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Volumn 1850, Issue 3, 2015, Pages 511-523

Crystallographic studies of pharmacological sites in pentameric ligand-gated ion channels

Author keywords

Allostery; Binding sites; Crystallography; Ligand gated ion channels; Neurotransmitters

Indexed keywords

ACETYLCHOLINE; ACETYLCHOLINE BINDING PROTEIN; ALCOHOL; ANESTHETIC AGENT; BENZODIAZEPINE DERIVATIVE; BINDING PROTEIN; ION TRANSPORT AFFECTING AGENT; LIGAND GATED ION CHANNEL; LIPID; OPEN CHANNEL PORE BLOCKER; PENTAMERIC LIGAND GATED ION CHANNEL; UNCLASSIFIED DRUG; LIGAND;

EID: 84921029711     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.05.007     Document Type: Review
Times cited : (47)

References (78)
  • 2
    • 69949159308 scopus 로고    scopus 로고
    • Nicotinic receptors: Allosteric transitions and therapeutic targets in the nervous system
    • A. Taly, P.J. Corringer, D. Guedin, P. Lestage, and J.P. Changeux Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system Nat. Rev. Drug Discov. 8 2009 733 750
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 733-750
    • Taly, A.1    Corringer, P.J.2    Guedin, D.3    Lestage, P.4    Changeux, J.P.5
  • 3
    • 84879882962 scopus 로고    scopus 로고
    • The concept of allosteric modulation: An overview
    • J.P. Changeux The concept of allosteric modulation: an overview Drug Discov. Today Technol. 10 2013 e223 e228
    • (2013) Drug Discov. Today Technol. , vol.10 , pp. e223-e228
    • Changeux, J.P.1
  • 4
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • N. Unwin Refined structure of the nicotinic acetylcholine receptor at 4A resolution J. Mol. Biol. 346 2005 967 989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 5
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • R.J. Hilf, and R. Dutzler X-ray structure of a prokaryotic pentameric ligand-gated ion channel Nature 452 2008 375 379
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 6
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • R.J. Hilf, and R. Dutzler Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel Nature 457 2009 115 118
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 7
  • 8
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • R.E. Hibbs, and E. Gouaux Principles of activation and permeation in an anion-selective Cys-loop receptor Nature 474 2011 54 60
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 10
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution
    • C.D. Dellisanti, Y. Yao, J.C. Stroud, Z.Z. Wang, and L. Chen Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution Nat. Neurosci. 10 2007 953 962
    • (2007) Nat. Neurosci. , vol.10 , pp. 953-962
    • Dellisanti, C.D.1    Yao, Y.2    Stroud, J.C.3    Wang, Z.Z.4    Chen, L.5
  • 11
    • 80053236857 scopus 로고    scopus 로고
    • Ligand-binding domain of an alpha7-nicotinic receptor chimera and its complex with agonist
    • S.X. Li, S. Huang, N. Bren, K. Noridomi, C.D. Dellisanti, S.M. Sine, and L. Chen Ligand-binding domain of an alpha7-nicotinic receptor chimera and its complex with agonist Nat. Neurosci. 14 2011 1253 1259
    • (2011) Nat. Neurosci. , vol.14 , pp. 1253-1259
    • Li, S.X.1    Huang, S.2    Bren, N.3    Noridomi, K.4    Dellisanti, C.D.5    Sine, S.M.6    Chen, L.7
  • 12
    • 82755162931 scopus 로고    scopus 로고
    • Creating an alpha7 nicotinic acetylcholine recognition domain from the acetylcholine-binding protein: Crystallographic and ligand selectivity analyses
    • A. Nemecz, and P. Taylor Creating an alpha7 nicotinic acetylcholine recognition domain from the acetylcholine-binding protein: crystallographic and ligand selectivity analyses J. Biol. Chem. 286 2011 42555 42565
    • (2011) J. Biol. Chem. , vol.286 , pp. 42555-42565
    • Nemecz, A.1    Taylor, P.2
  • 14
    • 80755185305 scopus 로고    scopus 로고
    • Unravelling the conformational plasticity of the extracellular domain of a prokaryotic nAChR homologue in solution by NMR
    • C.T. Chasapis, A.I. Argyriou, P.J. Corringer, D. Bentrop, and G.A. Spyroulias Unravelling the conformational plasticity of the extracellular domain of a prokaryotic nAChR homologue in solution by NMR Biochemistry 50 2011 9681 9683
    • (2011) Biochemistry , vol.50 , pp. 9681-9683
    • Chasapis, C.T.1    Argyriou, A.I.2    Corringer, P.J.3    Bentrop, D.4    Spyroulias, G.A.5
  • 16
    • 84885435090 scopus 로고    scopus 로고
    • Open-channel structures of the human glycine receptor alpha1 full-length transmembrane domain
    • D.D. Mowrey, T. Cui, Y. Jia, D. Ma, A.M. Makhov, P. Zhang, P. Tang, and Y. Xu Open-channel structures of the human glycine receptor alpha1 full-length transmembrane domain Structure 21 2013 1897 1904
    • (2013) Structure , vol.21 , pp. 1897-1904
    • Mowrey, D.D.1    Cui, T.2    Jia, Y.3    Ma, D.4    Makhov, A.M.5    Zhang, P.6    Tang, P.7    Xu, Y.8
  • 19
    • 84870266525 scopus 로고    scopus 로고
    • Inhibition of the prokaryotic pentameric ligand-gated ion channel ELIC by divalent cations
    • I. Zimmermann, A. Marabelli, C. Bertozzi, L.G. Sivilotti, and R. Dutzler Inhibition of the prokaryotic pentameric ligand-gated ion channel ELIC by divalent cations PLoS Biol. 10 2012 e1001429
    • (2012) PLoS Biol. , vol.10 , pp. e1001429
    • Zimmermann, I.1    Marabelli, A.2    Bertozzi, C.3    Sivilotti, L.G.4    Dutzler, R.5
  • 23
    • 68949105566 scopus 로고    scopus 로고
    • Molecular-dynamics simulations of ELIC - A prokaryotic homologue of the nicotinic acetylcholine receptor
    • X. Cheng, I. Ivanov, H. Wang, S.M. Sine, and J.A. McCammon Molecular-dynamics simulations of ELIC - a prokaryotic homologue of the nicotinic acetylcholine receptor Biophys. J. 96 2009 4502 4513
    • (2009) Biophys. J. , vol.96 , pp. 4502-4513
    • Cheng, X.1    Ivanov, I.2    Wang, H.3    Sine, S.M.4    McCammon, J.A.5
  • 27
    • 84887444038 scopus 로고    scopus 로고
    • Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography
    • G. Gonzalez-Gutierrez, L.G. Cuello, S.K. Nair, and C. Grosman Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography Proc. Natl. Acad. Sci. U. S. A. 110 2013 18716 18721
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 18716-18721
    • Gonzalez-Gutierrez, G.1    Cuello, L.G.2    Nair, S.K.3    Grosman, C.4
  • 29
    • 79954568593 scopus 로고    scopus 로고
    • Structure of the M2 transmembrane segment of GLIC, a prokaryotic Cys loop receptor homologue from Gloeobacter violaceus, probed by substituted cysteine accessibility
    • R.B. Parikh, M. Bali, and M.H. Akabas Structure of the M2 transmembrane segment of GLIC, a prokaryotic Cys loop receptor homologue from Gloeobacter violaceus, probed by substituted cysteine accessibility J. Biol. Chem. 286 2011 14098 14109
    • (2011) J. Biol. Chem. , vol.286 , pp. 14098-14109
    • Parikh, R.B.1    Bali, M.2    Akabas, M.H.3
  • 30
    • 84861537525 scopus 로고    scopus 로고
    • Desensitization mechanism in prokaryotic ligand-gated ion channel
    • P. Velisetty, and S. Chakrapani Desensitization mechanism in prokaryotic ligand-gated ion channel J. Biol. Chem. 287 2012 18467 18477
    • (2012) J. Biol. Chem. , vol.287 , pp. 18467-18477
    • Velisetty, P.1    Chakrapani, S.2
  • 31
    • 84868258417 scopus 로고    scopus 로고
    • Conformational transitions underlying pore opening and desensitization in membrane-embedded Gloeobacter violaceus ligand-gated ion channel (GLIC)
    • P. Velisetty, S.V. Chalamalasetti, and S. Chakrapani Conformational transitions underlying pore opening and desensitization in membrane-embedded Gloeobacter violaceus ligand-gated ion channel (GLIC) J. Biol. Chem. 287 2012 36864 36872
    • (2012) J. Biol. Chem. , vol.287 , pp. 36864-36872
    • Velisetty, P.1    Chalamalasetti, S.V.2    Chakrapani, S.3
  • 32
    • 0000791015 scopus 로고
    • Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: Serine-262 of the delta subunit is labeled by [3H]chlorpromazine
    • J. Giraudat, M. Dennis, T. Heidmann, J.Y. Chang, and J.P. Changeux Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: serine-262 of the delta subunit is labeled by [3H]chlorpromazine Proc. Natl. Acad. Sci. U. S. A. 83 1986 2719 2723
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 2719-2723
    • Giraudat, J.1    Dennis, M.2    Heidmann, T.3    Chang, J.Y.4    Changeux, J.P.5
  • 33
    • 0022458822 scopus 로고
    • The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits
    • F. Hucho, W. Oberthur, and F. Lottspeich The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits FEBS Lett. 205 1986 137 142
    • (1986) FEBS Lett. , vol.205 , pp. 137-142
    • Hucho, F.1    Oberthur, W.2    Lottspeich, F.3
  • 37
    • 0004936065 scopus 로고
    • Input-output relation of a single synapse
    • B. Katz, and R. Miledi Input-output relation of a single synapse Nature 212 1966 1242 1245
    • (1966) Nature , vol.212 , pp. 1242-1245
    • Katz, B.1    Miledi, R.2
  • 38
    • 0032032840 scopus 로고    scopus 로고
    • From muscle endplate to brain synapses: A short history of synapses and agonist-activated ion channels
    • D. Colquhoun, and B. Sakmann From muscle endplate to brain synapses: a short history of synapses and agonist-activated ion channels Neuron 20 1998 381 387
    • (1998) Neuron , vol.20 , pp. 381-387
    • Colquhoun, D.1    Sakmann, B.2
  • 39
    • 0033119869 scopus 로고    scopus 로고
    • Mutational analysis of the charge selectivity filter of the alpha7 nicotinic acetylcholine receptor
    • P.J. Corringer, S. Bertrand, J.L. Galzi, A. Devillers-Thiery, J.P. Changeux, and D. Bertrand Mutational analysis of the charge selectivity filter of the alpha7 nicotinic acetylcholine receptor Neuron 22 1999 831 843
    • (1999) Neuron , vol.22 , pp. 831-843
    • Corringer, P.J.1    Bertrand, S.2    Galzi, J.L.3    Devillers-Thiery, A.4    Changeux, J.P.5    Bertrand, D.6
  • 44
    • 84885651158 scopus 로고    scopus 로고
    • Structural insights into Cys-loop receptor function and ligand recognition
    • M. Nys, D. Kesters, and C. Ulens Structural insights into Cys-loop receptor function and ligand recognition Biochem. Pharmacol. 86 2013 1042 1053
    • (2013) Biochem. Pharmacol. , vol.86 , pp. 1042-1053
    • Nys, M.1    Kesters, D.2    Ulens, C.3
  • 45
    • 79953684899 scopus 로고    scopus 로고
    • A structural and mutagenic blueprint for molecular recognition of strychnine and d-tubocurarine by different cys-loop receptors
    • M. Brams, A. Pandya, D. Kuzmin, R. van Elk, L. Krijnen, J.L. Yakel, V. Tsetlin, A.B. Smit, and C. Ulens A structural and mutagenic blueprint for molecular recognition of strychnine and d-tubocurarine by different cys-loop receptors PLoS Biol. 9 2011 e1001034
    • (2011) PLoS Biol. , vol.9 , pp. e1001034
    • Brams, M.1    Pandya, A.2    Kuzmin, D.3    Van Elk, R.4    Krijnen, L.5    Yakel, J.L.6    Tsetlin, V.7    Smit, A.B.8    Ulens, C.9
  • 46
    • 84869992899 scopus 로고    scopus 로고
    • Structure, function, and modulation of GABA(A) receptors
    • E. Sigel, and M.E. Steinmann Structure, function, and modulation of GABA(A) receptors J. Biol. Chem. 287 2012 40224 40231
    • (2012) J. Biol. Chem. , vol.287 , pp. 40224-40231
    • Sigel, E.1    Steinmann, M.E.2
  • 48
    • 0026716690 scopus 로고
    • Potentiation of nicotinic receptor response by external calcium in rat central neurons
    • C. Mulle, C. Lena, and J.P. Changeux Potentiation of nicotinic receptor response by external calcium in rat central neurons Neuron 8 1992 937 945
    • (1992) Neuron , vol.8 , pp. 937-945
    • Mulle, C.1    Lena, C.2    Changeux, J.P.3
  • 49
    • 0026586188 scopus 로고
    • Calcium modulation and high calcium permeability of neuronal nicotinic acetylcholine receptors
    • S. Vernino, M. Amador, C.W. Luetje, J. Patrick, and J.A. Dani Calcium modulation and high calcium permeability of neuronal nicotinic acetylcholine receptors Neuron 8 1992 127 134
    • (1992) Neuron , vol.8 , pp. 127-134
    • Vernino, S.1    Amador, M.2    Luetje, C.W.3    Patrick, J.4    Dani, J.A.5
  • 50
    • 0023687394 scopus 로고
    • Divalent cations modulate 5-HT3 receptor-induced currents in N1E-115 neuroblastoma cells
    • J.A. Peters, T.G. Hales, and J.J. Lambert Divalent cations modulate 5-HT3 receptor-induced currents in N1E-115 neuroblastoma cells Eur. J. Pharmacol. 151 1988 491 495
    • (1988) Eur. J. Pharmacol. , vol.151 , pp. 491-495
    • Peters, J.A.1    Hales, T.G.2    Lambert, J.J.3
  • 52
    • 0028943569 scopus 로고
    • Modulation by zinc ions of native rat and recombinant human inhibitory glycine receptors
    • B. Laube, J. Kuhse, N. Rundstrom, J. Kirsch, V. Schmieden, and H. Betz Modulation by zinc ions of native rat and recombinant human inhibitory glycine receptors J. Physiol. 483 Pt 3 1995 613 619
    • (1995) J. Physiol. , vol.483 , Issue.PART 3 , pp. 613-619
    • Laube, B.1    Kuhse, J.2    Rundstrom, N.3    Kirsch, J.4    Schmieden, V.5    Betz, H.6
  • 53
    • 53549103853 scopus 로고    scopus 로고
    • Mapping a molecular link between allosteric inhibition and activation of the glycine receptor
    • P.S. Miller, M. Topf, and T.G. Smart Mapping a molecular link between allosteric inhibition and activation of the glycine receptor Nat. Struct. Mol. Biol. 15 2008 1084 1093
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1084-1093
    • Miller, P.S.1    Topf, M.2    Smart, T.G.3
  • 59
    • 84881474053 scopus 로고    scopus 로고
    • Inhibition versus potentiation of ligand-gated ion channels can be altered by a single mutation that moves ligands between intra- and intersubunit sites
    • T. Bromstrup, R.J. Howard, J.R. Trudell, R.A. Harris, and E. Lindahl Inhibition versus potentiation of ligand-gated ion channels can be altered by a single mutation that moves ligands between intra- and intersubunit sites Structure 21 2013 1307 1316
    • (2013) Structure , vol.21 , pp. 1307-1316
    • Bromstrup, T.1    Howard, R.J.2    Trudell, J.R.3    Harris, R.A.4    Lindahl, E.5
  • 60
    • 84863791625 scopus 로고    scopus 로고
    • Conscious processing: Implications for general anesthesia
    • J.P. Changeux Conscious processing: implications for general anesthesia Curr. Opin. Anaesthesiol. 25 2012 397 404
    • (2012) Curr. Opin. Anaesthesiol. , vol.25 , pp. 397-404
    • Changeux, J.P.1
  • 61
    • 74049110470 scopus 로고    scopus 로고
    • Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion channel
    • Y. Weng, L. Yang, P.J. Corringer, and J.M. Sonner Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion channel Anesth. Analg. 110 2010 59 63
    • (2010) Anesth. Analg. , vol.110 , pp. 59-63
    • Weng, Y.1    Yang, L.2    Corringer, P.J.3    Sonner, J.M.4
  • 63
    • 84874766162 scopus 로고    scopus 로고
    • Identification of propofol binding sites in a nicotinic acetylcholine receptor with a photoreactive propofol analog
    • S.S. Jayakar, W.P. Dailey, R.G. Eckenhoff, and J.B. Cohen Identification of propofol binding sites in a nicotinic acetylcholine receptor with a photoreactive propofol analog J. Biol. Chem. 288 2013 6178 6189
    • (2013) J. Biol. Chem. , vol.288 , pp. 6178-6189
    • Jayakar, S.S.1    Dailey, W.P.2    Eckenhoff, R.G.3    Cohen, J.B.4
  • 64
    • 84879038168 scopus 로고    scopus 로고
    • Propofol binding to the resting state of the gloeobacter violaceus ligand-gated ion channel (GLIC) induces structural changes in the inter- and intrasubunit transmembrane domain (TMD) cavities
    • B. Ghosh, K.A. Satyshur, and C. Czajkowski Propofol binding to the resting state of the gloeobacter violaceus ligand-gated ion channel (GLIC) induces structural changes in the inter- and intrasubunit transmembrane domain (TMD) cavities J. Biol. Chem. 288 2013 17420 17431
    • (2013) J. Biol. Chem. , vol.288 , pp. 17420-17431
    • Ghosh, B.1    Satyshur, K.A.2    Czajkowski, C.3
  • 66
    • 84897018301 scopus 로고    scopus 로고
    • GABA receptor transmembrane amino acids are critical for alcohol action: Disulfide crosslinking and alkyl methanethiosulfonate labeling reveal relative location of binding sites
    • C. Borghese, J.A. Hicks, D.J. Lapid, J.R. Trudell, and R.A. Harris GABA receptor transmembrane amino acids are critical for alcohol action: disulfide crosslinking and alkyl methanethiosulfonate labeling reveal relative location of binding sites J. Neurochem. 128 3 2013 363 375
    • (2013) J. Neurochem. , vol.128 , Issue.3 , pp. 363-375
    • Borghese, C.1    Hicks, J.A.2    Lapid, D.J.3    Trudell, J.R.4    Harris, R.A.5
  • 67
    • 33751119897 scopus 로고    scopus 로고
    • Identification of a GABAA receptor anesthetic binding site at subunit interfaces by photolabeling with an etomidate analog
    • G.D. Li, D.C. Chiara, G.W. Sawyer, S.S. Husain, R.W. Olsen, and J.B. Cohen Identification of a GABAA receptor anesthetic binding site at subunit interfaces by photolabeling with an etomidate analog J. Neurosci. 26 2006 11599 11605
    • (2006) J. Neurosci. , vol.26 , pp. 11599-11605
    • Li, G.D.1    Chiara, D.C.2    Sawyer, G.W.3    Husain, S.S.4    Olsen, R.W.5    Cohen, J.B.6
  • 70
    • 0034646853 scopus 로고    scopus 로고
    • Activation of rat recombinant alpha(1)beta(2)gamma(2S) GABA(A) receptor by the insecticide ivermectin
    • H. Adelsberger, A. Lepier, and J. Dudel Activation of rat recombinant alpha(1)beta(2)gamma(2S) GABA(A) receptor by the insecticide ivermectin Eur. J. Pharmacol. 394 2000 163 170
    • (2000) Eur. J. Pharmacol. , vol.394 , pp. 163-170
    • Adelsberger, H.1    Lepier, A.2    Dudel, J.3
  • 71
    • 0035918183 scopus 로고    scopus 로고
    • Ivermectin, an unconventional agonist of the glycine receptor chloride channel
    • Q. Shan, J.L. Haddrill, and J.W. Lynch Ivermectin, an unconventional agonist of the glycine receptor chloride channel J. Biol. Chem. 276 2001 12556 12564
    • (2001) J. Biol. Chem. , vol.276 , pp. 12556-12564
    • Shan, Q.1    Haddrill, J.L.2    Lynch, J.W.3
  • 73
    • 78149498460 scopus 로고    scopus 로고
    • 3D structure and allosteric modulation of the transmembrane domain of pentameric ligand-gated ion channels
    • J.E. Baenziger, and P.J. Corringer 3D structure and allosteric modulation of the transmembrane domain of pentameric ligand-gated ion channels Neuropharmacology 60 2011 116 125
    • (2011) Neuropharmacology , vol.60 , pp. 116-125
    • Baenziger, J.E.1    Corringer, P.J.2
  • 74
    • 84886530690 scopus 로고    scopus 로고
    • A distinct mechanism for activating uncoupled nicotinic acetylcholine receptors
    • C.J. daCosta, L. Dey, J.P. Therien, and J.E. Baenziger A distinct mechanism for activating uncoupled nicotinic acetylcholine receptors Nat. Chem. Biol. 9 2013 701 707
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 701-707
    • Dacosta, C.J.1    Dey, L.2    Therien, J.P.3    Baenziger, J.E.4
  • 75
    • 84876543856 scopus 로고    scopus 로고
    • Structural sensitivity of a prokaryotic pentameric ligand-gated ion channel to its membrane environment
    • J.M. Labriola, A. Pandhare, M. Jansen, M.P. Blanton, P.J. Corringer, and J.E. Baenziger Structural sensitivity of a prokaryotic pentameric ligand-gated ion channel to its membrane environment J. Biol. Chem. 288 2013 11294 11303
    • (2013) J. Biol. Chem. , vol.288 , pp. 11294-11303
    • Labriola, J.M.1    Pandhare, A.2    Jansen, M.3    Blanton, M.P.4    Corringer, P.J.5    Baenziger, J.E.6
  • 76
    • 0003443746 scopus 로고    scopus 로고
    • 3rd edition Sinauer Associates Inc. Sunderland, Massachusetts, USA
    • B. Hille Ion Channels of Excitable Membranes 3rd edition 2001 Sinauer Associates Inc. Sunderland, Massachusetts, USA
    • (2001) Ion Channels of Excitable Membranes
    • Hille, B.1
  • 77
    • 0025195179 scopus 로고
    • The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: Implications for the alpha-helical organization of regions MII and for the structure of the ion channel
    • F. Revah, J.L. Galzi, J. Giraudat, P.Y. Haumont, F. Lederer, and J.P. Changeux The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: implications for the alpha-helical organization of regions MII and for the structure of the ion channel Proc. Natl. Acad. Sci. U. S. A. 87 1990 4675 4679
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 4675-4679
    • Revah, F.1    Galzi, J.L.2    Giraudat, J.3    Haumont, P.Y.4    Lederer, F.5    Changeux, J.P.6
  • 78
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • A. Karlin Emerging structure of the nicotinic acetylcholine receptors Nat. Rev. Neurosci. 3 2002 102 114
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1


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