메뉴 건너뛰기




Volumn 63, Issue 2, 1999, Pages 293-307

Structural features of the glutamate transporter family

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; ION CHANNEL; NEUROTRANSMITTER;

EID: 0033032413     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/mmbr.63.2.293-307.1999     Document Type: Review
Times cited : (133)

References (116)
  • 2
    • 0027980858 scopus 로고
    • Counter-transport of potassium by the glutamate uptake carrier in glial cells isolated from the tiger salamander retina
    • London
    • Amato, A., B. Barbour, M. Szatkowski, and D. Attwell. 1994. Counter-transport of potassium by the glutamate uptake carrier in glial cells isolated from the tiger salamander retina. J. Physiol. (London) 479:371-380.
    • (1994) J. Physiol. , vol.479 , pp. 371-380
    • Amato, A.1    Barbour, B.2    Szatkowski, M.3    Attwell, D.4
  • 3
    • 0030932152 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance
    • Arriza, J. L., S. Eliasof, M. P. Kavanaugh, and S. G. Amara. 1997. Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance. Proc. Natl. Acad. Sci. USA 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
  • 4
    • 0028031487 scopus 로고
    • Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex
    • Arriza, J. L., W. A. Fairman, J. I. Wadiche, G. H. Murdoch, M. P. Kavanaugh, and S. G. Amara. 1994. Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. J. Neurosci. 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    Amara, S.G.6
  • 5
    • 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., M. P. Kavanaugh, W. A. Fairman, Y. N. Wu, G. H. Murdoch, R. A. North, and S. G. Amara. 1993. Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J. Biol. Chem. 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    North, R.A.6    Amara, S.G.7
  • 6
    • 0030474917 scopus 로고    scopus 로고
    • Utilization of orotate as a pyrimidine source by Salmonella typhimurium and Escherichia coli requires the dicarboxylate transport protein encoded by dctA
    • Baker, K. E., K. P. Ditullio, J. Neuhard, and R. A. Kelln. 1996. Utilization of orotate as a pyrimidine source by Salmonella typhimurium and Escherichia coli requires the dicarboxylate transport protein encoded by dctA. J. Bacteriol. 178:7099-7105.
    • (1996) J. Bacteriol. , vol.178 , pp. 7099-7105
    • Baker, K.E.1    Ditullio, K.P.2    Neuhard, J.3    Kelln, R.A.4
  • 7
    • 0023678757 scopus 로고
    • Electrogenic glutamate uptake in glial cells is activated by intracellular potassium
    • Barbour, B., H. Brew, and D. Attwell. 1988. Electrogenic glutamate uptake in glial cells is activated by intracellular potassium. Nature 335:433-435.
    • (1988) Nature , vol.335 , pp. 433-435
    • Barbour, B.1    Brew, H.2    Attwell, D.3
  • 8
    • 0029973191 scopus 로고    scopus 로고
    • Anion conductance behavior of the glutamate uptake carrier in salamander retinal glial cells
    • Billups, B., D. Rossi, and D. Attwell. 1996. Anion conductance behavior of the glutamate uptake carrier in salamander retinal glial cells. J. Neurosci. 16:6722-6731.
    • (1996) J. Neurosci. , vol.16 , pp. 6722-6731
    • Billups, B.1    Rossi, D.2    Attwell, D.3
  • 9
    • 85069241381 scopus 로고    scopus 로고
    • BLAST Website. 30 November
    • BLAST Website. 30 November 1998, revision date. [Online.] http://www .ncbi.nlm.nih.gov/BLAST. [30 November 1998, last date accessed.]
    • (1998)
  • 10
    • 0028341707 scopus 로고
    • A conformationally constrained competitive inhibitor of the sodium-dependent glutamate transporter in forebrain synaptosomes: L-anti-endo-3,4-methanopyrrolidine dicarboxylate
    • Bridges, R. J., F. E. Lovering, H. Koch, C. W. Cotman, and A. R. Chamberlin. 1994. A conformationally constrained competitive inhibitor of the sodium-dependent glutamate transporter in forebrain synaptosomes: L-anti-endo-3,4-methanopyrrolidine dicarboxylate. Neurosci. Lett. 174:193-197.
    • (1994) Neurosci. Lett. , vol.174 , pp. 193-197
    • Bridges, R.J.1    Lovering, F.E.2    Koch, H.3    Cotman, C.W.4    Chamberlin, A.R.5
  • 11
    • 0026080845 scopus 로고
    • Conformationally defined neurotransmitter analogues. Selective inhibition of glutamate uptake by one pyrrolidine-2,4-dicarboxylate diastereomer
    • Bridges, R. J., M. S. Stanley, M. W. Anderson, C. W. Cotman, and A. R. Chamberlin. 1991. Conformationally defined neurotransmitter analogues. Selective inhibition of glutamate uptake by one pyrrolidine-2,4-dicarboxylate diastereomer. J. Med. Chem. 34:717-725.
    • (1991) J. Med. Chem. , vol.34 , pp. 717-725
    • Bridges, R.J.1    Stanley, M.S.2    Anderson, M.W.3    Cotman, C.W.4    Chamberlin, A.R.5
  • 12
    • 0030960637 scopus 로고    scopus 로고
    • Abolition of substrate-dependent currents by tyrosine mutation in the transmembrane domain of glutamate transporter
    • Choi, I., and S. Y. Chiu. 1997. Abolition of substrate-dependent currents by tyrosine mutation in the transmembrane domain of glutamate transporter. FEBS Lett. 405:133-136.
    • (1997) FEBS Lett. , vol.405 , pp. 133-136
    • Choi, I.1    Chiu, S.Y.2
  • 13
    • 0028846037 scopus 로고
    • Functional analysis of the high affinity, Na(+)-dependent glutamate transporter GLAST-1 by site-directed mutagenesis
    • Conradt, M., and W. Stoffel. 1995. Functional analysis of the high affinity, Na(+)-dependent glutamate transporter GLAST-1 by site-directed mutagenesis. J. Biol. Chem. 270:25207-25212.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25207-25212
    • Conradt, M.1    Stoffel, W.2
  • 14
    • 85047690143 scopus 로고
    • Localization of N-glycosylation sites and functional role of the carbohydrate units of GLAST-1, a cloned rat brain L-glutamate/L-aspartate transporter
    • Conradt, M., T. Storck, and W. Stoffel. 1995. Localization of N-glycosylation sites and functional role of the carbohydrate units of GLAST-1, a cloned rat brain L-glutamate/L-aspartate transporter. Eur. J. Biochem. 229: 682-687.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 682-687
    • Conradt, M.1    Storck, T.2    Stoffel, W.3
  • 16
    • 0025316950 scopus 로고
    • Purification and reconstitution of the sodium- and potassium-coupled glutamate transport glycoprotein from rat brain
    • Danbolt, N. C., G. Pines, and B. I. Kanner. 1990. Purification and reconstitution of the sodium- and potassium-coupled glutamate transport glycoprotein from rat brain. Biochemistry 29:6734-6740.
    • (1990) Biochemistry , vol.29 , pp. 6734-6740
    • Danbolt, N.C.1    Pines, G.2    Kanner, B.I.3
  • 19
    • 0027497369 scopus 로고
    • Modeling alpha-helical transmembrane domains: The calculation and use of substitution tables for lipid-facing residues
    • Donnelly, D., J. P. Overington, S. V. Ruffle, J. H. Nugent, and T. L. Blundell. 1993. Modeling alpha-helical transmembrane domains: the calculation and use of substitution tables for lipid-facing residues. Protein Sci. 2:55-70.
    • (1993) Protein Sci. , vol.2 , pp. 55-70
    • Donnelly, D.1    Overington, J.P.2    Ruffle, S.V.3    Nugent, J.H.4    Blundell, T.L.5
  • 21
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. 1984. Three-dimensional structure of membrane and surface proteins. Annu. Rev. Biochem. 53:595-623.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 22
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg, D., R. M. Weiss, and T. C. Terwilliger. 1984. The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. USA 81:140-144.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 23
    • 0031972667 scopus 로고    scopus 로고
    • Excitatory amino acid transporters of the salamander retina: Identification, localization, and function
    • Eliasof, S., J. L. Arriza, B. H. Leighton, M. P. Kavanaugh, and S. G. Amara. 1998. Excitatory amino acid transporters of the salamander retina: identification, localization, and function. J. Neurosci. 18:698-712.
    • (1998) J. Neurosci. , vol.18 , pp. 698-712
    • Eliasof, S.1    Arriza, J.L.2    Leighton, B.H.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 25
    • 0020528956 scopus 로고
    • Aspartate transport in synaptosomes from rat brain
    • Erecinska, M., D. Wantorsky, and D. F. Wilson. 1983. Aspartate transport in synaptosomes from rat brain. J. Biol. Chem. 258:9069-9077.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9069-9077
    • Erecinska, M.1    Wantorsky, D.2    Wilson, D.F.3
  • 27
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • Fairman, W. A., R. J. Vandenberg, J. L. Arriza, M. P. Kavanaugh, and S. G. Amara. 1995. An excitatory amino-acid transporter with properties of a ligand-gated chloride channel. Nature 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
  • 28
    • 0003437299 scopus 로고
    • Distributed by the author. Department of Genetics, University of Washington, Seattle
    • Felsenstein, J. 1993. PHYLIP (Phylogeny Inference Package) version 3.5c. Distributed by the author. Department of Genetics, University of Washington, Seattle.
    • (1993) PHYLIP (Phylogeny Inference Package) Version 3.5c
    • Felsenstein, J.1
  • 29
    • 0024058612 scopus 로고
    • Mutants of Rhizobium meliloti defective in succinate metabolism
    • Finan, T. M., I. Oresnik, and A. Bottacin. 1988. Mutants of Rhizobium meliloti defective in succinate metabolism. J. Bacteriol. 170:3396-3403.
    • (1988) J. Bacteriol. , vol.170 , pp. 3396-3403
    • Finan, T.M.1    Oresnik, I.2    Bottacin, A.3
  • 30
    • 0019835657 scopus 로고
    • Succinate transport in Rhizobium leguminosarum
    • Finan, T. M., J. M. Wood, and D. C. Jordan. 1981. Succinate transport in Rhizobium leguminosarum. J. Bacteriol. 148:193-202.
    • (1981) J. Bacteriol. , vol.148 , pp. 193-202
    • Finan, T.M.1    Wood, J.M.2    Jordan, D.C.3
  • 31
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure function relationships in polytopic membrane proteins
    • Frillingos, S., M. Sahin-Toth, J. Wu, and H. R. Kaback. 1998. Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins. FASEB J. 12:1281-1299.
    • (1998) FASEB J. , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 32
    • 0029869003 scopus 로고    scopus 로고
    • Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus
    • Gaillard, I., D. J. Slotboom, J. Knol, J. S. Lolkema, and W. N. Konings. 1996. Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus. Biochemistry 35:6150-6156.
    • (1996) Biochemistry , vol.35 , pp. 6150-6156
    • Gaillard, I.1    Slotboom, D.J.2    Knol, J.3    Lolkema, J.S.4    Konings, W.N.5
  • 33
    • 0032169137 scopus 로고    scopus 로고
    • Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology
    • Grunewald, M., A. Bendahan, and B. I. Kanner. 1998. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Neuron 21:623-632.
    • (1998) Neuron , vol.21 , pp. 623-632
    • Grunewald, M.1    Bendahan, A.2    Kanner, B.I.3
  • 34
    • 0029041792 scopus 로고
    • Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states
    • Grunewald, M., and B. Kanner. 1995. Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states. J. Biol. Chem. 270:17017-17024.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17017-17024
    • Grunewald, M.1    Kanner, B.2
  • 35
    • 0026020593 scopus 로고
    • Sodium ion-dependent amino acid transport in membrane vesicles of Bacillus stearothermophilus
    • Heyne, R. I., W. de Vrij, W. Crielaard, and W. N. Konings. 1991. Sodium ion-dependent amino acid transport in membrane vesicles of Bacillus stearothermophilus. J. Bacteriol. 173:791-800.
    • (1991) J. Bacteriol. , vol.173 , pp. 791-800
    • Heyne, R.I.1    De Vrij, W.2    Crielaard, W.3    Konings, W.N.4
  • 36
    • 0027451724 scopus 로고
    • 4-dicarboxylate permease (DctA) as derived from protein fusions with Escherichia coli K12 alkaline phosphatase (PhoA) and beta-galactosidase (LacZ)
    • 4-dicarboxylate permease (DctA) as derived from protein fusions with Escherichia coli K12 alkaline phosphatase (PhoA) and beta-galactosidase (LacZ). Mol. Gen. Genet. 241:106-114.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 106-114
    • Jording, D.1    Puhler, A.2
  • 37
    • 0031398840 scopus 로고    scopus 로고
    • From membrane to molecule to the third amino acid from the left with a membrane transport protein
    • Kaback, H. R., and J. Wu. 1997. From membrane to molecule to the third amino acid from the left with a membrane transport protein. Q. Rev. Biophys. 30:333-364.
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 333-364
    • Kaback, H.R.1    Wu, J.2
  • 38
    • 0030858918 scopus 로고    scopus 로고
    • Family of neutral and acidic amino acid transporters: Molecular biology, physiology and medical implications
    • Kanai, Y. 1997. Family of neutral and acidic amino acid transporters: molecular biology, physiology and medical implications. Curr. Opin. Cell Biol. 9:565-572.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 565-572
    • Kanai, Y.1
  • 39
    • 0026458124 scopus 로고
    • Primary structure and functional characterization of a high-affinity glutamate transporter
    • Kanai, Y., and M. A. Hediger. 1992. Primary structure and functional characterization of a high-affinity glutamate transporter. Nature 360:467-471.
    • (1992) Nature , vol.360 , pp. 467-471
    • Kanai, Y.1    Hediger, M.A.2
  • 40
    • 0029035583 scopus 로고
    • Electrogenic properties of the epithelial and neuronal high affinity glutamate transporter
    • Kanai, Y., S. Nussberger, M. F. Romero, W. F. Boron, S. C. Hebert, and M. A. Hediger. 1995. Electrogenic properties of the epithelial and neuronal high affinity glutamate transporter. J. Biol. Chem. 270:16561-16568.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16561-16568
    • Kanai, Y.1    Nussberger, S.2    Romero, M.F.3    Boron, W.F.4    Hebert, S.C.5    Hediger, M.A.6
  • 41
    • 0027136017 scopus 로고
    • A new family of neurotransmitter transporters: The high-affinity glutamate transporters
    • Kanai, Y., C. P. Smith, and M. A. Hediger. 1993. A new family of neurotransmitter transporters: the high-affinity glutamate transporters. FASEB J. 7:1450-1459.
    • (1993) FASEB J. , vol.7 , pp. 1450-1459
    • Kanai, Y.1    Smith, C.P.2    Hediger, M.A.3
  • 42
    • 0344157756 scopus 로고    scopus 로고
    • Chimera analysis of glutamate transporter EAAC1 and GLT-1: A search for substrate binding sites
    • Kanai, Y., N. Utsunomiya-Tate, and H. Endou. 1998. Chimera analysis of glutamate transporter EAAC1 and GLT-1: a search for substrate binding sites. Soc. Neurosci. Abstr. 23:1485.
    • (1998) Soc. Neurosci. Abstr. , vol.23 , pp. 1485
    • Kanai, Y.1    Utsunomiya-Tate, N.2    Endou, H.3
  • 43
    • 0020448447 scopus 로고
    • Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain
    • Kanner, B. I., and A. Bendahan. 1982. Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain. Biochemistry 21:6327-6330.
    • (1982) Biochemistry , vol.21 , pp. 6327-6330
    • Kanner, B.I.1    Bendahan, A.2
  • 44
    • 0018132541 scopus 로고
    • Active transport of L-glutamate by membrane vesicles isolated from rat brain
    • Kanner, B. I., and I. Sharon. 1978. Active transport of L-glutamate by membrane vesicles isolated from rat brain. Biochemistry 17:3949-3953.
    • (1978) Biochemistry , vol.17 , pp. 3949-3953
    • Kanner, B.I.1    Sharon, I.2
  • 45
    • 0031028206 scopus 로고    scopus 로고
    • Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange
    • Kavanaugh, M. P., A. Bendahan, N. Zerangue, Y. Zhang, and B. I. Kanner. 1997. Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange. J. Biol. Chem. 272:1703-1708.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1703-1708
    • Kavanaugh, M.P.1    Bendahan, A.2    Zerangue, N.3    Zhang, Y.4    Kanner, B.I.5
  • 46
    • 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., P. D. Prasad, Y. J. Fei, V. Torres-Zamorano, S. Sinha, T. L. Yang-Feng, F. H. Leibach, and V. Ganapathy. 1996. Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line. J. Biol. Chem. 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    Yang-Feng, T.L.6    Leibach, F.H.7    Ganapathy, V.8
  • 48
    • 0027937049 scopus 로고
    • Functional properties and substrate specificity of the cloned L-glutamate/L-aspartate transporter GLAST-1 from rat brain expressed in Xenopus oocytes
    • Klockner, U., T. Storck, M. Conradt, and W. Stoffel. 1994. Functional properties and substrate specificity of the cloned L-glutamate/L-aspartate transporter GLAST-1 from rat brain expressed in Xenopus oocytes. J. Neurosci. 14:5759-5765.
    • (1994) J. Neurosci. , vol.14 , pp. 5759-5765
    • Storck, T.1    Conradt, M.2    Stoffel, W.3
  • 50
    • 0030808979 scopus 로고    scopus 로고
    • New beta-hydroxyaspartate derivatives are competitive blockers for the bovine glutamate/aspartate transporter
    • Lebrun, B., M. Sakaitani, K. Shimamoto, Y. Yasuda-Kamatani, and T. Nakajima. 1997. New beta-hydroxyaspartate derivatives are competitive blockers for the bovine glutamate/aspartate transporter. J. Biol. Chem. 272:20336-20339.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20336-20339
    • Lebrun, B.1    Sakaitani, M.2    Shimamoto, K.3    Yasuda-Kamatani, Y.4    Nakajima, T.5
  • 52
    • 0028933597 scopus 로고
    • Expression of a novel insulin-activated amino acid transporter gene during differentiation of 3T3-L1 preadipocytes into adipocytes
    • Liao, K., and M. D. Lane. 1995. Expression of a novel insulin-activated amino acid transporter gene during differentiation of 3T3-L1 preadipocytes into adipocytes. Biochem. Biophys. Res. Commun. 208:1008-1015.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 1008-1015
    • Liao, K.1    Lane, M.D.2
  • 53
    • 0032032013 scopus 로고    scopus 로고
    • Aberrant RNA processing in a neurodegenerative disease: The cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis
    • Lin, C. L., L. A. Bristol, L. Jin, M. Dykes-Hoberg, T. Crawford, L. Clawson, and J. D. Rothstein. 1998. Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. Neuron 20:589-602.
    • (1998) Neuron , vol.20 , pp. 589-602
    • Lin, C.L.1    Bristol, L.A.2    Jin, L.3    Dykes-Hoberg, M.4    Crawford, T.5    Clawson, L.6    Rothstein, J.D.7
  • 54
    • 0031920140 scopus 로고    scopus 로고
    • Estimation of structural similarity of membrane proteins by hydropathy profile alignment
    • Lolkema, J. S., and D. J. Slotboom. 1998. Estimation of structural similarity of membrane proteins by hydropathy profile alignment. Mol. Membr. Biol. 15:33-42.
    • (1998) Mol. Membr. Biol. , vol.15 , pp. 33-42
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 55
    • 0031765884 scopus 로고    scopus 로고
    • Hydropathy profile alignment. A tool to search for structural homologues of membrane proteins
    • Lolkema, J. S., and D. J. Slotboom. 1998. Hydropathy profile alignment. A tool to search for structural homologues of membrane proteins. FEMS Microbiol. Rev. 22:305-322.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 305-322
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 56
    • 0029012475 scopus 로고
    • Pore loops: An emerging theme in ion channel structure
    • MacKinnon, R. 1995. Pore loops: an emerging theme in ion channel structure. Neuron 14:889-892.
    • (1995) Neuron , vol.14 , pp. 889-892
    • MacKinnon, R.1
  • 57
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon, R., S. L. Cohen, A. Kuo, A. Lee, and B. T. Chait. 1998. Structural conservation in prokaryotic and eukaryotic potassium channels. Science 280:106-109.
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 58
    • 0025063609 scopus 로고
    • Excitatory amino acid neurotoxicity and neurodegenerative disease
    • Meldrum, B., and J. Garthwaite. 1990. Excitatory amino acid neurotoxicity and neurodegenerative disease. Trends Pharmacol. Sci. 11:379-387.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 379-387
    • Meldrum, B.1    Garthwaite, J.2
  • 59
    • 0028349645 scopus 로고
    • Glial contributions to excitatory neurotransmission in cultured hippocampal cells
    • Mennerick, S., and C. F. Zorumski. 1994. Glial contributions to excitatory neurotransmission in cultured hippocampal cells. Nature 368:59-62.
    • (1994) Nature , vol.368 , pp. 59-62
    • Mennerick, S.1    Zorumski, C.F.2
  • 60
    • 0032511029 scopus 로고    scopus 로고
    • Identification of functional domains of the human glutamate transporters EAAT1 and EAAT2
    • Mitrovic, A. D., S. G. Amara, G. A. Johnston, and R. J. Vandenberg. 1998. Identification of functional domains of the human glutamate transporters EAAT1 and EAAT2. J. Biol. Chem. 273:14698-14706.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14698-14706
    • Mitrovic, A.D.1    Amara, S.G.2    Johnston, G.A.3    Vandenberg, R.J.4
  • 61
    • 0025052336 scopus 로고
    • The release and uptake of excitatory amino acids
    • Nicholls, D., and D. Attwell. 1990. The release and uptake of excitatory amino acids. Trends. Pharmacol. Sci. 11:462-468.
    • (1990) Trends. Pharmacol. Sci. , vol.11 , pp. 462-468
    • Nicholls, D.1    Attwell, D.2
  • 62
    • 0032436625 scopus 로고    scopus 로고
    • +-coupled serine transporter from Escherichia coli and characteristics of the transporter
    • +-coupled serine transporter from Escherichia coli and characteristics of the transporter. J. Bacteriol. 180:6749-6752.
    • (1998) J. Bacteriol. , vol.180 , pp. 6749-6752
    • Ogawa, W.1    Kim, Y.M.2    Mizushima, T.3    Tsuchiya, T.4
  • 64
    • 0030761115 scopus 로고    scopus 로고
    • Postsynaptic glutamate transport at the climbing fiber-Purkinje cell synapse
    • Otis, T. S., M. P. Kavanaugh, and C. E. Jahr. 1997. Postsynaptic glutamate transport at the climbing fiber-Purkinje cell synapse. Science 277:1515-1518.
    • (1997) Science , vol.277 , pp. 1515-1518
    • Otis, T.S.1    Kavanaugh, M.P.2    Jahr, C.E.3
  • 66
    • 0032478498 scopus 로고    scopus 로고
    • Microbial genome analyses: Global comparisons of transport capabilities based on phytogenies, bioenergetics and substrate specificities
    • Paulsen, I. T., M. K. Sliwinski, and M. H. Saier, Jr. 1998. Microbial genome analyses: global comparisons of transport capabilities based on phytogenies, bioenergetics and substrate specificities. J. Mol. Biol. 277:573-592.
    • (1998) J. Mol. Biol. , vol.277 , pp. 573-592
    • Paulsen, I.T.1    Sliwinski, M.K.2    Saier M.H., Jr.3
  • 67
    • 0029077084 scopus 로고
    • Cone photoreceptors respond to their own glutamate release in the tiger salamander
    • Picaud, S., H. P. Larsson, D. P. Wellis, H. Lecar, and F. Werblin. 1995. Cone photoreceptors respond to their own glutamate release in the tiger salamander. Proc. Natl. Acad. Sci. USA 92:9417-9421.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9417-9421
    • Picaud, S.1    Larsson, H.P.2    Wellis, D.P.3    Lecar, H.4    Werblin, F.5
  • 69
    • 0025691629 scopus 로고
    • Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain
    • Pines, G., and B. I. Kanner. 1990. Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain. Biochemistry 29:11209-11214.
    • (1990) Biochemistry , vol.29 , pp. 11209-11214
    • Pines, G.1    Kanner, B.I.2
  • 70
  • 71
    • 0028239439 scopus 로고
    • A functional superfamily of sodium/solute symporters
    • Reizer, J., A. Reizer, and M. H. Saier, Jr. 1994. A functional superfamily of sodium/solute symporters. Biochim. Biophys. Acta 1197:133-166.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 133-166
    • Reizer, J.1    Reizer, A.2    Saier M.H., Jr.3
  • 73
    • 0028345374 scopus 로고
    • Computer-aided analyses of transport protein sequences: Gleaning evidence concerning function, structure, biogenesis, and evolution
    • Saier, M. H., Jr. 1994. Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution. Microbiol. Rev. 58:71-93.
    • (1994) Microbiol. Rev. , vol.58 , pp. 71-93
    • Saier M.H., Jr.1
  • 75
    • 0032434691 scopus 로고    scopus 로고
    • A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation
    • Seal, R. P., and S. G. Amara. 1998. A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation. Neuron 21:1487-1498.
    • (1998) Neuron , vol.21 , pp. 1487-1498
    • Seal, R.P.1    Amara, S.G.2
  • 78
    • 0029913959 scopus 로고    scopus 로고
    • Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family
    • Slotboom, D. J., J. S. Lolkema, and W. N. Konings. 1996. Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family. J. Biol. Chem. 271:31317-31321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31317-31321
    • Slotboom, D.J.1    Lolkema, J.S.2    Konings, W.N.3
  • 81
    • 0032518972 scopus 로고    scopus 로고
    • Modulation by zinc of the glutamate transporters in glial cells and cones isolated from the tiger salamander retina
    • London
    • Spiridon, M., D. Kamm, B. Billups, P. Mobbs, and D. Attwell. 1998. Modulation by zinc of the glutamate transporters in glial cells and cones isolated from the tiger salamander retina. J. Physiol. (London) 506:363-376.
    • (1998) J. Physiol. , vol.506 , pp. 363-376
    • Spiridon, M.1    Kamm, D.2    Billups, B.3    Mobbs, P.4    Attwell, D.5
  • 83
    • 0030001740 scopus 로고    scopus 로고
    • Expressed human hippocampal ASCT1 amino acid transporter exhibits a pH-dependent change in substrate specificity
    • Tamarappoo, B. K., K. K. McDonald, and M. S. Kilberg. 1996. Expressed human hippocampal ASCT1 amino acid transporter exhibits a pH-dependent change in substrate specificity. Biochim. Biophys. Acta 1279:131-136.
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 131-136
    • Tamarappoo, B.K.1    McDonald, K.K.2    Kilberg, M.S.3
  • 85
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 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
  • 86
    • 0026663307 scopus 로고
    • Characterization and functional expression in Escherichia coli of the sodium/proton/glutamate symport proteins of Bacillus stearothermophilus and Bacillus caldotenax
    • Tolner, B., B. Poolman, and W. N. Konings. 1992. Characterization and functional expression in Escherichia coli of the sodium/proton/glutamate symport proteins of Bacillus stearothermophilus and Bacillus caldotenax. Mol. Microbiol. 6:2845-2856.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2845-2856
    • Tolner, B.1    Poolman, B.2    Konings, W.N.3
  • 87
    • 0026602714 scopus 로고
    • Revised nucleotide sequence of the gltP gene, which encodes the proton-glutamate-aspartate transport protein of Escherichia coli K-12
    • Tolner, B., B. Poolman, B. Wallace, and W. N. Konings. 1992. Revised nucleotide sequence of the gltP gene, which encodes the proton-glutamate-aspartate transport protein of Escherichia coli K-12. J. Bacteriol. 174:2391-2393.
    • (1992) J. Bacteriol. , vol.174 , pp. 2391-2393
    • Tolner, B.1    Poolman, B.2    Wallace, B.3    Konings, W.N.4
  • 88
    • 0028803285 scopus 로고
    • Cationselectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: Dependence on the environment in which the proteins are expressed
    • Tolner, B., T. Ubbink-Kok, B. Poolman, and W. N. Konings. 1995. Cationselectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: dependence on the environment in which the proteins are expressed. Mol. Microbiol. 18:123-133.
    • (1995) Mol. Microbiol. , vol.18 , pp. 123-133
    • Tolner, B.1    Ubbink-Kok, T.2    Poolman, B.3    Konings, W.N.4
  • 89
    • 0029015369 scopus 로고
    • Characterization of the proton/glutamate symport protein of Bacillus subtilis and its functional expression in Escherichia coli
    • Tolner, B., T. Ubbink-Kok, B. Poolman, and W. N. Konings. 1995. Characterization of the proton/glutamate symport protein of Bacillus subtilis and its functional expression in Escherichia coli. J. Bacteriol. 177:2863-2869.
    • (1995) J. Bacteriol. , vol.177 , pp. 2863-2869
    • Tolner, B.1    Ubbink-Kok, T.2    Poolman, B.3    Konings, W.N.4
  • 90
    • 0026688543 scopus 로고
    • The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli
    • Traxler, B., C. Lee, D. Boyd, and J. Beckwith. 1992. The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli. J. Biol. Chem. 267:5339-5345.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5339-5345
    • Traxler, B.1    Lee, C.2    Boyd, D.3    Beckwith, J.4
  • 93
    • 0028953410 scopus 로고
    • Arachidonic acid inhibits a purified and reconstituted glutamate transporter directly from the water phase and not via the phospholipid membrane
    • Trotti, D., A. Volterra, K. P. Lehre, D. Rossi, O. Gjesdal, G. Racagni, and N. C. Danbolt. 1995. Arachidonic acid inhibits a purified and reconstituted glutamate transporter directly from the water phase and not via the phospholipid membrane. J. Biol. Chem. 270:9890-9895.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9890-9895
    • Trotti, D.1    Volterra, A.2    Lehre, K.P.3    Rossi, D.4    Gjesdal, O.5    Racagni, G.6    Danbolt, N.C.7
  • 95
    • 0031833248 scopus 로고    scopus 로고
    • Molecular pharmacology and physiology of glutamate transporters in the central nervous system
    • Vandenberg, R. J. 1998. Molecular pharmacology and physiology of glutamate transporters in the central nervous system. Clin. Exp. Pharmacol. Physiol. 25:393-400.
    • (1998) Clin. Exp. Pharmacol. Physiol. , vol.25 , pp. 393-400
    • Vandenberg, R.J.1
  • 96
    • 0029023101 scopus 로고
    • Constitutive ion fluxes and substrate binding domains of human glutamate transporters
    • Vandenberg, R. J., J. L. Arriza, S. G. Amara, and M. P. Kavanaugh. 1995. Constitutive ion fluxes and substrate binding domains of human glutamate transporters. J. Biol. Chem. 270:17668-17671.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17668-17671
    • Vandenberg, R.J.1    Arriza, J.L.2    Amara, S.G.3    Kavanaugh, M.P.4
  • 97
    • 0030946093 scopus 로고    scopus 로고
    • Contrasting modes of action of methylglutamate derivatives on the excitatory amino acid transporters, EAAT1 and EAAT2
    • Vandenberg, R. J., A. D. Mitrovic, M. Chebib, V. J. Balcar, and G. A. Johnston. 1997. Contrasting modes of action of methylglutamate derivatives on the excitatory amino acid transporters, EAAT1 and EAAT2. Mol. Pharmacol. 51:809-815.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 809-815
    • Vandenberg, R.J.1    Mitrovic, A.D.2    Chebib, M.3    Balcar, V.J.4    Johnston, G.A.5
  • 98
    • 0031849828 scopus 로고    scopus 로고
    • Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions
    • Vandenberg, R. J., A. D. Mitrovic, and G. A. Johnston. 1998. Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions. Mol. Pharmacol. 54:189-196.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 189-196
    • Vandenberg, R.J.1    Mitrovic, A.D.2    Johnston, G.A.3
  • 99
    • 0031953098 scopus 로고    scopus 로고
    • Serine-O-sulphate transport by the human glutamate transporter, EAAT2
    • Vandenberg, R. J., A. D. Mitrovic, and G. A. Johnston. 1998. Serine-O-sulphate transport by the human glutamate transporter, EAAT2. Br. J. Pharmacol. 123:1593-1600.
    • (1998) Br. J. Pharmacol. , vol.123 , pp. 1593-1600
    • Vandenberg, R.J.1    Mitrovic, A.D.2    Johnston, G.A.3
  • 100
    • 0027944554 scopus 로고
    • Glutamate uptake is inhibited by arachidonic acid and oxygen radicals via two distinct and additive mechanisms
    • Volterra, A., D. Trotti, and G. Racagni. 1994. Glutamate uptake is inhibited by arachidonic acid and oxygen radicals via two distinct and additive mechanisms. Mol. Pharmacol. 46:986-992.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 986-992
    • Volterra, A.1    Trotti, D.2    Racagni, G.3
  • 101
    • 0028208495 scopus 로고
    • Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes
    • Volterra, A., D. Trotti, C. Tromba, S. Floridi, and G. Racagni. 1994. Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14:2924-2932.
    • (1994) J. Neurosci. , vol.14 , pp. 2924-2932
    • Volterra, A.1    Trotti, D.2    Tromba, C.3    Floridi, S.4    Racagni, G.5
  • 102
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport
    • Wadiche, J. I., S. G. Amara, and M. P. Kavanaugh. 1995. Ion fluxes associated with excitatory amino acid transport. Neuron 15:721-728.
    • (1995) Neuron , vol.15 , pp. 721-728
    • Wadiche, J.I.1    Amara, S.G.2    Kavanaugh, M.P.3
  • 104
    • 0030471958 scopus 로고    scopus 로고
    • Membrane topology of the high-affinity L-glutamate transporter (GLAST-1) of the central nervous system
    • Wahle, S., and W. Stoffel. 1996. Membrane topology of the high-affinity L-glutamate transporter (GLAST-1) of the central nervous system. J. Cell Biol. 135:1867-1877.
    • (1996) J. Cell Biol. , vol.135 , pp. 1867-1877
    • Wahle, S.1    Stoffel, W.2
  • 105
    • 0025298360 scopus 로고
    • Cloning and sequencing of a gene encoding a glutamate and aspartate carrier of Escherichia coli K-12
    • Wallace, B., Y. J. Yang, J. S. Hong, and D. Lum. 1990. Cloning and sequencing of a gene encoding a glutamate and aspartate carrier of Escherichia coli K-12. J. Bacteriol. 172:3214-3220.
    • (1990) J. Bacteriol. , vol.172 , pp. 3214-3220
    • Wallace, B.1    Yang, Y.J.2    Hong, J.S.3    Lum, D.4
  • 106
    • 0026006986 scopus 로고
    • Site-directed mutagenesis of alpha 2A-adrenergic receptors: Identification of amino acids involved in ligand binding and receptor activation by agonists
    • Wang, C. D., M. A. Buck, and C. M. Fraser. 1991. Site-directed mutagenesis of alpha 2A-adrenergic receptors: identification of amino acids involved in ligand binding and receptor activation by agonists. Mol. Pharmacol. 40:168-179.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 168-179
    • Wang, C.D.1    Buck, M.A.2    Fraser, C.M.3
  • 109
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C. R., O. Kandler, and M. L. Wheelis. 1990. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. USA 87:4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 110
    • 0032486463 scopus 로고    scopus 로고
    • Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue
    • Zarbiv, R., M. Grunewald, M. P. Kavanaugh, and B. I. Kanner. 1998. Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue. J. Biol. Chem. 273:14231-14237.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14231-14237
    • Zarbiv, R.1    Grunewald, M.2    Kavanaugh, M.P.3    Kanner, B.I.4
  • 111
    • 0028911077 scopus 로고
    • Differential modulation of human glutamate transporter subtypes by arachidonic acid
    • Zerangue, N., J. L. Arriza, S. G. Amara, and M. P. Kavanaugh. 1995. Differential modulation of human glutamate transporter subtypes by arachidonic acid. J. Biol. Chem. 270:6433-6435.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6433-6435
    • Zerangue, N.1    Arriza, J.L.2    Amara, S.G.3    Kavanaugh, M.P.4
  • 112
    • 0029903720 scopus 로고    scopus 로고
    • ASCT-1 is a neutral amino acid exchanger with chloride channel activity
    • Zerangue, N., and M. P. Kavanaugh. 1996. ASCT-1 is a neutral amino acid exchanger with chloride channel activity. J. Biol. Chem. 271:27991-27994.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27991-27994
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 113
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue, N., and M. P. Kavanaugh. 1996. Flux coupling in a neuronal glutamate transporter. Nature 383:634-637.
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 114
    • 0029891464 scopus 로고    scopus 로고
    • Interaction of L-cysteine with a human excitatory amino acid transporter
    • London
    • Zerangue, N., and M. P. Kavanaugh. 1996. Interaction of L-cysteine with a human excitatory amino acid transporter. J. Physiol. (London) 493:419-423.
    • (1996) J. Physiol. , vol.493 , pp. 419-423
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 116


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.