메뉴 건너뛰기




Volumn 120, Issue , 1999, Pages 61-80

Evolving view of quaternary structures of ligand-gated ion channels

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE RECEPTOR; ION CHANNEL; NICOTINIC RECEPTOR; POTASSIUM CHANNEL; PURINE P2X RECEPTOR; TETRAMER;

EID: 0032849974     PISSN: 00796123     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0079-6123(08)63546-3     Document Type: Review
Times cited : (7)

References (144)
  • 1
    • 0028809730 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α-subunit
    • M.H. Akabas A. Karlin Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α-subunit Biochemistry 34 1995 12496 12500
    • (1995) Biochemistry , vol.34 , pp. 12496-12500
    • Akabas, M.H.1    Karlin, A.2
  • 2
    • 0025856536 scopus 로고
    • Neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes have a pentameric quaternary structure
    • R. Anand Conroy W.G. R. Schoepfer Whiting P. J. Lindstrom Neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes have a pentameric quaternary structure J. Biol. Chem. 266 1991 11192 11198
    • (1991) J. Biol. Chem. , vol.266 , pp. 11192-11198
    • Anand, R.1    Conroy, W.G.2    Schoepfer, R.3    Whiting, P.4    Lindstrom, J.5
  • 3
    • 0027185380 scopus 로고
    • Homomeric and native α7 acetylcholine receptors exhibit remarkably similar but non-identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex
    • R. Anand X. Peng J. Lindstrom Homomeric and native α7 acetylcholine receptors exhibit remarkably similar but non-identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex FEBS Lett. 327 1993 241 246
    • (1993) FEBS Lett. , vol.327 , pp. 241-246
    • Anand, R.1    Peng, X.2    Lindstrom, J.3
  • 6
    • 0030900752 scopus 로고    scopus 로고
    • Ionotropic glutamate receptors: New types and new concepts
    • E.A. Barnard Ionotropic glutamate receptors: New types and new concepts Trends Pharmacol. Sci. 18 1997 141 148
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 141-148
    • Barnard, E.A.1
  • 7
    • 0031242254 scopus 로고    scopus 로고
    • Nucleotide receptors in the nervous system. An abundant component using diverse transduction mechanisms
    • E.A. Barnard J. Simon T.E. Webb Nucleotide receptors in the nervous system. An abundant component using diverse transduction mechanisms Mol. Neurobiol. 15 1997 103 129
    • (1997) Mol. Neurobiol. , vol.15 , pp. 103-129
    • Barnard, E.A.1    Simon, J.2    Webb, T.E.3
  • 8
    • 0026612038 scopus 로고
    • Pharmacology and electrophysiology of ATP-activated ion channels
    • B.P. Bean Pharmacology and electrophysiology of ATP-activated ion channels Trends Pharmacol. Sci. 13 1992 87 90
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 87-90
    • Bean, B.P.1
  • 9
    • 0025119185 scopus 로고
    • Ligand-gated ion channels in the brain: The amino acid receptor superfamily
    • H. Betz Ligand-gated ion channels in the brain: The amino acid receptor superfamily Neuron 5 1990 383 392
    • (1990) Neuron , vol.5 , pp. 383-392
    • Betz, H.1
  • 10
    • 0026584503 scopus 로고
    • Biochemical characterization and localization of a non-N-methyl-D-aspartate glutamate receptor in rat brain
    • C.D. Blackstone S.J. Moss Martin L.J. A.I. Levey D.L. Price Huganir R.L. Biochemical characterization and localization of a non- N -methyl-D-aspartate glutamate receptor in rat brain J. Neurochem. 58 1992 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
  • 11
    • 0029813032 scopus 로고    scopus 로고
    • Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli
    • P. Blount S.I. Sukharev P.C. Moe M.J. Schroeder H.R. Guy Kung C. Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli EMBO J. 15 1996 4798 4805
    • (1996) EMBO J. , vol.15 , pp. 4798-4805
    • Blount, P.1    Sukharev, S.I.2    Moe, P.C.3    Schroeder, M.J.4    Guy, H.R.5    Kung, C.6
  • 12
    • 0026781536 scopus 로고
    • Solubilization and molecular size determination of the P2X purinoceptor from rat vas deferens
    • X. Bo J. Simon G. Burnstock E.A. Barnard Solubilization and molecular size determination of the P2X purinoceptor from rat vas deferens J. Biol. Chem. 267 1992 17581 17587
    • (1992) J. Biol. Chem. , vol.267 , pp. 17581-17587
    • Bo, X.1    Simon, J.2    Burnstock, G.3    Barnard, E.A.4
  • 13
    • 0028875979 scopus 로고
    • A P2X purinoceptor cDNA conferring a novel pharmacological profile
    • X.N. Bo Y. Zhang M. Nassar G. Burnstock R. Schoepfer A P2X purinoceptor cDNA conferring a novel pharmacological profile FEBS Lett. 375 1995 129 133
    • (1995) FEBS Lett. , vol.375 , pp. 129-133
    • Bo, X.N.1    Zhang, Y.2    Nassar, M.3    Burnstock, G.4    Schoepfer, R.5
  • 14
    • 0028985075 scopus 로고
    • Ultrastructure of the 5-hydroxytryptamine3 receptor
    • F.G. Boess R. Beroukhim I.L. Martin Ultrastructure of the 5-hydroxytryptamine3 receptor J. Neurochem. 64 1995 1401 1405
    • (1995) J. Neurochem. , vol.64 , pp. 1401-1405
    • Boess, F.G.1    Beroukhim, R.2    Martin, I.L.3
  • 15
    • 0026725944 scopus 로고
    • Molecular properties of 5-hydroxytryptamine3 receptor-type binding sites purified from NG108–15 cells
    • F.G. Boess S.C. Lummis I.L. Martin Molecular properties of 5-hydroxytryptamine3 receptor-type binding sites purified from NG108–15 cells J. Neurochem. 59 1992 1692 1701
    • (1992) J. Neurochem. , vol.59 , pp. 1692-1701
    • Boess, F.G.1    Lummis, S.C.2    Martin, I.L.3
  • 17
    • 0028025001 scopus 로고
    • Structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • A.J. Brake M.J. Wagenbach D. Julius Structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor Nature 371 1994 519 523
    • (1994) Nature , vol.371 , pp. 519-523
    • Brake, A.J.1    Wagenbach, M.J.2    Julius, D.3
  • 19
    • 0021930295 scopus 로고
    • Quaternary structure of the acetylcholine receptor
    • A. Brisson P.N. Unwin Quaternary structure of the acetylcholine receptor Nature 315 1985 474 477
    • (1985) Nature , vol.315 , pp. 474-477
    • Brisson, A.1    Unwin, P.N.2
  • 20
    • 0027490681 scopus 로고
    • Protein chemical characterization and immunocytochemical localization of the NMDA receptor subunit NMDA R1
    • N. Brose G.P. Gasic D.E. Vetter Sullivan J.M. S.F. Heinemann Protein chemical characterization and immunocytochemical localization of the NMDA receptor subunit NMDA R1 J. Biol. Chem. 268 1993 22663 22671
    • (1993) J. Biol. Chem. , vol.268 , pp. 22663-22671
    • Brose, N.1    Gasic, G.P.2    Vetter, D.E.3    Sullivan, J.M.4    Heinemann, S.F.5
  • 22
    • 0029671045 scopus 로고    scopus 로고
    • An antagonist-insensitive P2X receptor expressed in epithelia and brain
    • G. Buell C. Lewis G. Collo R.A. North A. Surprenant An antagonist-insensitive P2X receptor expressed in epithelia and brain EMBO J. 15 1996 55 62
    • (1996) EMBO J. , vol.15 , pp. 55-62
    • Buell, G.1    Lewis, C.2    Collo, G.3    North, R.A.4    Surprenant, A.5
  • 23
    • 0018191759 scopus 로고
    • Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor
    • Cake M.H. D.M. DiSorbo G. Litwack Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor J. Biol. Chem. 253 1978 4886 4891
    • (1978) J. Biol. Chem. , vol.253 , pp. 4886-4891
    • Cake, M.H.1    DiSorbo, D.M.2    Litwack, G.3
  • 26
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • G. Chang R.H. Spencer A.T. Lee M.T. Barclay D.C. Rees Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel Science 282 1998 2220 2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 27
    • 0029664746 scopus 로고    scopus 로고
    • Stoichiometry of a recombinant GABAA receptor
    • Y. Chang R. Wang S. Barot D.S. Weiss Stoichiometry of a recombinant GABAA receptor J. Neurosci. 16 1996 5415 5424
    • (1996) J. Neurosci. , vol.16 , pp. 5415-5424
    • Chang, Y.1    Wang, R.2    Barot, S.3    Weiss, D.S.4
  • 30
    • 0025615542 scopus 로고
    • Modelling of binding sites of the nicotinic acetylcholine receptor and their relation to models of the whole receptor
    • V.B. Cockcroft G.G. Lunt D.J. Osguthorpe Modelling of binding sites of the nicotinic acetylcholine receptor and their relation to models of the whole receptor Biochem. Soc. Symp. 57 1990 65 79
    • (1990) Biochem. Soc. Symp. , vol.57 , pp. 65-79
    • Cockcroft, V.B.1    Lunt, G.G.2    Osguthorpe, D.J.3
  • 31
    • 0027420865 scopus 로고
    • Homologies and disparities of glutamate receptors: A critical analysis
    • V.B. Cockcroft M.O. Ortells P. Thomas G.G. Lunt Homologies and disparities of glutamate receptors: A critical analysis Neurochem. Int. 23 1993 583 594
    • (1993) Neurochem. Int. , vol.23 , pp. 583-594
    • Cockcroft, V.B.1    Ortells, M.O.2    Thomas, P.3    Lunt, G.G.4
  • 32
    • 0029665752 scopus 로고    scopus 로고
    • Cloning of P2X5 and P2X6 receptors and the distribution and properties of an extended family of ATP-gated ion channels
    • G. Collo North R.A. E. Kawashima E. Merlo-Pich S. Neidhart A. Surprenant G. Buell Cloning of P2X5 and P2X6 receptors and the distribution and properties of an extended family of ATP-gated ion channels J. Neurosci. 16 1996 2495 2507
    • (1996) J. Neurosci. , vol.16 , pp. 2495-2507
    • Collo, G.1    North, R.A.2    Kawashima, E.3    Merlo-Pich, E.4    Neidhart, S.5    Surprenant, A.6    Buell, G.7
  • 33
    • 0025828670 scopus 로고
    • Pentameric structure and subunit stoichiometry of a neuronal nicotinic acetylcholine receptor
    • E. Cooper Couturier S. Ballivet M. Pentameric structure and subunit stoichiometry of a neuronal nicotinic acetylcholine receptor Nature 350 1991 235 238
    • (1991) Nature , vol.350 , pp. 235-238
    • Cooper, E.1    Couturier, S.2    Ballivet, M.3
  • 34
    • 0032570801 scopus 로고    scopus 로고
    • Number and stoichiometry of subunits in the native atrial G-protein-gated K* channel, IKACh
    • S. Corey Krapivinsky G. L. Krapivinsky D.E. Clapham Number and stoichiometry of subunits in the native atrial G-protein-gated K* channel, IKACh J. Biol. Chem. 273 1998 5271 5278
    • (1998) J. Biol. Chem. , vol.273 , pp. 5271-5278
    • Corey, S.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 35
    • 0032478834 scopus 로고    scopus 로고
    • The Phe-Met-Arg-Phe-amide-activated sodium channel is a tetramer
    • S. Coscoy Lingueglia E. M. Lazdunski P. Barbry The Phe-Met-Arg-Phe-amide-activated sodium channel is a tetramer J. Biol. Chem. 273 1998 8317 8322
    • (1998) J. Biol. Chem. , vol.273 , pp. 8317-8322
    • Coscoy, S.1    Lingueglia, E.2    Lazdunski, M.3    Barbry, P.4
  • 36
    • 0031596905 scopus 로고    scopus 로고
    • From GABAA receptor diversity emerges a unified vision of GABAergic inhibition
    • E. Costa From GABAA receptor diversity emerges a unified vision of GABAergic inhibition Annu. Rev. Pharmacol. Toxicol. 38 1998 321 350
    • (1998) Annu. Rev. Pharmacol. Toxicol. , vol.38 , pp. 321-350
    • Costa, E.1
  • 37
    • 0030866749 scopus 로고    scopus 로고
    • Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli
    • C.C. Cruickshank R.F. Minchin A.C. Le Dain B. Martinac Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli Biophys. J. 73 1997 1925 1931
    • (1997) Biophys. J. , vol.73 , pp. 1925-1931
    • Cruickshank, C.C.1    Minchin, R.F.2    Le Dain, A.C.3    Martinac, B.4
  • 39
    • 0029072385 scopus 로고
    • Structure and function of glutamate and nicotinic acetylcholine receptors
    • J.A. Dani M.L. Mayer Structure and function of glutamate and nicotinic acetylcholine receptors Curr. Opin. Neurobiol. 5 1995 310 317
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 310-317
    • Dani, J.A.1    Mayer, M.L.2
  • 41
    • 0027393311 scopus 로고
    • Core sequence of ATP regulatory module in receptor guanylate cyclases
    • T. Duda Goraczniak R.M. R.K. Sharma Core sequence of ATP regulatory module in receptor guanylate cyclases FEBS Lett. 315 1993 143 148
    • (1993) FEBS Lett. , vol.315 , pp. 143-148
    • Duda, T.1    Goraczniak, R.M.2    Sharma, R.K.3
  • 42
    • 0032053981 scopus 로고    scopus 로고
    • A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method
    • T.M. Egan Haines W.R. M.M. Voigt A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method J. Neurosci. 18 1998 2350 2359
    • (1998) J. Neurosci. , vol.18 , pp. 2350-2359
    • Egan, T.M.1    Haines, W.R.2    Voigt, M.M.3
  • 43
  • 44
    • 0032056332 scopus 로고    scopus 로고
    • Molecular composition of GABAc receptors
    • R. Enz G.R. Cutting Molecular composition of GABAc receptors Vision Res. 38 1998 1431 1441
    • (1998) Vision Res. , vol.38 , pp. 1431-1441
    • Enz, R.1    Cutting, G.R.2
  • 45
    • 0029088454 scopus 로고
    • Pharmacological characterization of heterologously expressed ATP-gated cation channels (P2x purinoceptors)
    • R.J. Evans C. Lewis G. Buell S. Valera North R.A. A. Surprenant Pharmacological characterization of heterologously expressed ATP-gated cation channels (P2x purinoceptors) Mol. Pharmacol. 48 1995 178 183
    • (1995) Mol. Pharmacol. , vol.48 , pp. 178-183
    • Evans, R.J.1    Lewis, C.2    Buell, G.3    Valera, S.4    North, R.A.5    Surprenant, A.6
  • 46
    • 0029955763 scopus 로고    scopus 로고
    • Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed in mammalian cells
    • R.J. Evans C. Lewis C. Virginio K. Lundstrom G. Buell A. Surprenant R.A. North Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed in mammalian cells J. Physiol. (Lond.) 497 1996 413 422
    • (1996) J. Physiol. (Lond.) , vol.497 , pp. 413-422
    • Evans, R.J.1    Lewis, C.2    Virginio, C.3    Lundstrom, K.4    Buell, G.5    Surprenant, A.6    North, R.A.7
  • 47
    • 0029917198 scopus 로고    scopus 로고
    • Pentameric subunit stoichiometry of a neuronal glutamate receptor
    • A.V. Ferrer-Montiel M. Montal Pentameric subunit stoichiometry of a neuronal glutamate receptor Proc. Natl. Acad. Sci. USA 93 1996 2741 2744
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2741-2744
    • Ferrer-Montiel, A.V.1    Montal, M.2
  • 48
    • 0032518665 scopus 로고    scopus 로고
    • The heterotetrameric architecture of the epithelial sodium channel (ENaC)
    • D. Firsov I. Gautschi A.M. Merillat Rossier B.C. L. Schild The heterotetrameric architecture of the epithelial sodium channel (ENaC) EMBO J. 17 1998 344 352
    • (1998) EMBO J. , vol.17 , pp. 344-352
    • Firsov, D.1    Gautschi, I.2    Merillat, A.M.3    Rossier, B.C.4    Schild, L.5
  • 49
    • 0032029114 scopus 로고    scopus 로고
    • Evidence that porcine native 5-HT3 receptors do not contain nicotinic acetylcholine receptor subunits
    • S. Fletcher J.M. Lindstrom R.M. McKernan N.M. Barnes Evidence that porcine native 5-HT3 receptors do not contain nicotinic acetylcholine receptor subunits Neuropharmacology 37 1998 397 399
    • (1998) Neuropharmacology , vol.37 , pp. 397-399
    • Fletcher, S.1    Lindstrom, J.M.2    McKernan, R.M.3    Barnes, N.M.4
  • 50
    • 0031668776 scopus 로고    scopus 로고
    • ATP binding site of P2X channel proteins: Structural similarities with class II aminoacyl-tRNA synthetases
    • W. Freist J.F. Verhey W. Stühmer Gauss D.H. ATP binding site of P2X channel proteins: Structural similarities with class II aminoacyl-tRNA synthetases FEBS Lett. 434 1998 61 65
    • (1998) FEBS Lett. , vol.434 , pp. 61-65
    • Freist, W.1    Verhey, J.F.2    Stühmer, W.3    Gauss, D.H.4
  • 51
    • 0028031541 scopus 로고
    • Neurotransmitter-gated ion channels as unconventional allosteric proteins
    • J.L. Galzi J.P. Changeux Neurotransmitter-gated ion channels as unconventional allosteric proteins Curr. Opin. Struct. Biol. 4 1994 554 565
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 554-565
    • Galzi, J.L.1    Changeux, J.P.2
  • 52
    • 0029046913 scopus 로고
    • Neuronal nicotinic receptors: molecular organization and regulations
    • J.L. Galzi J.P. Changeux Neuronal nicotinic receptors: molecular organization and regulations Neuropharmacology 34 1995 563 582
    • (1995) Neuropharmacology , vol.34 , pp. 563-582
    • Galzi, J.L.1    Changeux, J.P.2
  • 53
    • 0031033013 scopus 로고    scopus 로고
    • Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue
    • M. Garcia-Guzman F. Soto Gomez-Hernandez J.M. P.E. Lund W. Stühmer Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue Mol. Pharmaccl. 51 1997 109 118
    • (1997) Mol. Pharmaccl. , vol.51 , pp. 109-118
    • Garcia-Guzman, M.1    Soto, F.2    Gomez-Hernandez, J.M.3    Lund, P.E.4    Stühmer, W.5
  • 54
    • 0030591421 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a novel rat heart P2X purinoceptor
    • M. Garcia-Guzman F. Soto B. Laube W. Stühmer Molecular cloning and functional expression of a novel rat heart P2X purinoceptor FEBS Lett. 388 1996 123 127
    • (1996) FEBS Lett. , vol.388 , pp. 123-127
    • Garcia-Guzman, M.1    Soto, F.2    Laube, B.3    Stühmer, W.4
  • 55
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering
    • Y. Gavel G. Von Heijne Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering Protein Eng. 3 1990 433 442
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 57
    • 0028916670 scopus 로고
    • Expression of recombinant homo-oligomeric 5-hydroxytryptamine3 receptors provides new insights into their maturation and structure
    • Green T. K.A. Stauffer S.C. Lummis Expression of recombinant homo-oligomeric 5-hydroxytryptamine3 receptors provides new insights into their maturation and structure J. Biol. Chem. 270 1995 6056 6061
    • (1995) J. Biol. Chem. , vol.270 , pp. 6056-6061
    • Green, T.1    Stauffer, K.A.2    Lummis, S.C.3
  • 61
    • 0030011258 scopus 로고    scopus 로고
    • The emerging three-dimensional structure of a receptor. The nicotinic acetylcholine receptor
    • Hucho F. Tsetlin V.I. J. Machold The emerging three-dimensional structure of a receptor. The nicotinic acetylcholine receptor Eur. J. Biochem. 239 1996 539 557
    • (1996) Eur. J. Biochem. , vol.239 , pp. 539-557
    • Hucho, F.1    Tsetlin, V.I.2    Machold, J.3
  • 62
    • 0027078418 scopus 로고
    • Cooperative interactions among subunits of a voltage-dependent potassium channel. Evidence from expression of concatenated cDNAs
    • R.S. Hurst M.P. Kavanaugh J. Yakel J.P. Adelman R.A. North Cooperative interactions among subunits of a voltage-dependent potassium channel. Evidence from expression of concatenated cDNAs J. Biol. Chem. 267 1992 23742 23745
    • (1992) J. Biol. Chem. , vol.267 , pp. 23742-23745
    • Hurst, R.S.1    Kavanaugh, M.P.2    Yakel, J.3    Adelman, J.P.4    North, R.A.5
  • 63
    • 0028788140 scopus 로고
    • Chloride channel expression with the tandem construct of α6-β2 GABAA receptor subunit requires a monomeric subunit of α6 or γ2
    • W.B. Im J.F. Pregenzer J.A. Binder G.H. Dillon G.L. Alberts Chloride channel expression with the tandem construct of α6-β2 GABAA receptor subunit requires a monomeric subunit of α6 or γ2 J. Biol. Chem. 270 1995 26063 26066
    • (1995) J. Biol. Chem. , vol.270 , pp. 26063-26066
    • Im, W.B.1    Pregenzer, J.F.2    Binder, J.A.3    Dillon, G.H.4    Alberts, G.L.5
  • 64
    • 0028933233 scopus 로고
    • Cloning and functional characterization of a novel ATP-sensitive potassium channel ubiquitously expressed in rat tissues, including pancreatic islets, pituitary, skeletal muscle, and heart
    • N. Inagaki Tsuura Y. N. Namba K. Masuda T. Gonoi M. Horie Seino Y. M. Mizuta S. Seino Cloning and functional characterization of a novel ATP-sensitive potassium channel ubiquitously expressed in rat tissues, including pancreatic islets, pituitary, skeletal muscle, and heart J. Biol. Chem. 270 1995 5691 5694
    • (1995) J. Biol. Chem. , vol.270 , pp. 5691-5694
    • Inagaki, N.1    Tsuura, Y.2    Namba, N.3    Masuda, K.4    Gonoi, T.5    Horie, M.6    Seino, Y.7    Mizuta, M.8    Seino, S.9
  • 66
    • 0030222776 scopus 로고    scopus 로고
    • GABAC receptors: Relatively simple transmitter-gated ion channels?
    • G.A.R. Johnston GABAC receptors: Relatively simple transmitter-gated ion channels? Trends Pharmacol. Sci. 17 1996 319 323
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 319-323
    • Johnston, G.A.R.1
  • 67
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • A. Karlin M.H. Akabas Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins Neuron. 15 1995 1231 1244
    • (1995) Neuron. , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 68
    • 0025743037 scopus 로고
    • Interaction between tetraethylammonium and amino acid residues in the pore of cloned voltage-dependent potassium channels
    • M.P. Kavanaugh M.D. Varnum P.B. Osborne M.J. Christie A.E. Busch J.P. Adelman R.A. North Interaction between tetraethylammonium and amino acid residues in the pore of cloned voltage-dependent potassium channels J. Biol. Chem. 266 1991 7583 7587
    • (1991) J. Biol. Chem. , vol.266 , pp. 7583-7587
    • Kavanaugh, M.P.1    Varnum, M.D.2    Osborne, P.B.3    Christie, M.J.4    Busch, A.E.5    Adelman, J.P.6    North, R.A.7
  • 69
    • 0029099458 scopus 로고
    • A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem
    • K.A. Ketchum W.J. Joiner A.J. Sellers L.K. Kaczmarek S.A.N. Goldstein A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem Nature 376 1995 690 695
    • (1995) Nature , vol.376 , pp. 690-695
    • Ketchum, K.A.1    Joiner, W.J.2    Sellers, A.J.3    Kaczmarek, L.K.4    Goldstein, S.A.N.5
  • 70
    • 0028986090 scopus 로고
    • Electrophysiological properties of P2X purinoceptors in rat superior cervical, nodose and guinea-pig coeliac neurones
    • B.S. Khakh P.P.A. Humphrey A. Surprenant Electrophysiological properties of P2X purinoceptors in rat superior cervical, nodose and guinea-pig coeliac neurones J. Physiol. (Lond.) 484 1995 385 395
    • (1995) J. Physiol. (Lond.) , vol.484 , pp. 385-395
    • Khakh, B.S.1    Humphrey, P.P.A.2    Surprenant, A.3
  • 72
    • 0027723681 scopus 로고
    • Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons
    • J. Kirsch Wolters I. A. Triller H. Betz Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons Nature 366 1993 745 748
    • (1993) Nature , vol.366 , pp. 745-748
    • Kirsch, J.1    Wolters, I.2    Triller, A.3    Betz, H.4
  • 73
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • E.V. Koonin A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif J. Mol. Biol. 229 1993 1165 1174
    • (1993) J. Mol. Biol. , vol.229 , pp. 1165-1174
    • Koonin, E.V.1
  • 75
    • 0029044590 scopus 로고
    • The inhibitory glycine receptor: architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex
    • J. Kuhse Betz H. J. Kirsch The inhibitory glycine receptor: architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex Curr. Opin. Neurobiol. 5 1995 318 323
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 318-323
    • Kuhse, J.1    Betz, H.2    Kirsch, J.3
  • 76
    • 0027716526 scopus 로고
    • Assembly of the inhibitory glycine receptor: Identification of amino acid sequence motifs governing subunit stoichiometry
    • J. Kuhse B. Laube D. Magalei H. Betz Assembly of the inhibitory glycine receptor: Identification of amino acid sequence motifs governing subunit stoichiometry Neuron 11 1993 1049 1056
    • (1993) Neuron , vol.11 , pp. 1049-1056
    • Kuhse, J.1    Laube, B.2    Magalei, D.3    Betz, H.4
  • 77
    • 0030220889 scopus 로고    scopus 로고
    • Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines
    • T. Kuner Wollmuth I.P. A. Karlin P.H. Seeburg B. Sakmann Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines Neuron 17 1996 343 352
    • (1996) Neuron , vol.17 , pp. 343-352
    • Kuner, T.1    Wollmuth, I.P.2    Karlin, A.3    Seeburg, P.H.4    Sakmann, B.5
  • 78
    • 0030440992 scopus 로고    scopus 로고
    • Design and pharmacology of selective P2-purinoceptor antagonists
    • G. Lambrecht Design and pharmacology of selective P2-purinoceptor antagonists J. Auton. Pharmacol. 16 1996 341 344
    • (1996) J. Auton. Pharmacol. , vol.16 , pp. 341-344
    • Lambrecht, G.1
  • 79
    • 0001202076 scopus 로고
    • Conserved quarternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer
    • D. Langosch Thomas L. H. Betz Conserved quarternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer Proc. Natl. Acad. Sci. USA 85 1988 7394 7398
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7394-7398
    • Langosch, D.1    Thomas, L.2    Betz, H.3
  • 80
    • 0032523002 scopus 로고    scopus 로고
    • Evidence for a tetrameric structure of recombinant NMDA receptors
    • B. Laube J. Kuhse H. Betz Evidence for a tetrameric structure of recombinant NMDA receptors J. Neurosci. 18 1998 2954 2961
    • (1998) J. Neurosci. , vol.18 , pp. 2954-2961
    • Laube, B.1    Kuhse, J.2    Betz, H.3
  • 81
    • 0032529842 scopus 로고    scopus 로고
    • Central P2X4 and P2X6 channel subunits coassemble into a novel heteromeric ATP receptor
    • Lě K.T. K. Babinski P. Séguéla Central P2X4 and P2X6 channel subunits coassemble into a novel heteromeric ATP receptor J. Neurosci. 18 1998 7152 7159
    • (1998) J. Neurosci. , vol.18 , pp. 7152-7159
    • Lě, K.T.1    Babinski, K.2    Séguéla, P.3
  • 82
    • 0028982205 scopus 로고
    • Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons
    • C. Lewis S. Neidhart C. Holy R.A. North G. Buell A. Surprenant Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons Nature 377 1995 432 435
    • (1995) Nature , vol.377 , pp. 432-435
    • Lewis, C.1    Neidhart, S.2    Holy, C.3    North, R.A.4    Buell, G.5    Surprenant, A.6
  • 84
    • 0026485457 scopus 로고
    • Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs
    • E.R. Liman J. Tytgat P. Hess Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs Neuron 9 1992 861 871
    • (1992) Neuron , vol.9 , pp. 861-871
    • Liman, E.R.1    Tytgat, J.2    Hess, P.3
  • 85
    • 0018655548 scopus 로고
    • Biochemical properties of acteylcholine receptor subunits from Torpedo californica
    • J. Lindstrom J. Merlie G. Yogeeswaran Biochemical properties of acteylcholine receptor subunits from Torpedo californica Biochemistry 18 1979 4465 4470
    • (1979) Biochemistry , vol.18 , pp. 4465-4470
    • Lindstrom, J.1    Merlie, J.2    Yogeeswaran, G.3
  • 86
    • 0029619234 scopus 로고
    • Cloning of the amiloride-sensitive FMRFamide peptide-gated sodium channel
    • E. Lingueglia G. Champigny M. Lazdunski P. Barbry Cloning of the amiloride-sensitive FMRFamide peptide-gated sodium channel Nature 378 1995 730 733
    • (1995) Nature , vol.378 , pp. 730-733
    • Lingueglia, E.1    Champigny, G.2    Lazdunski, M.3    Barbry, P.4
  • 87
    • 0029743660 scopus 로고    scopus 로고
    • Two physically distinct pores in the dimeric CIC-0 chloride channel
    • U. Ludewig M. Pusch T.J. Jentsch Two physically distinct pores in the dimeric CIC-0 chloride channel Nature 383 1996 340 343
    • (1996) Nature , vol.383 , pp. 340-343
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 88
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • R. MacKinnon Determination of the subunit stoichiometry of a voltage-activated potassium channel Nature 350 1991 232 235
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 89
    • 0023298981 scopus 로고
    • The GABAA/benzodiazepine receptor is a heterotetramer of homologous α and β subunits
    • C. Mamalaki F.A. Stephenson E.A. Barnard The GABAA/benzodiazepine receptor is a heterotetramer of homologous α and β subunits EMBO J. 6 1987 561 565
    • (1987) EMBO J. , vol.6 , pp. 561-565
    • Mamalaki, C.1    Stephenson, F.A.2    Barnard, E.A.3
  • 90
    • 0032567729 scopus 로고    scopus 로고
    • A tetrameric subunit stoichiometry for a glutamate receptor-channel complex
    • I. Mano V.I. Teichberg A tetrameric subunit stoichiometry for a glutamate receptor-channel complex Neuroreport 9 1998 327 331
    • (1998) Neuroreport , vol.9 , pp. 327-331
    • Mano, I.1    Teichberg, V.I.2
  • 91
    • 0031896768 scopus 로고    scopus 로고
    • Structure and function of voltage-gated sodium channels
    • E. Marban T. Yamagishi G.F. Tomaselli Structure and function of voltage-gated sodium channels J. Physiol. (Lond.) 508 1998 647 657
    • (1998) J. Physiol. (Lond.) , vol.508 , pp. 647-657
    • Marban, E.1    Yamagishi, T.2    Tomaselli, G.F.3
  • 92
    • 0025997336 scopus 로고
    • Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel
    • A.V. Maricq A.S. Peterson A.J. Brake R.M. Myers D. Julius Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel Science 254 1991 432 437
    • (1991) Science , vol.254 , pp. 432-437
    • Maricq, A.V.1    Peterson, A.S.2    Brake, A.J.3    Myers, R.M.4    Julius, D.5
  • 93
    • 0028965629 scopus 로고
    • Physiological diversity of nicotinic acetylcholine receptors expressed by vertebrate neurons
    • D.S. McGehee L.W. Role Physiological diversity of nicotinic acetylcholine receptors expressed by vertebrate neurons Ann. Rev. Physiol. 57 1995 521 546
    • (1995) Ann. Rev. Physiol. , vol.57 , pp. 521-546
    • McGehee, D.S.1    Role, L.W.2
  • 95
    • 0028102941 scopus 로고
    • Purification, reconstitution, and subunit composition of a voltage-gated chloride channel from Torpedo electroplax
    • R.E. Middleton D.J. Pheasant C. Miller Purification, reconstitution, and subunit composition of a voltage-gated chloride channel from Torpedo electroplax Biochemistry 33 1994 13189 13198
    • (1994) Biochemistry , vol.33 , pp. 13189-13198
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 96
    • 0029661878 scopus 로고    scopus 로고
    • Homodimeric architecture of a CIC-type chloride ion channel
    • R.E. Middleton D.J. Pheasant C. Miller Homodimeric architecture of a CIC-type chloride ion channel Nature 383 1996 337 340
    • (1996) Nature , vol.383 , pp. 337-340
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 97
    • 0030611788 scopus 로고    scopus 로고
    • The InsP3 receptor and intracellular Ca2+ signaling
    • K. Mikoshiba The InsP3 receptor and intracellular Ca2+ signaling Curr. Opin. Neurobiol. 7 1997 339 345
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 339-345
    • Mikoshiba, K.1
  • 100
    • 0027976290 scopus 로고
    • Quaternary structure of the native GABAA receptor determined by electron microscopic image analysis
    • N. Nayeem Green T.P. I.L. Martin E.A. Barnard Quaternary structure of the native GABAA receptor determined by electron microscopic image analysis J. Neurochem. 62 1994 815 818
    • (1994) J. Neurochem. , vol.62 , pp. 815-818
    • Nayeem, N.1    Green, T.P.2    Martin, I.L.3    Barnard, E.A.4
  • 103
    • 0033041549 scopus 로고    scopus 로고
    • Blue native PAGE as a useful method for the analysis of the assembly of distinct combinations of nicotinic acetylcholine receptor subunits
    • A. Nicke J. Rettinger E. Mutschler G. Schmalzing Blue native PAGE as a useful method for the analysis of the assembly of distinct combinations of nicotinic acetylcholine receptor subunits J. Recept. Signal. Transduct. Res. 19 1999 493 507
    • (1999) J. Recept. Signal. Transduct. Res. , vol.19 , pp. 493-507
    • Nicke, A.1    Rettinger, J.2    Mutschler, E.3    Schmalzing, G.4
  • 104
    • 0030222204 scopus 로고    scopus 로고
    • Families of ion channels with two hydrophobic segments
    • R.A. North Families of ion channels with two hydrophobic segments Curr. Opin. Cell Biol. 8 1996 474 483
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 474-483
    • North, R.A.1
  • 105
    • 0030340238 scopus 로고    scopus 로고
    • P2X receptors: A third major class of ligand-gated ion channels
    • R.A. North P2X receptors: A third major class of ligand-gated ion channels Ciba Found. Symp. 198 1996 91 105
    • (1996) Ciba Found. Symp. , vol.198 , pp. 91-105
    • North, R.A.1
  • 106
    • 0030220611 scopus 로고    scopus 로고
    • P2X purinoceptor plethora
    • R.A. North P2X purinoceptor plethora Semin. Neurosci. 8 1996 187 194
    • (1996) Semin. Neurosci. , vol.8 , pp. 187-194
    • North, R.A.1
  • 108
    • 0028796049 scopus 로고
    • Evolutionary history of the ligand-gated ion-channel superfamily of receptors
    • M.O. Ortells G.G. Lunt Evolutionary history of the ligand-gated ion-channel superfamily of receptors Trends Neurosci. 18 1995 121 127
    • (1995) Trends Neurosci. , vol.18 , pp. 121-127
    • Ortells, M.O.1    Lunt, G.G.2
  • 109
    • 0029892533 scopus 로고    scopus 로고
    • Subunit positional effects revealed by novel heteromeric inwardly rectifying K+ channels
    • M. Pessia S.J. Tucker K. Lee C.T. Bond J.P. Adelman Subunit positional effects revealed by novel heteromeric inwardly rectifying K+ channels EMBO J. 15 1996 2980 2987
    • (1996) EMBO J. , vol.15 , pp. 2980-2987
    • Pessia, M.1    Tucker, S.J.2    Lee, K.3    Bond, C.T.4    Adelman, J.P.5
  • 110
    • 0020405932 scopus 로고
    • Purification by affinity chromatography of the glycine receptor of rat spinal cord
    • F. Pfeiffer D. Graham H. Betz Purification by affinity chromatography of the glycine receptor of rat spinal cord J. Biol. Chem. 257 1982 9389 9393
    • (1982) J. Biol. Chem. , vol.257 , pp. 9389-9393
    • Pfeiffer, F.1    Graham, D.2    Betz, H.3
  • 111
    • 0024405504 scopus 로고
    • Bivalent ligands and the message-address concept in the design of selective opioid receptor antagonists
    • P.S. Portoghese Bivalent ligands and the message-address concept in the design of selective opioid receptor antagonists Trends Pharmacol. Sci 10 1989 230 235
    • (1989) Trends Pharmacol. Sci , vol.10 , pp. 230-235
    • Portoghese, P.S.1
  • 112
    • 0030722469 scopus 로고    scopus 로고
    • Stoichiometry of recombinant N-methyl-D-aspartate receptor channels inferred from single-channel current patterns
    • L.S. Premkumar A. Auerbach Stoichiometry of recombinant N-methyl-D-aspartate receptor channels inferred from single-channel current patterns J. Gen. Physiol. 110 1997 485 502
    • (1997) J. Gen. Physiol. , vol.110 , pp. 485-502
    • Premkumar, L.S.1    Auerbach, A.2
  • 113
    • 0032584662 scopus 로고    scopus 로고
    • Tetrameric subunit structure of the native brain inwardly rectifying potassium channel Kir 2.2
    • K.F. Raab-Graham C.A. Vandenberg Tetrameric subunit structure of the native brain inwardly rectifying potassium channel Kir 2.2 J. Biol. Chem. 273 1998 19699 19707
    • (1998) J. Biol. Chem. , vol.273 , pp. 19699-19707
    • Raab-Graham, K.F.1    Vandenberg, C.A.2
  • 114
    • 0030879448 scopus 로고    scopus 로고
    • Baculovirus expression provides direct evidence for heteromeric assembly of P2X2 and P2X3 receptors
    • K.M. Radford C. Virginio A. Surprenant North R.A. E. Kawashima Baculovirus expression provides direct evidence for heteromeric assembly of P2X2 and P2X3 receptors J. Neurosci. 17 1997 6529 6533
    • (1997) J. Neurosci. , vol.17 , pp. 6529-6533
    • Radford, K.M.1    Virginio, C.2    Surprenant, A.3    North, R.A.4    Kawashima, E.5
  • 116
    • 0030962404 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the pore of a P2X receptor
    • F. Rassendren G. Buell A. Newbolt North R.A. A. Surprenant Identification of amino acid residues contributing to the pore of a P2X receptor EMBO J. 16 1997 3446 3454
    • (1997) EMBO J. , vol.16 , pp. 3446-3454
    • Rassendren, F.1    Buell, G.2    Newbolt, A.3    North, R.A.4    Surprenant, A.5
  • 117
    • 0028332337 scopus 로고
    • Biochemical analysis of the membrane topology of the amiloride-sensitive Na+ channel
    • S. Renard E. Lingueglia N. Voilley M. Lazdunski P. Barbry Biochemical analysis of the membrane topology of the amiloride-sensitive Na+ channel J. Biol. Chem. 269 1994 12981 12986
    • (1994) J. Biol. Chem. , vol.269 , pp. 12981-12986
    • Renard, S.1    Lingueglia, E.2    Voilley, N.3    Lazdunski, M.4    Barbry, P.5
  • 119
    • 0032486422 scopus 로고    scopus 로고
    • The tetrameric structure of a glutamate receptor channel
    • C. Rosenmund Y. Stern-Bach C.F. Stevens The tetrameric structure of a glutamate receptor channel Science 280 1998 1596 1599
    • (1998) Science , vol.280 , pp. 1596-1599
    • Rosenmund, C.1    Stern-Bach, Y.2    Stevens, C.F.3
  • 120
    • 0345543722 scopus 로고    scopus 로고
    • A hexameric transmembrane pore revealed by two-dimensional crystallization of the large mechanosensitive ion channel (MscL) of Escherichia coli
    • N. Saint J.J. Lacapere L.Q. Gu A. Ghazi B. Martinac J.L. Rigaud A hexameric transmembrane pore revealed by two-dimensional crystallization of the large mechanosensitive ion channel (MscL) of Escherichia coli J. Biol. Chem. 273 1998 14667 14670
    • (1998) J. Biol. Chem. , vol.273 , pp. 14667-14670
    • Saint, N.1    Lacapere, J.J.2    Gu, L.Q.3    Ghazi, A.4    Martinac, B.5    Rigaud, J.L.6
  • 121
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • H. Schägger G. von Jagow Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form Anal. Biochem. 199 1991 223 231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 122
    • 0027234701 scopus 로고
    • The TINS/TIPS Lecture. The molecular biology of mammalian glutamate receptor channels
    • P.H. Seeburg The TINS/TIPS Lecture. The molecular biology of mammalian glutamate receptor channels Trends Neurosci. 16 1993 359 365
    • (1993) Trends Neurosci. , vol.16 , pp. 359-365
    • Seeburg, P.H.1
  • 123
    • 0029670647 scopus 로고    scopus 로고
    • A novel neuronal P2x ATP receptor ion channel with widespread distribution in the brain
    • P. Séguéla A. Haghighi J.J. Soghomonian E. Cooper A novel neuronal P2x ATP receptor ion channel with widespread distribution in the brain J. Neurosci. 16 1996 448 455
    • (1996) J. Neurosci. , vol.16 , pp. 448-455
    • Séguéla, P.1    Haghighi, A.2    Soghomonian, J.J.3    Cooper, E.4
  • 124
    • 0030693304 scopus 로고    scopus 로고
    • The benzodiazepine binding site of GABAA receptors
    • E. Sigel Buhr A. The benzodiazepine binding site of GABAA receptors Trends Pharmacol. Sci. 18 1997 425 429
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 425-429
    • Sigel, E.1    Buhr, A.2
  • 125
    • 0031985150 scopus 로고    scopus 로고
    • Electrophysiological and biochemical evidence that DEG/ENaC cation channels are composed of nine subunits
    • P.M. Snyder Cheng C. L.S. Prince J.C. Rogers M.J. Welsh Electrophysiological and biochemical evidence that DEG/ENaC cation channels are composed of nine subunits J. Biol. Chem. 273 1998 681 684
    • (1998) J. Biol. Chem. , vol.273 , pp. 681-684
    • Snyder, P.M.1    Cheng, C.2    Prince, L.S.3    Rogers, J.C.4    Welsh, M.J.5
  • 128
    • 0030668707 scopus 로고    scopus 로고
    • Cloned ligand-gated channels activated by extracellular ATP (P2X receptors)
    • F. Soto M. Garcia-Guzman W. Stühmer Cloned ligand-gated channels activated by extracellular ATP (P2X receptors) J. Membr. Biol. 160 1997 91 100
    • (1997) J. Membr. Biol. , vol.160 , pp. 91-100
    • Soto, F.1    Garcia-Guzman, M.2    Stühmer, W.3
  • 129
    • 0019494706 scopus 로고
    • Active multi-subunit ACh receptor assembled by translation of heterologous mRNA in Xenopus oocytes
    • K. Sumikawa M. Houghton J.S. Emtage B.M. Richards E.A. Barnard Active multi-subunit ACh receptor assembled by translation of heterologous mRNA in Xenopus oocytes Nature. 292 1981 862 864
    • (1981) Nature. , vol.292 , pp. 862-864
    • Sumikawa, K.1    Houghton, M.2    Emtage, J.S.3    Richards, B.M.4    Barnard, E.A.5
  • 130
    • 0029665112 scopus 로고    scopus 로고
    • The cytolytic P2z receptor for extracellular ATP identified as a P2x receptor (P2X7)
    • A. Surprenant F. Rassendren E. Kawashima R.A. North G. Buell The cytolytic P2z receptor for extracellular ATP identified as a P2x receptor (P2X7) Science 272 1996 735 738
    • (1996) Science , vol.272 , pp. 735-738
    • Surprenant, A.1    Rassendren, F.2    Kawashima, E.3    North, R.A.4    Buell, G.5
  • 131
    • 0032549559 scopus 로고    scopus 로고
    • Topological analysis of the ATP-gated ionotrophic P2X2 receptor subunit
    • G.E. Torres Egan T.M. M.M. Voigt Topological analysis of the ATP-gated ionotrophic P2X2 receptor subunit FEBS Lett. 425 1998 19 23
    • (1998) FEBS Lett. , vol.425 , pp. 19-23
    • Torres, G.E.1    Egan, T.M.2    Voigt, M.M.3
  • 132
    • 0028279385 scopus 로고
    • The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites
    • T.W. Traut The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites Eur. J. Biochem. 222 1994 9 19
    • (1994) Eur. J. Biochem. , vol.222 , pp. 9-19
    • Traut, T.W.1
  • 133
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • N. Unwin Acetylcholine receptor channel imaged in the open state Nature. 373 1995 37 43
    • (1995) Nature. , vol.373 , pp. 37-43
    • Unwin, N.1
  • 134
    • 0028030797 scopus 로고
    • A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP
    • S. Valera Hussy N. R.J. Evans N. Adami R.A. North Suiprenant A. G. Buell A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP Nature 371 1994 516 519
    • (1994) Nature , vol.371 , pp. 516-519
    • Valera, S.1    Hussy, N.2    Evans, R.J.3    Adami, N.4    North, R.A.5    Suiprenant, A.6    Buell, G.7
  • 135
    • 0030836533 scopus 로고    scopus 로고
    • Native serotonin 5-HT3 receptors expressed in Xenopus oocytes differ from homopentameric 5-HT3 receptors
    • J.A. van Hooft A.P. Kreikamp H.P. Vijverberg Native serotonin 5-HT3 receptors expressed in Xenopus oocytes differ from homopentameric 5-HT3 receptors J. Neurochem. 69 1997 1318 1321
    • (1997) J. Neurochem. , vol.69 , pp. 1318-1321
    • van Hooft, J.A.1    Kreikamp, A.P.2    Vijverberg, H.P.3
  • 136
    • 0032530454 scopus 로고    scopus 로고
    • Promiscuous coassembly of serotonin 5-HT3 and nicotinic α4 receptor subunits into Ca2+-permeable ion channels
    • J.A. van Hooft A.D. Spier J.L. Yakel Lummis S.R. H.M. Vijverberg Promiscuous coassembly of serotonin 5-HT3 and nicotinic α4 receptor subunits into Ca2+-permeable ion channels Proc. Natl. Acad. Sci. USA 95 1998 11456 11461
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11456-11461
    • van Hooft, J.A.1    Spier, A.D.2    Yakel, J.L.3    Lummis, S.R.4    Vijverberg, H.M.5
  • 137
    • 0029870327 scopus 로고    scopus 로고
    • Cloning and pharmacological characterization of a fourth P2X receptor subtype widely expressed in brain and peripheral tissues including various endocrine tissues
    • C.Z. Wang N. Namba T. Gonoi N. Inagaki S. Seino Cloning and pharmacological characterization of a fourth P2X receptor subtype widely expressed in brain and peripheral tissues including various endocrine tissues Biochem. Biophys. Res. Commun. 220 1996 196 202
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 196-202
    • Wang, C.Z.1    Namba, N.2    Gonoi, T.3    Inagaki, N.4    Seino, S.5
  • 138
    • 0026531244 scopus 로고
    • Immunochemical characterization of the non-NMDA glutamate receptor using subunit-specific antibodies. Evidence for a hetero-oligomeric structure in rat brain
    • R.J. Wenthold N. Yokotani K. Doi Wada K. Immunochemical characterization of the non-NMDA glutamate receptor using subunit-specific antibodies. Evidence for a hetero-oligomeric structure in rat brain J. Biol. Chem. 267 1992 501 507
    • (1992) J. Biol. Chem. , vol.267 , pp. 501-507
    • Wenthold, R.J.1    Yokotani, N.2    Doi, K.3    Wada, K.4
  • 139
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Z.G. Wo R.E. Oswald Unraveling the modular design of glutamate-gated ion channels Trends Neurosci. 18 1995 161 168
    • (1995) Trends Neurosci. , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2
  • 140
    • 0029071823 scopus 로고
    • Structural conservation of ion conduction pathways in K channels and glutamate receptors
    • M.W. Wood VanDongen H.M. VanDongen A.M. Structural conservation of ion conduction pathways in K channels and glutamate receptors Proc. Natl. Acad. Sci. USA 92 1995 4882 4886
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4882-4886
    • Wood, M.W.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 141
    • 0029989334 scopus 로고    scopus 로고
    • A study of the oligomeric state of the α-amino-3-hydroxy-5-methyl-4-iso-xazolepropionic acid-preferring glutamate receptors in the synaptic junctions of porcine brain
    • T.Y. Wu C.I. Liu Y.C. Chang A study of the oligomeric state of the α-amino-3-hydroxy-5-methyl-4-iso-xazolepropionic acid-preferring glutamate receptors in the synaptic junctions of porcine brain Biochem. J. 319 1996 731 739
    • (1996) Biochem. J. , vol.319 , pp. 731-739
    • Wu, T.Y.1    Liu, C.I.2    Chang, Y.C.3
  • 142
    • 13344262697 scopus 로고
    • Determination of the subunit stoichiometry of an inwardly rectifying potassium channel
    • J. Yang Y.N. Jan L.Y. Jan Determination of the subunit stoichiometry of an inwardly rectifying potassium channel Neuron 15 1995 1441 1447
    • (1995) Neuron , vol.15 , pp. 1441-1447
    • Yang, J.1    Jan, Y.N.2    Jan, L.Y.3
  • 143
    • 0026058182 scopus 로고
    • Alteration of ionic selectivity of a K+ channel by mutation of the H5 region
    • A.J. Yool T.L. Schwarz Alteration of ionic selectivity of a K+ channel by mutation of the H5 region Nature 349 1991 700 704
    • (1991) Nature , vol.349 , pp. 700-704
    • Yool, A.J.1    Schwarz, T.L.2
  • 144
    • 0029998701 scopus 로고    scopus 로고
    • Structure and function of cyclic nucleotide-gated channels
    • Zagotta W.N. S.A. Siegelbaum Structure and function of cyclic nucleotide-gated channels Annu. Rev. Neurosci. 19 1996 235 263
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 235-263
    • Zagotta, W.N.1    Siegelbaum, S.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.