메뉴 건너뛰기




Volumn 31, Issue 3, 1999, Pages 619-634

Neurotoxic mechanisms of degeneration in motor neuron diseases

Author keywords

Amyotrophic lateral sclerosis; Cu Zn SOD; Excitotoxicity; Free radicals; Motor neuron disease

Indexed keywords

3 OXALYLAMINOALANINE; COPPER ZINC SUPEROXIDE DISMUTASE; FREE RADICAL; GLUTAMATE RECEPTOR; GLUTAMIC ACID;

EID: 0344631768     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.1081/DMR-100101938     Document Type: Conference Paper
Times cited : (7)

References (75)
  • 1
    • 0014682523 scopus 로고
    • Brain lesions in an infant rhesus monkey treated with monsodium glutamate
    • J. W. Olney and L. G. Sharpe, Brain lesions in an infant rhesus monkey treated with monsodium glutamate, Science, 166, 386-388 (1969).
    • (1969) Science , vol.166 , pp. 386-388
    • Olney, J.W.1    Sharpe, L.G.2
  • 2
    • 0024093449 scopus 로고
    • Glutamate neurotoxicity and diseases of the nervous system
    • D. W. Choi, Glutamate neurotoxicity and diseases of the nervous system, Neuron, 1, 623-634 (1987).
    • (1987) Neuron , vol.1 , pp. 623-634
    • Choi, D.W.1
  • 9
    • 0025995296 scopus 로고
    • RNA editing in brain controls a determinant of ion flow in glutamate-gated channels
    • B. Sommer, M. Kohler, R. Sprengel, and P. H. Seeburg, RNA editing in brain controls a determinant of ion flow in glutamate-gated channels, Cell, 67, 11-19 (1991).
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Kohler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 10
    • 0023137252 scopus 로고
    • Ionic dependence of glutamate neurotoxicity
    • D. W. Choi, Ionic dependence of glutamate neurotoxicity, J. Neurosci., 7, 369-379 (1987).
    • (1987) J. Neurosci. , vol.7 , pp. 369-379
    • Choi, D.W.1
  • 11
    • 0030638249 scopus 로고    scopus 로고
    • Neuronal necrosis and apoptosis: Two distinct events induced by exposure to glutamate or oxidative stress
    • P. Nicotera, M. Ankarcrona, E. Bonfoco, S. Orrenius, and S. A. Lipton, Neuronal necrosis and apoptosis: Two distinct events induced by exposure to glutamate or oxidative stress, Adv. Neurol., 72, 95-101 (1997).
    • (1997) Adv. Neurol. , vol.72 , pp. 95-101
    • Nicotera, P.1    Ankarcrona, M.2    Bonfoco, E.3    Orrenius, S.4    Lipton, S.A.5
  • 12
    • 0030273118 scopus 로고    scopus 로고
    • Ischemia-induced neuronal apoptosis
    • D. W. Choi, Ischemia-induced neuronal apoptosis, Curr. Opin. Neurobiol., 6, 667-672 (1996).
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 667-672
    • Choi, D.W.1
  • 14
    • 0021329454 scopus 로고
    • Immunohistochemical mapping of calcium-binding protein immunoreactivity in the rat central nervous system
    • L. M. Garcia-Segura, D. Baetens, J. Roth, A. W. Norman, and L. Orci, Immunohistochemical mapping of calcium-binding protein immunoreactivity in the rat central nervous system, Brain Res., 296, 75-86 (1984).
    • (1984) Brain Res. , vol.296 , pp. 75-86
    • Garcia-Segura, L.M.1    Baetens, D.2    Roth, J.3    Norman, A.W.4    Orci, L.5
  • 16
    • 0026584524 scopus 로고
    • Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?
    • M. F. Beal, Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses? Ann. Neurol., 31, 119-130 (1992).
    • (1992) Ann. Neurol. , vol.31 , pp. 119-130
    • Beal, M.F.1
  • 17
    • 0026609559 scopus 로고
    • Alternative excitotoxic hypotheses
    • R. L. Albin and J. T. Greenamyre, Alternative excitotoxic hypotheses, Neurology, 42, 733-739 (1992).
    • (1992) Neurology , vol.42 , pp. 733-739
    • Albin, R.L.1    Greenamyre, J.T.2
  • 18
    • 0027171494 scopus 로고
    • Excitotoxicity, energy metabolism and neurodegeneration
    • A. C. Ludolph, M. Riepe, and K. Ullrich, Excitotoxicity, energy metabolism and neurodegeneration, J. Inherit. Metab. Dis., 16, 716-723 (1993).
    • (1993) J. Inherit. Metab. Dis. , vol.16 , pp. 716-723
    • Ludolph, A.C.1    Riepe, M.2    Ullrich, K.3
  • 20
    • 0023123455 scopus 로고
    • Studies on the aetiology and pathogenesis of motor neuron diseases. 1. Lathyrism: Clinical findings in established cases
    • A. C. Ludolph, J. Hugon, M. P. Dwivedi, H. H. Schaumburg, and P. S. Spencer, Studies on the aetiology and pathogenesis of motor neuron diseases. 1. Lathyrism: clinical findings in established cases, Brain, 110, 149-165 (1987).
    • (1987) Brain , vol.110 , pp. 149-165
    • Ludolph, A.C.1    Hugon, J.2    Dwivedi, M.P.3    Schaumburg, H.H.4    Spencer, P.S.5
  • 21
    • 0026714914 scopus 로고
    • Are human neurodegenerative disorders linked to environmental chemicals with excitotoxic properties?
    • P. S. Spencer, A. C. Ludolph, and G. E. Kisby, Are human neurodegenerative disorders linked to environmental chemicals with excitotoxic properties? Ann. NY Acad. Sci., 648, 154-160 (1992).
    • (1992) Ann. NY Acad. Sci. , vol.648 , pp. 154-160
    • Spencer, P.S.1    Ludolph, A.C.2    Kisby, G.E.3
  • 22
    • 0029832232 scopus 로고    scopus 로고
    • Toxic models of upper motor neuron disease
    • A. C. Ludolph and P. S. Spencer, Toxic models of upper motor neuron disease, J. Neurol. Sci., 139 (Suppl.), 53-59 (1996).
    • (1996) J. Neurol. Sci. , vol.139 , Issue.SUPPL. , pp. 53-59
    • Ludolph, A.C.1    Spencer, P.S.2
  • 23
    • 0030273295 scopus 로고    scopus 로고
    • Mitochondria, free radicals, and neurodegeneration
    • M. F. Beal, Mitochondria, free radicals, and neurodegeneration, Curr. Opin. Neurobiol., 6, 661-666 (1996).
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 661-666
    • Beal, M.F.1
  • 24
    • 0002634911 scopus 로고
    • Clinical features and differential diagnosis of classical motor neuron disease
    • A. C. Williams, ed., Chapman & Hall Medical, London
    • R. Tandan, Clinical features and differential diagnosis of classical motor neuron disease, in Motor Neuron Disease (A. C. Williams, ed.), Chapman & Hall Medical, London, 1994, pp. 1-27.
    • (1994) Motor Neuron Disease , pp. 1-27
    • Tandan, R.1
  • 25
    • 0023918762 scopus 로고
    • Comparison of sporadic and familial disease amongst 580 cases of motor neuron disease
    • T. M. Li, E. Alberman, and M. Swash, Comparison of sporadic and familial disease amongst 580 cases of motor neuron disease, J. Neurol. Neurosurg. Psychiatry, 51, 778-784 (1988).
    • (1988) J. Neurol. Neurosurg. Psychiatry , vol.51 , pp. 778-784
    • Li, T.M.1    Alberman, E.2    Swash, M.3
  • 26
    • 0030070333 scopus 로고    scopus 로고
    • Copper/zinc superoxide dismutase expression in the human central nervous system. Correlation with selective neuronal vulnerability
    • C. Bergeron, C. Petrunka, and L. Weyer, Copper/zinc superoxide dismutase expression in the human central nervous system. Correlation with selective neuronal vulnerability, Am. J. Pathol., 148, 273-279 (1996).
    • (1996) Am. J. Pathol. , vol.148 , pp. 273-279
    • Bergeron, C.1    Petrunka, C.2    Weyer, L.3
  • 27
    • 0028815433 scopus 로고
    • Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons
    • C. A. Pardo, Z. Xu, D. R. Borchelt, D. L. Price, S. S. Sisodia, and D. W. Cleveland, Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc. Natl. Acad. Sci. USA, 92, 954-958 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3    Price, D.L.4    Sisodia, S.S.5    Cleveland, D.W.6
  • 28
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • I. Fridovich, Superoxide radical and superoxide dismutases, Annu. Rev. Biochem., 64, 97-112 (1995).
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 29
    • 0027456505 scopus 로고
    • Enzyme function of copper, zinc superoxide dismutase as a free radical generator
    • M. B. Yim, P. B. Chock, and E. R. Stadtman, Enzyme function of copper, zinc superoxide dismutase as a free radical generator, J. Biol. Chem., 268, 4099-4105 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4099-4105
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 32
    • 0029584941 scopus 로고
    • Superoxide dismutase in familial amyotrophic lateral sclerosis: Models for gain of function
    • R. H. Brown, Superoxide dismutase in familial amyotrophic lateral sclerosis: models for gain of function, Curr. Opin. Neurobiol., 5, 841-846 (1995).
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 841-846
    • Brown, R.H.1
  • 36
    • 0028933344 scopus 로고
    • Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS)
    • M. C. Dal Canto and M. E. Gurney, Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS), Brain Res., 676, 25-40 (1995).
    • (1995) Brain Res. , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 38
    • 0029966363 scopus 로고    scopus 로고
    • Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions
    • P. H. Tu, P. Raju, K. A. Robinson, M. E. Gurney, J. Q. Trojanowski, and V. M. Lee, Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions, Proc. Natl. Acad. Sci. USA, 93, 3155-3160 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3155-3160
    • Tu, P.H.1    Raju, P.2    Robinson, K.A.3    Gurney, M.E.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 41
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • M. Gurney, F. B. Cutting, P. Zhai, A. Doble, C. P. Taylor, P. K. Andrus, and E. D. Hall, Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis, Ann. Neurol., 39, 147-158 (1996).
    • (1996) Ann. Neurol. , vol.39 , pp. 147-158
    • Gurney, M.1    Cutting, F.B.2    Zhai, P.3    Doble, A.4    Taylor, C.P.5    Andrus, P.K.6    Hall, E.D.7
  • 42
    • 0030862630 scopus 로고    scopus 로고
    • The copper chelator d-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • A. Hottinger, E. G. Fine, M. E. Gurney, A. D. Zurn, and P. Aebischer, The copper chelator d-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis, Eur. J. Neurosci., 9, 2548-2552 (1997).
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 2548-2552
    • Hottinger, A.1    Fine, E.G.2    Gurney, M.E.3    Zurn, A.D.4    Aebischer, P.5
  • 43
    • 0027274623 scopus 로고
    • Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity
    • J. D. Rothstein, L. Jin, M. Dykes-Hoberg, and R. W. Kuncl, Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity, Proc. Natl. Acad. Sci. USA, 90, 6591-6595 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6591-6595
    • Rothstein, J.D.1    Jin, L.2    Dykes-Hoberg, M.3    Kuncl, R.W.4
  • 44
    • 13344261949 scopus 로고    scopus 로고
    • Motor neuron degeneration induced by excitotoxin agonists has features in common with those seen in the SOD-1 transgenic mouse model of amyotrophic lateral sclerosis
    • C. Ikonomidou, Y. Qin Qin, J. Labruyere, and J. W. Olney, Motor neuron degeneration induced by excitotoxin agonists has features in common with those seen in the SOD-1 transgenic mouse model of amyotrophic lateral sclerosis, J. Neuropathol. Exp. Neurol., 55, 211-224 (1996).
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 211-224
    • Ikonomidou, C.1    Qin Qin, Y.2    Labruyere, J.3    Olney, J.W.4
  • 45
    • 0030015076 scopus 로고    scopus 로고
    • Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro
    • S. G. Carriedo, H. Z. Yin, and J. H. Weiss, Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro, J. Neurosci., 16, 4069-4079 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 4069-4079
    • Carriedo, S.G.1    Yin, H.Z.2    Weiss, J.H.3
  • 46
    • 0032527065 scopus 로고    scopus 로고
    • Light and electron microscopic distribution of the AMPA receptor subunit, GluR2, in the spinal cord of control and G86R mutant superoxide dismutase transgenic mice
    • M. Morrison, W. G. M. Janssen, J. W. Gordon, and J. H. Morrison, Light and electron microscopic distribution of the AMPA receptor subunit, GluR2, in the spinal cord of control and G86R mutant superoxide dismutase transgenic mice, J. Comp. Neurol., 395, 523-534 (1998).
    • (1998) J. Comp. Neurol. , vol.395 , pp. 523-534
    • Morrison, M.1    Janssen, W.G.M.2    Gordon, J.W.3    Morrison, J.H.4
  • 48
    • 0030800468 scopus 로고    scopus 로고
    • Neurodegeneration in lurcher mice caused by mutation in delta2 glutamate receptor gene
    • J. Zuo, P. L. De Jager, K. A. Takahashi, W. Jiang, D. J. Linden, and N. Heintz, Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene, Nature, 388, 769-773 (1997).
    • (1997) Nature , vol.388 , pp. 769-773
    • Zuo, J.1    De Jager, P.L.2    Takahashi, K.A.3    Jiang, W.4    Linden, D.J.5    Heintz, N.6
  • 49
    • 0026597010 scopus 로고
    • Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis
    • J. D. Rothstein, L. J. Martin, and R. W. Kuncl, Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis, N. Engl. J. Med., 326, 1464-1468 (1992).
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1464-1468
    • Rothstein, J.D.1    Martin, L.J.2    Kuncl, R.W.3
  • 50
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • J. D. Rothstein, M. Van Kammen, A. I. Levey, L. J. Martin, and R. W. Kuncl, Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis, Ann. Neurol., 38, 73-84 (1995).
    • (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
  • 51
    • 0026489330 scopus 로고
    • Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain
    • T. Storck, S. Schulte, K. Hofmann, and W. Stoffel, Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain, Proc. Natl. Acad. Sci. USA, 89, 10,955-10,959 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10955-10959
    • Storck, T.1    Schulte, S.2    Hofmann, K.3    Stoffel, W.4
  • 52
    • 0026458124 scopus 로고
    • Primary structure and functional characterization of a high-affinity glutamate transporter
    • Y. Kanai and M. A. Hediger, Primary structure and functional characterization of a high-affinity glutamate transporter, Nature, 360, 467-471 (1992).
    • (1992) Nature , vol.360 , pp. 467-471
    • Kanai, Y.1    Hediger, M.A.2
  • 54
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • W. A. Fairman, R. J. Vandenberg, J. L. Arriza, M. P. Kavanaugh, and S. G. Amara, An excitatory amino-acid transporter with properties of a ligand-gated chloride channel, Nature, 375, 599-604 (1995).
    • (1995) Nature , vol.375 , pp. 599-604
    • Fairman, W.A.1    Vandenberg, R.J.2    Arriza, J.L.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 55
    • 0028031487 scopus 로고
    • Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex
    • J. L. Arriza, W. A. Fairman, J. I. Wadiche, G. H. Murdoch, M. P. Kavanaugh, and S. G. Amara, Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex, J. Neurosci., 14, 5559-5569 (1994).
    • (1994) J. Neurosci. , vol.14 , pp. 5559-5569
    • Arriza, J.L.1    Fairman, W.A.2    Wadiche, J.I.3    Murdoch, G.H.4    Kavanaugh, M.P.5    Amara, S.G.6
  • 56
    • 0030932152 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance
    • J. L. Arriza, S. Eliasof, M. P. Kavanaugh, and S. G. Amara, Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance, Proc. Natl. Acad. Sci. USA, 94, 4155-4160 (1997).
    • (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
  • 59
    • 0029811226 scopus 로고    scopus 로고
    • Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease
    • E. Masliah, M. Alford, R. DeTeresa, M. Mallory, and L. Hansen, Deficient glutamate transport is associated with neurodegeneration in Alzheimer's disease, Ann. Neurol., 40, 759-766 (1996).
    • (1996) Ann. Neurol. , vol.40 , pp. 759-766
    • Masliah, E.1    Alford, M.2    Deteresa, R.3    Mallory, M.4    Hansen, L.5
  • 60
    • 0032524290 scopus 로고    scopus 로고
    • Amyloid protein precursor stimulates excitatory amino acid transport. Implications for roles in neuroprotection and pathogenesis
    • E. Masliah, J. Raber, M. Alford, M. Mallory, M. P. Mattson, D. Yang, D. Wong, and L. Mucke, Amyloid protein precursor stimulates excitatory amino acid transport. Implications for roles in neuroprotection and pathogenesis, J. Biol. Chem., 273, 12,548-12,554 (1998).
    • (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.6    Wong, D.7    Mucke, L.8
  • 62
    • 0030889711 scopus 로고    scopus 로고
    • Genomic organization of the human excitatory amino acid transporter gene GLT-1
    • T. Meyer, A. C. Ludolph, M. Morkel, C. Hagemeier, and A. Speer, Genomic organization of the human excitatory amino acid transporter gene GLT-1, NeuroReport, 8, 775-777 (1997).
    • (1997) NeuroReport , vol.8 , pp. 775-777
    • Meyer, T.1    Ludolph, A.C.2    Morkel, M.3    Hagemeier, C.4    Speer, A.5
  • 63
    • 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
    • T. Meyer, C. Munch, H. Volkel, P. Booms, and A. C. Ludolph, 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, 594-596 (1998).
    • (1998) J. Neurol. Neurosurg. Psychiatry , vol.65 , pp. 594-596
    • Meyer, T.1    Munch, C.2    Volkel, H.3    Booms, P.4    Ludolph, A.C.5
  • 64
    • 0031957298 scopus 로고    scopus 로고
    • Mutations in the glutamate transporter EAAT2 gene do not cause abnormal EAAT2 transcripts in amyotrophic lateral sclerosis
    • M. Aoki, C. L. Lin, J. D. Rothstein, B. A. Geller, B. A. Hosler, T. L. Munsat, H. R. Horvitz, and R. H. Brown, Mutations in the glutamate transporter EAAT2 gene do not cause abnormal EAAT2 transcripts in amyotrophic lateral sclerosis, Ann. Neurol., 43, 645-653 (1998).
    • (1998) Ann. Neurol. , vol.43 , pp. 645-653
    • Aoki, M.1    Lin, C.L.2    Rothstein, J.D.3    Geller, B.A.4    Hosler, B.A.5    Munsat, T.L.6    Horvitz, H.R.7    Brown, R.H.8
  • 65
    • 0032032013 scopus 로고    scopus 로고
    • Aberrant RNA processing in a neurodegenerative disease: The cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis
    • C. L. Lin, L. A. Bristol, L. Jin, M. Dykes-Hoberg, T. Crawford, L. Clawson, and J. D. Rothstein, Aberrant RNA processing in a neurodegenerative disease: The cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis, Neuron, 20, 589-602 (1998).
    • (1998) Neuron , vol.20 , pp. 589-602
    • Lin, C.L.1    Bristol, L.A.2    Jin, L.3    Dykes-Hoberg, M.4    Crawford, T.5    Clawson, L.6    Rothstein, J.D.7
  • 68
    • 0032549709 scopus 로고    scopus 로고
    • Identification of alternative splicing forms of GLT-1 mRNA in the spinal cord of amyotrophic lateral sclerosis patients
    • M. Nagai, K. Abe, K. Okamoto, and Y. Itoyama, Identification of alternative splicing forms of GLT-1 mRNA in the spinal cord of amyotrophic lateral sclerosis patients, Neurosci. Lett., 244, 165-168 (1998).
    • (1998) Neurosci. Lett. , vol.244 , pp. 165-168
    • Nagai, M.1    Abe, K.2    Okamoto, K.3    Itoyama, Y.4
  • 69
    • 0029019529 scopus 로고
    • Studies of the coding region of the neuronal glutamate transporter gene in amyotrophic lateral sclerosis
    • T. Meyer, U. Lenk, G. Kuther, A. Weindl, A. Speer, and A. C. Ludolph, Studies of the coding region of the neuronal glutamate transporter gene in amyotrophic lateral sclerosis, Ann. Neurol., 37, 817-819 (1995).
    • (1995) Ann. Neurol. , vol.37 , pp. 817-819
    • Meyer, T.1    Lenk, U.2    Kuther, G.3    Weindl, A.4    Speer, A.5    Ludolph, A.C.6
  • 71
    • 0030716859 scopus 로고    scopus 로고
    • Tissue specific variants of glutamate transporter GLT-1
    • N. Utsunomiya-Tate, H. Endou, and Y. Kanai, Tissue specific variants of glutamate transporter GLT-1, FEBS Lett., 416, 312-316 (1997).
    • (1997) FEBS Lett. , vol.416 , pp. 312-316
    • Utsunomiya-Tate, N.1    Endou, H.2    Kanai, Y.3
  • 72
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • P. C. Wong, C. A. Pardo, D. R. Borchelt, M. K. Lee, N. G. Copeland, N. A. Jenkins, S. S. Sisodia, D. W. Cleveland, and D. L. Price, An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria, Neuron, 14, 1105-1116 (1995).
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 74
    • 0029788243 scopus 로고    scopus 로고
    • Mitochondrial depolarization in glutamate-stimulated neurons: An early signal specific to excitotoxin exposure
    • R. J. White and I. J. Reynolds, Mitochondrial depolarization in glutamate-stimulated neurons: An early signal specific to excitotoxin exposure, J. Neurosci., 16, 5688-5697 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 5688-5697
    • White, R.J.1    Reynolds, I.J.2
  • 75
    • 0029810095 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a primary event in glutamate neurotoxicity
    • A. F. Schinder, E. C. Olson, N. C. Spitzer, and M. Montai, Mitochondrial dysfunction is a primary event in glutamate neurotoxicity, J. Neurosci., 16, 6125-6133 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 6125-6133
    • Schinder, A.F.1    Olson, E.C.2    Spitzer, N.C.3    Montai, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.