메뉴 건너뛰기




Volumn 5-6, Issue , 2005, Pages 255-307

Amino Acid and Neurotransmitter Transporters

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85059600925     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B0-44-451924-6/00071-5     Document Type: Chapter
Times cited : (24)

References (317)
  • 1
    • 0034708480 scopus 로고    scopus 로고
    • The genome sequence of Drosophila melanogaster
    • Adams M.D., Celniker S.E., Holt R.A., et al. The genome sequence of Drosophila melanogaster. Science 2000, 287:2185-2195.
    • (2000) Science , vol.287 , pp. 2185-2195
    • Adams, M.D.1    Celniker, S.E.2    Holt, R.A.3
  • 2
    • 0037636773 scopus 로고    scopus 로고
    • Lysosomal amino acid transporter LYAAT-1 in the rat central nervous system: an in situ hybridization and immunohistochemical study
    • Agulhon C., Rostaing P., Ravassard P., Sagne C., Triller A., et al. Lysosomal amino acid transporter LYAAT-1 in the rat central nervous system: an in situ hybridization and immunohistochemical study. J. Comp. Neurol. 2003, 462:71-89.
    • (2003) J. Comp. Neurol. , vol.462 , pp. 71-89
    • Agulhon, C.1    Rostaing, P.2    Ravassard, P.3    Sagne, C.4    Triller, A.5
  • 3
    • 0034122744 scopus 로고    scopus 로고
    • Molecular cloning of a novel brain-type Na(+)-dependent inorganic phosphate cotransporter
    • Aihara Y., Mashima H., Onda H., Hisano S., Kasuya H., et al. Molecular cloning of a novel brain-type Na(+)-dependent inorganic phosphate cotransporter. J. Neurochem. 2000, 74:2622-2625.
    • (2000) J. Neurochem. , vol.74 , pp. 2622-2625
    • Aihara, Y.1    Mashima, H.2    Onda, H.3    Hisano, S.4    Kasuya, H.5
  • 4
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus-infection
    • Albritton L.M., Tseng L., Scadden D., Cunningham J.M. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus-infection. Cell 1989, 57:659-666.
    • (1989) Cell , vol.57 , pp. 659-666
    • Albritton, L.M.1    Tseng, L.2    Scadden, D.3    Cunningham, J.M.4
  • 5
    • 0035993231 scopus 로고    scopus 로고
    • Excitatory amino acid transporters: keeping up with glutamate
    • Amara S.G., Fontana A.C. Excitatory amino acid transporters: keeping up with glutamate. Neurochem. Int. 2002, 41:313-318.
    • (2002) Neurochem. Int. , vol.41 , pp. 313-318
    • Amara, S.G.1    Fontana, A.C.2
  • 6
    • 18844466989 scopus 로고
    • Effect of pH on phosphate transport in rat renal brush border membrane vesicles
    • Amstutz M., Mohrmann M., Gmaj P., Murer H. Effect of pH on phosphate transport in rat renal brush border membrane vesicles. Am. J. Physiol. 1985, 248:F705-F710.
    • (1985) Am. J. Physiol. , vol.248 , pp. F705-F710
    • Amstutz, M.1    Mohrmann, M.2    Gmaj, P.3    Murer, H.4
  • 7
    • 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 1997, 94:4155-4160.
    • (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
  • 8
    • 0028031487 scopus 로고
    • Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex
    • Arriza J.L., Fairman W.A., Wadiche J.I., Murdoch G.H., Kavanaugh M.P., et al. Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. J. Neurosci. 1994, 14:5559-5569.
    • (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
  • 9
    • 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., et al. Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J. Biol. Chem. 1993, 268:15329-15332.
    • (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
  • 10
    • 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 2000, 28:547-558.
    • (2000) Neuron , vol.28 , pp. 547-558
    • Auger, C.1    Attwell, D.2
  • 11
    • 0029608628 scopus 로고
    • + symporter in midgut brush-border membrane vesicles from larval Manduca sexta
    • + symporter in midgut brush-border membrane vesicles from larval Manduca sexta. J. Exp. Biol. 1995, 198:2599-2607.
    • (1995) J. Exp. Biol. , vol.198 , pp. 2599-2607
    • Bader, A.L.1    Parthasarathy, R.2    Harvey, W.R.3
  • 12
    • 0036022326 scopus 로고    scopus 로고
    • Drosophila as a new model organism for the neurobiology of aggression?
    • Baier A., Wittek B., Brembs B. Drosophila as a new model organism for the neurobiology of aggression?. J. Exp. Biol. 2002, 205:1233-1240.
    • (2002) J. Exp. Biol. , vol.205 , pp. 1233-1240
    • Baier, A.1    Wittek, B.2    Brembs, B.3
  • 13
    • 0032481251 scopus 로고    scopus 로고
    • TATI encodes a low-affinity histidine transporter in Saccharomyces cerevisiae
    • Bajmoczi M., Sneve M., Eide D.J., Drewes L.R. TATI encodes a low-affinity histidine transporter in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 1998, 243:205-209.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 205-209
    • Bajmoczi, M.1    Sneve, M.2    Eide, D.J.3    Drewes, L.R.4
  • 14
    • 0018267935 scopus 로고
    • A proline shuttle in insect flight muscle
    • Balboni E. A proline shuttle in insect flight muscle. Biochem. Biophys. Res. Commun. 1978, 85:1090-1096.
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 1090-1096
    • Balboni, E.1
  • 15
    • 0242404063 scopus 로고    scopus 로고
    • Identification and characterisation of human xCT that co-expresses, with 4F2 heavy chain, the amino acid transport activity system x(c) (-)
    • Bassi M.T., Gasol E., Manzoni M., Pineda M., Riboni M., et al. Identification and characterisation of human xCT that co-expresses, with 4F2 heavy chain, the amino acid transport activity system x(c) (-). Pflugers Archiv. 2001, 442:286-296.
    • (2001) Pflugers Archiv. , vol.442 , pp. 286-296
    • Bassi, M.T.1    Gasol, E.2    Manzoni, M.3    Pineda, M.4    Riboni, M.5
  • 16
    • 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., et al. The localization of the brain-specific inorganic phosphate transporter suggests a specific presynaptic role in glutamatergic transmission. J. Neurosci. 1998, 18:8648-8659.
    • (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
  • 17
    • 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., Edwards R.H. Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter. Science 2000, 289:957-960.
    • (2000) Science , vol.289 , pp. 957-960
    • Bellocchio, E.E.1    Reimer, R.J.2    Fremeau, R.T.3    Edwards, R.H.4
  • 18
    • 0344527986 scopus 로고    scopus 로고
    • Cellular and subcellular expression of monocarboxylate transporters in the pigment epithelium and retina of the rat
    • Bergersen L., Johannsson E., Veruki M.L., Nagelhus E.A., Halestrap A., et al. Cellular and subcellular expression of monocarboxylate transporters in the pigment epithelium and retina of the rat. Neuroscience 1999, 90:319-331.
    • (1999) Neuroscience , vol.90 , pp. 319-331
    • Bergersen, L.1    Johannsson, E.2    Veruki, M.L.3    Nagelhus, E.A.4    Halestrap, A.5
  • 19
    • 0036130456 scopus 로고    scopus 로고
    • Immunogold cytochemistry identifies specialized membrane domains for monocarboxylate transport in the central nervous system
    • Bergersen L., Rafiki A., Ottersen O.P. Immunogold cytochemistry identifies specialized membrane domains for monocarboxylate transport in the central nervous system. Neurochem. Res. 2002, 27:89-96.
    • (2002) Neurochem. Res. , vol.27 , pp. 89-96
    • Bergersen, L.1    Rafiki, A.2    Ottersen, O.P.3
  • 20
    • 0026741842 scopus 로고
    • Expression cloning of a cDNA from rabbit kidney cortex that induces a single transport system for cystine and dibasic and neutral amino acids
    • Bertran J., Werner A., Moore M.L., Stange G., Markovich D., et al. Expression cloning of a cDNA from rabbit kidney cortex that induces a single transport system for cystine and dibasic and neutral amino acids. Proc. Natl Acad. Sci. USA 1992, 89:5601-5605.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5601-5605
    • Bertran, J.1    Werner, A.2    Moore, M.L.3    Stange, G.4    Markovich, D.5
  • 21
    • 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. 1999, 443:97-104.
    • (1999) FEBS Lett. , vol.443 , pp. 97-104
    • Besson, M.T.1    Soustelle, L.2    Birman, S.3
  • 22
    • 0034708256 scopus 로고    scopus 로고
    • Selective high-affinity transport of aspartate by a Drosophila homologue of the excitatory amino-acid transporters
    • Besson M.T., Soustelle L., Birman S. Selective high-affinity transport of aspartate by a Drosophila homologue of the excitatory amino-acid transporters. Curr. Biol. 2000, 10:207-210.
    • (2000) Curr. Biol. , vol.10 , pp. 207-210
    • Besson, M.T.1    Soustelle, L.2    Birman, S.3
  • 23
    • 0035434727 scopus 로고    scopus 로고
    • Energizing epithelial transport with the vacuolar H(+)-ATPase
    • Beyenbach K.W. Energizing epithelial transport with the vacuolar H(+)-ATPase. News Physiol. Sci. 2001, 16:145-151.
    • (2001) News Physiol. Sci. , vol.16 , pp. 145-151
    • Beyenbach, K.W.1
  • 24
    • 0023879476 scopus 로고
    • Glutamate-like immunoreactivity in identified neuronal populations of insect nervous systems
    • Bicker G., Schafer S., Ottersen O.P., Storm-Mathisen J. Glutamate-like immunoreactivity in identified neuronal populations of insect nervous systems. J. Neurosci. 1988, 8:2108-2122.
    • (1988) J. Neurosci. , vol.8 , pp. 2108-2122
    • Bicker, G.1    Schafer, S.2    Ottersen, O.P.3    Storm-Mathisen, J.4
  • 25
    • 0030921440 scopus 로고    scopus 로고
    • Tyrosine 140 of the gamma-aminobutyric acid transporter GAT-1 plays a critical role in neurotransmitter recognition
    • Bismuth Y., Kavanaugh M.P., Kanner B.I. Tyrosine 140 of the gamma-aminobutyric acid transporter GAT-1 plays a critical role in neurotransmitter recognition. J. Biol. Chem. 1997, 272:16096-16102.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16096-16102
    • Bismuth, Y.1    Kavanaugh, M.P.2    Kanner, B.I.3
  • 26
    • 85069923683 scopus 로고    scopus 로고
    • The SLC36 family: proton-coupled transporters for the absorption of selected amino acids from extracellular and intracellular proteolysis
    • 2003 May 14 (Epub ahead of print)
    • Boll M., Daniel H., Gasnier B. The SLC36 family: proton-coupled transporters for the absorption of selected amino acids from extracellular and intracellular proteolysis. Pflugers Arch. 2003, 2003 May 14 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Boll, M.1    Daniel, H.2    Gasnier, B.3
  • 27
    • 0037603307 scopus 로고    scopus 로고
    • A cluster of proton/amino acid transporter genes in the human and mouse genomes
    • Boll M., Foltz M., Rubio-Aliaga I., Daniel H. A cluster of proton/amino acid transporter genes in the human and mouse genomes. Genomics 2003, 82:47-56.
    • (2003) Genomics , vol.82 , pp. 47-56
    • Boll, M.1    Foltz, M.2    Rubio-Aliaga, I.3    Daniel, H.4
  • 28
    • 0037151112 scopus 로고    scopus 로고
    • Functional characterization of two novel mammalian electrogenic proton-dependent amino acid cotransporters
    • Boll M., Foltz M., Rubio-Aliaga I., Kottra G., Daniel H. Functional characterization of two novel mammalian electrogenic proton-dependent amino acid cotransporters. J. Biol. Chem. 2002, 277:22966-22973.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22966-22973
    • Boll, M.1    Foltz, M.2    Rubio-Aliaga, I.3    Kottra, G.4    Daniel, H.5
  • 29
    • 0030026812 scopus 로고    scopus 로고
    • Expression cloning and functional characterization of the kidney cortex high-affinity proton-coupled peptide transporter
    • Boll M., Herget M., Wagener M., Weber W.M., Markovich D., et al. Expression cloning and functional characterization of the kidney cortex high-affinity proton-coupled peptide transporter. Proc. Natl Acad. Sci. USA 1996, 93:284-289.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 284-289
    • Boll, M.1    Herget, M.2    Wagener, M.3    Weber, W.M.4    Markovich, D.5
  • 30
    • 0027967880 scopus 로고
    • Expression cloning of a cDNA from rabbit small-intestine related to proton-coupled transport of peptides, beta-lactam antibiotics and Ace-inhibitors
    • Boll M., Markovich D., Weber W.M., Korte H., Daniel H., et al. Expression cloning of a cDNA from rabbit small-intestine related to proton-coupled transport of peptides, beta-lactam antibiotics and Ace-inhibitors. Pflugers Arch. 1994, 429:146-149.
    • (1994) Pflugers Arch. , vol.429 , pp. 146-149
    • Boll, M.1    Markovich, D.2    Weber, W.M.3    Korte, H.4    Daniel, H.5
  • 31
    • 0034002273 scopus 로고    scopus 로고
    • Lactate transporters (MCT proteins) in heart and skeletal muscles
    • Bonen A. Lactate transporters (MCT proteins) in heart and skeletal muscles. Med. Sci. Sports Exercise 2000, 32:778-789.
    • (2000) Med. Sci. Sports Exercise , vol.32 , pp. 778-789
    • Bonen, A.1
  • 32
    • 0033559841 scopus 로고    scopus 로고
    • Ion binding and permeation through the lepidopteran amino acid transporter KAAT1 expressed in Xenopus oocytes
    • Bossi E., Centinaio E., Castagna M., Giovannardi S., Vincenti S., et al. Ion binding and permeation through the lepidopteran amino acid transporter KAAT1 expressed in Xenopus oocytes. J. Physiol. -Lond. 1999, 515:729-742.
    • (1999) J. Physiol. -Lond. , vol.515 , pp. 729-742
    • Bossi, E.1    Centinaio, E.2    Castagna, M.3    Giovannardi, S.4    Vincenti, S.5
  • 33
    • 0000397349 scopus 로고    scopus 로고
    • Ionic selectivity of the coupled and uncoupled currents carried by the amino acid transporter KAAT1
    • Bossi E., Sacchi V.F., Peres A. Ionic selectivity of the coupled and uncoupled currents carried by the amino acid transporter KAAT1. Pflugers Archiv. 1999, 438:788-796.
    • (1999) Pflugers Archiv. , vol.438 , pp. 788-796
    • Bossi, E.1    Sacchi, V.F.2    Peres, A.3
  • 35
    • 0035909996 scopus 로고    scopus 로고
    • Alkalinization by chloride/bicarbonate pathway in larval mosquito midgut
    • Boudko D.Y., Moroz L.L., Harvey W.R., Linser P.J. Alkalinization by chloride/bicarbonate pathway in larval mosquito midgut. Proc. Natl Acad. Sci. USA 2001, 98:15354-15359.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 15354-15359
    • Boudko, D.Y.1    Moroz, L.L.2    Harvey, W.R.3    Linser, P.J.4
  • 36
    • 0035746142 scopus 로고    scopus 로고
    • In situ analysis of pH gradients in mosquito larvae using non-invasive, self-referencing, pH-sensitive microelectrodes
    • Boudko D.Y., Moroz L.L., Linser P.J., Trimarchi J.R., Smith P.J., et al. In situ analysis of pH gradients in mosquito larvae using non-invasive, self-referencing, pH-sensitive microelectrodes. J. Exp. Biol. 2001, 204:691-699.
    • (2001) J. Exp. Biol. , vol.204 , pp. 691-699
    • Boudko, D.Y.1    Moroz, L.L.2    Linser, P.J.3    Trimarchi, J.R.4    Smith, P.J.5
  • 37
    • 0025257629 scopus 로고
    • Regulation of high affinity choline uptake
    • Breer H., Knipper M. Regulation of high affinity choline uptake. J. Neurobiol. 1990, 21:269-275.
    • (1990) J. Neurobiol. , vol.21 , pp. 269-275
    • Breer, H.1    Knipper, M.2
  • 38
    • 0035169435 scopus 로고    scopus 로고
    • Structure, function, and regulation of human cystine/glutamate transporter in retinal pigment epithelial cells
    • Bridges C.C., Kekuda R., Wang H.P., Prasad P.D., Mehta P., et al. Structure, function, and regulation of human cystine/glutamate transporter in retinal pigment epithelial cells. Invest. Ophthalmol. Vis. Sci. 2001, 42:47-54.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 47-54
    • Bridges, C.C.1    Kekuda, R.2    Wang, H.P.3    Prasad, P.D.4    Mehta, P.5
  • 39
    • 0037085518 scopus 로고    scopus 로고
    • Regulation of the glutamine transporter SN1 by extracellular pH and intracellular sodium ions
    • Broer A., Albers A., Setiawan I., Edwards R.H., Chaudhry F.A., et al. Regulation of the glutamine transporter SN1 by extracellular pH and intracellular sodium ions. J. Physiol. -Lond. 2002, 539:3-14.
    • (2002) J. Physiol. -Lond. , vol.539 , pp. 3-14
    • Broer, A.1    Albers, A.2    Setiawan, I.3    Edwards, R.H.4    Chaudhry, F.A.5
  • 40
    • 0034254798 scopus 로고    scopus 로고
    • The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine
    • Broer A., Wagner C.A., Lang F., Broer S. The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine. Biochem. J. 2000, 349:787-795.
    • (2000) Biochem. J. , vol.349 , pp. 787-795
    • Broer, A.1    Wagner, C.A.2    Lang, F.3    Broer, S.4
  • 41
    • 0039351371 scopus 로고    scopus 로고
    • Characterization of the high-affinity monocarboxylate transporter MCT2 in Xenopus laevis oocytes
    • Broer S., Broer A., Schneider H.P., Stegen C., Halestrap A.P., et al. Characterization of the high-affinity monocarboxylate transporter MCT2 in Xenopus laevis oocytes. Biochem. J. 1999, 341:529-535.
    • (1999) Biochem. J. , vol.341 , pp. 529-535
    • Broer, S.1    Broer, A.2    Schneider, H.P.3    Stegen, C.4    Halestrap, A.P.5
  • 42
    • 0032127127 scopus 로고    scopus 로고
    • Characterization of the monocarboxylate transporter 1 expressed in Xenopus laevis oocytes by changes in cytosolic pH
    • Broer S., Schneider H.P., Broer A., Rahman B., Hamprecht B., et al. Characterization of the monocarboxylate transporter 1 expressed in Xenopus laevis oocytes by changes in cytosolic pH. Biochem. J. 1998, 333:167-174.
    • (1998) Biochem. J. , vol.333 , pp. 167-174
    • Broer, S.1    Schneider, H.P.2    Broer, A.3    Rahman, B.4    Hamprecht, B.5
  • 43
    • 0032105462 scopus 로고    scopus 로고
    • Chloride conductance and Pi transport are separate functions induced by the expression of NaPi-1 in Xenopus oocytes
    • Broer S., Schuster A., Wagner C.A., Broer A., Forster I., et al. Chloride conductance and Pi transport are separate functions induced by the expression of NaPi-1 in Xenopus oocytes. J. Membr. Biol. 1998, 164:71-77.
    • (1998) J. Membr. Biol. , vol.164 , pp. 71-77
    • Broer, S.1    Schuster, A.2    Wagner, C.A.3    Broer, A.4    Forster, I.5
  • 44
  • 45
    • 0029924158 scopus 로고    scopus 로고
    • Electrophysiological insights of type I and II Na/Pi transporters
    • Busch A.E., Biber J., Murer H., Lang F. Electrophysiological insights of type I and II Na/Pi transporters. Kidney Int. 1996, 49:986-987.
    • (1996) Kidney Int. , vol.49 , pp. 986-987
    • Busch, A.E.1    Biber, J.2    Murer, H.3    Lang, F.4
  • 46
    • 0029896232 scopus 로고    scopus 로고
    • Expression of a renal type I sodium/phosphate transporter (NaPi-1) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions
    • Busch A.E., Schuster A., Waldegger S., Wagner C.A., Zempel G., et al. Expression of a renal type I sodium/phosphate transporter (NaPi-1) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions. Proc. Natl Acad. Sci. USA 1996, 93:5347-5351.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5347-5351
    • Busch, A.E.1    Schuster, A.2    Waldegger, S.3    Wagner, C.A.4    Zempel, G.5
  • 47
    • 0001309854 scopus 로고
    • Synaptic transmission in the central nervous system
    • Pergamon Press, Oxford, G.A. Kerkut, L.I. Gilbert (Eds.)
    • Callec J.J. Synaptic transmission in the central nervous system. Comprehensive Insect Physiology, Biochemistry and Pharmacology 1985, vol. 5:139-179. Pergamon Press, Oxford. G.A. Kerkut, L.I. Gilbert (Eds.).
    • (1985) Comprehensive Insect Physiology, Biochemistry and Pharmacology , vol.5 , pp. 139-179
    • Callec, J.J.1
  • 48
    • 0030021048 scopus 로고    scopus 로고
    • Molecular enhancement of memory formation
    • Carew T.J. Molecular enhancement of memory formation. Neuron 1996, 16:5-8.
    • (1996) Neuron , vol.16 , pp. 5-8
    • Carew, T.J.1
  • 49
    • 0030956481 scopus 로고    scopus 로고
    • Molecular characteristics of mammalian and insect amino acid transporters: implications for amino acid homeostasis
    • Castagna M., Shayakul C., Trotti D., Sacchi V.F., Harvey W.R., et al. Molecular characteristics of mammalian and insect amino acid transporters: implications for amino acid homeostasis. J. Exp. Biol. 1997, 200:269-286.
    • (1997) J. Exp. Biol. , vol.200 , pp. 269-286
    • Castagna, M.1    Shayakul, C.2    Trotti, D.3    Sacchi, V.F.4    Harvey, W.R.5
  • 51
    • 0035984507 scopus 로고    scopus 로고
    • Inhibition of the lepidopteran amino acid co-transporter KAAT1 by phenylglyoxal: role of arginine 76
    • Castagna M., Vincenti S., Marciani P., Sacchi V.F. Inhibition of the lepidopteran amino acid co-transporter KAAT1 by phenylglyoxal: role of arginine 76. Insect Mol. Biol. 2002, 11:283-289.
    • (2002) Insect Mol. Biol. , vol.11 , pp. 283-289
    • Castagna, M.1    Vincenti, S.2    Marciani, P.3    Sacchi, V.F.4
  • 52
    • 0003343555 scopus 로고    scopus 로고
    • Neurotransmitter transporters in the insect nervous system
    • Caveney S., Donly B.C. Neurotransmitter transporters in the insect nervous system. Adv. Insect Physiol. 2002, 29:55-149.
    • (2002) Adv. Insect Physiol. , vol.29 , pp. 55-149
    • Caveney, S.1    Donly, B.C.2
  • 53
    • 0037126633 scopus 로고    scopus 로고
    • Coupled and uncoupled proton movement by amino acid transport system N
    • Chaudhry F.A., Krizaj D., Larsson P., Reimer R.J., Wreden C., et al. Coupled and uncoupled proton movement by amino acid transport system N. EMBO J. 2001, 20:7041-7051.
    • (2001) EMBO J. , vol.20 , pp. 7041-7051
    • Chaudhry, F.A.1    Krizaj, D.2    Larsson, P.3    Reimer, R.J.4    Wreden, C.5
  • 54
    • 0036196514 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a chicken intestinal peptide transporter (cPepT1) in Xenopus oocytes and Chinese hamster ovary cells
    • Chen H., Pan Y.X., Wong E.A., Bloomquist J.R., Webb K.E. Molecular cloning and functional expression of a chicken intestinal peptide transporter (cPepT1) in Xenopus oocytes and Chinese hamster ovary cells. J. Nutr. 2002, 132:387-393.
    • (2002) J. Nutr. , vol.132 , pp. 387-393
    • Chen, H.1    Pan, Y.X.2    Wong, E.A.3    Bloomquist, J.R.4    Webb, K.E.5
  • 55
    • 0242434154 scopus 로고    scopus 로고
    • Synaptic uptake and beyond: the sodium- and chloride-dependent neurotransmitter transporter family SLC6
    • 2003 Apr 29 (Epub ahead of print)
    • Chen N.H., Reith M.E., Quick M.W. Synaptic uptake and beyond: the sodium- and chloride-dependent neurotransmitter transporter family SLC6. Pflugers Arch. 2003, 2003 Apr 29 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Chen, N.H.1    Reith, M.E.2    Quick, M.W.3
  • 56
    • 77956770128 scopus 로고
    • Amino acid and protein metabolism in insect development
    • Chen P.S. Amino acid and protein metabolism in insect development. Adv. Insect Physiol. 1966, 3:53-132.
    • (1966) Adv. Insect Physiol. , vol.3 , pp. 53-132
    • Chen, P.S.1
  • 57
    • 0037343974 scopus 로고    scopus 로고
    • The glutamate transporters EAAT2 and EAAT3 mediate cysteine uptake in cortical neuron cultures
    • Chen Y., Swanson R.A. The glutamate transporters EAAT2 and EAAT3 mediate cysteine uptake in cortical neuron cultures. J. Neurochem. 2003, 84:1332-1339.
    • (2003) J. Neurochem. , vol.84 , pp. 1332-1339
    • Chen, Y.1    Swanson, R.A.2
  • 58
    • 0037440176 scopus 로고    scopus 로고
    • Structure, function and immunolocalization of a proton-coupled amino acid transporter (hPAT1) in the human intestinal cell line Caco-2
    • Chen Z., Fei Y.J., Anderson C.M., Wake K.A., Miyauchi S., et al. Structure, function and immunolocalization of a proton-coupled amino acid transporter (hPAT1) in the human intestinal cell line Caco-2. J. Physiol. 2003, 546:349-361.
    • (2003) J. Physiol. , vol.546 , pp. 349-361
    • Chen, Z.1    Fei, Y.J.2    Anderson, C.M.3    Wake, K.A.4    Miyauchi, S.5
  • 60
    • 8944233871 scopus 로고    scopus 로고
    • +L-like. A tertiary active transport mechanism for renal reabsorption of cystine and dibasic amino acids
    • +L-like. A tertiary active transport mechanism for renal reabsorption of cystine and dibasic amino acids. J. Biol. Chem. 1996, 271:17761-17770.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17761-17770
    • Chillaron, J.1    Estevez, R.2    Mora, C.3    Wagner, C.A.4    Suessbrich, H.5
  • 62
    • 0034476424 scopus 로고    scopus 로고
    • The transporter-like protein inebriated mediates hyperosmotic stimuli through intracellular signalling
    • Chiu C.-S., Ross L.S., Cohen B.N., Lester H.A., Gill S.S. The transporter-like protein inebriated mediates hyperosmotic stimuli through intracellular signalling. J. Exp. Biol. 2000, 203:3531-3546.
    • (2000) J. Exp. Biol. , vol.203 , pp. 3531-3546
    • Chiu, C.-S.1    Ross, L.S.2    Cohen, B.N.3    Lester, H.A.4    Gill, S.S.5
  • 63
    • 0000482172 scopus 로고
    • Transport system serving for mono-+ diamino acids
    • Christensen H.N. Transport system serving for mono-+ diamino acids. Proc. Natl Acad. Sci. USA 1964, 51:337-344.
    • (1964) Proc. Natl Acad. Sci. USA , vol.51 , pp. 337-344
    • Christensen, H.N.1
  • 64
    • 0020986761 scopus 로고
    • Isolation of separate apical, lateral and basal plasma membrane from cells of an insect epithelium. A procedure based on tissue organization and ultrastructure
    • Cioffi M., Wolfersberger M.G. Isolation of separate apical, lateral and basal plasma membrane from cells of an insect epithelium. A procedure based on tissue organization and ultrastructure. Tissue Cell 1983, 15:781-803.
    • (1983) Tissue Cell , vol.15 , pp. 781-803
    • Cioffi, M.1    Wolfersberger, M.G.2
  • 65
    • 0027604913 scopus 로고
    • Amino acid neurotransmitter transporters: structure, function, and molecular diversity
    • Clark J.A., Amara S.G. Amino acid neurotransmitter transporters: structure, function, and molecular diversity. Bioessays 1993, 15:323-332.
    • (1993) Bioessays , vol.15 , pp. 323-332
    • Clark, J.A.1    Amara, S.G.2
  • 67
    • 0036140958 scopus 로고    scopus 로고
    • Expression, regulation and function of carrier proteins for cationic amino acids
    • Closs E.I. Expression, regulation and function of carrier proteins for cationic amino acids. Curr. Opin. Nephrol. Hypertens. 2002, 11:99-107.
    • (2002) Curr. Opin. Nephrol. Hypertens. , vol.11 , pp. 99-107
    • Closs, E.I.1
  • 68
    • 0033617407 scopus 로고    scopus 로고
    • Vesicular ATPase-overexpressing cells determine the distribution of malaria parasite oocysts on the midguts of mosquitoes
    • Cociancich S.O., Park S.S., Fidock D.A., Shahabuddin M. Vesicular ATPase-overexpressing cells determine the distribution of malaria parasite oocysts on the midguts of mosquitoes. J. Biol. Chem. 1999, 274:12650-12655.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12650-12655
    • Cociancich, S.O.1    Park, S.S.2    Fidock, D.A.3    Shahabuddin, M.4
  • 69
    • 0001299838 scopus 로고
    • Small peptides, a life-long store of amino acid in adult Drosophila and Calliphora
    • Collett J.I. Small peptides, a life-long store of amino acid in adult Drosophila and Calliphora. J. Insect Physiol. 1976, 22:433-440.
    • (1976) J. Insect Physiol. , vol.22 , pp. 433-440
    • Collett, J.I.1
  • 70
    • 84920058620 scopus 로고    scopus 로고
    • The SLC20 family of proteins: dual functions as sodium-phosphate cotransporters and viral receptors
    • May 21 (Epub ahead of print)
    • Collins J.F., Bai L., Ghishan F.K. The SLC20 family of proteins: dual functions as sodium-phosphate cotransporters and viral receptors. Pflugers Arch. 2003, May 21 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Collins, J.F.1    Bai, L.2    Ghishan, F.K.3
  • 71
    • 0020413961 scopus 로고
    • Octopamine as the transmitter at the firefly lantern - presence of an octopamine-sensitive and a dopamine-sensitive adenylate-cyclase
    • Copeland J., Robertson H.A. Octopamine as the transmitter at the firefly lantern - presence of an octopamine-sensitive and a dopamine-sensitive adenylate-cyclase. Comp. Biochem. Physiol. C -Pharmacol. Toxicol. Endocrinol. 1982, 72:125-127.
    • (1982) Comp. Biochem. Physiol. C -Pharmacol. Toxicol. Endocrinol. , vol.72 , pp. 125-127
    • Copeland, J.1    Robertson, H.A.2
  • 72
    • 0027977071 scopus 로고
    • A cocaine-sensitive Drosophila serotonin transporter: cloning, expression, and electrophysiological characterization
    • Corey J.L., Quick M.W., Davidson N., Lester H.A., Guastella J. A cocaine-sensitive Drosophila serotonin transporter: cloning, expression, and electrophysiological characterization. Proc. Natl Acad. Sci. USA 1994, 91:1188-1192.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1188-1192
    • Corey, J.L.1    Quick, M.W.2    Davidson, N.3    Lester, H.A.4    Guastella, J.5
  • 73
  • 74
    • 0346941965 scopus 로고    scopus 로고
    • The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
    • 2003 Aug 7 (Epub ahead of print)
    • Daniel H., Kottra G. The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology. Pflugers Arch. 2003, 2003 Aug 7 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Daniel, H.1    Kottra, G.2
  • 75
    • 0034872801 scopus 로고    scopus 로고
    • The receptor of Bacillus sphaericus binary toxin in Culex pipiens (Diptera: Culicidae) midgut: molecular cloning and expression
    • Darboux I., Nielsen-LeRoux C., Charles J.F., Pauron D. The receptor of Bacillus sphaericus binary toxin in Culex pipiens (Diptera: Culicidae) midgut: molecular cloning and expression. Insect Biochem. Mol. Biol. 2001, 31:981-990.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 981-990
    • Darboux, I.1    Nielsen-LeRoux, C.2    Charles, J.F.3    Pauron, D.4
  • 76
    • 0042833748 scopus 로고    scopus 로고
    • Family of sodium-coupled transporters for GABA, glycine, proline, betaine, taurine, and creatine
    • Humana Press Inc., Totowa, New Jersey, M.E.A. Reith (Ed.)
    • Deken S.L., Fremeau R.T.J., Quick M.W. Family of sodium-coupled transporters for GABA, glycine, proline, betaine, taurine, and creatine. Neurotransmitter Transporters: Structure, Function and Regulation 2002, 193-234. Humana Press Inc., Totowa, New Jersey. M.E.A. Reith (Ed.).
    • (2002) Neurotransmitter Transporters: Structure, Function and Regulation , pp. 193-234
    • Deken, S.L.1    Fremeau, R.T.J.2    Quick, M.W.3
  • 77
    • 0028245452 scopus 로고
    • Cloning, expression, and localization of a chloride-facilitated, cocaine-sensitive serotonin transporter from Drosophila melanogaster
    • Demchyshyn L.L., Pristupa Z.B., Sugamori K.S., Barker E.L., Blakely R.D., et al. Cloning, expression, and localization of a chloride-facilitated, cocaine-sensitive serotonin transporter from Drosophila melanogaster. Proc. Natl Acad. Sci. USA 1994, 91:5158-5162.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5158-5162
    • Demchyshyn, L.L.1    Pristupa, Z.B.2    Sugamori, K.S.3    Barker, E.L.4    Blakely, R.D.5
  • 78
    • 0020468306 scopus 로고
    • Monocarboxylate transport in erythrocytes
    • Deuticke B. Monocarboxylate transport in erythrocytes. J. Membr. Biol. 1982, 70:89-103.
    • (1982) J. Membr. Biol. , vol.70 , pp. 89-103
    • Deuticke, B.1
  • 79
    • 0034663601 scopus 로고    scopus 로고
    • The low-affinity monocarboxylate transporter MCT4 is adapted to the export of lactate in highly glycolytic cells
    • Dimmer K.S., Friedrich B., Lang F., Deitmer J.W., Broer S. The low-affinity monocarboxylate transporter MCT4 is adapted to the export of lactate in highly glycolytic cells. Biochem. J. 2000, 350:219-227.
    • (2000) Biochem. J. , vol.350 , pp. 219-227
    • Dimmer, K.S.1    Friedrich, B.2    Lang, F.3    Deitmer, J.W.4    Broer, S.5
  • 81
    • 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. 2000, 30:369-376.
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 369-376
    • Donly, C.1    Jevnikar, J.2    McLean, H.3    Caveney, S.4
  • 82
    • 0035814914 scopus 로고    scopus 로고
    • Semisynthetic derivatives of concanamycin A and C, as inhibitors of V- and P-type ATPases: structure-activity investigations and developments of photoaffinity probes
    • Drose S., Boddien C., Gassel M., Ingenhorst G., Zeeck A., et al. Semisynthetic derivatives of concanamycin A and C, as inhibitors of V- and P-type ATPases: structure-activity investigations and developments of photoaffinity probes. Biochemistry 2001, 40:2816-2825.
    • (2001) Biochemistry , vol.40 , pp. 2816-2825
    • Drose, S.1    Boddien, C.2    Gassel, M.3    Ingenhorst, G.4    Zeeck, A.5
  • 83
    • 84859431227 scopus 로고    scopus 로고
    • The vesicular amine transporter family (SLC18): amine/proton antiporters required for vesicular accumulation and regulated exocytotic secretion of monoamines and acetylcholine
    • 2003 May 6 (Epub ahead of print)
    • Eiden L.E., Schafer M.K., Weihe E., Schutz B. The vesicular amine transporter family (SLC18): amine/proton antiporters required for vesicular accumulation and regulated exocytotic secretion of monoamines and acetylcholine. Pflugers Arch. 2003, 2003 May 6 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Eiden, L.E.1    Schafer, M.K.2    Weihe, E.3    Schutz, B.4
  • 84
    • 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 1992, 89:10993-10997.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10993-10997
    • Erickson, J.D.1    Eiden, L.E.2    Hoffman, B.J.3
  • 85
    • 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 1995, 375:599-603.
    • (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
  • 86
    • 0038113016 scopus 로고    scopus 로고
    • Modulation of early olfactory processing by an octopaminergic reinforcement pathway in the honeybee
    • Farooqui T., Robinson K., Vaessin H., Smith B.H. Modulation of early olfactory processing by an octopaminergic reinforcement pathway in the honeybee. J. Neurosci. 2003, 23:5370-5380.
    • (2003) J. Neurosci. , vol.23 , pp. 5370-5380
    • Farooqui, T.1    Robinson, K.2    Vaessin, H.3    Smith, B.H.4
  • 87
    • 0028333611 scopus 로고
    • Expression cloning of a mammalian proton-coupled oligopeptide transporter
    • Fei Y.J., Kanai Y., Nussberger S., Ganapathy V., Leibach F.H., et al. Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature 1994, 368:563-566.
    • (1994) Nature , vol.368 , pp. 563-566
    • Fei, Y.J.1    Kanai, Y.2    Nussberger, S.3    Ganapathy, V.4    Leibach, F.H.5
  • 89
    • 0037378774 scopus 로고    scopus 로고
    • Basolateral LAT-2 has a major role in the transepithelial flux of L-cystine in the renal proximal tubule cell line OK
    • Fernandez E., Torrents D., Chillaron J., Martin Del Rio R., Zorzano A., et al. Basolateral LAT-2 has a major role in the transepithelial flux of L-cystine in the renal proximal tubule cell line OK. J. Am. Soc. Nephrol. 2003, 14:837-847.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , pp. 837-847
    • Fernandez, E.1    Torrents, D.2    Chillaron, J.3    Martin Del Rio, R.4    Zorzano, A.5
  • 90
    • 0037023688 scopus 로고    scopus 로고
    • Translation mediated by the internal ribosome entry Site of the cat-1 mRNA is regulated by glucose availability in a PERK kinase-dependent manner
    • Fernandez J., Bode B., Koromilas A., Diehl J.A., Krukovets I., et al. Translation mediated by the internal ribosome entry Site of the cat-1 mRNA is regulated by glucose availability in a PERK kinase-dependent manner. J. Biol. Chem. 2002, 277:11780-11787.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11780-11787
    • Fernandez, J.1    Bode, B.2    Koromilas, A.3    Diehl, J.A.4    Krukovets, I.5
  • 91
    • 0032145770 scopus 로고    scopus 로고
    • Cloning of the v-ATPase B subunit from Culex Quinquefasciatus and expression of the B and C subunits in mosquitoes
    • Filippova M., Ross L.S., Gill S.S. Cloning of the v-ATPase B subunit from Culex Quinquefasciatus and expression of the B and C subunits in mosquitoes. Insect Mol. Biol. 1998, 7:223-232.
    • (1998) Insect Mol. Biol. , vol.7 , pp. 223-232
    • Filippova, M.1    Ross, L.S.2    Gill, S.S.3
  • 92
    • 0037195086 scopus 로고    scopus 로고
    • The identification of vesicular glutamate transporter 3 suggests novel modes of signaling by glutamate
    • Fremeau R.T., Burman J., Qureshi T., Tran C.H., Proctor J., et al. The identification of vesicular glutamate transporter 3 suggests novel modes of signaling by glutamate. Proc. Natl Acad. Sci. USA 2002, 99:14488-14493.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14488-14493
    • Fremeau, R.T.1    Burman, J.2    Qureshi, T.3    Tran, C.H.4    Proctor, J.5
  • 93
    • 0013198358 scopus 로고    scopus 로고
    • The expression of vesicular glutamate transporters defines two classes of excitatory synapse
    • Fremeau R.T., Troyer M.D., Pahner I., Nygaard G.O., Tran C.H., et al. The expression of vesicular glutamate transporters defines two classes of excitatory synapse. Neuron 2001, 31:247-260.
    • (2001) Neuron , vol.31 , pp. 247-260
    • Fremeau, R.T.1    Troyer, M.D.2    Pahner, I.3    Nygaard, G.O.4    Tran, C.H.5
  • 94
    • 0037593543 scopus 로고    scopus 로고
    • Novel neuroglial and glioglial relationships mediated by L-serine metabolism
    • Furuya S., Watanabe M. Novel neuroglial and glioglial relationships mediated by L-serine metabolism. Arch. Histol. Cytol. 2003, 66:109-121.
    • (2003) Arch. Histol. Cytol. , vol.66 , pp. 109-121
    • Furuya, S.1    Watanabe, M.2
  • 97
    • 0037293942 scopus 로고    scopus 로고
    • Functionally distinct dopamine and octopamine transporters in the CNS of the cabbage looper moth
    • Gallant P., Malutan T., McLean H., Verellen L., Caveney S., et al. Functionally distinct dopamine and octopamine transporters in the CNS of the cabbage looper moth. Eur. J. Biochem. 2003, 270:664-674.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 664-674
    • Gallant, P.1    Malutan, T.2    McLean, H.3    Verellen, L.4    Caveney, S.5
  • 98
    • 0033166035 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a GABA transporter from the CNS of the cabbage looper, Trichoplusia ni
    • Gao X.J., McLean H., Caveney S., Donly C. Molecular cloning and functional characterization of a GABA transporter from the CNS of the cabbage looper, Trichoplusia ni. Insect Biochem. Mol. Biol. 1999, 29:609-623.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 609-623
    • Gao, X.J.1    McLean, H.2    Caveney, S.3    Donly, C.4
  • 99
    • 0028909335 scopus 로고
    • CDNA cloning of MCT2, a second monocarboxylate transporter expressed in different cells than MCT1
    • Garcia C.K., Brown M.S., Pathak R.K., Goldstein J.L. cDNA cloning of MCT2, a second monocarboxylate transporter expressed in different cells than MCT1. J. Biol. Chem. 1995, 270:1843-1849.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1843-1849
    • Garcia, C.K.1    Brown, M.S.2    Pathak, R.K.3    Goldstein, J.L.4
  • 100
    • 0027939545 scopus 로고
    • CDNA cloning of the human monocarboxylate transporter-1 and chromosomal localization of the Slc16a1 locus to 1p13.2-P12
    • Garcia C.K., Li X., Luna J., Francke U. cDNA cloning of the human monocarboxylate transporter-1 and chromosomal localization of the Slc16a1 locus to 1p13.2-P12. Genomics 1994, 23:500-503.
    • (1994) Genomics , vol.23 , pp. 500-503
    • Garcia, C.K.1    Li, X.2    Luna, J.3    Francke, U.4
  • 101
    • 0036736401 scopus 로고    scopus 로고
    • Cellular distribution of a high-affinity glutamate transporter in the nervous system of the cabbage looper Trichoplusia ni
    • Gardiner R.B., Ullensvang K., Danbolt N.C., Caveney S., Donly B.C. Cellular distribution of a high-affinity glutamate transporter in the nervous system of the cabbage looper Trichoplusia ni. J. Exp. Biol. 2002, 205:2605-2614.
    • (2002) J. Exp. Biol. , vol.205 , pp. 2605-2614
    • Gardiner, R.B.1    Ullensvang, K.2    Danbolt, N.C.3    Caveney, S.4    Donly, B.C.5
  • 102
    • 0026596478 scopus 로고
    • Molecular neurobiology of glutamate receptors
    • Gasic G.P., Hollmann M. Molecular neurobiology of glutamate receptors. Annu. Rev. Physiol. 1992, 54:507-536.
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 507-536
    • Gasic, G.P.1    Hollmann, M.2
  • 103
    • 84859435227 scopus 로고    scopus 로고
    • The SLC32 transporter, a key protein for the synaptic release of inhibitory amino acids
    • 2003 May 16 (Epub ahead of print)
    • Gasnier B. The SLC32 transporter, a key protein for the synaptic release of inhibitory amino acids. Pflugers Arch. 2003, 2003 May 16 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Gasnier, B.1
  • 104
    • 0028535228 scopus 로고
    • Thermodynamics of symport and antiport catalyzed by cloned or native transporters
    • Gerencser G.A., Stevens B.R. Thermodynamics of symport and antiport catalyzed by cloned or native transporters. J. Exp. Biol. 1994, 196:59-75.
    • (1994) J. Exp. Biol. , vol.196 , pp. 59-75
    • Gerencser, G.A.1    Stevens, B.R.2
  • 105
    • 0028254688 scopus 로고
    • + symport in lepidopteran larval midgut
    • + symport in lepidopteran larval midgut. J. Exp. Biol. 1994, 196:145-155.
    • (1994) J. Exp. Biol. , vol.196 , pp. 145-155
    • Giordana, B.1    Parenti, P.2
  • 106
    • 0024396720 scopus 로고
    • Amino acid transport systems in intestinal brush-border membranes from lepidopteran larvae
    • Giordana B., Sacchi V.F., Parenti P., Hanozet G.M. Amino acid transport systems in intestinal brush-border membranes from lepidopteran larvae. Am. J. Physiol. 1989, 257:R494-R500.
    • (1989) Am. J. Physiol. , vol.257 , pp. R494-R500
    • Giordana, B.1    Sacchi, V.F.2    Parenti, P.3    Hanozet, G.M.4
  • 107
    • 0043199579 scopus 로고    scopus 로고
    • The vesicular glutamate transporter 1 (xVGlut1) is expressed in discrete regions of the developing Xenopus laevis nervous system
    • Gleason K.K., Dondeti V.R., Hsia H.L., Cochran E.R., Gumulak-Smith J., et al. The vesicular glutamate transporter 1 (xVGlut1) is expressed in discrete regions of the developing Xenopus laevis nervous system. Gene Expr. Patterns 2003, 3:503-507.
    • (2003) Gene Expr. Patterns , vol.3 , pp. 503-507
    • Gleason, K.K.1    Dondeti, V.R.2    Hsia, H.L.3    Cochran, E.R.4    Gumulak-Smith, J.5
  • 108
    • 0035079905 scopus 로고    scopus 로고
    • The transport activity of the human cationic amino acid transporter hCAT-1 is downregulated by activation of protein kinase C
    • Graf P., Forstermann U., Closs E.I. The transport activity of the human cationic amino acid transporter hCAT-1 is downregulated by activation of protein kinase C. Br. J. Pharmacol. 2001, 132:1193-1200.
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 1193-1200
    • Graf, P.1    Forstermann, U.2    Closs, E.I.3
  • 109
    • 0025048435 scopus 로고
    • Cloning and expression of a rat brain GABA transporter
    • Guastella J., Nelson N., Nelson H., Czyzyk L., Keynan S., et al. Cloning and expression of a rat brain GABA transporter. Science 1990, 249:1303-1306.
    • (1990) Science , vol.249 , pp. 1303-1306
    • Guastella, J.1    Nelson, N.2    Nelson, H.3    Czyzyk, L.4    Keynan, S.5
  • 110
    • 0346941963 scopus 로고    scopus 로고
    • The SLC16 gene family - from monocarboxylate transporters (MCTs) to aromatic amino acid transporters and beyond
    • Aug 28 (Epub ahead of print)
    • Halestrap A.P., Meredith D. The SLC16 gene family - from monocarboxylate transporters (MCTs) to aromatic amino acid transporters and beyond. Pflugers Arch. 2003, Aug 28 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Halestrap, A.P.1    Meredith, D.2
  • 111
    • 0019323439 scopus 로고
    • +-dependent phenylalanine uptake in membrane vesicles isolated from the midgut of Philosamia cynthia larvae
    • +-dependent phenylalanine uptake in membrane vesicles isolated from the midgut of Philosamia cynthia larvae. Biochim. Biophys. Acta. 1980, 596:481-486.
    • (1980) Biochim. Biophys. Acta. , vol.596 , pp. 481-486
    • Hanozet, G.M.1    Giordana, B.2    Sacchi, V.F.3
  • 112
    • 0026947856 scopus 로고
    • Physiology of V-ATPases
    • Harvey W.R. Physiology of V-ATPases. J. Exp. Biol. 1992, 172:1-17.
    • (1992) J. Exp. Biol. , vol.172 , pp. 1-17
    • Harvey, W.R.1
  • 114
    • 0014253423 scopus 로고
    • Active transport by the Cecropia midgut. III. Midgut potential generated directly by active K-transport
    • Harvey W.R., Haskell J.A., Nedergaard S. Active transport by the Cecropia midgut. III. Midgut potential generated directly by active K-transport. J. Exp Biol. 1968, 48:1-12.
    • (1968) J. Exp Biol. , vol.48 , pp. 1-12
    • Harvey, W.R.1    Haskell, J.A.2    Nedergaard, S.3
  • 115
    • 0014073269 scopus 로고
    • Active transport of potassium and oxygen consumption in the isolated midgut of Hyalophora cecropia
    • Harvey W.R., Haskell J.A., Zerahn K. Active transport of potassium and oxygen consumption in the isolated midgut of Hyalophora cecropia. J. Exp. Biol. 1967, 46:235-248.
    • (1967) J. Exp. Biol. , vol.46 , pp. 235-248
    • Harvey, W.R.1    Haskell, J.A.2    Zerahn, K.3
  • 116
    • 22044446866 scopus 로고    scopus 로고
    • + V-ATPases energize animal plasma membranes for secretion and absorption of ions and fluids
    • + V-ATPases energize animal plasma membranes for secretion and absorption of ions and fluids. Am. Zool. 1998, 38:426-441.
    • (1998) Am. Zool. , vol.38 , pp. 426-441
    • Harvey, W.R.1    Maddrell, S.H.P.2    Telfer, W.H.3    Wieczorek, H.4
  • 118
    • 0141618502 scopus 로고    scopus 로고
    • Expression and localization of vesicular glutamate transporters in pancreatic islets, upper gastrointestinal tract, and testis
    • Hayashi M., Morimoto R., Yamamoto A., Moriyama Y. Expression and localization of vesicular glutamate transporters in pancreatic islets, upper gastrointestinal tract, and testis. J. Histochem. Cytochem. 2003, 51:1375-1390.
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 1375-1390
    • Hayashi, M.1    Morimoto, R.2    Yamamoto, A.3    Moriyama, Y.4
  • 119
    • 0035900698 scopus 로고    scopus 로고
    • +-dependent inorganic phosphate cotransporter (DNPI) is a vesicular glutamate transporter in endocrine glutamatergic systems
    • +-dependent inorganic phosphate cotransporter (DNPI) is a vesicular glutamate transporter in endocrine glutamatergic systems. J. Biol. Chem. 2001, 276:43400-43406.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43400-43406
    • Hayashi, M.1    Otsuka, M.2    Morimoto, R.3    Hirota, S.4    Yatsushiro, S.5
  • 120
    • 0019940581 scopus 로고
    • Characterization of antigen recognized by the monoclonal antibody (4F2): different molecular forms on human T and B lymphoblastoid cell lines
    • Hemler M.E., Strominger J.L. Characterization of antigen recognized by the monoclonal antibody (4F2): different molecular forms on human T and B lymphoblastoid cell lines. J. Immunol. 1982, 129:623-628.
    • (1982) J. Immunol. , vol.129 , pp. 623-628
    • Hemler, M.E.1    Strominger, J.L.2
  • 121
    • 0027153978 scopus 로고
    • Neutral amino acid symport in larval Manduca sexta midgut brush-border membrane vesicles deduced from cation-dependent uptake of leucine, alanine, and phenylalanine
    • Hennigan B.B., Wolfersberger M.G., Harvey W.R. Neutral amino acid symport in larval Manduca sexta midgut brush-border membrane vesicles deduced from cation-dependent uptake of leucine, alanine, and phenylalanine. Biochim. Biophys. Acta 1993, 1148:216-222.
    • (1993) Biochim. Biophys. Acta , vol.1148 , pp. 216-222
    • Hennigan, B.B.1    Wolfersberger, M.G.2    Harvey, W.R.3
  • 122
    • 0027297731 scopus 로고
    • Cation-dependent leucine, alanine, and phenylalanine uptake at pH 10 in brush-border membrane vesicles from larval Manduca sexta midgut
    • Hennigan B.B., Wolfersberger M.G., Parthasarathy R., Harvey W.R. Cation-dependent leucine, alanine, and phenylalanine uptake at pH 10 in brush-border membrane vesicles from larval Manduca sexta midgut. Biochim. Biophys. Acta 1993, 1148:209-215.
    • (1993) Biochim. Biophys. Acta , vol.1148 , pp. 209-215
    • Hennigan, B.B.1    Wolfersberger, M.G.2    Parthasarathy, R.3    Harvey, W.R.4
  • 123
    • 0037020114 scopus 로고    scopus 로고
    • The genome sequence of the malaria mosquito Anopheles gambiae
    • Holt R.A., Subramanian G.M., Halpern A., et al. The genome sequence of the malaria mosquito Anopheles gambiae. Science 2002, 298:129-149.
    • (2002) Science , vol.298 , pp. 129-149
    • Holt, R.A.1    Subramanian, G.M.2    Halpern, A.3
  • 124
    • 0036467839 scopus 로고    scopus 로고
    • Neurotransmitters and neuropeptides in the brain of the locust
    • Homberg U. Neurotransmitters and neuropeptides in the brain of the locust. Microsc. Res. Tech. 2002, 56:189-209.
    • (2002) Microsc. Res. Tech. , vol.56 , pp. 189-209
    • Homberg, U.1
  • 125
    • 0036185936 scopus 로고    scopus 로고
    • The Drosophila inebriated-encoded neurotransmitter/osmolyte transporter: dual roles in the control of neuronal excitability and the osmotic stress response
    • Huang X., Huang Y., Chinnappan R., Bocchini C., Gustin M.C., et al. The Drosophila inebriated-encoded neurotransmitter/osmolyte transporter: dual roles in the control of neuronal excitability and the osmotic stress response. Genetics 2002, 160:561-569.
    • (2002) Genetics , vol.160 , pp. 561-569
    • Huang, X.1    Huang, Y.2    Chinnappan, R.3    Bocchini, C.4    Gustin, M.C.5
  • 126
    • 0036523034 scopus 로고    scopus 로고
    • In vivo properties of the Drosophila inebriated-encoded neurotransmitter transporter
    • Huang Y., Stern M. In vivo properties of the Drosophila inebriated-encoded neurotransmitter transporter. J. Neurosci. 2002, 22:1698-1708.
    • (2002) J. Neurosci. , vol.22 , pp. 1698-1708
    • Huang, Y.1    Stern, M.2
  • 127
    • 0036865272 scopus 로고    scopus 로고
    • The glutamate transporter GLAST-1 (EAAT-1) is expressed in the plasma membrane of osteocytes and is responsive to extracellular glutamate concentration
    • Huggett J.F., Mustafa A., O'Neal L., Mason D.J. The glutamate transporter GLAST-1 (EAAT-1) is expressed in the plasma membrane of osteocytes and is responsive to extracellular glutamate concentration. Biochem. Soc. Trans. 2002, 30:890-893.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 890-893
    • Huggett, J.F.1    Mustafa, A.2    O'Neal, L.3    Mason, D.J.4
  • 128
    • 0030909127 scopus 로고    scopus 로고
    • Cloning of the monocarboxylate transporter isoform MCT2 from rat testis provides evidence that expression in tissues is species-specific and may involve post-transcriptional regulation
    • Jackson V.N., Price N.T., Carpenter L., Halestrap A.P. Cloning of the monocarboxylate transporter isoform MCT2 from rat testis provides evidence that expression in tissues is species-specific and may involve post-transcriptional regulation. Biochem. J. 1997, 324:447-453.
    • (1997) Biochem. J. , vol.324 , pp. 447-453
    • Jackson, V.N.1    Price, N.T.2    Carpenter, L.3    Halestrap, A.P.4
  • 129
    • 0017149332 scopus 로고
    • L-glutamate as an excitatory transmitter at the Drosophila larval neuromuscular junction
    • Jan L.Y., Jan Y.N. L-glutamate as an excitatory transmitter at the Drosophila larval neuromuscular junction. J. Physiol. 1976, 262:215-236.
    • (1976) J. Physiol. , vol.262 , pp. 215-236
    • Jan, L.Y.1    Jan, Y.N.2
  • 130
    • 0017089101 scopus 로고
    • Properties of the larval neuromuscular junction in Drosophila melanogaster
    • Jan L.Y., Jan Y.N. Properties of the larval neuromuscular junction in Drosophila melanogaster. J. Physiol. 1976, 262:189-214.
    • (1976) J. Physiol. , vol.262 , pp. 189-214
    • Jan, L.Y.1    Jan, Y.N.2
  • 131
    • 0028021627 scopus 로고
    • Sequence similarities and evolutionary relationships of microbial, plant and animal alpha-amylases
    • Janecek S. Sequence similarities and evolutionary relationships of microbial, plant and animal alpha-amylases. Eur. J. Biochem. 1994, 224:519-524.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 519-524
    • Janecek, S.1
  • 132
    • 0036186510 scopus 로고    scopus 로고
    • Dual-function vector for protein expression in both mammalian cells and Xenopus laevis oocytes
    • 540
    • Jespersen T., Grunnet M., Angelo K., Klaerke D.A., Olesen S.P. Dual-function vector for protein expression in both mammalian cells and Xenopus laevis oocytes. Biotechniques 2002, 32:536-538. 540.
    • (2002) Biotechniques , vol.32 , pp. 536-538
    • Jespersen, T.1    Grunnet, M.2    Angelo, K.3    Klaerke, D.A.4    Olesen, S.P.5
  • 133
    • 0041707787 scopus 로고    scopus 로고
    • Identification, functional characterization and expression of a LAT type amino acid transporter from the mosquito Aedes aegypti
    • Jin X., Aimanova K., Ross L.S., Gill S.S. Identification, functional characterization and expression of a LAT type amino acid transporter from the mosquito Aedes aegypti. Insect Biochem. Mol. Biol. 2003, 33:815-827.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 815-827
    • Jin, X.1    Aimanova, K.2    Ross, L.S.3    Gill, S.S.4
  • 134
    • 0033566581 scopus 로고    scopus 로고
    • Bloated tubules (blot) encodes a Drosophila member of the neurotransmitter transporter family required for organisation of the apical cytocortex
    • Johnson K., Knust E., Skaer H. bloated tubules (blot) encodes a Drosophila member of the neurotransmitter transporter family required for organisation of the apical cytocortex. Devel. Biol. 1999, 212:440-454.
    • (1999) Devel. Biol. , vol.212 , pp. 440-454
    • Johnson, K.1    Knust, E.2    Skaer, H.3
  • 135
    • 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 1992, 360:467-471.
    • (1992) Nature , vol.360 , pp. 467-471
    • Kanai, Y.1    Hediger, M.A.2
  • 136
    • 0027205324 scopus 로고
    • The elusive transporters with a high affinity for glutamate
    • Kanai Y., Smith C.P., Hediger M.A. The elusive transporters with a high affinity for glutamate. Trends Neurosci. 1993, 16:365-370.
    • (1993) Trends Neurosci. , vol.16 , pp. 365-370
    • Kanai, Y.1    Smith, C.P.2    Hediger, M.A.3
  • 137
    • 0037608598 scopus 로고    scopus 로고
    • The high-affinity glutamate and neutral amino-acid transporter family
    • Humana Press Inc., Totowa, New Jersey, M.E.A. Reith (Ed.)
    • Kanai Y., Trotti D., Berger U.V. The high-affinity glutamate and neutral amino-acid transporter family. Neurotransmitter Transporters: Structure, Function and Regulation 2002, 255-312. Humana Press Inc., Totowa, New Jersey. M.E.A. Reith (Ed.).
    • (2002) Neurotransmitter Transporters: Structure, Function and Regulation , pp. 255-312
    • Kanai, Y.1    Trotti, D.2    Berger, U.V.3
  • 138
    • 0028341123 scopus 로고
    • Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters
    • Kavanaugh M.P., Miller D.G., Zhang W., Law W., Kozak S.L., et al. Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters. Proc. Natl Acad. Sci. USA 1994, 91:7071-7075.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7071-7075
    • Kavanaugh, M.P.1    Miller, D.G.2    Zhang, W.3    Law, W.4    Kozak, S.L.5
  • 139
    • 0029744420 scopus 로고    scopus 로고
    • Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line
    • Kekuda R., Prasad P.D., Fei Y.J., Torres-Zamorano V., Sinha S., et al. Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line. J. Biol. Chem. 1996, 271:18657-18661.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18657-18661
    • Kekuda, R.1    Prasad, P.D.2    Fei, Y.J.3    Torres-Zamorano, V.4    Sinha, S.5
  • 140
    • 0035703933 scopus 로고    scopus 로고
    • The human T-type amino acid transporter-1: characterization, gene organization, and chromosomal location
    • Kim do K., Kanai Y., Matsuo H., Kim J.Y., Chairoungdua A., et al. The human T-type amino acid transporter-1: characterization, gene organization, and chromosomal location. Genomics 2002, 79:95-103.
    • (2002) Genomics , vol.79 , pp. 95-103
    • Kim do, K.1    Kanai, Y.2    Matsuo, H.3    Kim, J.Y.4    Chairoungdua, A.5
  • 141
    • 0026463075 scopus 로고
    • Cdna Cloning of Mev, a mutant protein that facilitates cellular uptake of mevalonate, and identification of the point mutation responsible for its gain of function
    • Kim C.M., Goldstein J.L., Brown M.S. Cdna Cloning of Mev, a mutant protein that facilitates cellular uptake of mevalonate, and identification of the point mutation responsible for its gain of function. J. Biol. Chem. 1992, 267:23113-23121.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23113-23121
    • Kim, C.M.1    Goldstein, J.L.2    Brown, M.S.3
  • 142
    • 84920052731 scopus 로고    scopus 로고
    • Identification and characterization of a novel epithelial aromatic amino acid transporter TAT1
    • Kim D.K., Kanai Y., Chairoungdua A., Enomoto A., Inatomi J., et al. Identification and characterization of a novel epithelial aromatic amino acid transporter TAT1. Jap. J. Pharmacol. 2002, 88:223P.
    • (2002) Jap. J. Pharmacol. , vol.88 , pp. 223P
    • Kim, D.K.1    Kanai, Y.2    Chairoungdua, A.3    Enomoto, A.4    Inatomi, J.5
  • 143
    • 0035907362 scopus 로고    scopus 로고
    • +-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters
    • +-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J. Biol. Chem. 2001, 276:17221-17228.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17221-17228
    • Kim, D.K.1    Kanai, Y.2    Chairoungdua, A.3    Matsuo, H.4    Cha, S.H.5
  • 144
    • 0025784145 scopus 로고
    • Transport of cationic amino acids by the mouse ecotropic retrovirus receptor
    • Kim J.W., Closs E.I., Albritton L.M., Cunningham J.M. Transport of cationic amino acids by the mouse ecotropic retrovirus receptor. Nature 1991, 352:725-728.
    • (1991) Nature , vol.352 , pp. 725-728
    • Kim, J.W.1    Closs, E.I.2    Albritton, L.M.3    Cunningham, J.M.4
  • 145
    • 0034254638 scopus 로고    scopus 로고
    • CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression
    • Kirk P., Wilson M.C., Heddle C., Brown M.H., Barclay A.N., et al. CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. EMBO J. 2000, 19:3896-3904.
    • (2000) EMBO J. , vol.19 , pp. 3896-3904
    • Kirk, P.1    Wilson, M.C.2    Heddle, C.3    Brown, M.H.4    Barclay, A.N.5
  • 146
    • 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 1994, 24:218-224.
    • (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
  • 147
    • 0032579413 scopus 로고    scopus 로고
    • Structure and organization of the Drosophila cholinergic locus
    • Kitamoto T., Wang W., Salvaterra P.M. Structure and organization of the Drosophila cholinergic locus. J. Biol. Chem. 1998, 273:2706-2713.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2706-2713
    • Kitamoto, T.1    Wang, W.2    Salvaterra, P.M.3
  • 148
    • 0033970873 scopus 로고    scopus 로고
    • Isolation and characterization of mutants for the vesicular acetylcholine transporter gene in Drosophila melanogaster
    • Kitamoto T., Xie X., Wu C.F., Salvaterra P.M. Isolation and characterization of mutants for the vesicular acetylcholine transporter gene in Drosophila melanogaster. J. Neurobiol. 2000, 42:161-171.
    • (2000) J. Neurobiol. , vol.42 , pp. 161-171
    • Kitamoto, T.1    Xie, X.2    Wu, C.F.3    Salvaterra, P.M.4
  • 149
    • 0033970873 scopus 로고    scopus 로고
    • Isolation and characterization of mutants for the vesicular acetylcholine transporter gene in Drosophila melanogaster
    • Kitamoto T., Xie X., Wu C.-F., Salvaterra P.M. Isolation and characterization of mutants for the vesicular acetylcholine transporter gene in Drosophila melanogaster. J. Neurobiol. 2000, 42:161-171.
    • (2000) J. Neurobiol. , vol.42 , pp. 161-171
    • Kitamoto, T.1    Xie, X.2    Wu, C.-F.3    Salvaterra, P.M.4
  • 150
    • 0016489452 scopus 로고
    • Selective uptake of indolamine into nervous fibers in brain of desert locust, Schistocerca-Gregaria Forskal (Insecta) - fluorescence and electron-microscopic investigation
    • Klemm N., Schneider L. Selective uptake of indolamine into nervous fibers in brain of desert locust, Schistocerca-Gregaria Forskal (Insecta) - fluorescence and electron-microscopic investigation. Comp. Biochem. Physiol. CPharmacol. Toxicol. Endocrinol. 1975, 50:177-182.
    • (1975) Comp. Biochem. Physiol. CPharmacol. Toxicol. Endocrinol. , vol.50 , pp. 177-182
    • Klemm, N.1    Schneider, L.2
  • 151
    • 38249025370 scopus 로고
    • Monoclonal antibodies against the high affinity choline transport system
    • Knipper M., Strotmann J., Mädler U., Kahle C., Breer H. Monoclonal antibodies against the high affinity choline transport system. Neurochem. Int. 1989, 14:217-222.
    • (1989) Neurochem. Int. , vol.14 , pp. 217-222
    • Knipper, M.1    Strotmann, J.2    Mädler, U.3    Kahle, C.4    Breer, H.5
  • 152
    • 0016773878 scopus 로고
    • Aggressive behavior and brain serotonin and catecholamines in ants (Formica rufa)
    • Kostowski W., Tarchalska-Krynska B., Markowska L. Aggressive behavior and brain serotonin and catecholamines in ants (Formica rufa). Pharmacol. Biochem. Behav. 1975, 3:717-719.
    • (1975) Pharmacol. Biochem. Behav. , vol.3 , pp. 717-719
    • Kostowski, W.1    Tarchalska-Krynska, B.2    Markowska, L.3
  • 153
    • 32844461029 scopus 로고    scopus 로고
    • Neurotransmitter transporters
    • Oxford University Press, Oxford, H. Bellen (Ed.)
    • Krantz D.E., Chaudhry F.A., Edwards R.H. Neurotransmitter transporters. Neurotransmitter Release 1999, 145-207. Oxford University Press, Oxford. H. Bellen (Ed.).
    • (1999) Neurotransmitter Release , pp. 145-207
    • Krantz, D.E.1    Chaudhry, F.A.2    Edwards, R.H.3
  • 154
    • 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 2000, 242:399-405.
    • (2000) Gene , vol.242 , pp. 399-405
    • Kucharski, R.1    Ball, E.E.2    Hayward, D.C.3    Maleszka, R.4
  • 156
    • 0037083070 scopus 로고    scopus 로고
    • Pharmacological evidence for GABAergic regulation of specific behaviors in Drosophila melanogaster
    • Leal S.M., Neckameyer W.S. Pharmacological evidence for GABAergic regulation of specific behaviors in Drosophila melanogaster. J. Neurobiol. 2002, 50:245-261.
    • (2002) J. Neurobiol. , vol.50 , pp. 245-261
    • Leal, S.M.1    Neckameyer, W.S.2
  • 157
    • 0038312898 scopus 로고    scopus 로고
    • Octopaminergic modulation of synaptic transmission between an identified sensory afferent and flight motorneuron in the locust
    • Leitch B., Judge S., Pitman R.M. Octopaminergic modulation of synaptic transmission between an identified sensory afferent and flight motorneuron in the locust. J. Comp. Neurol. 2003, 462:55-70.
    • (2003) J. Comp. Neurol. , vol.462 , pp. 55-70
    • Leitch, B.1    Judge, S.2    Pitman, R.M.3
  • 158
    • 0035656478 scopus 로고    scopus 로고
    • Role of specific activators of intestinal amino acid transport in Bombyx mori larval growth and nutrition
    • Leonardi M.G., Casartelli M., Fiandra L., Parenti P., Giordana B. Role of specific activators of intestinal amino acid transport in Bombyx mori larval growth and nutrition. Arch. Insect Biochem. Physiol. 2001, 48:190-198.
    • (2001) Arch. Insect Biochem. Physiol. , vol.48 , pp. 190-198
    • Leonardi, M.G.1    Casartelli, M.2    Fiandra, L.3    Parenti, P.4    Giordana, B.5
  • 160
    • 0016135898 scopus 로고
    • Exchange of neurotransmitter amino-acid at nerve-endings can simulate high affinity uptake
    • Levi G., Raiteri M. Exchange of neurotransmitter amino-acid at nerve-endings can simulate high affinity uptake. Nature 1974, 250:735-737.
    • (1974) Nature , vol.250 , pp. 735-737
    • Levi, G.1    Raiteri, M.2
  • 161
    • 0042529207 scopus 로고    scopus 로고
    • Expression of neutral amino acid transporter ASCT2 in human prostate
    • Li R., Younes M., Frolov A., Wheeler T.M., Scardino P., et al. Expression of neutral amino acid transporter ASCT2 in human prostate. Anticancer Res. 2003, 23:3413-3418.
    • (2003) Anticancer Res. , vol.23 , pp. 3413-3418
    • Li, R.1    Younes, M.2    Frolov, A.3    Wheeler, T.M.4    Scardino, P.5
  • 163
    • 0031714178 scopus 로고    scopus 로고
    • - neurotransmitter transporters
    • - neurotransmitter transporters. Meth. Enzymol. 1998, 296:425-436.
    • (1998) Meth. Enzymol. , vol.296 , pp. 425-436
    • Lill, H.1    Nelson, N.2
  • 164
    • 0032582702 scopus 로고    scopus 로고
    • Human monocarboxylate transporter 2 (MCT2) is a high affinity pyruvate transporter
    • Lin R.Y., Vera J.C., Chaganti R.S., Golde D.W. Human monocarboxylate transporter 2 (MCT2) is a high affinity pyruvate transporter. J. Biol. Chem. 1998, 273:28959-28965.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28959-28965
    • Lin, R.Y.1    Vera, J.C.2    Chaganti, R.S.3    Golde, D.W.4
  • 167
    • 0029942876 scopus 로고    scopus 로고
    • + and zwitterionic lysine uptake by System B in brush border membrane vesicles from larval Manduca sexta midgut
    • + and zwitterionic lysine uptake by System B in brush border membrane vesicles from larval Manduca sexta midgut. Biochim. Biophys. Acta 1996, 1282:32-38.
    • (1996) Biochim. Biophys. Acta , vol.1282 , pp. 32-38
    • Liu, Z.1    Harvey, W.R.2
  • 168
    • 0030014883 scopus 로고    scopus 로고
    • +, in brush border membrane vesicles from larval Manduca sexta midgut
    • +, in brush border membrane vesicles from larval Manduca sexta midgut. Biochim. Biophys. Acta 1996, 1282:25-31.
    • (1996) Biochim. Biophys. Acta , vol.1282 , pp. 25-31
    • Liu, Z.1    Harvey, W.R.2
  • 169
    • 0347787053 scopus 로고    scopus 로고
    • + amino acid transporter KAAT1 mutant Y147F has increased transport activity and altered substrate selectivity
    • + amino acid transporter KAAT1 mutant Y147F has increased transport activity and altered substrate selectivity. J. Exp. Biol. 2003, 206:245-254.
    • (2003) J. Exp. Biol. , vol.206 , pp. 245-254
    • Liu, Z.1    Stevens, B.R.2    Feldman, D.H.3    Hediger, M.A.4    Harvey, W.R.5
  • 170
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes
    • MacGregor E.A., Janecek S., Svensson B. Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim. Biophys. Acta 2001, 1546:1-20.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 171
    • 2342514379 scopus 로고    scopus 로고
    • Sodium-coupled neutral amino acid (System N/A) transporters of the SLC38 gene family
    • 2003 Jul 4 (Epub ahead of print)
    • Mackenzie B., Erickson J.D. Sodium-coupled neutral amino acid (System N/A) transporters of the SLC38 gene family. Pflugers Arch. 2003, 2003 Jul 4 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Mackenzie, B.1    Erickson, J.D.2
  • 172
    • 0542424245 scopus 로고
    • A diuretic hormone in Rhodnius Prolixus Stal
    • Maddrell S.H. A diuretic hormone in Rhodnius Prolixus Stal. Nature 1962, 194:605-606.
    • (1962) Nature , vol.194 , pp. 605-606
    • Maddrell, S.H.1
  • 174
    • 0033825689 scopus 로고    scopus 로고
    • Pharmacological interference with glutamate re-uptake impairs long-term memory in the honeybee, Apis mellifera
    • Maleszka R., Helliwell P., Kucharski R. Pharmacological interference with glutamate re-uptake impairs long-term memory in the honeybee, Apis mellifera. Behav. Brain Res. 2000, 115:49-53.
    • (2000) Behav. Brain Res. , vol.115 , pp. 49-53
    • Maleszka, R.1    Helliwell, P.2    Kucharski, R.3
  • 175
    • 0036489172 scopus 로고    scopus 로고
    • A high-affinity octopamine transporter cloned from the central nervous system of cabbage looper Trichoplusia ni
    • Malutan T., McLean H., Caveney S., Donly C. A high-affinity octopamine transporter cloned from the central nervous system of cabbage looper Trichoplusia ni. Insect Biochem. Mol. Biol. 2002, 32:343-357.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 343-357
    • Malutan, T.1    McLean, H.2    Caveney, S.3    Donly, C.4
  • 176
    • 0018845431 scopus 로고
    • Coupling between oxidative metabolism and active transport in the midgut of tobacco hornworm
    • Mandel L.J., Moffett D.F., Riddle T.G., Grafton M.M. Coupling between oxidative metabolism and active transport in the midgut of tobacco hornworm. Am. J. Physiol. 1980, 238:C1-C9.
    • (1980) Am. J. Physiol. , vol.238 , pp. C1-C9
    • Mandel, L.J.1    Moffett, D.F.2    Riddle, T.G.3    Grafton, M.M.4
  • 177
    • 0034525940 scopus 로고    scopus 로고
    • Characterisation of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscle
    • Manning Fox J.E., Meredith D., Halestrap A.P. Characterisation of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscle. J. Physiol. 2000, 529:285-293.
    • (2000) J. Physiol. , vol.529 , pp. 285-293
    • Manning Fox, J.E.1    Meredith, D.2    Halestrap, A.P.3
  • 178
    • 0037370550 scopus 로고    scopus 로고
    • N-linked glycosylation and sequence changes in a critical negative control region of the ASCT1 and ASCT2 neutral amino acid transporters determine their retroviral receptor functions
    • Marin M., Lavillette D., Kelly S.M., Kabat D. N-linked glycosylation and sequence changes in a critical negative control region of the ASCT1 and ASCT2 neutral amino acid transporters determine their retroviral receptor functions. J. Virol. 2003, 77:2936-2945.
    • (2003) J. Virol. , vol.77 , pp. 2936-2945
    • Marin, M.1    Lavillette, D.2    Kelly, S.M.3    Kabat, D.4
  • 179
    • 0032852641 scopus 로고    scopus 로고
    • Neurotransmitter transporters in the central nervous system
    • Masson J., Sagne C., Hamon M., El Mestikawy S. Neurotransmitter transporters in the central nervous system. Pharmacol. Rev. 1999, 51:439-464.
    • (1999) Pharmacol. Rev. , vol.51 , pp. 439-464
    • Masson, J.1    Sagne, C.2    Hamon, M.3    El Mestikawy, S.4
  • 180
    • 0032541636 scopus 로고    scopus 로고
    • Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family
    • Mastroberardino L., Spindler B., Pfeiffer R., Skelly P.J., Loffing J., et al. Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family. Nature 1998, 395:288-291.
    • (1998) Nature , vol.395 , pp. 288-291
    • Mastroberardino, L.1    Spindler, B.2    Pfeiffer, R.3    Skelly, P.J.4    Loffing, J.5
  • 181
    • 0037444545 scopus 로고    scopus 로고
    • Neuronal glutamate uptake contributes to GABA synthesis and inhibitory synaptic strength
    • Mathews G.C., Diamond J.S. Neuronal glutamate uptake contributes to GABA synthesis and inhibitory synaptic strength. J. Neurosci. 2003, 23:2040-2048.
    • (2003) J. Neurosci. , vol.23 , pp. 2040-2048
    • Mathews, G.C.1    Diamond, J.S.2
  • 182
    • 0036052825 scopus 로고    scopus 로고
    • Amplification of representative cDNA samples from microscopic amounts of invertebrate tissue to search for new genes
    • Matz M.V. Amplification of representative cDNA samples from microscopic amounts of invertebrate tissue to search for new genes. Methods Mol. Biol. 2002, 183:3-18.
    • (2002) Methods Mol. Biol. , vol.183 , pp. 3-18
    • Matz, M.V.1
  • 183
    • 0028949668 scopus 로고
    • Cloning, functional expression, and pharmacology of a GABA transporter from Manduca sexta
    • Mbungu D., Ross L.S., Gill S.S. Cloning, functional expression, and pharmacology of a GABA transporter from Manduca sexta. Arch. Biochem. Biophys. 1995, 318:489-497.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 489-497
    • Mbungu, D.1    Ross, L.S.2    Gill, S.S.3
  • 184
    • 0016412954 scopus 로고
    • Neuromuscular pharmacology of insects
    • McDonald T.J. Neuromuscular pharmacology of insects. Ann. Rev. Entomol. 1975, 20:151-166.
    • (1975) Ann. Rev. Entomol. , vol.20 , pp. 151-166
    • McDonald, T.J.1
  • 185
    • 0027272707 scopus 로고
    • Genes required for GABA function in Caenorhabditis elegans
    • McIntire S.L., Jorgensen E., Horvitz H.R. Genes required for GABA function in Caenorhabditis elegans. Nature 1993, 364:334-337.
    • (1993) Nature , vol.364 , pp. 334-337
    • McIntire, S.L.1    Jorgensen, E.2    Horvitz, H.R.3
  • 186
  • 187
    • 0037083854 scopus 로고    scopus 로고
    • Activation of system L heterodimeric amino acid exchangers by intracellular substrates
    • Meier C., Ristic Z., Klauser S., Verrey F. Activation of system L heterodimeric amino acid exchangers by intracellular substrates. EMBO J. 2002, 21:580-589.
    • (2002) EMBO J. , vol.21 , pp. 580-589
    • Meier, C.1    Ristic, Z.2    Klauser, S.3    Verrey, F.4
  • 188
    • 0036386887 scopus 로고    scopus 로고
    • Functional and molecular characterisation of lactic acid transport in bovine articular chondrocytes
    • Meredith D., Bell P., McClure B., Wilkins R. Functional and molecular characterisation of lactic acid transport in bovine articular chondrocytes. Cell. Physiol. Biochem. 2002, 12:227-234.
    • (2002) Cell. Physiol. Biochem. , vol.12 , pp. 227-234
    • Meredith, D.1    Bell, P.2    McClure, B.3    Wilkins, R.4
  • 189
    • 1242312682 scopus 로고    scopus 로고
    • OX47 (basigin) may act as a chaperone for expression of the monocarboxylate transporter MCT1 at the plasma membrane of Xenopus laevis oocytes
    • Meredith D., Halestrap A.P. OX47 (basigin) may act as a chaperone for expression of the monocarboxylate transporter MCT1 at the plasma membrane of Xenopus laevis oocytes. J. Physiol. Lond. 2000, 526:23P-24P.
    • (2000) J. Physiol. Lond. , vol.526 , pp. 23P-24P
    • Meredith, D.1    Halestrap, A.P.2
  • 190
    • 0028874157 scopus 로고
    • Cloning and functional expression of a Na(+)-dependent phosphate co-transporter from human kidney: cDNA cloning and functional expression
    • Miyamoto K., Tatsumi S., Sonoda T., Yamamoto H., Minami H., et al. Cloning and functional expression of a Na(+)-dependent phosphate co-transporter from human kidney: cDNA cloning and functional expression. Biochem. J. 1995, 305:81-85.
    • (1995) Biochem. J. , vol.305 , pp. 81-85
    • Miyamoto, K.1    Tatsumi, S.2    Sonoda, T.3    Yamamoto, H.4    Minami, H.5
  • 191
    • 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. 1989, 29:365-402.
    • (1989) Annu. Rev. Pharmacol. Toxicol. , vol.29 , pp. 365-402
    • Monaghan, D.T.1    Bridges, R.J.2    Cotman, C.W.3
  • 192
    • 0033561212 scopus 로고    scopus 로고
    • Biogenic amine systems in the fruit fly Drosophila melanogaster
    • Monastirioti M. Biogenic amine systems in the fruit fly Drosophila melanogaster. Microsc. Res. Tech. 1999, 45:106-121.
    • (1999) Microsc. Res. Tech. , vol.45 , pp. 106-121
    • Monastirioti, M.1
  • 193
    • 13844317210 scopus 로고    scopus 로고
    • The sodium phosphate cotransporter family SLC34
    • Murer H., Forster I., Biber J. The sodium phosphate cotransporter family SLC34. Pflugers Arch. 2003, 16:16.
    • (2003) Pflugers Arch. , vol.16 , pp. 16
    • Murer, H.1    Forster, I.2    Biber, J.3
  • 194
    • 0033775213 scopus 로고    scopus 로고
    • Proximal tubular phosphate reabsorption: molecular mechanisms
    • Murer H., Hernando N., Forster I., Biber J. Proximal tubular phosphate reabsorption: molecular mechanisms. Physiol. Rev. 2000, 80:1373-1409.
    • (2000) Physiol. Rev. , vol.80 , pp. 1373-1409
    • Murer, H.1    Hernando, N.2    Forster, I.3    Biber, J.4
  • 195
    • 0017893589 scopus 로고
    • The role of serotonin in regulation of the circadian rhythm of locomotor activity in the cricket (Acheta domesticus L.) II. Distribution of serotonin and variations in different brain structure
    • Muszynska-Pytel M., Cymboroski B. The role of serotonin in regulation of the circadian rhythm of locomotor activity in the cricket (Acheta domesticus L.) II. Distribution of serotonin and variations in different brain structure. Comp. Biochem. Physiol. C 1978, 59:17-20.
    • (1978) Comp. Biochem. Physiol. C , vol.59 , pp. 17-20
    • Muszynska-Pytel, M.1    Cymboroski, B.2
  • 196
    • 0017879156 scopus 로고
    • The role of serotonin in regulation of the circadian rhythms of locomotor activity in the cricket (Acheta domesticus L.) I. Circadian variations in serotonin concentration in the brain and hemolymph
    • Muzynska-Pytel M., Cymborowski B. The role of serotonin in regulation of the circadian rhythms of locomotor activity in the cricket (Acheta domesticus L.) I. Circadian variations in serotonin concentration in the brain and hemolymph. Comp. Biochem. Physiol. C 1978, 59:13-15.
    • (1978) Comp. Biochem. Physiol. C , vol.59 , pp. 13-15
    • Muzynska-Pytel, M.1    Cymborowski, B.2
  • 197
    • 0037031543 scopus 로고    scopus 로고
    • A trace amine, tyramine, functions as a neuromodulator in Drosophila melanogaster
    • Nagaya Y., Kutsukake M., Chigusa S.I., Komatsu A. A trace amine, tyramine, functions as a neuromodulator in Drosophila melanogaster. Neurosci. Lett. 2002, 329:324-328.
    • (2002) Neurosci. Lett. , vol.329 , pp. 324-328
    • Nagaya, Y.1    Kutsukake, M.2    Chigusa, S.I.3    Komatsu, A.4
  • 199
    • 0032458568 scopus 로고    scopus 로고
    • Dopamine and mushroom bodies in Drosophila: experience-dependent and-independent aspects of sexual behavior
    • Neckameyer W.S. Dopamine and mushroom bodies in Drosophila: experience-dependent and-independent aspects of sexual behavior. Learn. Mem. 1998, 5:157-165.
    • (1998) Learn. Mem. , vol.5 , pp. 157-165
    • Neckameyer, W.S.1
  • 200
    • 0344905168 scopus 로고
    • Active transport of alpha-aminoisobutyric acid by the isolated midgut of Hyalophora cecropia
    • Nedergaard S. Active transport of alpha-aminoisobutyric acid by the isolated midgut of Hyalophora cecropia. J. Exp. Biol. 1972, 56:167-172.
    • (1972) J. Exp. Biol. , vol.56 , pp. 167-172
    • Nedergaard, S.1
  • 201
    • 0028535329 scopus 로고
    • Porters and neurotransmitter transporters
    • Nelson N., Lill H. Porters and neurotransmitter transporters. J. Exp. Biol. 1994, 196:213-228.
    • (1994) J. Exp. Biol. , vol.196 , pp. 213-228
    • Nelson, N.1    Lill, H.2
  • 202
    • 0036843663 scopus 로고    scopus 로고
    • The significance of molecular slips in transport systems
    • Nelson N., Sacher A., Nelson H. The significance of molecular slips in transport systems. Nat. Rev. Mol. Cell. Biol. 2002, 3:876-881.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 876-881
    • Nelson, N.1    Sacher, A.2    Nelson, H.3
  • 203
    • 0028233971 scopus 로고
    • Cloning and expression of a cDNA encoding a brain-specific Na(+)-dependent inorganic phosphate cotransporter
    • Ni B., Rosteck P.R., Nadi N.S., Paul S.M. Cloning and expression of a cDNA encoding a brain-specific Na(+)-dependent inorganic phosphate cotransporter. Proc. Natl Acad. Sci. USA 1994, 91:5607-5611.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5607-5611
    • Ni, B.1    Rosteck, P.R.2    Nadi, N.S.3    Paul, S.M.4
  • 204
    • 0026492498 scopus 로고
    • Binding of Bacillus sphaericus binary toxin to a specific receptor on midgut brush-border membranes from mosquito larvae
    • Nielsen-LeRoux C., Charles J.-F. Binding of Bacillus sphaericus binary toxin to a specific receptor on midgut brush-border membranes from mosquito larvae. Eur. J. Biochem. 1992, 210:585-590.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 585-590
    • Nielsen-LeRoux, C.1    Charles, J.-F.2
  • 205
    • 0028473229 scopus 로고
    • Serotonin depletion affects blood-feeding but not host-seeking ability in Aedes triseriatus (Diptera: Culicidae)
    • Novak M.G., Rowley W.A. Serotonin depletion affects blood-feeding but not host-seeking ability in Aedes triseriatus (Diptera: Culicidae). J. Med. Entomol. 1994, 31:600-606.
    • (1994) J. Med. Entomol. , vol.31 , pp. 600-606
    • Novak, M.G.1    Rowley, W.A.2
  • 206
    • 0021436627 scopus 로고
    • Secretion by the Malpighian tubules of Rhodnius prolixus stal: electrical events
    • O'Donnell M.J., Maddrell S.H. Secretion by the Malpighian tubules of Rhodnius prolixus stal: electrical events. J. Exp. Biol. 1984, 110:275-290.
    • (1984) J. Exp. Biol. , vol.110 , pp. 275-290
    • O'Donnell, M.J.1    Maddrell, S.H.2
  • 207
    • 0034602564 scopus 로고    scopus 로고
    • Functional characterization of the human high-affinity choline transporter
    • Okuda T., Haga T. Functional characterization of the human high-affinity choline transporter. FEBS Lett. 2000, 484:92-97.
    • (2000) FEBS Lett. , vol.484 , pp. 92-97
    • Okuda, T.1    Haga, T.2
  • 208
    • 0028090524 scopus 로고
    • The cellular receptor for gibbon ape leukemia virus is a novel high affinity sodium-dependent phosphate transporter
    • Olah Z., Lehel C., Anderson W.B., Eiden M.V., Wilson C.A. The cellular receptor for gibbon ape leukemia virus is a novel high affinity sodium-dependent phosphate transporter. J. Biol. Chem. 1994, 269:25426-25431.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25426-25431
    • Olah, Z.1    Lehel, C.2    Anderson, W.B.3    Eiden, M.V.4    Wilson, C.A.5
  • 209
    • 0029876591 scopus 로고    scopus 로고
    • Insect neurotransmission: neurotransmitters and their receptors
    • Osborne R.H. Insect neurotransmission: neurotransmitters and their receptors. Pharmacol. Ther. 1996, 69:117-142.
    • (1996) Pharmacol. Ther. , vol.69 , pp. 117-142
    • Osborne, R.H.1
  • 210
    • 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. 1996, 16:1634-1644.
    • (1996) J. Neurosci. , vol.16 , pp. 1634-1644
    • Otis, T.S.1    Wu, Y.C.2    Trussell, L.O.3
  • 211
    • 0026433037 scopus 로고
    • Expression cloning of a cocaine- and antidepressant-sensitive human noradrenaline transporter
    • Pacholczyk T., Blakely R.D., Amara S.D. Expression cloning of a cocaine- and antidepressant-sensitive human noradrenaline transporter. Nature 1991, 350:350-354.
    • (1991) Nature , vol.350 , pp. 350-354
    • Pacholczyk, T.1    Blakely, R.D.2    Amara, S.D.3
  • 212
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: an application to display phylogenetic trees on personal computers
    • Page R.D. TreeView: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 1996, 12:357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 213
    • 0031751209 scopus 로고    scopus 로고
    • Molecular biology of mammalian plasma membrane amino acid transporters
    • Palacin M., Estevez R., Bertran J., Zorzano A. Molecular biology of mammalian plasma membrane amino acid transporters. Physiol. Rev. 1998, 78:969-1054.
    • (1998) Physiol. Rev. , vol.78 , pp. 969-1054
    • Palacin, M.1    Estevez, R.2    Bertran, J.3    Zorzano, A.4
  • 214
    • 0347572869 scopus 로고    scopus 로고
    • The ancillary proteins of HATs: SLC3 family of amino acid transporters
    • 2003 Jun 11 (Epub ahead of print)
    • Palacin M., Kanai Y. The ancillary proteins of HATs: SLC3 family of amino acid transporters. Pflugers Arch. 2003, 2003 Jun 11 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Palacin, M.1    Kanai, Y.2
  • 216
    • 0026736022 scopus 로고
    • Kinetics of leucine transport in brush border membrane vesicles from lepidopteran larvae midgut
    • Parenti P., Villa M., Hanozet G.M. Kinetics of leucine transport in brush border membrane vesicles from lepidopteran larvae midgut. J. Biol. Chem. 1992, 267:15391-15397.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15391-15397
    • Parenti, P.1    Villa, M.2    Hanozet, G.M.3
  • 217
    • 0033675272 scopus 로고    scopus 로고
    • Transport mechanisms in acetylcholine and monoamine storage
    • Parsons S.M. Transport mechanisms in acetylcholine and monoamine storage. FASEB J. 2000, 14:2423-2434.
    • (2000) FASEB J. , vol.14 , pp. 2423-2434
    • Parsons, S.M.1
  • 218
    • 0034144037 scopus 로고    scopus 로고
    • The physiology of salinity tolerance in larvae of two species of Culex mosquitoes: the role of compatible solutes
    • Patrick M.L., Bradley T.J. The physiology of salinity tolerance in larvae of two species of Culex mosquitoes: the role of compatible solutes. J. Exp. Biol. 2000, 203:821-830.
    • (2000) J. Exp. Biol. , vol.203 , pp. 821-830
    • Patrick, M.L.1    Bradley, T.J.2
  • 219
    • 0027408932 scopus 로고
    • Topology, structure and evolution of 2 families of proteins involved in antibiotic and antiseptic resistance in Eukaryotes and Prokaryotes - an analysis
    • Paulsen I.T., Skurray R.A. Topology, structure and evolution of 2 families of proteins involved in antibiotic and antiseptic resistance in Eukaryotes and Prokaryotes - an analysis. Gene 1993, 124:1-11.
    • (1993) Gene , vol.124 , pp. 1-11
    • Paulsen, I.T.1    Skurray, R.A.2
  • 220
    • 0001468817 scopus 로고    scopus 로고
    • Dissecting the molecular mechanisms of neurotransmitter release in Drosophila
    • Oxford University Press, Oxford, H. Bellen (Ed.)
    • Pennetta G., Wu M., Bellen H.J. Dissecting the molecular mechanisms of neurotransmitter release in Drosophila. Neurotransmitter Release 1999, 304-351. Oxford University Press, Oxford. H. Bellen (Ed.).
    • (1999) Neurotransmitter Release , pp. 304-351
    • Pennetta, G.1    Wu, M.2    Bellen, H.J.3
  • 221
    • 0034658569 scopus 로고    scopus 로고
    • Effects of pH on the uncoupled, coupled and pre-steady-state currents at the amino acid transporter KAAT1 expressed in Xenopus oocytes
    • Peres A., Bossi E. Effects of pH on the uncoupled, coupled and pre-steady-state currents at the amino acid transporter KAAT1 expressed in Xenopus oocytes. J. Physiol. Lond. 2000, 525:83-89.
    • (2000) J. Physiol. Lond. , vol.525 , pp. 83-89
    • Peres, A.1    Bossi, E.2
  • 222
    • 0031445676 scopus 로고    scopus 로고
    • Genetic analysis of glutamate receptors in Drosophila reveals a retrograde signal regulating presynaptic transmitter release
    • Petersen S.A., Fetter R.D., Noordermeer J.N., Goodman C.S., DiAntonio A. Genetic analysis of glutamate receptors in Drosophila reveals a retrograde signal regulating presynaptic transmitter release. Neuron 1997, 19:1237-1248.
    • (1997) Neuron , vol.19 , pp. 1237-1248
    • Petersen, S.A.1    Fetter, R.D.2    Noordermeer, J.N.3    Goodman, C.S.4    DiAntonio, A.5
  • 223
    • 0033521614 scopus 로고    scopus 로고
    • Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family
    • Pfeiffer R., Rossier G., Spindler B., Meier C., Kuhn L., et al. Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. EMBO J. 1999, 18:49-57.
    • (1999) EMBO J. , vol.18 , pp. 49-57
    • Pfeiffer, R.1    Rossier, G.2    Spindler, B.3    Meier, C.4    Kuhn, L.5
  • 224
    • 0032514944 scopus 로고    scopus 로고
    • Functional heterodimeric amino acid transporters lacking cysteine residues involved in disulfide bond
    • Pfeiffer R., Spindler B., Loffing J., Skelly P.J., Shoemaker C.B., et al. Functional heterodimeric amino acid transporters lacking cysteine residues involved in disulfide bond. FEBS Lett. 1998, 439:157-162.
    • (1998) FEBS Lett. , vol.439 , pp. 157-162
    • Pfeiffer, R.1    Spindler, B.2    Loffing, J.3    Skelly, P.J.4    Shoemaker, C.B.5
  • 225
    • 0035030802 scopus 로고    scopus 로고
    • Mouse MCT3 gene is expressed preferentially in retinal pigment and choroid plexus epithelia
    • Philp N.J., Yoon H.Y., Lombardi L. Mouse MCT3 gene is expressed preferentially in retinal pigment and choroid plexus epithelia. Am. J. Physiol. -Cell Physiol. 2001, 280:C1319-C1326.
    • (2001) Am. J. Physiol. -Cell Physiol. , vol.280 , pp. C1319-C1326
    • Philp, N.J.1    Yoon, H.Y.2    Lombardi, L.3
  • 227
    • 0035162154 scopus 로고    scopus 로고
    • The antidepressant-sensitive dopamine transporter in Drosophila melanogaster: a primordial carrier for catecholamines
    • Porzgen P., Park S.K., Hirsh J., Sonders M.S., Amara S.G. The antidepressant-sensitive dopamine transporter in Drosophila melanogaster: a primordial carrier for catecholamines. Mol. Pharmacol. 2001, 59:83-95.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 83-95
    • Porzgen, P.1    Park, S.K.2    Hirsh, J.3    Sonders, M.S.4    Amara, S.G.5
  • 228
    • 0032518981 scopus 로고    scopus 로고
    • Cloning and sequencing of four new mammalian monocarboxylate transporter (MCT) homologues confirms the existence of a transporter family with an ancient past
    • Price N.T., Jackson V.N., Halestrap A.P. Cloning and sequencing of four new mammalian monocarboxylate transporter (MCT) homologues confirms the existence of a transporter family with an ancient past. Biochem. J. 1998, 329:321-328.
    • (1998) Biochem. J. , vol.329 , pp. 321-328
    • Price, N.T.1    Jackson, V.N.2    Halestrap, A.P.3
  • 229
    • 0035823592 scopus 로고    scopus 로고
    • Amino acid transporter CAATCH1 is also an amino acid-gated cation channel
    • Quick M., Stevens B.R. Amino acid transporter CAATCH1 is also an amino acid-gated cation channel. J. Biol. Chem. 2001, 276:33413-33418.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33413-33418
    • Quick, M.1    Stevens, B.R.2
  • 230
    • 0033664316 scopus 로고    scopus 로고
    • Neurogenetics of vesicular transporters in C. elegans
    • Rand J.B., Duerr J.S., Frisby D.L. Neurogenetics of vesicular transporters in C. elegans. FASEB J. 2000, 14:2414-2422.
    • (2000) FASEB J. , vol.14 , pp. 2414-2422
    • Rand, J.B.1    Duerr, J.S.2    Frisby, D.L.3
  • 232
    • 4844229051 scopus 로고    scopus 로고
    • Organic anion transport is the primary function of the SLC17/type I phosphate transporter family
    • 2003 Jun 17 (Epub ahead of print)
    • Reimer R.J., Edwards R.H. Organic anion transport is the primary function of the SLC17/type I phosphate transporter family. Pflugers Arch. 2003, 2003 Jun 17 (Epub ahead of print).
    • (2003) Pflugers Arch.
    • Reimer, R.J.1    Edwards, R.H.2
  • 233
    • 0028207043 scopus 로고
    • Proline transport into brush border membrane vesicles from the midgut of Manduca sexta larvae
    • Reuveni M., Dunn P.E. Proline transport into brush border membrane vesicles from the midgut of Manduca sexta larvae. Comp. Biochem. Physiol. Comp. Physiol. 1994, 107:685-691.
    • (1994) Comp. Biochem. Physiol. Comp. Physiol. , vol.107 , pp. 685-691
    • Reuveni, M.1    Dunn, P.E.2
  • 235
    • 0016891923 scopus 로고
    • Octopamine - presence in firefly lantern suggests a transmitter role
    • Robertson H.A., Carlson A.D. Octopamine - presence in firefly lantern suggests a transmitter role. J. Exp. Zool. 1976, 195:159-164.
    • (1976) J. Exp. Zool. , vol.195 , pp. 159-164
    • Robertson, H.A.1    Carlson, A.D.2
  • 236
    • 0032801719 scopus 로고    scopus 로고
    • Octopamine in invertebrates
    • Roeder T. Octopamine in invertebrates. Progr. Neurobiol. 1999, 59:533-561.
    • (1999) Progr. Neurobiol. , vol.59 , pp. 533-561
    • Roeder, T.1
  • 237
    • 0031671716 scopus 로고    scopus 로고
    • The opt1 gene of Drosophila melanogaster encodes a proton-dependent dipeptide transporter
    • Roman G., Meller V., Wu K.H., Davis R.L. The opt1 gene of Drosophila melanogaster encodes a proton-dependent dipeptide transporter. Am. J. Physiol. Cell Physiol. 1998, 44:C857-C869.
    • (1998) Am. J. Physiol. Cell Physiol. , vol.44 , pp. C857-C869
    • Roman, G.1    Meller, V.2    Wu, K.H.3    Davis, R.L.4
  • 238
    • 0033520913 scopus 로고    scopus 로고
    • LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine
    • Rossier G., Meier C., Bauch C., Summa V., Sordat B., et al. LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. J. Biol. Chem. 1999, 274:34948-34954.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34948-34954
    • Rossier, G.1    Meier, C.2    Bauch, C.3    Summa, V.4    Sordat, B.5
  • 239
    • 0029889988 scopus 로고    scopus 로고
    • PHD: predicting one-dimensional protein structure by profile-based neural networks
    • Rost B. PHD: predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 1996, 266:525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 240
    • 13344286293 scopus 로고    scopus 로고
    • Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate
    • Rothstein J.D., Dykes-Hoberg M., Pardo C.A., Bristol L.A., Jin L., et al. Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate. Neuron 1996, 16:675-686.
    • (1996) Neuron , vol.16 , pp. 675-686
    • Rothstein, J.D.1    Dykes-Hoberg, M.2    Pardo, C.A.3    Bristol, L.A.4    Jin, L.5
  • 241
    • 0034710819 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding the mouse peptide transporter PEPT2
    • Rubio-Aliaga I., Boll M., Daniel H. Cloning and characterization of the gene encoding the mouse peptide transporter PEPT2. Biochem. Biophys. Res. Commun. 2000, 276:734-741.
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 734-741
    • Rubio-Aliaga, I.1    Boll, M.2    Daniel, H.3
  • 242
    • 0041386430 scopus 로고    scopus 로고
    • Glutamate 59 is critical for transport function of the amino acid cotransporter KAAT1
    • Sacchi V.F., Castagna M., Mari S.A., Perego C., Bossi E., et al. Glutamate 59 is critical for transport function of the amino acid cotransporter KAAT1. Am. J. Physiol. Cell Physiol. 2003, 285:C623-C632.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285 , pp. C623-C632
    • Sacchi, V.F.1    Castagna, M.2    Mari, S.A.3    Perego, C.4    Bossi, E.5
  • 243
    • 0035912839 scopus 로고    scopus 로고
    • Identification and characterization of a lysosomal transporter for small neutral amino acids
    • Sagne C., Agulhon C., Ravassard P., Darmon M., Hamon M., et al. Identification and characterization of a lysosomal transporter for small neutral amino acids. Proc. Natl Acad. Sci. USA 2001, 98:7206-7211.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7206-7211
    • Sagne, C.1    Agulhon, C.2    Ravassard, P.3    Darmon, M.4    Hamon, M.5
  • 244
    • 0030840107 scopus 로고    scopus 로고
    • Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases
    • Sagne C., El Mestikawy S., Isambert M.F., Hamon M., Henry J.P., et al. Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases. FEBS Lett. 1997, 417:177-183.
    • (1997) FEBS Lett. , vol.417 , pp. 177-183
    • Sagne, C.1    El Mestikawy, S.2    Isambert, M.F.3    Hamon, M.4    Henry, J.P.5
  • 245
    • 0033821267 scopus 로고    scopus 로고
    • Vectorial metabolism and the evolution of transport systems
    • Saier M.H. Vectorial metabolism and the evolution of transport systems. J. Bacteriol. 2000, 182:5029-5035.
    • (2000) J. Bacteriol. , vol.182 , pp. 5029-5035
    • Saier, M.H.1
  • 246
    • 0343603660 scopus 로고    scopus 로고
    • A functional-phylogenetic classification system for transmembrane solute transporters
    • Saier M.H. A functional-phylogenetic classification system for transmembrane solute transporters. Microbiol. Mol. Biol. Rev. 2000, 64:354-411.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 354-411
    • Saier, M.H.1
  • 248
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 250
    • 0036837291 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a proline transporter from Manduca sexta
    • Sandhu S.K., Ross L.S., Gill S.S. Molecular cloning and functional expression of a proline transporter from Manduca sexta. Insect Biochem. Mol. Biol. 2002, 32:1391-1400.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1391-1400
    • Sandhu, S.K.1    Ross, L.S.2    Gill, S.S.3
  • 251
    • 0036041879 scopus 로고    scopus 로고
    • A cocaine insensitive chimeric insect serotonin transporter reveals domains critical for cocaine interaction
    • Sandhu S.K., Ross L.S., Gill S.S. A cocaine insensitive chimeric insect serotonin transporter reveals domains critical for cocaine interaction. Eur. J. Biochem. 2002, 269:3934-3944.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3934-3944
    • Sandhu, S.K.1    Ross, L.S.2    Gill, S.S.3
  • 252
    • 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. 1999, 274:11455-11458.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3    Bannai, S.4
  • 253
    • 0037107162 scopus 로고    scopus 로고
    • Distribution of cystine/glutamate exchange transporter, system x(c) (-), in the mouse brain
    • Sato H., Tamba M., Okuno S., Sato K., Keino-Masu K., et al. Distribution of cystine/glutamate exchange transporter, system x(c) (-), in the mouse brain. J. Neurosci. 2002, 22:8028-8033.
    • (2002) J. Neurosci. , vol.22 , pp. 8028-8033
    • Sato, H.1    Tamba, M.2    Okuno, S.3    Sato, K.4    Keino-Masu, K.5
  • 254
    • 0022788872 scopus 로고
    • Absorption and transport of radioactive-tracers in the midgut of the malaria mosquito, Anopheles-Stephensi
    • Schneider M., Rudin W., Hecker H. Absorption and transport of radioactive-tracers in the midgut of the malaria mosquito, Anopheles-Stephensi. J. Ultrastruct. Mol. Struct. Res. 1986, 97:50-63.
    • (1986) J. Ultrastruct. Mol. Struct. Res. , vol.97 , pp. 50-63
    • Schneider, M.1    Rudin, W.2    Hecker, H.3
  • 255
    • 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. 1995, 75:369-392.
    • (1995) Physiol. Rev. , vol.75 , pp. 369-392
    • Schuldiner, S.1    Shirvan, A.2    Linial, M.3
  • 257
    • 0036979049 scopus 로고    scopus 로고
    • A role for octopamine in honey bee division of labor
    • Schulz D.J., Barron A.B., Robinson G.E. A role for octopamine in honey bee division of labor. Brain Behav. Evol. 2002, 60:350-359.
    • (2002) Brain Behav. Evol. , vol.60 , pp. 350-359
    • Schulz, D.J.1    Barron, A.B.2    Robinson, G.E.3
  • 258
    • 0026095585 scopus 로고
    • Molecular cloning of an invertebrate glutamate receptor subunit expression in Drosophila muscle
    • Schuster C.M., Ultsch A., Schloss P., Cox J.A., Schmitt B., et al. Molecular cloning of an invertebrate glutamate receptor subunit expression in Drosophila muscle. Science 1991, 254:112-114.
    • (1991) Science , vol.254 , pp. 112-114
    • Schuster, C.M.1    Ultsch, A.2    Schloss, P.3    Cox, J.A.4    Schmitt, B.5
  • 259
    • 0032925862 scopus 로고    scopus 로고
    • Excitatory amino acid transporters: a family in flux
    • Seal R.P., Amara S. Excitatory amino acid transporters: a family in flux. Annu. Rev. Pharmacol. Toxicol. 1999, 39:431-456.
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 431-456
    • Seal, R.P.1    Amara, S.2
  • 260
    • 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., Amara S. Identification and characterization of a cDNA encoding a neuronal glutamate transporter from Drosophila melanogaster. Recept. Channels 1998, 6:51-64.
    • (1998) Recept. Channels , vol.6 , pp. 51-64
    • Seal, R.P.1    Daniels, G.M.2    Wolfgang, W.J.3    Forte, M.4    Amara, S.5
  • 261
    • 0002248054 scopus 로고    scopus 로고
    • Lysinuric protein intolerance and other cationic amino acidurias
    • McGraw-Hill, New York, C.R. Scriver, S.W. Beaudet (Eds.)
    • Simell O. Lysinuric protein intolerance and other cationic amino acidurias. Metabolic and Molecular Bases of Inherited Diseases 2001, 4933-4956. McGraw-Hill, New York. C.R. Scriver, S.W. Beaudet (Eds.).
    • (2001) Metabolic and Molecular Bases of Inherited Diseases , pp. 4933-4956
    • Simell, O.1
  • 262
    • 0028299687 scopus 로고
    • Octopamine-like immunoreactivity in the dorsal unpaired median (Dum) neurons innervating the accessory-gland of the male cockroach Periplaneta-Americana
    • Sinakevitch I.G., Geffard M., Pelhate M., Lapied B. Octopamine-like immunoreactivity in the dorsal unpaired median (Dum) neurons innervating the accessory-gland of the male cockroach Periplaneta-Americana. Cell Tiss. Res. 1994, 276:15-21.
    • (1994) Cell Tiss. Res. , vol.276 , pp. 15-21
    • Sinakevitch, I.G.1    Geffard, M.2    Pelhate, M.3    Lapied, B.4
  • 264
  • 265
    • 0038028658 scopus 로고    scopus 로고
    • Hygienic behavior in the honey bee (Apis mellifera L.) and the modulatory role of octopamine
    • Spivak M., Masterman R., Ross R., Mesce K.A. Hygienic behavior in the honey bee (Apis mellifera L.) and the modulatory role of octopamine. J. Neurobiol. 2003, 55:341-354.
    • (2003) J. Neurobiol. , vol.55 , pp. 341-354
    • Spivak, M.1    Masterman, R.2    Ross, R.3    Mesce, K.A.4
  • 266
    • 0029144324 scopus 로고
    • The PTR family: a new group of peptide transporters
    • Steiner H.Y., Naider F., Becker J.M. The PTR family: a new group of peptide transporters. Mol. Microbiol. 1995, 16:825-834.
    • (1995) Mol. Microbiol. , vol.16 , pp. 825-834
    • Steiner, H.Y.1    Naider, F.2    Becker, J.M.3
  • 267
    • 0026920582 scopus 로고
    • Identification and characterization of inebriated, a gene affecting neuronal excitability in Drosophila
    • Stern M., Ganetzky B. Identification and characterization of inebriated, a gene affecting neuronal excitability in Drosophila. J. Neurogenet. 1992, 8:157-172.
    • (1992) J. Neurogenet. , vol.8 , pp. 157-172
    • Stern, M.1    Ganetzky, B.2
  • 268
    • 0036670202 scopus 로고    scopus 로고
    • Conserved tyrosine-147 plays a critical role in the ligand-gated current of the epithelial cation/amino acid transporter/channel CAATCH1
    • Stevens B.R., Feldman D.H., Liu Z., Harvey W.R. Conserved tyrosine-147 plays a critical role in the ligand-gated current of the epithelial cation/amino acid transporter/channel CAATCH1. J. Exp. Biol. 2002, 205:2545-2553.
    • (2002) J. Exp. Biol. , vol.205 , pp. 2545-2553
    • Stevens, B.R.1    Feldman, D.H.2    Liu, Z.3    Harvey, W.R.4
  • 269
    • 0033103189 scopus 로고    scopus 로고
    • From fruit flies to barnacles, histamine is the neurotransmitter of arthropod photoreceptors
    • Stuart A.E. From fruit flies to barnacles, histamine is the neurotransmitter of arthropod photoreceptors. Neuron 1999, 22:431-433.
    • (1999) Neuron , vol.22 , pp. 431-433
    • Stuart, A.E.1
  • 270
    • 0037316679 scopus 로고    scopus 로고
    • The 'glial' glutamate transporter, EAAT2 (Glt-1) accounts for high affinity glutamate uptake into adult rodent nerve endings
    • Suchak S.K., Baloyianni N.V., Perkinton M.S., Williams R.J., Meldrum B.S., et al. The 'glial' glutamate transporter, EAAT2 (Glt-1) accounts for high affinity glutamate uptake into adult rodent nerve endings. J. Neurochem. 2003, 84:522-532.
    • (2003) J. Neurochem. , vol.84 , pp. 522-532
    • Suchak, S.K.1    Baloyianni, N.V.2    Perkinton, M.S.3    Williams, R.J.4    Meldrum, B.S.5
  • 271
    • 0026056119 scopus 로고
    • Phylogenetic studies on the synaptic vesicle glutamate transport system
    • Tabb J.S., Ueda T. Phylogenetic studies on the synaptic vesicle glutamate transport system. J. Neurosci. 1991, 11:1822-1828.
    • (1991) J. Neurosci. , vol.11 , pp. 1822-1828
    • Tabb, J.S.1    Ueda, T.2
  • 272
    • 0035891724 scopus 로고    scopus 로고
    • Identification of differentiation-associated brain-specific phosphate transporter as a second vesicular glutamate transporter (VGLUT2)
    • Takamori S., Rhee J.S., Rosenmund C., Jahn R. Identification of differentiation-associated brain-specific phosphate transporter as a second vesicular glutamate transporter (VGLUT2). J. Neurosci. 2001, 21:RC182.
    • (2001) J. Neurosci. , vol.21 , pp. RC182
    • Takamori, S.1    Rhee, J.S.2    Rosenmund, C.3    Jahn, R.4
  • 273
    • 0026500961 scopus 로고
    • Expression cloning of a Na(+)-independent neutral amino acid transporter from rat kidney
    • Tate S.S., Yan N., Udenfriend S. Expression cloning of a Na(+)-independent neutral amino acid transporter from rat kidney. Proc. Natl Acad. Sci. USA 1992, 89:1-5.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 1-5
    • Tate, S.S.1    Yan, N.2    Udenfriend, S.3
  • 274
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 275
    • 0042866085 scopus 로고    scopus 로고
    • Expression and regulation of L-cystine transporter, system x(c) (-), in the newly developed rat retinal Muller cell line (TR-MUL)
    • Tomi M., Funaki T., Abukawa H., Katayama K., Kondo T., et al. Expression and regulation of L-cystine transporter, system x(c) (-), in the newly developed rat retinal Muller cell line (TR-MUL). Glia 2003, 43:208-217.
    • (2003) Glia , vol.43 , pp. 208-217
    • Tomi, M.1    Funaki, T.2    Abukawa, H.3    Katayama, K.4    Kondo, T.5
  • 276
    • 0028881522 scopus 로고
    • +/dipeptide cotransporter and distribution of the transport activity in isolated rabbit intestinal epithelial cells
    • +/dipeptide cotransporter and distribution of the transport activity in isolated rabbit intestinal epithelial cells. J. Pharmacol. Exp. Ther. 1995, 272:63-69.
    • (1995) J. Pharmacol. Exp. Ther. , vol.272 , pp. 63-69
    • Tomita, Y.1    Takano, M.2    Yasuhara, M.3    Hori, R.4    Inui, K.I.5
  • 277
    • 0037264650 scopus 로고    scopus 로고
    • Plasma membrane monoamine transporters: structure, regulation and function
    • Torres G.E., Gainetdinov R.R., Caron M.G. Plasma membrane monoamine transporters: structure, regulation and function. Nat. Rev. Neurosci. 2003, 4:13-25.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 13-25
    • Torres, G.E.1    Gainetdinov, R.R.2    Caron, M.G.3
  • 278
    • 0035827612 scopus 로고    scopus 로고
    • Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to RhoGTPase signaling
    • Toure A., Morin L., Pineau C., Becq F., Dorseuil O., et al. Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to RhoGTPase signaling. J. Biol. Chem. 2001, 276:20309-20315.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20309-20315
    • Toure, A.1    Morin, L.2    Pineau, C.3    Becq, F.4    Dorseuil, O.5
  • 279
    • 0038235586 scopus 로고    scopus 로고
    • Functional characterization of a glutamate/aspartate transporter from the mosquito Aedes aegypti
    • Umesh A., Cohen B.N., Ross L.S., Gill S.S. Functional characterization of a glutamate/aspartate transporter from the mosquito Aedes aegypti. J. Exp. Biol. 2003, 206:2241-2255.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2241-2255
    • Umesh, A.1    Cohen, B.N.2    Ross, L.S.3    Gill, S.S.4
  • 280
    • 0037043141 scopus 로고    scopus 로고
    • Immunocytochemical localization of a Manduca sexta gamma-aminobutyric acid transporter
    • Umesh A., Gill S.S. Immunocytochemical localization of a Manduca sexta gamma-aminobutyric acid transporter. J. Comp. Neurol. 2002, 448:388-398.
    • (2002) J. Comp. Neurol. , vol.448 , pp. 388-398
    • Umesh, A.1    Gill, S.S.2
  • 283
    • 0036140131 scopus 로고    scopus 로고
    • +/P-I transporter as a novel vesicular glutamate transporter expressed in a distinct set of glutamatergic synapses
    • +/P-I transporter as a novel vesicular glutamate transporter expressed in a distinct set of glutamatergic synapses. J. Neurosci. 2002, 22:142-155.
    • (2002) J. Neurosci. , vol.22 , pp. 142-155
    • Varoqui, H.1    Schafer, M.K.H.2    Zhu, H.M.3    Weihe, E.4    Erickson, J.D.5
  • 284
    • 0036140131 scopus 로고    scopus 로고
    • +/PI transporter as a novel vesicular glutamate transporter expressed in a distinct set of glutamatergic synapses
    • +/PI transporter as a novel vesicular glutamate transporter expressed in a distinct set of glutamatergic synapses. J. Neurosci. 2002, 22:142-155.
    • (2002) J. Neurosci. , vol.22 , pp. 142-155
    • Varoqui, H.1    Schafer, M.K.2    Zhu, H.3    Weihe, E.4    Erickson, J.D.5
  • 286
    • 0041562743 scopus 로고    scopus 로고
    • Molecular and functional characterisation of the zebrafish (Danio rerio) PEPT1-type peptide transporter
    • Verri T., Kottra G., Romano A., Tiso N., Peric M., et al. Molecular and functional characterisation of the zebrafish (Danio rerio) PEPT1-type peptide transporter. FEBS Lett. 2003, 549:115-122.
    • (2003) FEBS Lett. , vol.549 , pp. 115-122
    • Verri, T.1    Kottra, G.2    Romano, A.3    Tiso, N.4    Peric, M.5
  • 287
    • 0034176259 scopus 로고    scopus 로고
    • Substrate selectivity and pH dependence of KAAT1 expressed in Xenopus laevis oocytes
    • Vincenti S., Castagna M., Peres A., Sacchi V.F. Substrate selectivity and pH dependence of KAAT1 expressed in Xenopus laevis oocytes. J. Membr. Biol. 2000, 174:213-224.
    • (2000) J. Membr. Biol. , vol.174 , pp. 213-224
    • Vincenti, S.1    Castagna, M.2    Peres, A.3    Sacchi, V.F.4
  • 288
    • 0037646994 scopus 로고    scopus 로고
    • Molecular and functional characterization of SLC26A11, a sodium-independent sulfate transporter from high endothelial venules
    • Vincourt J.B., Jullien D., Amalric F., Girard J.P. Molecular and functional characterization of SLC26A11, a sodium-independent sulfate transporter from high endothelial venules. FASEB J. 2003, 17:890-892.
    • (2003) FASEB J. , vol.17 , pp. 890-892
    • Vincourt, J.B.1    Jullien, D.2    Amalric, F.3    Girard, J.P.4
  • 289
    • 0038239858 scopus 로고    scopus 로고
    • Expression of the activity of cystine/glutamate exchange transporter, system x(c) (-), by xCT and rBAT
    • Wang H.Y., Tamba M., Kimata M., Sakamoto K., Bannai S., et al. Expression of the activity of cystine/glutamate exchange transporter, system x(c) (-), by xCT and rBAT. Biochem. Biophys. Res. Commun. 2003, 305:611-618.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 611-618
    • Wang, H.Y.1    Tamba, M.2    Kimata, M.3    Sakamoto, K.4    Bannai, S.5
  • 290
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 angstrom resolution: structural characterization of proline-substitution sites for protein thermostabilization
    • Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 angstrom resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol. 1997, 269:142-153.
    • (1997) J. Mol. Biol. , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 291
    • 0036467656 scopus 로고    scopus 로고
    • Synaptic structure, distribution, and circuitry in the central nervous system of the locust and related insects
    • Watson A.H.D., Schurmann F.-W. Synaptic structure, distribution, and circuitry in the central nervous system of the locust and related insects. Microsc. Res. Tech. 2002, 56:210-226.
    • (2002) Microsc. Res. Tech. , vol.56 , pp. 210-226
    • Watson, A.H.D.1    Schurmann, F.-W.2
  • 292
    • 0026755231 scopus 로고
    • Cloning of a rat kidney cDNA that stimulates dibasic and neutral amino acid transport and has sequence similarity to glucosidases
    • Wells R.G., Hediger M.A. Cloning of a rat kidney cDNA that stimulates dibasic and neutral amino acid transport and has sequence similarity to glucosidases. Proc. Natl Acad. Sci. USA 1992, 89:5596-5600.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5596-5600
    • Wells, R.G.1    Hediger, M.A.2
  • 293
    • 0025942998 scopus 로고
    • Cloning and expression of cDNA for a Na/Pi cotransport system of kidney cortex
    • Werner A., Moore M.L., Mantei N., Biber J., Semenza G., et al. Cloning and expression of cDNA for a Na/Pi cotransport system of kidney cortex. Proc. Natl Acad. Sci. USA 1991, 88:9608-9612.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9608-9612
    • Werner, A.1    Moore, M.L.2    Mantei, N.3    Biber, J.4    Semenza, G.5
  • 297
    • 0024962175 scopus 로고
    • A vacuolar-type proton pump in a vesicle fraction enriched with potassium transporting plasma membranes from tobacco hornworm midgut
    • Wieczorek H., Weerth S., Schindlbeck M., Klein U. A vacuolar-type proton pump in a vesicle fraction enriched with potassium transporting plasma membranes from tobacco hornworm midgut. J. Biol. Chem. 1989, 264:11143-11148.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11143-11148
    • Wieczorek, H.1    Weerth, S.2    Schindlbeck, M.3    Klein, U.4
  • 298
    • 7144253117 scopus 로고    scopus 로고
    • Lactic acid efflux from white skeletal muscle is catalyzed by the monocarboxylate transporter isoform MCT3
    • Wilson M.C., Jackson V.N., Heddle C., Price N.T., Pilegaard H., et al. Lactic acid efflux from white skeletal muscle is catalyzed by the monocarboxylate transporter isoform MCT3. J. Biol. Chem. 1998, 273:15920-15926.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15920-15926
    • Wilson, M.C.1    Jackson, V.N.2    Heddle, C.3    Price, N.T.4    Pilegaard, H.5
  • 299
    • 0036479231 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer studies on the interaction between the lactate transporter MCT1 and CD147 provide information on the topology and stoichiometry of the complex in situ
    • Wilson M.C., Meredith D., Halestrap A.P. Fluorescence resonance energy transfer studies on the interaction between the lactate transporter MCT1 and CD147 provide information on the topology and stoichiometry of the complex in situ. J. Biol. Chem. 2002, 277:3666-3672.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3666-3672
    • Wilson, M.C.1    Meredith, D.2    Halestrap, A.P.3
  • 300
    • 0036495003 scopus 로고    scopus 로고
    • Conservation of amino acid transporters in fungi, plants and animals
    • Wipf D., Ludewig U., Tegeder M., Rentsch D., Koch W., et al. Conservation of amino acid transporters in fungi, plants and animals. Trends Biochem. Sci. 2002, 27:139-147.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 139-147
    • Wipf, D.1    Ludewig, U.2    Tegeder, M.3    Rentsch, D.4    Koch, W.5
  • 301
    • 0036828359 scopus 로고    scopus 로고
    • Putative histamine-gated chloride channel subunits of the insect visual system and thoracic ganglion
    • Witte I., Kreienkamp H.-J., Gewecke M., Roeder T. Putative histamine-gated chloride channel subunits of the insect visual system and thoracic ganglion. J. Neurochem. 2002, 83:504-514.
    • (2002) J. Neurochem. , vol.83 , pp. 504-514
    • Witte, I.1    Kreienkamp, H.-J.2    Gewecke, M.3    Roeder, T.4
  • 302
    • 0037097030 scopus 로고    scopus 로고
    • Expression of solute carrier 7A4 (SLC7A4) in the plasma membrane is not sufficient to mediate amino acid transport activity
    • Wolf S., Janzen A., Vekony N., Martine U., Strand D., et al. Expression of solute carrier 7A4 (SLC7A4) in the plasma membrane is not sufficient to mediate amino acid transport activity. Biochem. J. 2002, 364:767-775.
    • (2002) Biochem. J. , vol.364 , pp. 767-775
    • Wolf, S.1    Janzen, A.2    Vekony, N.3    Martine, U.4    Strand, D.5
  • 303
    • 0034070706 scopus 로고    scopus 로고
    • Amino acid transport in insects
    • Wolfersberger M.G. Amino acid transport in insects. Annu. Rev. Entomol. 2000, 45:111-120.
    • (2000) Annu. Rev. Entomol. , vol.45 , pp. 111-120
    • Wolfersberger, M.G.1
  • 304
    • 0037263730 scopus 로고    scopus 로고
    • Epidermal growth factor activation of intestinal glutamine transport is mediated by mitogen-activated protein kinases
    • Wolfgang C.L., Lin C., Meng Q., Karinch A.M., Vary T.C., et al. Epidermal growth factor activation of intestinal glutamine transport is mediated by mitogen-activated protein kinases. J. Gastrointest. Surg. 2003, 7:149-156.
    • (2003) J. Gastrointest. Surg. , vol.7 , pp. 149-156
    • Wolfgang, C.L.1    Lin, C.2    Meng, Q.3    Karinch, A.M.4    Vary, T.C.5
  • 305
    • 0028500550 scopus 로고
    • Anomalous glutamate/alkali cation symport in larval Manduca sexta midgut
    • Xie T., Parthasarathy R., Wolfersberger M.G., Harvey W.R. Anomalous glutamate/alkali cation symport in larval Manduca sexta midgut. J. Exp. Biol. 1994, 194:181-194.
    • (1994) J. Exp. Biol. , vol.194 , pp. 181-194
    • Xie, T.1    Parthasarathy, R.2    Wolfersberger, M.G.3    Harvey, W.R.4
  • 306
    • 0030892082 scopus 로고    scopus 로고
    • Cloning and functional expression of a brain peptide/histidine transporter
    • Yamashita T., Shimada S., Guo W., Sato K., Kohmura E., et al. Cloning and functional expression of a brain peptide/histidine transporter. J. Biol. Chem. 1997, 272:10205-10211.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10205-10211
    • Yamashita, T.1    Shimada, S.2    Guo, W.3    Sato, K.4    Kohmura, E.5
  • 307
    • 0037041294 scopus 로고    scopus 로고
    • Synaptic organization of the mushroom body calyx in Drosophila melanogaster
    • Yasuyama K., Meinertzhagen I.A., Schurmann F.W. Synaptic organization of the mushroom body calyx in Drosophila melanogaster. J. Comp. Neurol. 2002, 445:211-226.
    • (2002) J. Comp. Neurol. , vol.445 , pp. 211-226
    • Yasuyama, K.1    Meinertzhagen, I.A.2    Schurmann, F.W.3
  • 308
    • 0029583203 scopus 로고
    • The pharmacological profile of the vesicular monoamine transporter resembles that of multidrug transporters
    • Yelin R., Schuldiner S. The pharmacological profile of the vesicular monoamine transporter resembles that of multidrug transporters. FEBS Lett. 1995, 377:201-207.
    • (1995) FEBS Lett. , vol.377 , pp. 201-207
    • Yelin, R.1    Schuldiner, S.2
  • 310
    • 0030993370 scopus 로고    scopus 로고
    • Conserved and sexually dimorphic behavioral responses to biogenic amines in decapitated Drosophila
    • Yellman C., Tao H., He B., Hirsh J. Conserved and sexually dimorphic behavioral responses to biogenic amines in decapitated Drosophila. Proc. Natl Acad. Sci. USA 1997, 94:4131-4136.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4131-4136
    • Yellman, C.1    Tao, H.2    He, B.3    Hirsh, J.4
  • 311
    • 0030982108 scopus 로고    scopus 로고
    • Identification of a unique monocarboxylate transporter (MCT3) in retinal pigment epithelium
    • Yoon H.Y., Fanelli A., Grollman E.F., Philp N.J. Identification of a unique monocarboxylate transporter (MCT3) in retinal pigment epithelium. Biochem. Biophys. Res. Commun. 1997, 234:90-94.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 90-94
    • Yoon, H.Y.1    Fanelli, A.2    Grollman, E.F.3    Philp, N.J.4
  • 313
    • 0035140273 scopus 로고    scopus 로고
    • Expression and distribution of lactate/monocarboxylate transporter isoforms in pancreatic islets and the exocrine pancreas
    • Zhao C., Wilson M.C., Schuit F., Halestrap A.P., Rutter G.A. Expression and distribution of lactate/monocarboxylate transporter isoforms in pancreatic islets and the exocrine pancreas. Diabetes 2001, 50:361-366.
    • (2001) Diabetes , vol.50 , pp. 361-366
    • Zhao, C.1    Wilson, M.C.2    Schuit, F.3    Halestrap, A.P.4    Rutter, G.A.5
  • 315
    • 0033200321 scopus 로고    scopus 로고
    • Antibody to H(+) V-ATPase subunit E colocalizes with portasomes in alkaline larval midgut of a freshwater mosquito (Aedes aegypti)
    • Zhuang Z., Linser P.J., Harvey W.R. Antibody to H(+) V-ATPase subunit E colocalizes with portasomes in alkaline larval midgut of a freshwater mosquito (Aedes aegypti). J. Exp. Biol. 1999, 202:2449-2460.
    • (1999) J. Exp. Biol. , vol.202 , pp. 2449-2460
    • Zhuang, Z.1    Linser, P.J.2    Harvey, W.R.3
  • 316
    • 85069925611 scopus 로고    scopus 로고
    • - Proteome Bio Tuat
    • - Proteome Bio Tuat. http://sosui.proteome.bio.tuat.ac.jp.
  • 317
    • 85069942137 scopus 로고    scopus 로고
    • - NCBI
    • - NCBI. http://www.ncbi.nlm.nih.gov.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.