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Volumn , Issue , 2001, Pages 41-55

Structure of ionotropic glutamate receptors

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EID: 84884084214     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (80)
  • 1
    • 0031961764 scopus 로고    scopus 로고
    • Identification of amino acid residues of the NR2A subunit that control glutamate potency in recombinant NR1/NR2A NMDA receptors
    • Anson, L.C., Chen, P.E., Wyllie, D.J.A., Colquhoun, D. and Schoepfer, R. (1998) ‘Identification of amino acid residues of the NR2A subunit that control glutamate potency in recombinant NR1/NR2A NMDA receptors’, J. Neurosci. 18: 581-589.
    • (1998) J. Neurosci , vol.18 , pp. 581-589
    • Anson, L.C.1    Chen, P.E.2    Wyllie, D.J.A.3    Colquhoun, D.4    Schoepfer, R.5
  • 2
    • 0032174052 scopus 로고    scopus 로고
    • Binding sites for permeant ions in the channel of NMDA receptors and their effects on channel block
    • Antonov, S.M., Gmiro, V.E. and Johnson, J.W. (1998) ‘Binding sites for permeant ions in the channel of NMDA receptors and their effects on channel block’, Nat. Neurosci. 1: 451-461.
    • (1998) Nat. Neurosci , vol.1 , pp. 451-461
    • Antonov, S.M.1    Gmiro, V.E.2    Johnson, J.W.3
  • 3
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong, N., Sun, Y., Chen, G.Q. and Gouaux, E. (1998) ‘Structure of a glutamate-receptor ligand-binding core in complex with kainate’, Nature 395: 913-917.
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 4
    • 0033103522 scopus 로고    scopus 로고
    • NMDAR channel segments forming the extracellular vestibule inferred from the accessibility of substituted cysteines
    • Beck, C., Wollmuth, L.P., Seeburg, P.H., Sakmann, B. and Kuner, T. (1999) ‘NMDAR channel segments forming the extracellular vestibule inferred from the accessibility of substituted cysteines’, Neuron 22: 559-570.
    • (1999) Neuron , vol.22 , pp. 559-570
    • Beck, C.1    Wollmuth, L.P.2    Seeburg, P.H.3    Sakmann, B.4    Kuner, T.5
  • 6
    • 0028819612 scopus 로고
    • Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining reentrant membrane loop
    • Bennett, J.A. and Dingledine, R. (1995) ‘Topology profile for a glutamate receptor: three transmembrane domains and a channel-lining reentrant membrane loop’, Neuron 14: 373-384.
    • (1995) Neuron , vol.14 , pp. 373-384
    • Bennett, J.A.1    Dingledine, R.2
  • 7
    • 0026584503 scopus 로고
    • Biochemical characterization and localization of a non-N-methyl-D-aspartate glutamate receptor in rat brain
    • Blackstone, C.D., Moss, S.J., Martin, L.J., Levey, A.I., Price, D.L. and Huganir, R.L. (1992) ‘Biochemical characterization and localization of a non-N-methyl-D-aspartate glutamate receptor in rat brain’, J. Neurochem. 58: 1118-1126.
    • (1992) J. Neurochem , vol.58 , pp. 1118-1126
    • Blackstone, C.D.1    Moss, S.J.2    Martin, L.J.3    Levey, A.I.4    Price, D.L.5    Huganir, R.L.6
  • 8
    • 0027209993 scopus 로고
    • A single amino acid determines the subunit-specific spider toxin block of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate/kainate receptor channels
    • Blaschke, M., Keller, B.U., Rivosecchi, R., Hollmann, M., Heinemann, S. and Konnerth, A. (1993) ‘A single amino acid determines the subunit-specific spider toxin block of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate/kainate receptor channels’, Proc. Natl. Acad. Sci. USA 90: 6528-6532.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6528-6532
    • Blaschke, M.1    Keller, B.U.2    Rivosecchi, R.3    Hollmann, M.4    Heinemann, S.5    Konnerth, A.6
  • 9
    • 0029979667 scopus 로고    scopus 로고
    • Pharmacological discrimination of GluR5 and GluR6 kainate receptor subtypes by (3S,4aR,6R,8aR)-6-[2-(1(2)H-tetrazole-5-yl)ethyl]decahyd roisdoquinoline-3 carboxylicacid
    • Bleakman, R., Schoepp, D.D., Ballyk, B., Bufton, H., Sharpe, E.F., Thomas, K., Ornstein, P.L. and Kamboj, R.K. (1996) ‘Pharmacological discrimination of GluR5 and GluR6 kainate receptor subtypes by (3S,4aR,6R,8aR)-6-[2-(1(2)H-tetrazole-5-yl)ethyl]decahyd roisdoquinoline-3 carboxylicacid’, Mol. Pharmacol. 49: 581-585.
    • (1996) Mol. Pharmacol , vol.49 , pp. 581-585
    • Bleakman, R.1    Schoepp, D.D.2    Ballyk, B.3    Bufton, H.4    Sharpe, E.F.5    Thomas, K.6    Ornstein, P.L.7    Kamboj, R.K.8
  • 11
    • 0027490681 scopus 로고
    • ‘Protein chemical characterization and immunocytochemical localization of the NMDA receptor subunit NMDA R1'
    • Brose, N., Gasic, G.P., Vetter, D.E., Sullivan, J.M. and Heinemann, S.F. (1993) ‘Protein chemical characterization and immunocytochemical localization of the NMDA receptor subunit NMDA R1', J. Biol. Chem. 268: 22,663-22,671.
    • (1993) J. Biol. Chem , vol.268 , pp. 22,663-22,671
    • Brose, N.1    Gasic, G.P.2    Vetter, D.E.3    Sullivan, J.M.4    Heinemann, S.F.5
  • 12
    • 0027991388 scopus 로고
    • The molecular basis of NMDA receptor subtypes: Native receptor diversity is predicted by subunit composition
    • Buller, A.L., Larson, H.C., Schneider, B.E., Beaton, J.A., Morrisett, R.A. and Monaghan, D.T. (1994) ‘The molecular basis of NMDA receptor subtypes: native receptor diversity is predicted by subunit composition’, J. Neurosci. 14: 5471-5484.
    • (1994) J. Neurosci , vol.14 , pp. 5471-5484
    • Buller, A.L.1    Larson, H.C.2    Schneider, B.E.3    Beaton, J.A.4    Morrisett, R.A.5    Monaghan, D.T.6
  • 13
    • 0026727807 scopus 로고
    • Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor
    • Burnashev, N., Schoepfer, R., Monyer, H., Ruppersberg, J.P., Gunther, W., Seeburg, P.H. and Sakmann, B. (1992) ‘Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor’, Science 257: 1415-1419.
    • (1992) Science , vol.257 , pp. 1415-1419
    • Burnashev, N.1    Schoepfer, R.2    Monyer, H.3    Ruppersberg, J.P.4    Gunther, W.5    Seeburg, P.H.6    Sakmann, B.7
  • 14
    • 2542550010 scopus 로고    scopus 로고
    • Dimensions and ion selectivity of recombinant AMPA and kainate receptor channels and their dependence on Q/R site residues
    • Burnashev, N., Villarroel, A. and Sakmann, B. (1996) ‘Dimensions and ion selectivity of recombinant AMPA and kainate receptor channels and their dependence on Q/R site residues’, J. Physiol. (Lond.) 496: 165-173.
    • (1996) J. Physiol. (Lond.) , vol.496 , pp. 165-173
    • Burnashev, N.1    Villarroel, A.2    Sakmann, B.3
  • 15
    • 0033576612 scopus 로고    scopus 로고
    • Functional characterization of a potassium-selective prokaryotic glutamate receptor
    • Chen, G.Q., Cui, C., Mayer, M.L. and Gouaux, E. (1999) ‘Functional characterization of a potassium-selective prokaryotic glutamate receptor’, Nature 402: 817-821.
    • (1999) Nature , vol.402 , pp. 817-821
    • Chen, G.Q.1    Cui, C.2    Mayer, M.L.3    Gouaux, E.4
  • 16
    • 0031471216 scopus 로고    scopus 로고
    • Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of a novel protein folding screen
    • Chen, G.Q. and Gouaux, E. (1997) ‘Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen’, Proc. Natl. Acad. Sci. USA 94: 13,431-13,436.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13,431-13,436
    • Chen, G.Q.1    Gouaux, E.2
  • 18
    • 0033136273 scopus 로고    scopus 로고
    • Identification and mechanism of action of two histidine residues underlying high-affinity Zn2+ inhibition of the NMDA receptor
    • Choi, Y.B. and Lipton, S.A. (1999) ‘Identification and mechanism of action of two histidine residues underlying high-affinity Zn2+ inhibition of the NMDA receptor’, Neuron 23: 171-180.
    • (1999) Neuron , vol.23 , pp. 171-180
    • Choi, Y.B.1    Lipton, S.A.2
  • 19
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun, D. (1998) ‘Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors’, Br. J. Pharmacol. 125: 924-947.
    • (1998) Br. J. Pharmacol , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 22
    • 0026675738 scopus 로고
    • Structural determinants of barium permeation and rectification in non-NMDA glutamate receptor channels
    • Dingledine, R., Hume, R.I. and Heinemann, S.F. (1992) ‘Structural determinants of barium permeation and rectification in non-NMDA glutamate receptor channels’, J. Neurosci. 12: 4080-4087.
    • (1992) J. Neurosci , vol.12 , pp. 4080-4087
    • Dingledine, R.1    Hume, R.I.2    Heinemann, S.F.3
  • 24
    • 0033697745 scopus 로고    scopus 로고
    • Four residues of the extracellular N-terminal domain of the NR2A subunit control high-affinity Zn2+ binding to NMDA receptors
    • Fayyazuddin, A., Villarroel, A., Le Goff, A., Lerma, J. and Neyton, J. (2000) ‘Four residues of the extracellular N-terminal domain of the NR2A subunit control high-affinity Zn2+ binding to NMDA receptors’, Neuron 25: 683-694.
    • (2000) Neuron , vol.25 , pp. 683-694
    • Fayyazuddin, A.1    Villarroel, A.2    Le Goff, A.3    Lerma, J.4    Neyton, J.5
  • 25
    • 0032004097 scopus 로고    scopus 로고
    • Structural determinants of the blocker binding site in glutamate and NMDA receptor channels
    • Ferrer-Montiel, A.V., Merino, J.M., Planells-Cases, R., Sun, W. and Montal, M. (1998) ‘Structural determinants of the blocker binding site in glutamate and NMDA receptor channels’, Neuropharmacology 37: 139-147.
    • (1998) Neuropharmacology , vol.37 , pp. 139-147
    • Ferrer-Montiel, A.V.1    Merino, J.M.2    Planells-Cases, R.3    Sun, W.4    Montal, M.5
  • 26
    • 0029759751 scopus 로고    scopus 로고
    • A single tryptophan on M2 of glutamate receptor channels confers high permeability to divalent cations
    • Ferrer-Montiel, A.V., Sun, W. and Montal, M. (1996) ‘A single tryptophan on M2 of glutamate receptor channels confers high permeability to divalent cations’, Biophys. J. 71: 749-758.
    • (1996) Biophys. J , vol.71 , pp. 749-758
    • Ferrer-Montiel, A.V.1    Sun, W.2    Montal, M.3
  • 27
    • 0032032015 scopus 로고    scopus 로고
    • Molecular neurobiology and genetics: Investigation of neural function and dysfunction
    • Green, T., Heinemann, S.F. and Gusella, J.F. (1998) ‘Molecular neurobiology and genetics: investigation of neural function and dysfunction’, Neuron 20: 427-444.
    • (1998) Neuron , vol.20 , pp. 427-444
    • Green, T.1    Heinemann, S.F.2    Gusella, J.F.3
  • 28
    • 0029893942 scopus 로고    scopus 로고
    • The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: Identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region
    • Hirai, H., Kirsch, J., Laube, B., Betz, H. and Kuhse, J. (1996) ‘The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region’, Proc. Natl. Acad. Sci. USA 93: 6031-6036.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6031-6036
    • Hirai, H.1    Kirsch, J.2    Laube, B.3    Betz, H.4    Kuhse, J.5
  • 30
    • 0028596211 scopus 로고
    • ‘N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1'
    • Hollmann, M., Maron, C. and Heinemann, S. (1994) ‘N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1', Neuron 13: 1331-1343.
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 31
    • 0025784548 scopus 로고
    • Identification of a site in glutamate receptor subunits that controls calcium permeability
    • Hume, R.I., Dingledine, R. and Heinemann, S.F. (1991) ‘Identification of a site in glutamate receptor subunits that controls calcium permeability’, Science 253: 1028-1031.
    • (1991) Science , vol.253 , pp. 1028-1031
    • Hume, R.I.1    Dingledine, R.2    Heinemann, S.F.3
  • 32
    • 0026572771 scopus 로고
    • Solubilization and purification of an alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid binding protein from bovine brain
    • Hunter, C. and Wenthold, R.J. (1992) ‘Solubilization and purification of an alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid binding protein from bovine brain’, J. Neurochem. 58: 1379-1385.
    • (1992) J. Neurochem , vol.58 , pp. 1379-1385
    • Hunter, C.1    Wenthold, R.J.2
  • 33
    • 0032493660 scopus 로고    scopus 로고
    • Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit
    • Ivanovic, A., Reilander, H., Laube, B. and Kuhse, J. (1998) ‘Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit’, J. Biol. Chem. 273: 19,933-19,937.
    • (1998) J. Biol. Chem , vol.273 , pp. 19,933-19,937
    • Ivanovic, A.1    Reilander, H.2    Laube, B.3    Kuhse, J.4
  • 34
    • 0029023325 scopus 로고
    • Impairment of motor coordination, Purkinje cell synapse formation, and cerebellar long-term depression in GluR delta 2 mutant mice
    • Kashiwabuchi, N., Ikeda, K., Araki, K., Hirano, T., Shibuki, K., Takayama, C., Inoue, Y., Kutsuwada, T., Yagi, T., Kang, Y., et al. (1995) ‘Impairment of motor coordination, Purkinje cell synapse formation, and cerebellar long-term depression in GluR delta 2 mutant mice’, Cell 81: 245-252.
    • (1995) Cell , vol.81 , pp. 245-252
    • Kashiwabuchi, N.1    Ikeda, K.2    Araki, K.3    Hirano, T.4    Shibuki, K.5    Takayama, C.6    Inoue, Y.7    Kutsuwada, T.8    Yagi, T.9    Kang, Y.10
  • 35
    • 0027385330 scopus 로고
    • Multiple structural determinants of voltage-dependent magnesium block in recombinant NMDA receptors
    • Kawajiri, S. and Dingledine, R. (1993) ‘Multiple structural determinants of voltage-dependent magnesium block in recombinant NMDA receptors’, Neuropharmacology 32: 1203-1211.
    • (1993) Neuropharmacology , vol.32 , pp. 1203-1211
    • Kawajiri, S.1    Dingledine, R.2
  • 36
    • 0034114521 scopus 로고    scopus 로고
    • Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties
    • Kohda, K., Wang, Y. and Yuzaki, M. (2000) ‘Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties’, Nat. Neurosci. 3: 315-322.
    • (2000) Nat. Neurosci , vol.3 , pp. 315-322
    • Kohda, K.1    Wang, Y.2    Yuzaki, M.3
  • 37
    • 0032006313 scopus 로고    scopus 로고
    • N-terminal domains in the NR2 subunit control desensitization of NMDA receptors
    • Krupp, J.J., Vissel, B., Heinemann, S.F. and Westbrook, G.L. (1998) ‘N-terminal domains in the NR2 subunit control desensitization of NMDA receptors’, Neuron 20: 317-327.
    • (1998) Neuron , vol.20 , pp. 317-327
    • Krupp, J.J.1    Vissel, B.2    Heinemann, S.F.3    Westbrook, G.L.4
  • 38
    • 0030220889 scopus 로고    scopus 로고
    • Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines
    • Kuner, T., Wollmuth, L.P., Karlin, A., Seeburg, P.H. and Sakmann, B. (1996) ‘Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines’, Neuron 17: 343-352.
    • (1996) Neuron , vol.17 , pp. 343-352
    • Kuner, T.1    Wollmuth, L.P.2    Karlin, A.3    Seeburg, P.H.4    Sakmann, B.5
  • 39
    • 0028284469 scopus 로고
    • Mutational analysis of the glycine-binding site of the NMDA receptor: Structural similarity with bacterial amino acid-binding proteins
    • Kuryatov, A., Laube, B., Betz, H. and Kuhse, J. (1994) ‘Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins’, Neuron 12: 1291-1300.
    • (1994) Neuron , vol.12 , pp. 1291-1300
    • Kuryatov, A.1    Laube, B.2    Betz, H.3    Kuhse, J.4
  • 40
    • 0032878510 scopus 로고    scopus 로고
    • Oligomerization and ligandbinding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD
    • Kuusinen, A., Abele, R., Madden, D.R. and Keinanen, K. (1999) ‘Oligomerization and ligandbinding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD’, J. Biol. Chem. 274: 28,937-28,943.
    • (1999) J. Biol. Chem , vol.274 , pp. 28,937-28,943
    • Kuusinen, A.1    Abele, R.2    Madden, D.R.3    Keinanen, K.4
  • 41
    • 0029583151 scopus 로고
    • Molecular dissection of the agonist binding site of an AMPA receptor
    • Kuusinen, A., Arvola, M. and Keinanen, K. (1995) ‘Molecular dissection of the agonist binding site of an AMPA receptor’, Embo. J. 14: 6327-6332.
    • (1995) Embo. J , vol.14 , pp. 6327-6332
    • Kuusinen, A.1    Arvola, M.2    Keinanen, K.3
  • 42
    • 0030991790 scopus 로고    scopus 로고
    • Molecular determinants of agonist discrimination by NMDA receptor subunits: Analysis of the glutamate binding site on the NR2B subunit
    • Laube, B., Hirai, H., Sturgess, M., Betz, H. and Kuhse, J. (1997) ‘Molecular determinants of agonist discrimination by NMDA receptor subunits: analysis of the glutamate binding site on the NR2B subunit’, Neuron 18: 493-503.
    • (1997) Neuron , vol.18 , pp. 493-503
    • Laube, B.1    Hirai, H.2    Sturgess, M.3    Betz, H.4    Kuhse, J.5
  • 43
    • 0033546277 scopus 로고    scopus 로고
    • Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains
    • Leuschner, W.D. and Hoch, W. (1999) ‘Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains’, J. Biol. Chem. 274: 16,907-16,916.
    • (1999) J. Biol. Chem , vol.274 , pp. 16,907-16,916
    • Leuschner, W.D.1    Hoch, W.2
  • 44
    • 0027454751 scopus 로고
    • The rat delta-1 and delta-2 subunits extend the excitatory amino acid receptor family
    • Lomeli, H., Sprengel, R., Laurie, D.J., Kohr, G., Herb, A., Seeburg, P.H. and Wisden, W. (1993) ‘The rat delta-1 and delta-2 subunits extend the excitatory amino acid receptor family’, FEBS Lett. 315: 318-322.
    • (1993) FEBS Lett , vol.315 , pp. 318-322
    • Lomeli, H.1    Sprengel, R.2    Laurie, D.J.3    Kohr, G.4    Herb, A.5    Seeburg, P.H.6    Wisden, W.7
  • 45
    • 0034718494 scopus 로고    scopus 로고
    • Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors
    • Low, C.M., Zheng, F., Lyuboslavsky, P. and Traynelis, S.F. (2000) ‘Molecular determinants of coordinated proton and zinc inhibition of N-methyl-D-aspartate NR1/NR2A receptors’, Proc. Natl. Acad. Sci. USA 97: 11,062-11,067.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11,062-11,067
    • Low, C.M.1    Zheng, F.2    Lyuboslavsky, P.3    Traynelis, S.F.4
  • 46
    • 0029899637 scopus 로고    scopus 로고
    • A venus flytrap mechanism for activation and desensitization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors
    • Mano, I., Lamed, Y. and Teichberg, V.I. (1996) ‘A venus flytrap mechanism for activation and desensitization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors’, J. Biol. Chem. 271: 15,299-15,302.
    • (1996) J. Biol. Chem , vol.271 , pp. 15,299-15,302
    • Mano, I.1    Lamed, Y.2    Teichberg, V.I.3
  • 48
    • 0025221685 scopus 로고
    • A family of glutamate receptor genes: Evidence for the formation of heteromultimeric receptors with distinct channel properties
    • Nakanishi, N., Shneider, N.A. and Axel, R. (1990) ‘A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties’, Neuron 5: 569-581.
    • (1990) Neuron , vol.5 , pp. 569-581
    • Nakanishi, N.1    Shneider, N.A.2    Axel, R.3
  • 50
    • 17144450204 scopus 로고    scopus 로고
    • Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate
    • Paas, Y., Eisenstein, M., Medevielle, F., Teichberg, V.I. and Devillers-Thiery, A. (1996) ‘Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate’, Neuron 17: 979-990.
    • (1996) Neuron , vol.17 , pp. 979-990
    • Paas, Y.1    Eisenstein, M.2    Medevielle, F.3    Teichberg, V.I.4    Devillers-Thiery, A.5
  • 51
    • 0028935086 scopus 로고
    • Structural determinants of allosteric regulation in alternatively spliced AMPA receptors
    • Partin, K.M., Bowie, D. and Mayer, M.L. (1995) ‘Structural determinants of allosteric regulation in alternatively spliced AMPA receptors’, Neuron 14: 833-843.
    • (1995) Neuron , vol.14 , pp. 833-843
    • Partin, K.M.1    Bowie, D.2    Mayer, M.L.3
  • 52
    • 0027715150 scopus 로고
    • Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A
    • Partin, K.M., Patneau, D.K., Winters, C.A., Mayer, M.L. and Buonanno, A. (1993) ‘Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A’, Neuron 11: 1069-1082.
    • (1993) Neuron , vol.11 , pp. 1069-1082
    • Partin, K.M.1    Patneau, D.K.2    Winters, C.A.3    Mayer, M.L.4    Buonanno, A.5
  • 53
    • 0031047595 scopus 로고    scopus 로고
    • Subconductance states of a mutant NMDA receptor channel kinetics, calcium, and voltage dependence
    • Premkumar, L.S., Qin, F. and Auerbach, A. (1997) ‘Subconductance states of a mutant NMDA receptor channel kinetics, calcium, and voltage dependence’, J. Gen. Physiol. 109: 181-189.
    • (1997) J. Gen. Physiol , vol.109 , pp. 181-189
    • Premkumar, L.S.1    Qin, F.2    Auerbach, A.3
  • 55
    • 0032486422 scopus 로고    scopus 로고
    • The tetrameric structure of a glutamate receptor channel
    • Rosenmund, C., Stern-Bach, Y. and Stevens, C.F. (1998) ‘The tetrameric structure of a glutamate receptor channel’, Science 280: 1596-1599.
    • (1998) Science , vol.280 , pp. 1596-1599
    • Rosenmund, C.1    Stern-Bach, Y.2    Stevens, C.F.3
  • 56
    • 0027339551 scopus 로고
    • Alteration of Ca2+ permeability and sensitivity to Mg2+ and channel blockers by a single amino acid substitution in the N-methyl-D-aspartate receptor
    • Sakurada, K., Masu, M. and Nakanishi, S. (1993) ‘Alteration of Ca2+ permeability and sensitivity to Mg2+ and channel blockers by a single amino acid substitution in the N-methyl-D-aspartate receptor’, J. Biol. Chem. 268: 410-415.
    • (1993) J. Biol. Chem , vol.268 , pp. 410-415
    • Sakurada, K.1    Masu, M.2    Nakanishi, S.3
  • 57
    • 0030810255 scopus 로고    scopus 로고
    • Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate
    • Schiffer, H.H., Swanson, G.T. and Heinemann, S.F. (1997) ‘Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate’, Neuron 19: 1141-1146.
    • (1997) Neuron , vol.19 , pp. 1141-1146
    • Schiffer, H.H.1    Swanson, G.T.2    Heinemann, S.F.3
  • 58
    • 0031943577 scopus 로고    scopus 로고
    • Altered voltage dependence of fractional Ca2+ current in N-methyl-D-aspartate channel pore mutants with a decreased Ca2+ permeability
    • Schneggenburger, R. (1998) ‘Altered voltage dependence of fractional Ca2+ current in N-methyl-D-aspartate channel pore mutants with a decreased Ca2+ permeability’, Biophys. J. 74: 1790-1794.
    • (1998) Biophys. J , vol.74 , pp. 1790-1794
    • Schneggenburger, R.1
  • 59
    • 0031576342 scopus 로고    scopus 로고
    • Xenopus oocytes express a unitary glutamate receptor endogenously
    • Soloviev, M.M. and Barnard, E.A. (1997) ‘Xenopus oocytes express a unitary glutamate receptor endogenously’, J. Mol. Biol. 273: 14-18.
    • (1997) J. Mol. Biol , vol.273 , pp. 14-18
    • Soloviev, M.M.1    Barnard, E.A.2
  • 60
    • 0025995296 scopus 로고
    • RNA editing in brain controls a determinant of ion flow in glutamate-gated channels
    • Sommer, B., Kohler, M., Sprengel, R. and Seeburg, P.H. (1991) ‘RNA editing in brain controls a determinant of ion flow in glutamate-gated channels’, Cell 67: 11-19.
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Kohler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 62
    • 0028559605 scopus 로고
    • Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
    • Stern-Bach, Y., Bettler, B., Hartley, M., Sheppard, P.O., O’Hara, P.J. and Heinemann, S.F. (1994) ‘Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins’, Neuron 13: 1345-1357.
    • (1994) Neuron , vol.13 , pp. 1345-1357
    • Stern-Bach, Y.1    Bettler, B.2    Hartley, M.3    Sheppard, P.O.4    O’Hara, P.J.5    Heinemann, S.F.6
  • 63
    • 0032191104 scopus 로고    scopus 로고
    • A point mutation in the glutamate binding site blocks desensitization of AMPA receptors
    • Stern-Bach, Y., Russo, S., Neuman, M. and Rosenmund, C. (1998) ‘A point mutation in the glutamate binding site blocks desensitization of AMPA receptors’, Neuron 21: 907-918.
    • (1998) Neuron , vol.21 , pp. 907-918
    • Stern-Bach, Y.1    Russo, S.2    Neuman, M.3    Rosenmund, C.4
  • 64
    • 0029864050 scopus 로고    scopus 로고
    • Effect of RNA editing and subunit co-assembly single-channel properties of recombinant kainate receptors
    • Swanson, G.T., Feldmeyer, D., Kaneda, M. and Cull-Candy, S.G. (1996) ‘Effect of RNA editing and subunit co-assembly single-channel properties of recombinant kainate receptors’, J. Physiol. (Lond.) 492: 129-142.
    • (1996) J. Physiol. (Lond.) , vol.492 , pp. 129-142
    • Swanson, G.T.1    Feldmeyer, D.2    Kaneda, M.3    Cull-Candy, S.G.4
  • 65
    • 0030777076 scopus 로고    scopus 로고
    • Identification of amino acid residues that control functional behavior in GluR5 and GluR6 kainate receptors
    • Swanson, G.T., Gereau, R.W.T., Green, T. and Heinemann, S.F. (1997a) ‘Identification of amino acid residues that control functional behavior in GluR5 and GluR6 kainate receptors’, Neuron 19: 913-926.
    • (1997) Neuron , vol.19 , pp. 913-926
    • Swanson, G.T.1    Gereau, R.W.T.2    Green, T.3    Heinemann, S.F.4
  • 66
    • 0031015614 scopus 로고    scopus 로고
    • Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition
    • Swanson, G.T., Kamboj, S.K. and Cull-Candy, S.G. (1997b) ‘Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition’, J. Neurosci. 17: 58-69.
    • (1997) J. Neurosci , vol.17 , pp. 58-69
    • Swanson, G.T.1    Kamboj, S.K.2    Cull-Candy, S.G.3
  • 67
    • 0031750767 scopus 로고    scopus 로고
    • Kainate receptors exhibit differential sensitivities to (S)-5-iodowillardiine
    • Swanson, G.T., Green, T. and Heinemann, S.F. (1998) ‘Kainate receptors exhibit differential sensitivities to (S)-5-iodowillardiine’, Mol. Pharmacol. 53: 942-949.
    • (1998) Mol. Pharmacol , vol.53 , pp. 942-949
    • Swanson, G.T.1    Green, T.2    Heinemann, S.F.3
  • 68
    • 0034708631 scopus 로고    scopus 로고
    • The Lurcher mutation of an alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit enhances potency of glutamate and converts an antagonist to an agonist
    • Taverna, F., Xiong, Z.G., Brandes, L., Roder, J.C., Salter, M.W. and MacDonald, J.F. (2000) ‘The Lurcher mutation of an alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit enhances potency of glutamate and converts an antagonist to an agonist’, J. Biol. Chem. 275: 8475-8479.
    • (2000) J. Biol. Chem , vol.275 , pp. 8475-8479
    • Taverna, F.1    Xiong, Z.G.2    Brandes, L.3    Roder, J.C.4    Salter, M.W.5    MacDonald, J.F.6
  • 69
    • 0032529588 scopus 로고    scopus 로고
    • Control of voltage-independent zinc inhibition of NMDA receptors by the NR1 subunit
    • Traynelis, S.F., Burgess, M.F., Zheng, F., Lyuboslavsky, P. and Powers, J.L. (1998) ‘Control of voltage-independent zinc inhibition of NMDA receptors by the NR1 subunit’, J. Neurosci. 18: 6163-6175.
    • (1998) J. Neurosci , vol.18 , pp. 6163-6175
    • Traynelis, S.F.1    Burgess, M.F.2    Zheng, F.3    Lyuboslavsky, P.4    Powers, J.L.5
  • 70
    • 0026686125 scopus 로고
    • Mutations in a putative agonist binding region of the AMPA-selective glutamate receptor channel
    • Uchino, S., Sakimura, K., Nagahari, K. and Mishina, M. (1992) ‘Mutations in a putative agonist binding region of the AMPA-selective glutamate receptor channel’, FEBS Lett. 308: 253-257.
    • (1992) FEBS Lett , vol.308 , pp. 253-257
    • Uchino, S.1    Sakimura, K.2    Nagahari, K.3    Mishina, M.4
  • 71
    • 0028945477 scopus 로고
    • Dimensions of the narrow portion of a recombinant NMDA receptor channel
    • Villarroel, A., Burnashev, N. and Sakmann, B. (1995) ‘Dimensions of the narrow portion of a recombinant NMDA receptor channel’, Biophys. J. 68: 866-875.
    • (1995) Biophys. J , vol.68 , pp. 866-875
    • Villarroel, A.1    Burnashev, N.2    Sakmann, B.3
  • 72
    • 0033783080 scopus 로고    scopus 로고
    • Resolution, configurational assignment, and enantiopharmacology of 2-amino-3-[3-hydroxy-5-(2-methyl-2H-tetrazol-5-yl)isoxazol-4-yl]propionic acid, a potent GluR3- and GluR4-preferring AMPA receptor agonist
    • Vogensen, S.B., Jensen, H.S., Stensbol, T.B., Frydenvang, K., Bang-Andersen, B., Johansen, T.N., Egebjerg, J. and Krogsgaard-Larsen, P. (2000) ‘Resolution, configurational assignment, and enantiopharmacology of 2-amino-3-[3-hydroxy-5-(2-methyl-2H-tetrazol-5-yl)isoxazol-4-yl]propionic acid, a potent GluR3- and GluR4-preferring AMPA receptor agonist’, Chirality 12: 705-713.
    • (2000) Chirality , vol.12 , pp. 705-713
    • Vogensen, S.B.1    Jensen, H.S.2    Stensbol, T.B.3    Frydenvang, K.4    Bang-Andersen, B.5    Johansen, T.N.6    Egebjerg, J.7    Krogsgaard-Larsen, P.8
  • 73
    • 0028921951 scopus 로고
    • Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site
    • Wafford, K.A., Kathoria, M., Bain, C.J., Marshall, G., Le Bourdelles, B., Kemp, J.A. and Whiting, P.J. (1995) ‘Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site’, Mol. Pharmacol. 47: 374-380.
    • (1995) Mol. Pharmacol , vol.47 , pp. 374-380
    • Wafford, K.A.1    Kathoria, M.2    Bain, C.J.3    Marshall, G.4    Le Bourdelles, B.5    Kemp, J.A.6    Whiting, P.J.7
  • 74
    • 0029921964 scopus 로고    scopus 로고
    • Activation of N-methyl-D-aspartate receptors by glycine: Role of an aspartate residue in the M3-M4 loop of the NR1 subunit
    • Williams, K., Chao, J., Kashiwagi, K., Masuko, T. and Igarashi, K. (1996) ‘Activation of N-methyl-D-aspartate receptors by glycine: role of an aspartate residue in the M3-M4 loop of the NR1 subunit’, Mol. Pharmacol. 50: 701-708.
    • (1996) Mol. Pharmacol , vol.50 , pp. 701-708
    • Williams, K.1    Chao, J.2    Kashiwagi, K.3    Masuko, T.4    Igarashi, K.5
  • 75
    • 0028364252 scopus 로고
    • Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation
    • Wo, Z.G. and Oswald, R.E. (1994) ‘Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation’, Proc. Natl. Acad. Sci. USA 91: 7154-7158.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7154-7158
    • Wo, Z.G.1    Oswald, R.E.2
  • 76
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo, Z. and Oswald, R. (1995) ‘Unraveling the modular design of glutamate-gated ion channels’, Trends Neurosci. 18: 161-168.
    • (1995) Trends Neurosci , vol.18 , pp. 161-168
    • Wo, Z.1    Oswald, R.2
  • 77
    • 0031973709 scopus 로고    scopus 로고
    • ‘Adjacent asparagines in the NR2-subunit of the NMDA receptor channel control the voltage-dependent block by extracellular Mg2+'
    • Wollmuth, L.P., Kuner, T. and Sakmann, B. (1998) ‘Adjacent asparagines in the NR2-subunit of the NMDA receptor channel control the voltage-dependent block by extracellular Mg2+', J. Physiol. (Lond.) 506: 13-32.
    • (1998) J. Physiol. (Lond.) , vol.506 , pp. 13-32
    • Wollmuth, L.P.1    Kuner, T.2    Sakmann, B.3
  • 78
    • 0029887686 scopus 로고    scopus 로고
    • Differential contribution of the NR1- and NR2A-subunits to the selectivity filter of recombinant NMDA receptor channels
    • Wollmuth, L.P., Kuner, T., Seeburg, P.H. and Sakmann, B. (1996) ‘Differential contribution of the NR1- and NR2A-subunits to the selectivity filter of recombinant NMDA receptor channels’, J. Physiol. (Lond.) 491: 779-797.
    • (1996) J. Physiol. (Lond.) , vol.491 , pp. 779-797
    • Wollmuth, L.P.1    Kuner, T.2    Seeburg, P.H.3    Sakmann, B.4
  • 79
    • 0028307255 scopus 로고
    • Hydrodynamic and pharmacological characterization of putative alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/kainate-sensitive L-glutamate receptors solubilized from pig brain
    • Wu, T.Y. and Chang, Y.C. (1994) ‘Hydrodynamic and pharmacological characterization of putative alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/kainate-sensitive L-glutamate receptors solubilized from pig brain’, Biochem. J. 300: 365-371.
    • (1994) Biochem. J , vol.300 , pp. 365-371
    • Wu, T.Y.1    Chang, Y.C.2
  • 80
    • 0030800468 scopus 로고    scopus 로고
    • Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene
    • Zuo, J., De Jager, P.L., Takahashi, K.A., Jiang, W., Linden, D.J. and Heintz, N. (1997) ‘Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene’, Nature 388: 769-773.
    • (1997) Nature , vol.388 , pp. 769-773
    • Zuo, J.1    De Jager, P.L.2    Takahashi, K.A.3    Jiang, W.4    Linden, D.J.5    Heintz, N.6


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