메뉴 건너뛰기




Volumn 71, Issue 2, 1996, Pages 749-758

A single tryptophan on M2 of glutamate receptor channels confers high permeability to divalent cations

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; AMPA RECEPTOR; BARIUM ION; CALCIUM ION; GLUTAMATE RECEPTOR; ION CHANNEL; KAINIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; RECEPTOR SUBTYPE; SODIUM ION; TRYPTOPHAN;

EID: 0029759751     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79274-3     Document Type: Article
Times cited : (18)

References (68)
  • 1
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit
    • Akabas, M. H., C. Kaufmann, P. Archdeacon, and A. Karlin. 1994. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit. Neuron. 13:919-927.
    • (1994) Neuron. , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 2
    • 0023929233 scopus 로고
    • The role of divalent cations in the N-methyl-D-aspartate responses of mouse central neurons in culture
    • Ascher, P., and L. Nowak. 1988. The role of divalent cations in the N-methyl-D-aspartate responses of mouse central neurons in culture. J. Physiol. (Lond.). 399:247-266.
    • (1988) J. Physiol. (Lond.) , vol.399 , pp. 247-266
    • Ascher, P.1    Nowak, L.2
  • 4
    • 0028819612 scopus 로고
    • Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining reentrant membrane loop
    • Bennett, J. A., and R. Dingledine. 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
  • 5
    • 0027209993 scopus 로고
    • A single amino acid determines the subunit-specific spider toxin block of α-amino-3-hydroxy-5-methylisoxazole-4-propionate/kainate receptor channels
    • Blaschke, M., B. U. Keller, R. Rivosecchi, M. Hollmann, S. F. Heinemann, and A. Konnerth. 1993. A single amino acid determines the subunit-specific spider toxin block of α-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.F.5    Konnerth, A.6
  • 6
    • 0026543243 scopus 로고
    • Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit
    • Burnashev, N., H. Monyer, P. H. Seeburg, and B. Sakmann. 1992a. Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit. Neuron. 8:189-198.
    • (1992) Neuron. , vol.8 , pp. 189-198
    • Burnashev, N.1    Monyer, H.2    Seeburg, P.H.3    Sakmann, B.4
  • 7
  • 8
    • 0027116042 scopus 로고
    • Bench to bedside - The glutamate connection
    • Choi, D. W. 1992. Bench to bedside - the glutamate connection. Science. 258:241-243.
    • (1992) Science , vol.258 , pp. 241-243
    • Choi, D.W.1
  • 9
    • 0025265926 scopus 로고
    • The role of glutamate neurotoxicity in hypoxic ischemic neuronal death
    • Choi, D. W., and S. M. Rothmann. 1990. The role of glutamate neurotoxicity in hypoxic ischemic neuronal death. Annu. Rev. Neurosci. 13: 171-182.
    • (1990) Annu. Rev. Neurosci. , vol.13 , pp. 171-182
    • Choi, D.W.1    Rothmann, S.M.2
  • 10
    • 0024829451 scopus 로고
    • Excitatory amino acid receptors in the vertebrate central nervous system
    • Collingridge, G. L., and R. A. J. Lester. 1989. Excitatory amino acid receptors in the vertebrate central nervous system. Pharmacol. Rev. 40:143-210.
    • (1989) Pharmacol. Rev. , vol.40 , pp. 143-210
    • Collingridge, G.L.1    Lester, R.A.J.2
  • 12
    • 0026534723 scopus 로고
    • In the GluR1 glutamate receptor subunit a glutamine to histidine point mutation suppresses inward rectification but not calcium permeability
    • Curutchet, P., P. Bochet, L. Prado de Calvalho, B. Lambolez, J. Stinnakre, and J. Rossier. 1992. In the GluR1 glutamate receptor subunit a glutamine to histidine point mutation suppresses inward rectification but not calcium permeability. Biochem. Biophys. Res. Commun. 182: 1089-1093.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1089-1093
    • Curutchet, P.1    Bochet, P.2    Prado De Calvalho, L.3    Lambolez, B.4    Stinnakre, J.5    Rossier, J.6
  • 13
    • 0026675738 scopus 로고
    • Structural determinants of barium permeation and rectification in non-NMDA receptor channels
    • Dingledine, R., R. I. Hume, and S. F. Heinemann. 1992. Structural determinants of barium permeation and rectification in non-NMDA 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
  • 14
    • 0027339321 scopus 로고
    • 2+ permeability of unedited and edited versions of the kainate selective glutamate receptor GluR6
    • 2+ permeability of unedited and edited versions of the kainate selective glutamate receptor GluR6. Proc. Natl. Acad. Sci. USA. 90:755-759.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 755-759
    • Egebjerg, J.1    Heinemann, S.F.2
  • 15
    • 0027336478 scopus 로고
    • A negative charge in the M2 transmembrane segment of the neuronal α7 acetylcholine receptor increases permeability to divalent cations
    • Ferrer-Montiel, A. V., and M. Montal. 1993. A negative charge in the M2 transmembrane segment of the neuronal α7 acetylcholine receptor increases permeability to divalent cations. FEBS Lett. 324:185-190.
    • (1993) FEBS Lett. , vol.324 , pp. 185-190
    • Ferrer-Montiel, A.V.1    Montal, M.2
  • 16
    • 0002930534 scopus 로고
    • Structure-function relations in ligand-gated ion channels: Reconstitution in lipid bilayers and heterologous expression in Xenopus oocytes
    • Ferrer-Montiel, A. V., and M. Montal. 1994. Structure-function relations in ligand-gated ion channels: reconstitution in lipid bilayers and heterologous expression in Xenopus oocytes. Methods: Companion to Methods Enzymol. 6:60-69.
    • (1994) Methods: Companion to Methods Enzymol. , vol.6 , pp. 60-69
    • Ferrer-Montiel, A.V.1    Montal, M.2
  • 17
    • 0029917198 scopus 로고    scopus 로고
    • Pentameric subunit stoichiometry of a neuronal glutamate receptor
    • Ferrer-Montiel, A. V., and M. Montal. 1996. Pentameric subunit stoichiometry of a neuronal glutamate receptor. Proc. Natl. Acad. Sci. USA. 93:2741-2744.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2741-2744
    • Ferrer-Montiel, A.V.1    Montal, M.2
  • 18
    • 3142607409 scopus 로고
    • Molecular design of an AMPA/KA receptor highly permeable to divalent cations
    • Ferrer-Montiel, A. V., W. Sun, and M. Montal. 1995a. Molecular design of an AMPA/KA receptor highly permeable to divalent cations. Biophys. J. 68:A149.
    • (1995) Biophys. J. , vol.68
    • Ferrer-Montiel, A.V.1    Sun, W.2    Montal, M.3
  • 19
    • 0028979826 scopus 로고
    • Molecular architecture of the NMDA receptor binding site for PCP and MK-801
    • Ferrer-Montiel, A. V., W. Sun, and M. Montal. 1995b. Molecular architecture of the NMDA receptor binding site for PCP and MK-801. Proc. Natl. Acad. Sci. USA. 92:8021-8025.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8021-8025
    • Ferrer-Montiel, A.V.1    Sun, W.2    Montal, M.3
  • 20
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • Galzi, J. L., A. Devillers-Thiéry, N. Hussy, S. Bertrand, J.-P. Changeux, and D. Bertrand. 1992. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature. 359:500-505.
    • (1992) Nature. , vol.359 , pp. 500-505
    • Galzi, J.L.1    Devillers-Thiéry, A.2    Hussy, N.3    Bertrand, S.4    Changeux, J.-P.5    Bertrand, D.6
  • 21
    • 0026596478 scopus 로고
    • Molecular neurobiology of glutamate receptors
    • Gasic, G. P., and M. Hollmann. 1992. Molecular neurobiology of glutamate receptors. Annu. Rev. Physiol. 54:507-536.
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 507-536
    • Gasic, G.P.1    Hollmann, M.2
  • 22
    • 0028105127 scopus 로고
    • Transfer of the scorpion toxin receptor to an insensitive potassium channel
    • Gross, A., T. Abramson, and R. MacKinnon. 1994. Transfer of the scorpion toxin receptor to an insensitive potassium channel. Neuron. 13: 961-966.
    • (1994) Neuron. , vol.13 , pp. 961-966
    • Gross, A.1    Abramson, T.2    MacKinnon, R.3
  • 23
    • 0025806145 scopus 로고
    • Permeation of calcium ions through non-NMDA glutamate channels in retinal bipolar cells
    • Gilbertson, T. A., R. Scobey, and M. Wilson. 1991. Permeation of calcium ions through non-NMDA glutamate channels in retinal bipolar cells. Science. 251:1613-1615.
    • (1991) Science , vol.251 , pp. 1613-1615
    • Gilbertson, T.A.1    Scobey, R.2    Wilson, M.3
  • 26
    • 0028596211 scopus 로고
    • N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann, M., C. Maron, and S. F. Heinemann. 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.F.3
  • 27
    • 0025784548 scopus 로고
    • Identification of a site in glutamate receptor subunits that controls calcium permeability
    • Hume, R. I., R. Dingledine, and S. F. Heinemann. 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
  • 28
    • 0025360229 scopus 로고
    • Permeation of calcium through excitatory amino acid receptor channels in cultured rat hippocampal neurons
    • Iino, M., S. Ozawa, and K. Tsuzuki. 1990. Permeation of calcium through excitatory amino acid receptor channels in cultured rat hippocampal neurons. J. Physiol. (Lond). 424:151-165.
    • (1990) J. Physiol. (Lond). , vol.424 , pp. 151-165
    • Iino, M.1    Ozawa, S.2    Tsuzuki, K.3
  • 29
    • 0027141145 scopus 로고
    • Calcium permeability of the N-methyl-D-aspartate receptor channel in hippocampal neurons in culture
    • Jahr, C. E., and C. F. Stevens. 1993. Calcium permeability of the N-methyl-D-aspartate receptor channel in hippocampal neurons in culture. Proc. Natl. Acad. Sci. USA. 90:11573-11577.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11573-11577
    • Jahr, C.E.1    Stevens, C.F.2
  • 30
    • 0027348039 scopus 로고
    • Synaptic transmission: A bidirectional and self-modifiable form of cell-cell communication
    • Jessell, T. M., and E. R. Kandel. 1993. Synaptic transmission: a bidirectional and self-modifiable form of cell-cell communication. Cell. 72/ Neuron. 10(Suppl.):1-30.
    • (1993) Cell. 72/ Neuron. 10 , Issue.SUPPL. , pp. 1-30
    • Jessell, T.M.1    Kandel, E.R.2
  • 31
    • 0028849250 scopus 로고
    • Molecular mechanisms controlling calcium entry through AMPA-type glutamate receptor channels
    • Jonas, P., and N. Burnashev. 1995. Molecular mechanisms controlling calcium entry through AMPA-type glutamate receptor channels. Neuron. 15:987-990.
    • (1995) Neuron. , vol.15 , pp. 987-990
    • Jonas, P.1    Burnashev, N.2
  • 32
    • 0027339892 scopus 로고
    • 2+ permeability in both TM1 and TM2 of high affinity kainate receptor channels: Diversity by RNA editing
    • 2+ permeability in both TM1 and TM2 of high affinity kainate receptor channels: diversity by RNA editing. Neuron. 10: 491-500.
    • (1993) Neuron. , vol.10 , pp. 491-500
    • Köhler, M.1    Burnashev, N.2    Sakmann, B.3    Seeburg, P.H.4
  • 33
    • 0023623129 scopus 로고
    • In vitro synthesis with SP6 RNA polymerase
    • Kreig, P. A., and D. A. Melton. 1984. In vitro synthesis with SP6 RNA polymerase. Methods Enzymol. 155:397-415.
    • (1984) Methods Enzymol. , vol.155 , pp. 397-415
    • Kreig, P.A.1    Melton, D.A.2
  • 34
    • 0027436998 scopus 로고
    • A mechanism for ion selectivity in potassium channels: Computational studies of cation-π interactions
    • Kumpf, R. A., and D. A. Dougherty. 1993. A mechanism for ion selectivity in potassium channels: computational studies of cation-π interactions. Science. 261:1708-1710.
    • (1993) Science , vol.261 , pp. 1708-1710
    • Kumpf, R.A.1    Dougherty, D.A.2
  • 35
    • 3142601590 scopus 로고
    • Probing the cytoplasmic face of the NMDA receptor channel pore in cysteine-substitution mutants
    • Kuner, T., L. P. Wollmuth, P. H. Seeburg. and B. Sakmann. 1995. Probing the cytoplasmic face of the NMDA receptor channel pore in cysteine-substitution mutants. Soc: Neurosci. Abstr. 21:85.
    • (1995) Soc: Neurosci. Abstr. , vol.21 , pp. 85
    • Kuner, T.1    Wollmuth, L.P.2    Seeburg, P.H.3    Sakmann, B.4
  • 36
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1991. Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204:125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 37
    • 0028206275 scopus 로고
    • Cloning, functional expression and pharmacological characterisation of human cDNAs encoding NMDA receptor NR1 and NR2A subunits
    • Le Bourdelles, B., K. A. Wafford, J. A. Kemp, G. Marshall, C. Bain, A. S. Wilcox, J. M. Sikela, and P. J. Whiting. 1994. Cloning, functional expression and pharmacological characterisation of human cDNAs encoding NMDA receptor NR1 and NR2A subunits. J. Neurochem. 62: 2091-2098.
    • (1994) J. Neurochem. , vol.62 , pp. 2091-2098
    • Le Bourdelles, B.1    Wafford, K.A.2    Kemp, J.A.3    Marshall, G.4    Bain, C.5    Wilcox, A.S.6    Sikela, J.M.7    Whiting, P.J.8
  • 38
    • 0018333437 scopus 로고
    • Ion-concentration dependence of the reversal potential and the single channel conductance of ion channels at the frog neuromuscular junction
    • Lewis, C. A. 1979. Ion-concentration dependence of the reversal potential and the single channel conductance of ion channels at the frog neuromuscular junction. J. Physiol. (Lond.). 286:417-445.
    • (1979) J. Physiol. (Lond.). , vol.286 , pp. 417-445
    • Lewis, C.A.1
  • 39
    • 0023492484 scopus 로고
    • Permeation and block of N-methyl-D-aspartic acid receptor channels by divalent cations in mouse cultured central neurons
    • Mayer, M. L., and G. L. Westbrook. 1987. Permeation and block of N-methyl-D-aspartic acid receptor channels by divalent cations in mouse cultured central neurons. J. Physiol. (Lond.). 394:501-527.
    • (1987) J. Physiol. (Lond.). , vol.394 , pp. 501-527
    • Mayer, M.L.1    Westbrook, G.L.2
  • 41
    • 0029012475 scopus 로고
    • Pore loops: An emerging theme in ion channel structure
    • McKinnon, R. 1995. Pore loops: an emerging theme in ion channel structure. Neuron. 14:889-892.
    • (1995) Neuron. , vol.14 , pp. 889-892
    • McKinnon, R.1
  • 42
    • 0021646375 scopus 로고
    • Chloride current induced by injection of calcium into Xenopus oocytes
    • Miledi, R., and I. Parker. 1984. Chloride current induced by injection of calcium into Xenopus oocytes. J. Physiol. (Lond.). 357:173-183.
    • (1984) J. Physiol. (Lond.) , vol.357 , pp. 173-183
    • Miledi, R.1    Parker, I.2
  • 44
    • 0029150299 scopus 로고
    • Design of molecular function: Channels of communication
    • Montai, M. 1995. Design of molecular function: channels of communication. Annu. Rev. Biophys. Biomol. Struct. 24:31-57.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 31-57
    • Montai, M.1
  • 46
    • 0026437728 scopus 로고
    • Molecular diversity of glutamate receptors and implications for brain function
    • Nakanishi, S. 1992. Molecular diversity of glutamate receptors and implications for brain function. Science. 258:597-603.
    • (1992) Science , vol.258 , pp. 597-603
    • Nakanishi, S.1
  • 47
    • 0028340001 scopus 로고
    • Molecular diversity and functions of glutamate receptors
    • Nakanishi, S., and M. Masu. 1994. Molecular diversity and functions of glutamate receptors. Annu. Rev. Biophys. Biomol. Struct. 23:319-348.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 319-348
    • Nakanishi, S.1    Masu, M.2
  • 48
    • 0029111692 scopus 로고
    • Transient and persistent phosphorylation of AMPA-type glutamate receptor subunits in cerebellar Purkinje cells
    • Nakazawa, K., S. Mikawa, T. Hashikawa, and M. Ito. 1995. Transient and persistent phosphorylation of AMPA-type glutamate receptor subunits in cerebellar Purkinje cells. Neuron. 15:697-709.
    • (1995) Neuron. , vol.15 , pp. 697-709
    • Nakazawa, K.1    Mikawa, S.2    Hashikawa, T.3    Ito, M.4
  • 49
    • 0025304789 scopus 로고
    • Excitotoxic amino acid and neuropsychiatric disorders
    • Olney, J. W. 1990. Excitotoxic amino acid and neuropsychiatric disorders. Annu. Rev. Pharmacol. Toxicol. 30:47-71.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 47-71
    • Olney, J.W.1
  • 50
    • 0027200341 scopus 로고
    • Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain
    • Planells-Cases, R., W. Sun, A. V. Ferrer-Montiel, and M. Montal. 1994. Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain. Proc. Natl. Acad. Sci. USA. 90:5057-5061.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5057-5061
    • Planells-Cases, R.1    Sun, W.2    Ferrer-Montiel, A.V.3    Montal, M.4
  • 51
    • 0027970167 scopus 로고
    • PVP-containing solutions for analysis of divalent cation-dependent NMDA responses in Xenopus oocytes
    • Raditsch, M., and V. Witzemann. 1994. PVP-containing solutions for analysis of divalent cation-dependent NMDA responses in Xenopus oocytes. FEBS Lett. 354:177-182.
    • (1994) FEBS Lett. , vol.354 , pp. 177-182
    • Raditsch, M.1    Witzemann, V.2
  • 52
    • 0027412240 scopus 로고
    • Phosphorylation and modulation of recombinant GluR6 glutamate receptors by cAMP-dependent protein kinase
    • Raymond, L. A., C. D. Blackstone, and R. L. Huganir. 1993. Phosphorylation and modulation of recombinant GluR6 glutamate receptors by cAMP-dependent protein kinase. Nature. 361:637-641.
    • (1993) Nature , vol.361 , pp. 637-641
    • Raymond, L.A.1    Blackstone, C.D.2    Huganir, R.L.3
  • 53
    • 0028242501 scopus 로고
    • Transmembrane topology of the glutamate receptor subunit GluR6
    • Roche, K. W., L. A. Raymond, D. Blackstone, and R. L. Huganir. 1994. Transmembrane topology of the glutamate receptor subunit GluR6. J. Biol. Chem. 269:11679-11682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11679-11682
    • Roche, K.W.1    Raymond, L.A.2    Blackstone, D.3    Huganir, R.L.4
  • 54
    • 0027339551 scopus 로고
    • 2+ and channel blockers by a single amino acid substitution in the N-methyl-D-aspartate receptor
    • 2+ 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
  • 55
    • 0025995296 scopus 로고
    • RNA editing in brain controls a determinant of ion flow in glutamate-gated channels
    • Sommer, B., M. Köhler, R. Sprengel, and P. H. Seeburg. 1991. RNA editing in brain controls a determinant of ion flow in glutamate-gated channels. Cell. 67:11-20.
    • (1991) Cell , vol.67 , pp. 11-20
    • Sommer, B.1    Köhler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 56
    • 0028559605 scopus 로고
    • Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
    • Stern-Bach, Y., B. Bettler, M. Hartley, P. O. Sheppard, P. J. O'Hara, and S. F. Heinemann. 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
  • 57
    • 0027348873 scopus 로고
    • Quantal release of neurotransmitter and long-term potentiation
    • Stevens, C. F. 1993. Quantal release of neurotransmitter and long-term potentiation. Cell. 72/Neuron. 10(Suppl.):55-63.
    • (1993) Cell. 72/Neuron. 10 , Issue.SUPPL. , pp. 55-63
    • Stevens, C.F.1
  • 59
    • 0029966280 scopus 로고    scopus 로고
    • Three-dimensional models of non-NMDA glutamate receptors
    • Sutcliffe, M. J., G. Z. Wo, and R. E. Oswald. 1996. Three-dimensional models of non-NMDA glutamate receptors. Biophys. J. 70:1575-1589.
    • (1996) Biophys. J. , vol.70 , pp. 1575-1589
    • Sutcliffe, M.J.1    Wo, G.Z.2    Oswald, R.E.3
  • 60
    • 0028224795 scopus 로고
    • A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides
    • Taverna, F. A., L. Wang, J. F. McDonald, and D. R. Hampson. 1994. A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides. J. Biol. Chem. 269:14159-14164.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14159-14164
    • Taverna, F.A.1    Wang, L.2    McDonald, J.F.3    Hampson, D.R.4
  • 61
    • 0027348041 scopus 로고
    • Neurotransmitter action: Opening of ligand-gated ion channels
    • Unwin, N. 1993a. Neurotransmitter action: opening of ligand-gated ion channels. Cell. 72/Neuron. 10(Suppl.):31-41.
    • (1993) Cell. 72/Neuron. 10 , Issue.SUPPL. , pp. 31-41
    • Unwin, N.1
  • 62
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin, N. 1993b. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol Biol. 229:1101-1124.
    • (1993) J. Mol Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 63
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. 1995. Acetylcholine receptor channel imaged in the open state. Nature. 373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 64
    • 0025879427 scopus 로고
    • Structural determinants of ion flow through recombinant glutamate receptor channels
    • Verdoorn, T. A., N. Burnashev, H. Monyer, P. H. Seeburg, and B. Sakmann. 1991. Structural determinants of ion flow through recombinant glutamate receptor channels. Science. 252:1715-1718.
    • (1991) Science , vol.252 , pp. 1715-1718
    • Verdoorn, T.A.1    Burnashev, N.2    Monyer, H.3    Seeburg, P.H.4    Sakmann, B.5
  • 65
    • 0027407112 scopus 로고
    • Phosphorylation and modulation of a kainate receptor, GluR6, by cAMP-dependent protein kinase
    • Wang, L.-Y., F. A. Taverna, X.-P. Huang, J. F. McDonald, and D. R. Hampson. 1993. Phosphorylation and modulation of a kainate receptor, GluR6, by cAMP-dependent protein kinase. Science. 259:1173-1175.
    • (1993) Science , vol.259 , pp. 1173-1175
    • Wang, L.-Y.1    Taverna, F.A.2    Huang, X.-P.3    McDonald, J.F.4    Hampson, D.R.5
  • 66
    • 0028364252 scopus 로고
    • Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation
    • Wo, Z. G., and R. E. Oswald. 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
  • 67
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo, Z. G., and R. E. Oswald. 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.G.1    Oswald, R.E.2
  • 68
    • 0027983013 scopus 로고
    • Ionic permeability characteristics of the N-methyl-D-aspartate receptor channel
    • Zarei, M. M., and J. A. Dani. 1994. Ionic permeability characteristics of the N-methyl-D-aspartate receptor channel. J. Gen. Physiol. 103:231-248.
    • (1994) J. Gen. Physiol. , vol.103 , pp. 231-248
    • Zarei, M.M.1    Dani, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.