1    Oestreicher, A.B.2    Van Der Krift, T.P.3    Gispen, W.H.4    Verkleij, A.J.5
  • 1143
    • 0031833248 scopus 로고    scopus 로고
    • Molecular pharmacology and physiology of glutamate transporters in the central nervous system
    • Vandenberg R.J. Molecular pharmacology and physiology of glutamate transporters in the central nervous system. Clin. Exp. Pharmacol. Physiol. 25:1998;393-400.
    • (1998) Clin. Exp. Pharmacol. Physiol. , vol.25 , pp. 393-400
    • Vandenberg, R.J.1
  • 1144
    • 0029023101 scopus 로고
    • Constitutive ion fluxes and substrate binding domains of human glutamate transporters
    • Vandenberg R.J., Arriza J.L., Amara S.G., Kavanaugh M.P. Constitutive ion fluxes and substrate binding domains of human glutamate transporters. J. Biol. Chem. 270:1995;17668-17671.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17668-17671
    • Vandenberg, R.J.1    Arriza, J.L.2    Amara, S.G.3    Kavanaugh, M.P.4
  • 1145
    • 0030946093 scopus 로고    scopus 로고
    • Contrasting modes of action of methylglutamate derivatives on the excitatory amino acid transporters, EAAT1 and EAAT2
    • Vandenberg R.J., Mitrovic A.D., Chebib M., Balcar V.J., Johnston G.A.R. Contrasting modes of action of methylglutamate derivatives on the excitatory amino acid transporters, EAAT1 and EAAT2. Mol. Pharmacol. 51:1997;809-815.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 809-815
    • Vandenberg, R.J.1    Mitrovic, A.D.2    Chebib, M.3    Balcar, V.J.4    Johnston, G.A.R.5
  • 1146
    • 0031849828 scopus 로고    scopus 로고
    • Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions
    • Vandenberg R.J., Mitrovic A.D., Johnston G.A.R. Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions. Mol. Pharmacol. 54:1998;189-196.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 189-196
    • Vandenberg, R.J.1    Mitrovic, A.D.2    Johnston, G.A.R.3
  • 1147
    • 0031953098 scopus 로고    scopus 로고
    • Serine-O-sulphate transport by the human glutamate transporter, EAAT2
    • Vandenberg R.J., Mitrovic A.D., Johnston G.A.R. Serine-O-sulphate transport by the human glutamate transporter, EAAT2. Br. J. Pharmacol. 123:1998;1593-1600.
    • (1998) Br. J. Pharmacol. , vol.123 , pp. 1593-1600
    • Vandenberg, R.J.1    Mitrovic, A.D.2    Johnston, G.A.R.3
  • 1148
    • 0029861246 scopus 로고    scopus 로고
    • Active transport of acetylcholine by the human vesicular acetylcholine transporter
    • Varoqui H., Erickson J.D. Active transport of acetylcholine by the human vesicular acetylcholine transporter. J. Biol. Chem. 271:1996;27229-27232.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27229-27232
    • Varoqui, H.1    Erickson, J.D.2
  • 1149
    • 0031240873 scopus 로고    scopus 로고
    • Vesicular neurotransmitter transporters. Potential sites for the regulation of synaptic function
    • Varoqui H., Erickson J.D. Vesicular neurotransmitter transporters. Potential sites for the regulation of synaptic function. Mol. Neurobiol. 15:1997;165-191.
    • (1997) Mol. Neurobiol. , vol.15 , pp. 165-191
    • Varoqui, H.1    Erickson, J.D.2
  • 1150
    • 0028195078 scopus 로고
    • Cloning and expression of the vesamicol binding protein from the marine ray Torpedo. Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans
    • Varoqui H., Diebler M.F., Meunier F.M., Rand J.B., Usdin T.B., Bonner T.I., Eiden L.E., Erickson J.D. Cloning and expression of the vesamicol binding protein from the marine ray Torpedo. Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans. FEBS Lett. 342:1994;97-102.
    • (1994) FEBS Lett. , vol.342 , pp. 97-102
    • Varoqui, H.1    Diebler, M.F.2    Meunier, F.M.3    Rand, J.B.4    Usdin, T.B.5    Bonner, T.I.6    Eiden, L.E.7    Erickson, J.D.8
  • 1151
    • 0034635496 scopus 로고    scopus 로고
    • Cloning and functional identification of a neuronal glutamine transporter
    • Varoqui H., Zhu H., Yao D., Ming H., Erickson J.D. Cloning and functional identification of a neuronal glutamine transporter. J. Biol. Chem. 275:2000;4049-4054.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4049-4054
    • Varoqui, H.1    Zhu, H.2    Yao, D.3    Ming, H.4    Erickson, J.D.5
  • 1153
    • 0034244041 scopus 로고    scopus 로고
    • A Brownian simulation model of glutamate synaptic diffusion in the femtosecond time scale
    • Ventriglia F., Dimaio V. A Brownian simulation model of glutamate synaptic diffusion in the femtosecond time scale. Biol. Cybern. 83:2000;93-109.
    • (2000) Biol. Cybern. , vol.83 , pp. 93-109
    • Ventriglia, F.1    Dimaio, V.2
  • 1154
    • 0033566709 scopus 로고    scopus 로고
    • Three-dimensional relationships between hippocampal synapses and astrocytes
    • Ventura R., Harris K.M. Three-dimensional relationships between hippocampal synapses and astrocytes. J. Neurosci. 19:1999;6897-6906.
    • (1999) J. Neurosci. , vol.19 , pp. 6897-6906
    • Ventura, R.1    Harris, K.M.2
  • 1156
    • 0030174947 scopus 로고    scopus 로고
    • Glia-neuron intercommunications and synaptic plasticity
    • Vernadakis A. Glia-neuron intercommunications and synaptic plasticity. Prog. Neurobiol. 49:1996;185-214.
    • (1996) Prog. Neurobiol. , vol.49 , pp. 185-214
    • Vernadakis, A.1
  • 1157
    • 0030818670 scopus 로고    scopus 로고
    • HIV-1 gp120 glycoprotein affects the astrocyte control of extracellular glutamate by both inhibiting the uptake and stimulating the release of the amino acid
    • Vesce S., Bezzi P., Rossi D., Meldolesi J., Volterra A. HIV-1 gp120 glycoprotein affects the astrocyte control of extracellular glutamate by both inhibiting the uptake and stimulating the release of the amino acid. FEBS Lett. 411:1997;107-109.
    • (1997) FEBS Lett. , vol.411 , pp. 107-109
    • Vesce, S.1    Bezzi, P.2    Rossi, D.3    Meldolesi, J.4    Volterra, A.5
  • 1158
    • 0029018838 scopus 로고
    • Glutamate increases cytosolic calcium in GH3 pituitary cells acting via a high-affinity glutamate transporter
    • Villalobos C., García-Sancho J. Glutamate increases cytosolic calcium in GH3 pituitary cells acting via a high-affinity glutamate transporter. FASEB J. 9:1995;815-819.
    • (1995) FASEB J. , vol.9 , pp. 815-819
    • Villalobos, C.1    García-Sancho, J.2
  • 1159
    • 0018890873 scopus 로고
    • A comparison of sodium-dependent glutamate binding with high affinity glutamate uptake in rat stratum
    • Vincent S.R., McGeer G. A comparison of sodium-dependent glutamate binding with high affinity glutamate uptake in rat stratum. Brain Res. 184:1980;99-108.
    • (1980) Brain Res. , vol.184 , pp. 99-108
    • Vincent, S.R.1    McGeer, G.2
  • 1160
    • 0026062606 scopus 로고
    • Glucocorticoids inhibit glucose transport and glutamate uptake in hippocampal astrocytes: Implications for glucocorticoid neurotoxicity
    • Virgin C.E.J.r., Ha T.P.T., Packan D.R., Tombaugh G.C., Yang S.H., Horner H.C., Sapolsky R.M. Glucocorticoids inhibit glucose transport and glutamate uptake in hippocampal astrocytes: implications for glucocorticoid neurotoxicity. J. Neurochem. 57:1991;1422-1428.
    • (1991) J. Neurochem. , vol.57 , pp. 1422-1428
    • Virgin, C.E.J.R.1    Ha, T.P.T.2    Packan, D.R.3    Tombaugh, G.C.4    Yang, S.H.5    Horner, H.C.6    Sapolsky, R.M.7
  • 1161
    • 0034005665 scopus 로고    scopus 로고
    • Role of high-affinity receptors and membrane transporters in nonsynaptic communication and drug action in the central nervous system
    • Vizi E.S. Role of high-affinity receptors and membrane transporters in nonsynaptic communication and drug action in the central nervous system. Pharmacol. Rev. 52:2000;63-89.
    • (2000) Pharmacol. Rev. , vol.52 , pp. 63-89
    • Vizi, E.S.1
  • 1162
    • 0033514444 scopus 로고    scopus 로고
    • Glutamate and gamma-aminobutyric acid mediate a heterosynaptic depression at mossy fiber synapses in the hippocampus
    • Vogt K.E., Nicoll R.A. Glutamate and gamma-aminobutyric acid mediate a heterosynaptic depression at mossy fiber synapses in the hippocampus. Proc. Natl. Acad. Sci. USA. 96:1999;1118-1122.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1118-1122
    • Vogt, K.E.1    Nicoll, R.A.2
  • 1163
    • 0027529818 scopus 로고
    • Plasticity of astroglial glutamate and gamma-aminobutyric acid uptake in cell cultures derived from postnatal mouse cerebellum
    • Voisin P., Viratelle O., Girault J.M., Morrison-Bogorad M., Labouesse J. Plasticity of astroglial glutamate and gamma-aminobutyric acid uptake in cell cultures derived from postnatal mouse cerebellum. J. Neurochem. 60:1993;114-127.
    • (1993) J. Neurochem. , vol.60 , pp. 114-127
    • Voisin, P.1    Viratelle, O.2    Girault, J.M.3    Morrison-Bogorad, M.4    Labouesse, J.5
  • 1164
    • 0026634153 scopus 로고
    • High sensitivity of glutamate uptake to extracellular free arachidonic acid levels in rat cortical synaptosomes and astrocytes
    • Volterra A., Trotti D., Cassutti P., Tromba C., Salvaggio A., Melcangi R.C., Racagni G. High sensitivity of glutamate uptake to extracellular free arachidonic acid levels in rat cortical synaptosomes and astrocytes. J. Neurochem. 59:1992;600-606.
    • (1992) J. Neurochem. , vol.59 , pp. 600-606
    • Volterra, A.1    Trotti, D.2    Cassutti, P.3    Tromba, C.4    Salvaggio, A.5    Melcangi, R.C.6    Racagni, G.7
  • 1165
    • 0028208495 scopus 로고
    • Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes
    • Volterra A., Trotti D., Tromba C., Floridi S., Racagni G. Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14:1994;2924-2932.
    • (1994) J. Neurosci. , vol.14 , pp. 2924-2932
    • Volterra, A.1    Trotti, D.2    Tromba, C.3    Floridi, S.4    Racagni, G.5
  • 1166
    • 0027944554 scopus 로고
    • Glutamate uptake is inhibited by arachidonic acid and oxygen radicals via two distinct and additive mechanisms
    • Volterra A., Trotti D., Racagni G. Glutamate uptake is inhibited by arachidonic acid and oxygen radicals via two distinct and additive mechanisms. Mol. Pharmacol. 46:1994;986-992.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 986-992
    • Volterra, A.1    Trotti, D.2    Racagni, G.3
  • 1167
    • 0029743194 scopus 로고    scopus 로고
    • The competitive transport inhibitor L-trans-pyrrolidine-2,4-dicarboxylate triggers excitotoxicity in rat cortical neuron-astrocyte co-cultures via glutamate release rather than uptake inhibition
    • Volterra A., Bezzi P., Rizzini B.L., Trotti D., Ullensvang K., Danbolt N.C., Racagni G. The competitive transport inhibitor L-trans-pyrrolidine-2,4-dicarboxylate triggers excitotoxicity in rat cortical neuron-astrocyte co-cultures via glutamate release rather than uptake inhibition. Eur. J. Neurosci. 8:1996;2019-2028.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 2019-2028
    • Volterra, A.1    Bezzi, P.2    Rizzini, B.L.3    Trotti, D.4    Ullensvang, K.5    Danbolt, N.C.6    Racagni, G.7
  • 1168
    • 0343471501 scopus 로고    scopus 로고
    • Cytoskeleton-membrane connections in the human erythrocyte membrane: Band 4, 1 binds to tetrameric band 3 protein
    • von Rückmann B., Jons T., Dölle F., Drenckhahn D., Schubert D. Cytoskeleton-membrane connections in the human erythrocyte membrane: band 4, 1 binds to tetrameric band 3 protein. Biochim. Biophys. Acta. 1325:1997;226-234.
    • (1997) Biochim. Biophys. Acta , vol.1325 , pp. 226-234
    • Von Rückmann, B.1    Jons, T.2    Dölle, F.3    Drenckhahn, D.4    Schubert, D.5
  • 1169
    • 0032189020 scopus 로고    scopus 로고
    • Macroscopic and microscopic properties of a cloned glutamate transporter chloride channel
    • Wadiche J.I., Kavanaugh M.P. Macroscopic and microscopic properties of a cloned glutamate transporter chloride channel. J. Neurosci. 18:1998;7650-7661.
    • (1998) J. Neurosci. , vol.18 , pp. 7650-7661
    • Wadiche, J.I.1    Kavanaugh, M.P.2
  • 1170
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport
    • Wadiche J.I., Amara S.G., Kavanaugh M.P. Ion fluxes associated with excitatory amino acid transport. Neuron. 15:1995;721-728.
    • (1995) Neuron , vol.15 , pp. 721-728
    • Wadiche, J.I.1    Amara, S.G.2    Kavanaugh, M.P.3
  • 1172
    • 0030471958 scopus 로고    scopus 로고
    • Membrane topology of the high-affinity L-glutamate transporter (GLAST-1) of the central nervous system
    • Wahle S., Stoffel W. Membrane topology of the high-affinity L-glutamate transporter (GLAST-1) of the central nervous system. J. Cell Biol. 135:1996;1867-1877.
    • (1996) J. Cell Biol. , vol.135 , pp. 1867-1877
    • Wahle, S.1    Stoffel, W.2
  • 1173
    • 0018969025 scopus 로고
    • Biochemical evidence for glutamate as a transmitter in hippocampal efferents to the basal forebrain and hypothalamus in the rat brain
    • Walaas I., Fonnum F. Biochemical evidence for glutamate as a transmitter in hippocampal efferents to the basal forebrain and hypothalamus in the rat brain. Neuroscience. 5:1980;1691-1698.
    • (1980) Neuroscience , vol.5 , pp. 1691-1698
    • Walaas, I.1    Fonnum, F.2
  • 1174
    • 0025994387 scopus 로고
    • Protein phosphorylation and neuronal function
    • Walaas S.I., Greengard P. Protein phosphorylation and neuronal function. Pharmacol. Rev. 43:1991;299-349.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 299-349
    • Walaas, S.I.1    Greengard, P.2
  • 1175
    • 0021088202 scopus 로고
    • Effect of regional cortical ablations on high-affinity D-aspartate uptake in striatum, olfactory tubercle, and pyriform cortex of the rat
    • Walker J.E., Fonnum F. Effect of regional cortical ablations on high-affinity D-aspartate uptake in striatum, olfactory tubercle, and pyriform cortex of the rat. Brain Res. 278:1983;283-286.
    • (1983) Brain Res. , vol.278 , pp. 283-286
    • Walker, J.E.1    Fonnum, F.2
  • 1176
    • 0020530227 scopus 로고
    • Regional cortical glutamergic and aspartergic projections to the amygdala and thalamus of the rat
    • Walker J.E., Fonnum F. Regional cortical glutamergic and aspartergic projections to the amygdala and thalamus of the rat. Brain Res. 267:1983;371-374.
    • (1983) Brain Res. , vol.267 , pp. 371-374
    • Walker, J.E.1    Fonnum, F.2
  • 1178
    • 0021219191 scopus 로고
    • Characterization of L-glutamic acid transport by glioma cells in culture: Evidence for sodium-independent, chloride-dependent high affinity influx
    • Waniewski R.A., Martin D.L. Characterization of L-glutamic acid transport by glioma cells in culture: evidence for sodium-independent, chloride-dependent high affinity influx. J. Neurosci. 4:1984;2237-2246.
    • (1984) J. Neurosci. , vol.4 , pp. 2237-2246
    • Waniewski, R.A.1    Martin, D.L.2
  • 1179
    • 0033082865 scopus 로고    scopus 로고
    • Modulation of extracellular glutamate concentration in rat brain slices by cystine-glutamate exchange
    • Warr O., Takahashi M., Attwell D. Modulation of extracellular glutamate concentration in rat brain slices by cystine-glutamate exchange. J. Physiol. (Lond.). 514:1999;783-793.
    • (1999) J. Physiol. (Lond.) , vol.514 , pp. 783-793
    • Warr, O.1    Takahashi, M.2    Attwell, D.3
  • 1180
    • 0034613310 scopus 로고    scopus 로고
    • Bilirubin does not modulate ionotropic glutamate receptors or glutamate transporters
    • Warr O., Mort D., Attwell D. Bilirubin does not modulate ionotropic glutamate receptors or glutamate transporters. Brain Res. 879:2000;13-16.
    • (2000) Brain Res. , vol.879 , pp. 13-16
    • Warr, O.1    Mort, D.2    Attwell, D.3
  • 1181
    • 0000940099 scopus 로고    scopus 로고
    • Developmental dynamics of gene expression for NMDA receptor channel
    • D.T. Monaghan, & R.J. Wenthold. Totowa, NJ: Humana Press
    • Watanabe M. Developmental dynamics of gene expression for NMDA receptor channel. Monaghan D.T., Wenthold R.J. Ionotropic Glutamate Receptors. 1997;189-218 Humana Press, Totowa, NJ.
    • (1997) Ionotropic Glutamate Receptors , pp. 189-218
    • Watanabe, M.1
  • 1182
    • 0032873812 scopus 로고    scopus 로고
    • Amygdala-kindled and pentylenetetrazole-induced seizures in glutamate transporter GLAST-deficient mice
    • Watanabe, T., Morimoto, K., Hirao, T., Suwaki, H., Watase, K., Tanaka, K., 1999. Amygdala-kindled and pentylenetetrazole-induced seizures in glutamate transporter GLAST-deficient mice. Brain Res. 845, 92-96.
    • (1999) Brain Res. , vol.845 , pp. 92-96
    • Watanabe, T.1    Morimoto, K.2    Hirao, T.3    Suwaki, H.4    Watase, K.5    Tanaka, K.6
  • 1185
    • 15844394296 scopus 로고    scopus 로고
    • Differential expression of glutamate receptor subtypes in rat pancreatic islets
    • Weaver C.D., Yao T.L., Powers A.C., Verdoorn T.A. Differential expression of glutamate receptor subtypes in rat pancreatic islets. J. Biol. Chem. 271:1996;12977-12984.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12977-12984
    • Weaver, C.D.1    Yao, T.L.2    Powers, A.C.3    Verdoorn, T.A.4
  • 1186
    • 0031891008 scopus 로고    scopus 로고
    • A high affinity glutamate/aspartate transport system in pancreatic islets of Langerhans modulates glucose-stimulated insulin secretion
    • Weaver C.D., Gundersen V., Verdoorn T.A. A high affinity glutamate/aspartate transport system in pancreatic islets of Langerhans modulates glucose-stimulated insulin secretion. J. Biol. Chem. 273:1998;1647-1653.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1647-1653
    • Weaver, C.D.1    Gundersen, V.2    Verdoorn, T.A.3
  • 1187
    • 0026069733 scopus 로고
    • Sodium bicarbonate in CPR
    • Weisfeldt M.L., Guerci A.D. Sodium bicarbonate in CPR. JAMA. 266:1991;2129-2130.
    • (1991) JAMA , vol.266 , pp. 2129-2130
    • Weisfeldt, M.L.1    Guerci, A.D.2
  • 1188
    • 0023751240 scopus 로고
    • Beta-N-methylamino-L-alanine neurotoxicity: Requirement for bicarbonate as a cofactor
    • Weiss J.H., Choi D.W. Beta-N-methylamino-L-alanine neurotoxicity: requirement for bicarbonate as a cofactor. Science. 241:1988;973-975.
    • (1988) Science , vol.241 , pp. 973-975
    • Weiss, J.H.1    Choi, D.W.2
  • 1189
    • 0032742481 scopus 로고    scopus 로고
    • Glutamate transport and renal function
    • Welbourne T.C., Matthews J.C. Glutamate transport and renal function. Am. J. Physiol. 277:1999;F501-F505.
    • (1999) Am. J. Physiol. , vol.277 , pp. 501-F505
    • Welbourne, T.C.1    Matthews, J.C.2
  • 1190
    • 0026658241 scopus 로고
    • Structure and specificities of anti-ganglioside autoantibodies associated with motor neuropathies
    • Weng N.P., Yu-Lee L.Y., Sanz I., Patten B.M., Marcus D.M. Structure and specificities of anti-ganglioside autoantibodies associated with motor neuropathies. J. Immunol. 149:1992;2518-2529.
    • (1992) J. Immunol. , vol.149 , pp. 2518-2529
    • Weng, N.P.1    Yu-Lee, L.Y.2    Sanz, I.3    Patten, B.M.4    Marcus, D.M.5
  • 1191
    • 0031733134 scopus 로고    scopus 로고
    • The organization and regulation of non-NMDA receptors in neurons
    • Wenthold R.J., Roche K.W. The organization and regulation of non-NMDA receptors in neurons. Prog. Brain Res. 116:1998;133-152.
    • (1998) Prog. Brain Res. , vol.116 , pp. 133-152
    • Wenthold, R.J.1    Roche, K.W.2
  • 1192
    • 0026012569 scopus 로고
    • The influence of long-term potentiation on the spatial relationship between astrocyte processes and potentiated synapses in the dentate gyrus neuropil of rat brain
    • Wenzel J., Lammert G., Meyer U., Krug M. The influence of long-term potentiation on the spatial relationship between astrocyte processes and potentiated synapses in the dentate gyrus neuropil of rat brain. Brain Res. 560:1991;122-131.
    • (1991) Brain Res. , vol.560 , pp. 122-131
    • Wenzel, J.1    Lammert, G.2    Meyer, U.3    Krug, M.4
  • 1193
    • 0028879327 scopus 로고
    • Metabolic trafficking between neurons and astrocytes: The glutamate glutamine cycle revisited
    • Westergaard N., Sonnewald U., Schousboe A. Metabolic trafficking between neurons and astrocytes: the glutamate glutamine cycle revisited. Dev. Neurosci. 17:1995;203-211.
    • (1995) Dev. Neurosci. , vol.17 , pp. 203-211
    • Westergaard, N.1    Sonnewald, U.2    Schousboe, A.3
  • 1194
    • 0023196861 scopus 로고
    • Are there both low- And high-affinity glutamate transporters in rat cortical synaptosomes?
    • Wheeler D.D. Are there both low- and high-affinity glutamate transporters in rat cortical synaptosomes? Neurochem. Res. 12:1987;667-681.
    • (1987) Neurochem. Res. , vol.12 , pp. 667-681
    • Wheeler, D.D.1
  • 1195
    • 0027157676 scopus 로고
    • Biology of disease - Neuroexcitation, excitotoxicity and human neurological disease
    • Whetsell W.O., Shapira N.A. Biology of disease - neuroexcitation, excitotoxicity and human neurological disease. Lab. Invest. 68:1993;372-387.
    • (1993) Lab. Invest. , vol.68 , pp. 372-387
    • Whetsell, W.O.1    Shapira, N.A.2
  • 1196
    • 51849178119 scopus 로고
    • Toxicity of cycads
    • Whiting M.G. Toxicity of cycads. Econ. Bot. 17:1964;64-71.
    • (1964) Econ. Bot. , vol.17 , pp. 64-71
    • Whiting, M.G.1
  • 1198
    • 0032741628 scopus 로고    scopus 로고
    • Neuroepidemiologic research initiatives on Guam: Past and present
    • Wiederholt W.C. Neuroepidemiologic research initiatives on Guam: past and present. Neuroepidemiology. 18:1999;279-291.
    • (1999) Neuroepidemiology , vol.18 , pp. 279-291
    • Wiederholt, W.C.1
  • 1199
    • 0022344980 scopus 로고
    • Hypoglycemia-induced neuronal damage prevented by an N-methyl-D-aspartate antagonist
    • Wieloch T. Hypoglycemia-induced neuronal damage prevented by an N-methyl-D-aspartate antagonist. Science. 230:1985;681-683.
    • (1985) Science , vol.230 , pp. 681-683
    • Wieloch, T.1
  • 1200
    • 0019970939 scopus 로고
    • Putative acidic amino acid transmitters in the cerebellum. II. Electron microscopic localization of transport sites
    • Wilkin G.P., Garthwaite J., Balazs R. Putative acidic amino acid transmitters in the cerebellum. II. Electron microscopic localization of transport sites. Brain Res. 244:1982;69-80.
    • (1982) Brain Res. , vol.244 , pp. 69-80
    • Wilkin, G.P.1    Garthwaite, J.2    Balazs, R.3
  • 1202
    • 0032847877 scopus 로고    scopus 로고
    • Effects of chronic alcohol consumption on the expression of different NR1 splice variants in the brain of AA and ANA lines of rats
    • Winkler A., Mahal B., Kiianmaa K., Zieglgansberger W., Spanagel R. Effects of chronic alcohol consumption on the expression of different NR1 splice variants in the brain of AA and ANA lines of rats. Mol. Brain Res. 72:1999;166-175.
    • (1999) Mol. Brain Res. , vol.72 , pp. 166-175
    • Winkler, A.1    Mahal, B.2    Kiianmaa, K.3    Zieglgansberger, W.4    Spanagel, R.5
  • 1203
    • 0015069366 scopus 로고
    • A unique synaptosomal fraction, which accumulates glutamic and aspartic acids, in brain tissue
    • Wofsey A.R., Kuhar M.J., Snyder S.H. A unique synaptosomal fraction, which accumulates glutamic and aspartic acids, in brain tissue. Proc. Natl. Acad. Sci. USA. 68:1971;1102-1106.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1102-1106
    • Wofsey, A.R.1    Kuhar, M.J.2    Snyder, S.H.3
  • 1204
    • 0033052828 scopus 로고    scopus 로고
    • Ionotropic glutamate receptors as sites of action for ethanol in the brain
    • Woodward J.J. Ionotropic glutamate receptors as sites of action for ethanol in the brain. Neurochem. Int. 35:1999;107-113.
    • (1999) Neurochem. Int. , vol.35 , pp. 107-113
    • Woodward, J.J.1
  • 1205
    • 0026627947 scopus 로고
    • Estradiol mediates fluctuation in hippocampal synapse density during the estrous cycle in the adult rat
    • Woolley C.S., McEwen B.S. Estradiol mediates fluctuation in hippocampal synapse density during the estrous cycle in the adult rat. J. Neurosci. 12:1992;2549-2554.
    • (1992) J. Neurosci. , vol.12 , pp. 2549-2554
    • Woolley, C.S.1    McEwen, B.S.2
  • 1206
    • 0029888215 scopus 로고    scopus 로고
    • The effect of age on susceptibility to brain damage in a model of global hemispheric hypoxia-ischemia
    • Yager J.Y., Shuaib A., Thornhill J. The effect of age on susceptibility to brain damage in a model of global hemispheric hypoxia-ischemia. Dev. Brain Res. 93:1996;143-154.
    • (1996) Dev. Brain Res. , vol.93 , pp. 143-154
    • Yager, J.Y.1    Shuaib, A.2    Thornhill, J.3
  • 1208
    • 0029958203 scopus 로고    scopus 로고
    • EAAT4 is a post-synaptic glutamate transporter at Purkinje cell synapses
    • Yamada K., Watanabe M., Shibata T., Tanaka K., Wada K., Inoue Y. EAAT4 is a post-synaptic glutamate transporter at Purkinje cell synapses. Neuroreport. 7:1996;2013-2017.
    • (1996) Neuroreport , vol.7 , pp. 2013-2017
    • Yamada, K.1    Watanabe, M.2    Shibata, T.3    Tanaka, K.4    Wada, K.5    Inoue, Y.6
  • 1209
    • 0032146774 scopus 로고    scopus 로고
    • Glutamate transporter GLT-1 is transiently localized on growing axons of the mouse spinal cord before establishing astrocytic expression
    • Yamada K., Watanabe M., Shibata T., Nagashima M., Tanaka K., Inoue Y. Glutamate transporter GLT-1 is transiently localized on growing axons of the mouse spinal cord before establishing astrocytic expression. J. Neurosci. 18:1998;5706-5713.
    • (1998) J. Neurosci. , vol.18 , pp. 5706-5713
    • Yamada, K.1    Watanabe, M.2    Shibata, T.3    Nagashima, M.4    Tanaka, K.5    Inoue, Y.6
  • 1210
    • 0029893179 scopus 로고    scopus 로고
    • Changes in glutamate/aspartate transporter (GLAST/glut-1) mRNA expression following facial nerve transection
    • Yamashita T., Kohmura E., Yuguchi T., Shimada S., Tanaka K., Hayakawa T., Tohyama M. Changes in glutamate/aspartate transporter (GLAST/glut-1) mRNA expression following facial nerve transection. Mol. Brain Res. 38:1996;294-299.
    • (1996) Mol. Brain Res. , vol.38 , pp. 294-299
    • Yamashita, T.1    Kohmura, E.2    Yuguchi, T.3    Shimada, S.4    Tanaka, K.5    Hayakawa, T.6    Tohyama, M.7
  • 1211
    • 0032536353 scopus 로고    scopus 로고
    • Effect of glutamate transporter on neuronal damage induced by photochemical thrombotic brain ischemia
    • Yan Y.P., Yin K.J., Sun F.Y. Effect of glutamate transporter on neuronal damage induced by photochemical thrombotic brain ischemia. Neuroreport. 9:1998;441-446.
    • (1998) Neuroreport , vol.9 , pp. 441-446
    • Yan, Y.P.1    Yin, K.J.2    Sun, F.Y.3
  • 1213
    • 0003364645 scopus 로고    scopus 로고
    • Oxygen radicals in glutamate toxicity of C6 glioma cells via transporter system
    • L. Packer, M. Hiramatsu, & T. Yoshikawa. San Diegi, CA: Academic Press
    • Yasui Y., Mawatari K., Higuchi Y., Tanii H., Kato S. Oxygen radicals in glutamate toxicity of C6 glioma cells via transporter system. Packer L., Hiramatsu M., Yoshikawa T. Free Radicals in Brain Physiology and Disorders. 1996;51-67 Academic Press, San Diegi, CA.
    • (1996) Free Radicals in Brain Physiology and Disorders , pp. 51-67
    • Yasui, Y.1    Mawatari, K.2    Higuchi, Y.3    Tanii, H.4    Kato, S.5
  • 1215
    • 0029804572 scopus 로고    scopus 로고
    • Cytokine modulation of glial glutamate uptake: A possible involvement of nitric oxide
    • Ye Z.C., Sontheimer H. Cytokine modulation of glial glutamate uptake: a possible involvement of nitric oxide. Neuroreport. 7:1996;2181-2185.
    • (1996) Neuroreport , vol.7 , pp. 2181-2185
    • Ye, Z.C.1    Sontheimer, H.2
  • 1216
    • 0033198997 scopus 로고    scopus 로고
    • Glioma cells release excitotoxic concentrations of glutamate
    • Ye Z.C., Sontheimer H. Glioma cells release excitotoxic concentrations of glutamate. Cancer Res. 59:1999;4383-4391.
    • (1999) Cancer Res. , vol.59 , pp. 4383-4391
    • Ye, Z.C.1    Sontheimer, H.2
  • 1217
    • 0033573392 scopus 로고    scopus 로고
    • Compromised glutamate transport in human glioma cells: Reduction-mislocalization of sodium-dependent glutamate transporters and enhanced activity of cystine-glutamate exchange
    • Ye Z.C., Rothstein J.D., Sontheimer H. Compromised glutamate transport in human glioma cells: reduction-mislocalization of sodium-dependent glutamate transporters and enhanced activity of cystine-glutamate exchange. J. Neurosci. 19:1999;10767-10777.
    • (1999) J. Neurosci. , vol.19 , pp. 10767-10777
    • Ye, Z.C.1    Rothstein, J.D.2    Sontheimer, H.3
  • 1218
    • 0031899788 scopus 로고    scopus 로고
    • Altered expression of glutamate transporter GLAST mRNA in rat brain after photochemically induced focal ischemia
    • Yin K.J., Yan Y.P., Sun F.Y. Altered expression of glutamate transporter GLAST mRNA in rat brain after photochemically induced focal ischemia. Anat. Rec. 251:1998;9-14.
    • (1998) Anat. Rec. , vol.251 , pp. 9-14
    • Yin, K.J.1    Yan, Y.P.2    Sun, F.Y.3
  • 1219
    • 0030835921 scopus 로고    scopus 로고
    • Deleterious network: A testable pathogenetic concept of Alzheimer's disease
    • Ying W.H. Deleterious network: a testable pathogenetic concept of Alzheimer's disease. Gerontology. 43:1997;242-253.
    • (1997) Gerontology , vol.43 , pp. 242-253
    • Ying, W.H.1
  • 1220
    • 0026778734 scopus 로고
    • Isolated bovine spinal motoneurons have specific ganglioside antigens recognized by sera from patients with motor neuron disease and motor neuropathy
    • Yoshino H., Miyatani N., Saito M., Ariga T., Lugaresi A., Latov N., Kushi Y., Kasama T., Yu R.K. Isolated bovine spinal motoneurons have specific ganglioside antigens recognized by sera from patients with motor neuron disease and motor neuropathy. J. Neurochem. 59:1992;1684-1691.
    • (1992) J. Neurochem. , vol.59 , pp. 1684-1691
    • Yoshino, H.1    Miyatani, N.2    Saito, M.3    Ariga, T.4    Lugaresi, A.5    Latov, N.6    Kushi, Y.7    Kasama, T.8    Yu, R.K.9
  • 1221
    • 0022476899 scopus 로고
    • Effects of arachidonic acid on glutamate and gamma-aminobutyric acid uptake in primary cultures of rat cerebral cortical astrocytes and neurons
    • Yu A.C.H., Chan P.H., Fishman R.A. Effects of arachidonic acid on glutamate and gamma-aminobutyric acid uptake in primary cultures of rat cerebral cortical astrocytes and neurons. J. Neurochem. 47:1986;1181-1189.
    • (1986) J. Neurochem. , vol.47 , pp. 1181-1189
    • Yu, A.C.H.1    Chan, P.H.2    Fishman, R.A.3
  • 1222
  • 1223
    • 0032478315 scopus 로고    scopus 로고
    • Effects of feline immunodeficiency virus on astrocyte glutamate uptake: Implications for lentivirus-induced central nervous system diseases
    • Yu N., Billaud J.N., Phillips T.R. Effects of feline immunodeficiency virus on astrocyte glutamate uptake: implications for lentivirus-induced central nervous system diseases. Proc. Natl. Acad. Sci. USA. 95:1998;2624-2629.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2624-2629
    • Yu, N.1    Billaud, J.N.2    Phillips, T.R.3
  • 1224
    • 0023091127 scopus 로고
    • Characteristics of chloride-dependent incorporation of glutamate into brain membranes argue against a receptor binding site
    • Zaczek R., Arlis S., Markl A., Murphy T., Drucker H., Coyle J.T. Characteristics of chloride-dependent incorporation of glutamate into brain membranes argue against a receptor binding site. Neuropharmacology. 26:1987;281-287.
    • (1987) Neuropharmacology , vol.26 , pp. 281-287
    • Zaczek, R.1    Arlis, S.2    Markl, A.3    Murphy, T.4    Drucker, H.5    Coyle, J.T.6
  • 1225
    • 0025147233 scopus 로고
    • Arachidonic acid inhibits glycine transport in cultured glial cells
    • Zafra F., Alcántara R., Gomeza J., Aragón C., Gimenez C. Arachidonic acid inhibits glycine transport in cultured glial cells. Biochem. J. 271:1990;237-242.
    • (1990) Biochem. J. , vol.271 , pp. 237-242
    • Zafra, F.1    Alcántara, R.2    Gomeza, J.3    Aragón, C.4    Gimenez, C.5
  • 1227
    • 0031172640 scopus 로고    scopus 로고
    • Neuronal dependency of the glycine transporter GLYT1 expression in glial cells
    • Zafra F., Poyatos I., Gimenez C. Neuronal dependency of the glycine transporter GLYT1 expression in glial cells. Glia. 20:1997;155-162.
    • (1997) Glia , vol.20 , pp. 155-162
    • Zafra, F.1    Poyatos, I.2    Gimenez, C.3
  • 1228
    • 0032486463 scopus 로고    scopus 로고
    • Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue
    • Zarbiv R., Grunewald M., Kavanaugh M.P., Kanner B.I. Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue. J. Biol. Chem. 273:1998;14231-14237.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14231-14237
    • Zarbiv, R.1    Grunewald, M.2    Kavanaugh, M.P.3    Kanner, B.I.4
  • 1230
    • 0033769126 scopus 로고    scopus 로고
    • Degradation of glial glutamate transporter mRNAs is selectively blocked by inhibition of cellular transcription
    • Zelenaia O.A., Robinson M.B. Degradation of glial glutamate transporter mRNAs is selectively blocked by inhibition of cellular transcription. J. Neurochem. 75:2000;2252-2258.
    • (2000) J. Neurochem. , vol.75 , pp. 2252-2258
    • Zelenaia, O.A.1    Robinson, M.B.2
  • 1231
    • 0034038270 scopus 로고    scopus 로고
    • Epidermal growth factor receptor agonists increase expression of glutamate transporter GLT-1 in astrocytes through pathways dependent on phosphatidylinositol 3-kinase and transcription factor NF-kappa B
    • Zelenaia O., Schlag B.D., Gochenauer G.E., Ganel R., Song W., Beesley J.S., Grinspan J.B., Rothstein J.D., Robinson M.B. Epidermal growth factor receptor agonists increase expression of glutamate transporter GLT-1 in astrocytes through pathways dependent on phosphatidylinositol 3-kinase and transcription factor NF-kappa B. Mol. Pharmacol. 57:2000;667-678.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 667-678
    • Zelenaia, O.1    Schlag, B.D.2    Gochenauer, G.E.3    Ganel, R.4    Song, W.5    Beesley, J.S.6    Grinspan, J.B.7    Rothstein, J.D.8    Robinson, M.B.9
  • 1232
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue N., Kavanaugh M.P. Flux coupling in a neuronal glutamate transporter. Nature. 383:1996;634-637.
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 1233
    • 0029891464 scopus 로고    scopus 로고
    • Interaction of L-cysteine with a human excitatory amino acid transporter - Short paper given rapid review
    • Zerangue N., Kavanaugh M.P. Interaction of L-cysteine with a human excitatory amino acid transporter - short paper given rapid review. J. Physiol. (Lond.). 493:1996;419-423.
    • (1996) J. Physiol. (Lond.) , vol.493 , pp. 419-423
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 1234
    • 0028911077 scopus 로고
    • Differential modulation of human glutamate transporter subtypes by arachidonic acid
    • Zerangue N., Arriza J.L., Amara S.G., Kavanaugh M.P. Differential modulation of human glutamate transporter subtypes by arachidonic acid. J. Biol. Chem. 270:1995;6433-6435.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6433-6435
    • Zerangue, N.1    Arriza, J.L.2    Amara, S.G.3    Kavanaugh, M.P.4
  • 1235
    • 0033573907 scopus 로고    scopus 로고
    • Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitter
    • Zhang Y.M., Kanner B.I. Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitter. Proc. Natl. Acad. Sci. USA. 96:1999;1710-1715.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1710-1715
    • Zhang, Y.M.1    Kanner, B.I.2
  • 1238
    • 0011352859 scopus 로고
    • A model system for quantitation in single and double labelling postembedding electron microscopic immunocytochemistry
    • 93-050-13. Elsevier, Amsterdam
    • Zhang, N., Storm-Mathisen, J., Ottersen, O.P., 1993. A model system for quantitation in single and double labelling postembedding electron microscopic immunocytochemistry. Elsevier Neuroscience Protocols, 93-050-13. Elsevier, Amsterdam, pp. 1-20.
    • (1993) Elsevier Neuroscience Protocols , pp. 1-20
    • Zhang, N.1    Storm-Mathisen, J.2    Ottersen, O.P.3
  • 1239
    • 0031025786 scopus 로고    scopus 로고
    • Delta-glutamate receptors are differentially distributed at parallel and climbing fiber synapses on Purkinje cells
    • Zhao H.M., Wenthold R.J., Wang Y.X., Petralia R.S. Delta-glutamate receptors are differentially distributed at parallel and climbing fiber synapses on Purkinje cells. J. Neurochem. 68:1997;1041-1052.
    • (1997) J. Neurochem. , vol.68 , pp. 1041-1052
    • Zhao, H.M.1    Wenthold, R.J.2    Wang, Y.X.3    Petralia, R.S.4
  • 1240
    • 0032528151 scopus 로고    scopus 로고
    • Glutamate receptor targeting to synaptic populations on Purkinje cells is developmentally regulated
    • Zhao H.M., Wenthold R.J., Petralia R.S. Glutamate receptor targeting to synaptic populations on Purkinje cells is developmentally regulated. J. Neurosci. 18:1998;5517-5528.
    • (1998) J. Neurosci. , vol.18 , pp. 5517-5528
    • Zhao, H.M.1    Wenthold, R.J.2    Petralia, R.S.3
  • 1241
    • 0032695071 scopus 로고    scopus 로고
    • Ammonia downregulates GLAST mRNA glutamate transporter in rat astrocyte cultures
    • Zhou B.G., Norenberg M.D. Ammonia downregulates GLAST mRNA glutamate transporter in rat astrocyte cultures. Neurosci. Lett. 276:1999;145-148.
    • (1999) Neurosci. Lett. , vol.276 , pp. 145-148
    • Zhou, B.G.1    Norenberg, M.D.2
  • 1242
    • 0031019118 scopus 로고    scopus 로고
    • Down-regulation of norepinephrine transporters on PC12 cells by transporter inhibitors
    • Zhu M.Y., Ordway G.A. Down-regulation of norepinephrine transporters on PC12 cells by transporter inhibitors. J. Neurochem. 68:1997;134-141.
    • (1997) J. Neurochem. , vol.68 , pp. 134-141
    • Zhu, M.Y.1    Ordway, G.A.2
  • 1243
    • 0030922926 scopus 로고    scopus 로고
    • Activation of protein kinase C inhibits uptake, currents and binding associated with the human dopamine transporter expressed in Xenopus oocytes
    • Zhu S.J., Kavanaugh M.P., Sonders M.S., Amara S.G., Zahniser N.R. Activation of protein kinase C inhibits uptake, currents and binding associated with the human dopamine transporter expressed in Xenopus oocytes. J. Pharmacol. Exp. Ther. 282:1997;1358-1365.
    • (1997) J. Pharmacol. Exp. Ther. , vol.282 , pp. 1358-1365
    • Zhu, S.J.1    Kavanaugh, M.P.2    Sonders, M.S.3    Amara, S.G.4    Zahniser, N.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.