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Volumn 48, Issue 1, 2013, Pages 97-108

The structural mechanism of the cys-loop receptor desensitization

Author keywords

Coupling energy; Cys loop receptor; Desensitization; Gating strength; Nicotinic acetylcholine receptor

Indexed keywords

4 AMINOBUTYRIC ACID RECEPTOR; CYSTEINE LOOP LIGAND GATED ION CHANNEL RECEPTOR;

EID: 84880898531     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-013-8420-z     Document Type: Review
Times cited : (24)

References (87)
  • 1
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective cys-loop receptor
    • 21572436 10.1038/nature10139 1:CAS:528:DC%2BC3MXmsFyqt7Y%3D
    • Hibbs RE, Gouaux E (2011) Principles of activation and permeation in an anion-selective cys-loop receptor. Nature 474:54-60
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 2
    • 79951674390 scopus 로고    scopus 로고
    • The structural basis of function in cys-loop receptors
    • 20849671 10.1017/S0033583510000168 1:CAS:528:DC%2BC3cXhsVGitbfL
    • Thompson AJ, Lester HA, Lummis SC (2010) The structural basis of function in cys-loop receptors. Q Rev Biophys 43:449-499
    • (2010) Q Rev Biophys , vol.43 , pp. 449-499
    • Thompson, A.J.1    Lester, H.A.2    Lummis, S.C.3
  • 3
    • 77949538692 scopus 로고    scopus 로고
    • Atomic structure and dynamics of pentameric ligand-gated ion channels: New insight from bacterial homologues
    • 19995852 10.1113/jphysiol.2009.183160 1:CAS:528:DC%2BC3cXisVeksL0%3D
    • Corringer PJ, Baaden M, Bocquet N, Delarue M, Dufresne V, Nury H, Prevost M, Van Renterghem C (2010) Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues. J Physiol 588:565-572
    • (2010) J Physiol , vol.588 , pp. 565-572
    • Corringer, P.J.1    Baaden, M.2    Bocquet, N.3    Delarue, M.4    Dufresne, V.5    Nury, H.6    Prevost, M.7    Van Renterghem, C.8
  • 4
    • 69249088472 scopus 로고    scopus 로고
    • A prokaryotic perspective on pentameric ligand-gated ion channel structure
    • 19646860 10.1016/j.sbi.2009.07.006 1:CAS:528:DC%2BD1MXhtVKktbvJ
    • Hilf RJ, Dutzler R (2009) A prokaryotic perspective on pentameric ligand-gated ion channel structure. Curr Opin Struct Biol 19:418-424
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 418-424
    • Hilf, R.J.1    Dutzler, R.2
  • 5
    • 77950494200 scopus 로고    scopus 로고
    • Binding, activation and modulation of cys-loop receptors
    • 20096941 10.1016/j.tips.2009.12.005 1:CAS:528:DC%2BC3cXjvFKksbg%3D
    • Miller PS, Smart TG (2010) Binding, activation and modulation of cys-loop receptors. Trends Pharmacol Sci 31:161-174
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 161-174
    • Miller, P.S.1    Smart, T.G.2
  • 6
    • 0242353157 scopus 로고    scopus 로고
    • EXP-1 is an excitatory GABA-gated cation channel
    • 14555952 10.1038/nn1136 1:CAS:528:DC%2BD3sXosVOiurY%3D
    • Beg AA, Jorgensen EM (2003) EXP-1 is an excitatory GABA-gated cation channel. Nat Neurosci 6:1145-1152
    • (2003) Nat Neurosci , vol.6 , pp. 1145-1152
    • Beg, A.A.1    Jorgensen, E.M.2
  • 7
    • 0034707063 scopus 로고    scopus 로고
    • MOD-1 is a serotonin-gated chloride channel that modulates locomotory behaviour in C. elegans
    • 11100728 10.1038/35044083 1:CAS:528:DC%2BD3cXos1Srtr0%3D
    • Ranganathan R, Cannon SC, Horvitz HR (2000) MOD-1 is a serotonin-gated chloride channel that modulates locomotory behaviour in C. elegans. Nature 408:470-475
    • (2000) Nature , vol.408 , pp. 470-475
    • Ranganathan, R.1    Cannon, S.C.2    Horvitz, H.R.3
  • 8
    • 0036829880 scopus 로고    scopus 로고
    • The target of Drosophila photoreceptor synaptic transmission is a histamine-gated chloride channel encoded by ort (hclA)
    • 12196539 10.1074/jbc.M207133200 1:CAS:528:DC%2BD38XotF2gtL8%3D
    • Gengs C, Leung HT, Skingsley DR, Iovchev MI, Yin Z, Semenov EP, Burg MG, Hardie RC, Pak WL (2002) The target of Drosophila photoreceptor synaptic transmission is a histamine-gated chloride channel encoded by ort (hclA). J Biol Chem 277:42113-42120
    • (2002) J Biol Chem , vol.277 , pp. 42113-42120
    • Gengs, C.1    Leung, H.T.2    Skingsley, D.R.3    Iovchev, M.I.4    Yin, Z.5    Semenov, E.P.6    Burg, M.G.7    Hardie, R.C.8    Pak, W.L.9
  • 9
    • 1942470079 scopus 로고    scopus 로고
    • Esophageal foreign body in neonates
    • 15129878 1:STN:280:DC%2BD2c3jtVOnuw%3D%3D
    • Tasneem Z, Khan MA, Uddin N (2004) Esophageal foreign body in neonates. J Pak Med Assoc 54:159-161
    • (2004) J Pak Med Assoc , vol.54 , pp. 159-161
    • Tasneem, Z.1    Khan, M.A.2    Uddin, N.3
  • 10
    • 84965075853 scopus 로고
    • A study of the desensitization produced by acetylcholine at the motor end-plate
    • 13463799 1:STN:280:DyaG1c%2Fgs1Cmug%3D%3D
    • Katz B, Thesleff S (1957) A study of the desensitization produced by acetylcholine at the motor end-plate. J Physiol 138:63-80
    • (1957) J Physiol , vol.138 , pp. 63-80
    • Katz, B.1    Thesleff, S.2
  • 11
    • 0031870973 scopus 로고    scopus 로고
    • Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism
    • 9689026 10.1085/jgp.112.2.181 1:CAS:528:DyaK1cXlsVWqsLY%3D
    • Auerbach A, Akk G (1998) Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism. J Gen Physiol 112:181-197
    • (1998) J Gen Physiol , vol.112 , pp. 181-197
    • Auerbach, A.1    Akk, G.2
  • 12
    • 20744449198 scopus 로고    scopus 로고
    • Desensitization of nicotinic ACh receptors: Shaping cholinergic signaling
    • 15979501 10.1016/j.tins.2005.04.009 1:CAS:528:DC%2BD2MXlsVequ7w%3D
    • Giniatullin R, Nistri A, Yakel J (2005) Desensitization of nicotinic ACh receptors: shaping cholinergic signaling. Trends Neurosci 28:371-378
    • (2005) Trends Neurosci , vol.28 , pp. 371-378
    • Giniatullin, R.1    Nistri, A.2    Yakel, J.3
  • 13
    • 67549125013 scopus 로고    scopus 로고
    • Allosteric activation mechanism of the cys-loop receptors
    • 19444220 10.1038/aps.2009.51
    • Chang Y-c WW, J-l Z, Huang Y (2009) Allosteric activation mechanism of the cys-loop receptors. Acta Pharmacol Sin 30:663-672
    • (2009) Acta Pharmacol Sin , vol.30 , pp. 663-672
    • Chang, Y.-C.W.W.1    Huang, Y.2
  • 14
    • 33746788525 scopus 로고    scopus 로고
    • An interaction involving an arginine residue in the cytoplasmic domain of the 5-HT3A receptor contributes to receptor desensitization mechanism
    • 16754678 10.1074/jbc.M600676200 1:CAS:528:DC%2BD28XnsVOntbY%3D
    • Hu XQ (2006) An interaction involving an arginine residue in the cytoplasmic domain of the 5-HT3A receptor contributes to receptor desensitization mechanism. J Biol Chem 281:21781-21788
    • (2006) J Biol Chem , vol.281 , pp. 21781-21788
    • Hu, X.Q.1
  • 15
    • 0030025395 scopus 로고    scopus 로고
    • The impact of receptor desensitization on fast synaptic transmission
    • 9054063 10.1016/S0166-2236(96)80037-3 1:CAS:528:DyaK28XhtlSntr0%3D
    • Jones MV, Westbrook GL (1996) The impact of receptor desensitization on fast synaptic transmission. Trends Neurosci 19:96-101
    • (1996) Trends Neurosci , vol.19 , pp. 96-101
    • Jones, M.V.1    Westbrook, G.L.2
  • 17
    • 0034932799 scopus 로고    scopus 로고
    • Acetylcholine receptor delta subunit mutations underlie a fast-channel myasthenic syndrome and arthrogryposis multiplex congenita
    • 11435464 1:CAS:528:DC%2BD3MXkvVarsL4%3D
    • Brownlow S, Webster R, Croxen R, Brydson M, Neville B, Lin JP, Vincent A, Newsom-Davis J, Beeson D (2001) Acetylcholine receptor delta subunit mutations underlie a fast-channel myasthenic syndrome and arthrogryposis multiplex congenita. J Clin Invest 108:125-130
    • (2001) J Clin Invest , vol.108 , pp. 125-130
    • Brownlow, S.1    Webster, R.2    Croxen, R.3    Brydson, M.4    Neville, B.5    Lin, J.P.6    Vincent, A.7    Newsom-Davis, J.8    Beeson, D.9
  • 18
    • 0035057060 scopus 로고    scopus 로고
    • A single amino-acid in the TM1 domain is an important determinant of the desensitization kinetics of recombinant human and guinea pig alpha-homomeric 5-hydroxytryptamine type 3 receptors
    • 11259629 1:CAS:528:DC%2BD3MXisVSqs7o%3D
    • Lobitz N, Gisselmann G, Hatt H, Wetzel CH (2001) A single amino-acid in the TM1 domain is an important determinant of the desensitization kinetics of recombinant human and guinea pig alpha-homomeric 5-hydroxytryptamine type 3 receptors. Mol Pharmacol 59:844-851
    • (2001) Mol Pharmacol , vol.59 , pp. 844-851
    • Lobitz, N.1    Gisselmann, G.2    Hatt, H.3    Wetzel, C.H.4
  • 19
    • 0023159126 scopus 로고
    • Two distinct kinetic phases of desensitization of acetylcholine receptors of clonal rat PC12 cells
    • 2445978 1:CAS:528:DyaL2sXkvFSmur8%3D
    • Boyd ND (1987) Two distinct kinetic phases of desensitization of acetylcholine receptors of clonal rat PC12 cells. J Physiol 389:45-67
    • (1987) J Physiol , vol.389 , pp. 45-67
    • Boyd, N.D.1
  • 20
    • 19444377836 scopus 로고    scopus 로고
    • Desensitized nicotinic receptors in brain
    • 15914250 10.1016/j.brainresrev.2004.09.003 1:CAS:528:DC%2BD2MXks1Cksrs%3D
    • Wang H, Sun X (2005) Desensitized nicotinic receptors in brain. Brain Res Rev 48:420-437
    • (2005) Brain Res Rev , vol.48 , pp. 420-437
    • Wang, H.1    Sun, X.2
  • 22
    • 0025202331 scopus 로고
    • Regulation of neurotransmitter receptor desensitization by protein phosphorylation
    • 1699566 10.1016/0896-6273(90)90211-W 1:CAS:528:DyaK3MXlt1OjtrY%3D
    • Huganir RL, Greengard P (1990) Regulation of neurotransmitter receptor desensitization by protein phosphorylation. Neuron 5:555-567
    • (1990) Neuron , vol.5 , pp. 555-567
    • Huganir, R.L.1    Greengard, P.2
  • 23
    • 0034126122 scopus 로고    scopus 로고
    • Chronic nicotine administration in the drinking water affects the striatal dopamine in mice
    • 10837848 10.1016/S0091-3057(00)00235-5 1:CAS:528:DC%2BD3cXjs1Cgu7w%3D
    • Pietila K, Ahtee L (2000) Chronic nicotine administration in the drinking water affects the striatal dopamine in mice. Pharmacol Biochem Behav 66:95-103
    • (2000) Pharmacol Biochem Behav , vol.66 , pp. 95-103
    • Pietila, K.1    Ahtee, L.2
  • 24
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • 18987633 10.1038/nature07462 1:CAS:528:DC%2BD1MXhtVGhug%3D%3D
    • Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux JP, Delarue M, Corringer PJ (2009) X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457:111-114
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1    Nury, H.2    Baaden, M.3    Le Poupon, C.4    Changeux, J.P.5    Delarue, M.6    Corringer, P.J.7
  • 25
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • 18987630 10.1038/nature07461 1:CAS:528:DC%2BD1MXhtVGgsA%3D%3D
    • Hilf RJ, Dutzler R (2009) Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457:115-118
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 26
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • 18322461 10.1038/nature06717 1:CAS:528:DC%2BD1cXjsFCnsLw%3D
    • Hilf RJ, Dutzler R (2008) X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452:375-379
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 27
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • 12827192 10.1038/nature01748 1:CAS:528:DC%2BD3sXkvVKmsrY%3D
    • Miyazawa A, Fujiyoshi Y, Unwin N (2003) Structure and gating mechanism of the acetylcholine receptor pore. Nature 423:949-955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 28
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • 14343300 10.1016/S0022-2836(65)80285-6 1:CAS:528:DyaF2MXkt1Ghsb4%3D
    • Monod J, Wyman J, Changeux JP (1965) On the nature of allosteric transitions: a plausible model. J Mol Biol 12:88-118
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 29
    • 0014072741 scopus 로고
    • On the arginase of the Shope papillomas
    • 6022698 10.1016/0042-6822(67)90206-1 1:CAS:528:DyaF2sXhtFansrc%3D
    • Orth G, Vielle F, Changeux JP (1967) On the arginase of the Shope papillomas. Virology 31:729-732
    • (1967) Virology , vol.31 , pp. 729-732
    • Orth, G.1    Vielle, F.2    Changeux, J.P.3
  • 30
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • 5938952 10.1021/bi00865a047 1:CAS:528:DyaF28XivVGnsw%3D%3D
    • Koshland DE Jr, Nemethy G, Filmer D (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365-385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, Jr.D.E.1    Nemethy, G.2    Filmer, D.3
  • 31
    • 79960120380 scopus 로고    scopus 로고
    • Desensitization of 7 nicotinic receptor is governed by coupling strength relative to gate tightness
    • 21610071 10.1074/jbc.M111.221754 1:CAS:528:DC%2BC3MXosFGmtbs%3D
    • Zhang J, Xue F, Whiteaker P, Li C, Wu W, Shen B, Huang Y, Lukas RJ, Chang Y (2011) Desensitization of 7 nicotinic receptor is governed by coupling strength relative to gate tightness. J Biol Chem 286:25331-25340
    • (2011) J Biol Chem , vol.286 , pp. 25331-25340
    • Zhang, J.1    Xue, F.2    Whiteaker, P.3    Li, C.4    Wu, W.5    Shen, B.6    Huang, Y.7    Lukas, R.J.8    Chang, Y.9
  • 32
    • 77949497067 scopus 로고    scopus 로고
    • The gating isomerization of neuromuscular acetylcholine receptors
    • 19933754 10.1113/jphysiol.2009.182774 1:CAS:528:DC%2BC3cXisVeksLo%3D
    • Auerbach A (2010) The gating isomerization of neuromuscular acetylcholine receptors. J Physiol 588:573-586
    • (2010) J Physiol , vol.588 , pp. 573-586
    • Auerbach, A.1
  • 33
    • 49649102025 scopus 로고    scopus 로고
    • On the nature of partial agonism in the nicotinic receptor superfamily
    • 18633353 1:CAS:528:DC%2BD1cXps1Snsrg%3D
    • Lape R, Colquhoun D, Sivilotti LG (2008) On the nature of partial agonism in the nicotinic receptor superfamily. Nature 454:722-727
    • (2008) Nature , vol.454 , pp. 722-727
    • Lape, R.1    Colquhoun, D.2    Sivilotti, L.G.3
  • 34
    • 70349584397 scopus 로고    scopus 로고
    • Single-channel kinetic analysis for activation and desensitization of homomeric 5-HT(3)A receptors
    • 19720021 10.1016/j.bpj.2009.06.018 1:CAS:528:DC%2BD1MXhsVCjsrrE
    • Corradi J, Gumilar F, Bouzat C (2009) Single-channel kinetic analysis for activation and desensitization of homomeric 5-HT(3)A receptors. Biophys J 97:1335-1345
    • (2009) Biophys J , vol.97 , pp. 1335-1345
    • Corradi, J.1    Gumilar, F.2    Bouzat, C.3
  • 35
    • 67349279395 scopus 로고    scopus 로고
    • Detection and trapping of intermediate states priming nicotinic receptor channel opening
    • 19339970 10.1038/nature07923 1:CAS:528:DC%2BD1MXjvV2lurY%3D
    • Mukhtasimova N, Lee WY, Wang HL, Sine SM (2009) Detection and trapping of intermediate states priming nicotinic receptor channel opening. Nature 459:451-454
    • (2009) Nature , vol.459 , pp. 451-454
    • Mukhtasimova, N.1    Lee, W.Y.2    Wang, H.L.3    Sine, S.M.4
  • 36
    • 0036813523 scopus 로고    scopus 로고
    • Coupled and uncoupled gating and desensitization effects by pore domain mutations in GABA(A) receptors
    • 12351715 1:CAS:528:DC%2BD38Xns1Cju74%3D
    • Scheller M, Forman SA (2002) Coupled and uncoupled gating and desensitization effects by pore domain mutations in GABA(A) receptors. J Neurosci 22:8411-8421
    • (2002) J Neurosci , vol.22 , pp. 8411-8421
    • Scheller, M.1    Forman, S.A.2
  • 37
    • 0032945358 scopus 로고    scopus 로고
    • GABAA receptor subunit gamma2 and delta subtypes confer unique kinetic properties on recombinant GABAA receptor currents in mouse fibroblasts
    • 9831714 10.1111/j.1469-7793.1999.027af.x 1:CAS:528:DyaK1MXhsFWisro%3D
    • Haas KF, Macdonald RL (1999) GABAA receptor subunit gamma2 and delta subtypes confer unique kinetic properties on recombinant GABAA receptor currents in mouse fibroblasts. J Physiol 514(Pt 1):27-45
    • (1999) J Physiol , vol.514 , Issue.PART 1 , pp. 27-45
    • Haas, K.F.1    MacDonald, R.L.2
  • 38
    • 0034143449 scopus 로고    scopus 로고
    • Effects of halothane on GABA(A) receptor kinetics: Evidence for slowed agonist unbinding
    • 10648694 1:CAS:528:DC%2BD3cXhtFGqt70%3D
    • Li X, Pearce RA (2000) Effects of halothane on GABA(A) receptor kinetics: evidence for slowed agonist unbinding. J Neurosci 20:899-907
    • (2000) J Neurosci , vol.20 , pp. 899-907
    • Li, X.1    Pearce, R.A.2
  • 39
    • 0034740987 scopus 로고    scopus 로고
    • Mutation of the 9' leucine in the GABA(A) receptor gamma2L subunit produces an apparent decrease in desensitization by stabilizing open states without altering desensitized states
    • 11640928 10.1016/S0028-3908(01)00132-0 1:CAS:528:DC%2BD3MXnsFyqu7s%3D
    • Bianchi MT, Macdonald RL (2001) Mutation of the 9' leucine in the GABA(A) receptor gamma2L subunit produces an apparent decrease in desensitization by stabilizing open states without altering desensitized states. Neuropharmacology 41:737-744
    • (2001) Neuropharmacology , vol.41 , pp. 737-744
    • Bianchi, M.T.1    MacDonald, R.L.2
  • 40
    • 50349093448 scopus 로고    scopus 로고
    • The interface between extracellular and transmembrane domains of homomeric cys-loop receptors governs open-channel lifetime and rate of desensitization
    • 18667613 10.1523/JNEUROSCI.0448-08.2008 1:CAS:528:DC%2BD1cXpsFOks74%3D
    • Bouzat C, Bartos M, Corradi J, Sine SM (2008) The interface between extracellular and transmembrane domains of homomeric cys-loop receptors governs open-channel lifetime and rate of desensitization. J Neurosci 28:7808-7819
    • (2008) J Neurosci , vol.28 , pp. 7808-7819
    • Bouzat, C.1    Bartos, M.2    Corradi, J.3    Sine, S.M.4
  • 41
    • 36849075297 scopus 로고    scopus 로고
    • Differential effects of serotonin and dopamine on human 5-HT3A receptor kinetics: Interpretation within an allosteric kinetic model
    • 18045909 10.1523/JNEUROSCI.3772-07.2007 1:CAS:528:DC%2BD2sXhsVeku7jF
    • Solt K, Ruesch D, Forman SA, Davies PA, Raines DE (2007) Differential effects of serotonin and dopamine on human 5-HT3A receptor kinetics: interpretation within an allosteric kinetic model. J Neurosci 27:13151-13160
    • (2007) J Neurosci , vol.27 , pp. 13151-13160
    • Solt, K.1    Ruesch, D.2    Forman, S.A.3    Davies, P.A.4    Raines, D.E.5
  • 42
    • 77952908488 scopus 로고    scopus 로고
    • Desensitization and models of receptor-channel activation
    • 20436045 10.1113/jphysiol.2010.188664 1:CAS:528:DC%2BC3cXmtlWiurc%3D
    • Shelley C, Cull-Candy SG (2010) Desensitization and models of receptor-channel activation. J Physiol 588:1395-1397
    • (2010) J Physiol , vol.588 , pp. 1395-1397
    • Shelley, C.1    Cull-Candy, S.G.2
  • 43
    • 0024312649 scopus 로고
    • Desensitization of the acetylcholine receptor of frog end-plates measured in a Vaseline-gap voltage clamp
    • 2561785 1:CAS:528:DyaL1MXksFSqt74%3D
    • Cachelin AB, Colquhoun D (1989) Desensitization of the acetylcholine receptor of frog end-plates measured in a Vaseline-gap voltage clamp. J Physiol 415:159-188
    • (1989) J Physiol , vol.415 , pp. 159-188
    • Cachelin, A.B.1    Colquhoun, D.2
  • 44
    • 0027509690 scopus 로고
    • A molecular scheme for the reaction between acetylcholine and nicotinic channels
    • 7681332 10.1016/S0006-3495(93)81374-2 1:CAS:528:DyaK3sXhvVCis70%3D
    • Franke C, Parnas H, Hovav G, Dudel J (1993) A molecular scheme for the reaction between acetylcholine and nicotinic channels. Biophys J 64:339-356
    • (1993) Biophys J , vol.64 , pp. 339-356
    • Franke, C.1    Parnas, H.2    Hovav, G.3    Dudel, J.4
  • 45
    • 0037107163 scopus 로고    scopus 로고
    • Desensitization mechanism of GABA receptors revealed by single oocyte binding and receptor function
    • 12223551 1:CAS:528:DC%2BD38Xnt12ksLs%3D
    • Chang Y, Ghansah E, Chen Y, Ye J, Weiss DS (2002) Desensitization mechanism of GABA receptors revealed by single oocyte binding and receptor function. J Neurosci 22:7982-7990
    • (2002) J Neurosci , vol.22 , pp. 7982-7990
    • Chang, Y.1    Ghansah, E.2    Chen, Y.3    Ye, J.4    Weiss, D.S.5
  • 46
    • 0038149197 scopus 로고    scopus 로고
    • Life at the top: The transition state of AChR gating
    • 12824477 10.1126/stke.2003.188.re11
    • Auerbach A (2003) Life at the top: the transition state of AChR gating. Sci STKE 2003(188):re11
    • (2003) Sci STKE , vol.2003 , Issue.188 , pp. 11
    • Auerbach, A.1
  • 47
    • 41649119572 scopus 로고    scopus 로고
    • Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer
    • 18376414 10.1038/nsmb.1407 1:CAS:528:DC%2BD1cXktFyjtb8%3D
    • Cymes GD, Grosman C (2008) Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer. Nat Struct Mol Biol 15:389-396
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 389-396
    • Cymes, G.D.1    Grosman, C.2
  • 48
    • 65949085351 scopus 로고    scopus 로고
    • Number and locations of agonist binding sites required to activate homomeric cys-loop receptors
    • 19420269 10.1523/JNEUROSCI.0627-09.2009 1:CAS:528:DC%2BD1MXlvVGntL4%3D
    • Rayes D, De Rosa MJ, Sine SM, Bouzat C (2009) Number and locations of agonist binding sites required to activate homomeric cys-loop receptors. J Neurosci 29:6022-6032
    • (2009) J Neurosci , vol.29 , pp. 6022-6032
    • Rayes, D.1    De Rosa, M.J.2    Sine, S.M.3    Bouzat, C.4
  • 49
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • 15701510 10.1016/j.jmb.2004.12.031 1:CAS:528:DC%2BD2MXhtFGrsbs%3D
    • Unwin N (2005) Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J Mol Biol 346:967-989
    • (2005) J Mol Biol , vol.346 , pp. 967-989
    • Unwin, N.1
  • 50
    • 0037448581 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in the GABA(A) receptor
    • 12529644 10.1038/nature01280 1:CAS:528:DC%2BD3sXjsF2htA%3D%3D
    • Kash TL, Jenkins A, Kelley JC, Trudell JR, Harrison NL (2003) Coupling of agonist binding to channel gating in the GABA(A) receptor. Nature 421:272-275
    • (2003) Nature , vol.421 , pp. 272-275
    • Kash, T.L.1    Jenkins, A.2    Kelley, J.C.3    Trudell, J.R.4    Harrison, N.L.5
  • 51
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel
    • 15318223 10.1038/nature02753 1:CAS:528:DC%2BD2cXmslCnuro%3D
    • Bouzat C, Gumilar F, Spitzmaul G, Wang HL, Rayes D, Hansen SB, Taylor P, Sine SM (2004) Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel. Nature 430:896-900
    • (2004) Nature , vol.430 , pp. 896-900
    • Bouzat, C.1    Gumilar, F.2    Spitzmaul, G.3    Wang, H.L.4    Rayes, D.5    Hansen, S.B.6    Taylor, P.7    Sine, S.M.8
  • 52
    • 1842686239 scopus 로고    scopus 로고
    • Gating dynamics of the acetylcholine receptor extracellular domain
    • 15051806 10.1085/jgp.200309004 1:CAS:528:DC%2BD2cXjs1aitLY%3D
    • Chakrapani S, Bailey TD, Auerbach A (2004) Gating dynamics of the acetylcholine receptor extracellular domain. J Gen Physiol 123:341-356
    • (2004) J Gen Physiol , vol.123 , pp. 341-356
    • Chakrapani, S.1    Bailey, T.D.2    Auerbach, A.3
  • 53
    • 27744438169 scopus 로고    scopus 로고
    • Principal pathway coupling agonist binding to channel gating in nicotinic receptors
    • 16281039 10.1038/nature04156 1:CAS:528:DC%2BD2MXhtF2nsrjE
    • Lee WY, Sine SM (2005) Principal pathway coupling agonist binding to channel gating in nicotinic receptors. Nature 438:243-247
    • (2005) Nature , vol.438 , pp. 243-247
    • Lee, W.Y.1    Sine, S.M.2
  • 54
    • 27744608733 scopus 로고    scopus 로고
    • Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
    • 16281040 10.1038/nature04130 1:CAS:528:DC%2BD2MXhtF2nsrjL
    • Lummis SC, Beene DL, Lee LW, Lester HA, Broadhurst RW, Dougherty DA (2005) Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature 438:248-252
    • (2005) Nature , vol.438 , pp. 248-252
    • Lummis, S.C.1    Beene, D.L.2    Lee, L.W.3    Lester, H.A.4    Broadhurst, R.W.5    Dougherty, D.A.6
  • 55
    • 29344468233 scopus 로고    scopus 로고
    • Improved gating of a chimeric alpha7-5HT3A receptor upon mutations at the M2-M3 extracellular loop
    • 16364316 10.1016/j.febslet.2005.12.010 1:CAS:528:DC%2BD28Xkslyn
    • Castillo M, Mulet J, Bernal JA, Criado M, Sala F, Sala S (2006) Improved gating of a chimeric alpha7-5HT3A receptor upon mutations at the M2-M3 extracellular loop. FEBS Lett 580:256-260
    • (2006) FEBS Lett , vol.580 , pp. 256-260
    • Castillo, M.1    Mulet, J.2    Bernal, J.A.3    Criado, M.4    Sala, F.5    Sala, S.6
  • 56
    • 33644520967 scopus 로고    scopus 로고
    • Charged residues in the alpha1 and beta2 pre-M1 regions involved in GABAA receptor activation
    • 16481436 10.1523/JNEUROSCI.4555-05.2006 1:CAS:528:DC%2BD28XitVansLc%3D
    • Mercado J, Czajkowski C (2006) Charged residues in the alpha1 and beta2 pre-M1 regions involved in GABAA receptor activation. J Neurosci 26:2031-2040
    • (2006) J Neurosci , vol.26 , pp. 2031-2040
    • Mercado, J.1    Czajkowski, C.2
  • 57
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • 9009272 10.1093/emboj/16.1.110 1:CAS:528:DyaK2sXot1GmtQ%3D%3D
    • Lynch JW, Rajendra S, Pierce KD, Handford CA, Barry PH, Schofield PR (1997) Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel. EMBO J 16:110-120
    • (1997) EMBO J , vol.16 , pp. 110-120
    • Lynch, J.W.1    Rajendra, S.2    Pierce, K.D.3    Handford, C.A.4    Barry, P.H.5    Schofield, P.R.6
  • 58
    • 0032520102 scopus 로고    scopus 로고
    • Properties of human glycine receptors containing the hyperekplexia mutation alpha1(K276E), expressed in Xenopus oocytes
    • 9490812 10.1111/j.1469-7793.1998.025bu.x 1:CAS:528:DyaK1cXhslyjsb0%3D
    • Lewis TM, Sivilotti LG, Colquhoun D, Gardiner RM, Schoepfer R, Rees M (1998) Properties of human glycine receptors containing the hyperekplexia mutation alpha1(K276E), expressed in Xenopus oocytes. J Physiol 507(Pt 1):25-40
    • (1998) J Physiol , vol.507 , Issue.PART 1 , pp. 25-40
    • Lewis, T.M.1    Sivilotti, L.G.2    Colquhoun, D.3    Gardiner, R.M.4    Schoepfer, R.5    Rees, M.6
  • 59
    • 0010214174 scopus 로고
    • Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor
    • 6320162 10.1073/pnas.81.1.155 1:CAS:528:DyaL2cXotVSjuw%3D%3D
    • Finer-Moore J, Stroud RM (1984) Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor. Proc Natl Acad Sci U S A 81:155-159
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 155-159
    • Finer-Moore, J.1    Stroud, R.M.2
  • 60
    • 77949521932 scopus 로고    scopus 로고
    • Advances and hold-ups in the study of structure, function and regulation of cys-loop ligand-gated ion channels and receptors
    • 20173078 10.1113/jphysiol.2009.185488 1:CAS:528:DC%2BC3cXisVeksL8%3D
    • Yakel J (2010) Advances and hold-ups in the study of structure, function and regulation of cys-loop ligand-gated ion channels and receptors. J Physiol 588:555-556
    • (2010) J Physiol , vol.588 , pp. 555-556
    • Yakel, J.1
  • 61
    • 77949521702 scopus 로고    scopus 로고
    • Novel structural determinants of single channel conductance and ion selectivity in 5-hydroxytryptamine type 3 and nicotinic acetylcholine receptors
    • 19933751 10.1113/jphysiol.2009.183137 1:CAS:528:DC%2BC3cXisVeksLs%3D
    • Peters JA, Cooper MA, Carland JE, Livesey MR, Hales TG, Lambert JJ (2010) Novel structural determinants of single channel conductance and ion selectivity in 5-hydroxytryptamine type 3 and nicotinic acetylcholine receptors. J Physiol 588:587-596
    • (2010) J Physiol , vol.588 , pp. 587-596
    • Peters, J.A.1    Cooper, M.A.2    Carland, J.E.3    Livesey, M.R.4    Hales, T.G.5    Lambert, J.J.6
  • 62
    • 41649109805 scopus 로고    scopus 로고
    • Influence of the M3-M4 intracellular domain upon nicotinic acetylcholine receptor assembly, targeting and function
    • 18204482 10.1038/sj.bjp.0707676 1:CAS:528:DC%2BD1cXktVWmsrs%3D
    • Kracun S, Harkness PC, Gibb AJ, Millar NS (2008) Influence of the M3-M4 intracellular domain upon nicotinic acetylcholine receptor assembly, targeting and function. Br J Pharmacol 153:1474-1484
    • (2008) Br J Pharmacol , vol.153 , pp. 1474-1484
    • Kracun, S.1    Harkness, P.C.2    Gibb, A.J.3    Millar, N.S.4
  • 63
    • 0041806486 scopus 로고    scopus 로고
    • A cytoplasmic region determines single-channel conductance in 5-HT3 receptors
    • 12867984 10.1038/nature01788 1:CAS:528:DC%2BD3sXlsVGjs7k%3D
    • Kelley SP, Dunlop JI, Kirkness EF, Lambert JJ, Peters JA (2003) A cytoplasmic region determines single-channel conductance in 5-HT3 receptors. Nature 424:321-324
    • (2003) Nature , vol.424 , pp. 321-324
    • Kelley, S.P.1    Dunlop, J.I.2    Kirkness, E.F.3    Lambert, J.J.4    Peters, J.A.5
  • 64
    • 26844573941 scopus 로고    scopus 로고
    • A role for the 1-2 loop in the gating of 5-HT3 receptors
    • 16221844 10.1523/JNEUROSCI.1045-05.2005 1:CAS:528:DC%2BD2MXhtFGmu7rI
    • Reeves DC (2005) A role for the 1-2 loop in the gating of 5-HT3 receptors. J Neurosci 25:9358-9366
    • (2005) J Neurosci , vol.25 , pp. 9358-9366
    • Reeves, D.C.1
  • 65
    • 38749094806 scopus 로고    scopus 로고
    • Modular design of cys-loop ligand-gated ion channels: Functional 5-HT3 and GABA rho1 receptors lacking the large cytoplasmic M3M4 loop
    • 18227272 10.1085/jgp.200709896 1:CAS:528:DC%2BD1cXis1WktLY%3D
    • Jansen M, Bali M, Akabas MH (2008) Modular design of cys-loop ligand-gated ion channels: functional 5-HT3 and GABA rho1 receptors lacking the large cytoplasmic M3M4 loop. J Gen Physiol 131:137-146
    • (2008) J Gen Physiol , vol.131 , pp. 137-146
    • Jansen, M.1    Bali, M.2    Akabas, M.H.3
  • 67
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • 11836518 10.1038/nrn731 1:CAS:528:DC%2BD38Xhslyju7Y%3D
    • Karlin A (2002) Emerging structure of the nicotinic acetylcholine receptors. Nat Rev Neurosci 3:102-114
    • (2002) Nat Rev Neurosci , vol.3 , pp. 102-114
    • Karlin, A.1
  • 68
    • 33744477329 scopus 로고    scopus 로고
    • Block of muscle nicotinic receptors by choline suggests that the activation and desensitization gates act as distinct molecular entities
    • 16735755 10.1085/jgp.200509437 1:CAS:528:DC%2BD28Xms1SitLw%3D
    • Purohit Y, Grosman C (2006) Block of muscle nicotinic receptors by choline suggests that the activation and desensitization gates act as distinct molecular entities. J Gen Physiol 127:703-717
    • (2006) J Gen Physiol , vol.127 , pp. 703-717
    • Purohit, Y.1    Grosman, C.2
  • 69
    • 33644870155 scopus 로고    scopus 로고
    • Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP
    • 16505382 10.1073/pnas.0507889103 1:CAS:528:DC%2BD28XivFWju74%3D
    • Ulens C, Hogg RC, Celie PH, Bertrand D, Tsetlin V, Smit AB, Sixma TK (2006) Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP. Proc Natl Acad Sci U S A 103:3615-3620
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3615-3620
    • Ulens, C.1    Hogg, R.C.2    Celie, P.H.3    Bertrand, D.4    Tsetlin, V.5    Smit, A.B.6    Sixma, T.K.7
  • 71
    • 0027194134 scopus 로고
    • Single amino acid substitution affects desensitization of the 5-hydroxytryptamine type 3 receptor expressed in Xenopus oocytes
    • 8506347 10.1073/pnas.90.11.5030 1:CAS:528:DyaK2cXjtFKjsL4%3D
    • Yakel JL, Lagrutta A, Adelman JP, North RA (1993) Single amino acid substitution affects desensitization of the 5-hydroxytryptamine type 3 receptor expressed in Xenopus oocytes. Proc Natl Acad Sci U S A 90:5030-5033
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 5030-5033
    • Yakel, J.L.1    Lagrutta, A.2    Adelman, J.P.3    North, R.A.4
  • 72
    • 0031967525 scopus 로고    scopus 로고
    • Substitutions of the highly conserved M2 leucine create spontaneously opening rho1 gamma-aminobutyric acid receptors
    • 9495819 1:CAS:528:DyaK1cXhslCnu7o%3D
    • Chang Y, Weiss DS (1998) Substitutions of the highly conserved M2 leucine create spontaneously opening rho1 gamma-aminobutyric acid receptors. Mol Pharmacol 53:511-523
    • (1998) Mol Pharmacol , vol.53 , pp. 511-523
    • Chang, Y.1    Weiss, D.S.2
  • 73
    • 0033359997 scopus 로고    scopus 로고
    • Channel opening locks agonist onto the GABAC receptor
    • 10195213 10.1038/6313 1:CAS:528:DyaK1MXhsl2gurc%3D
    • Chang Y, Weiss DS (1999) Channel opening locks agonist onto the GABAC receptor. Nat Neurosci 2:219-225
    • (1999) Nat Neurosci , vol.2 , pp. 219-225
    • Chang, Y.1    Weiss, D.S.2
  • 74
    • 0032728861 scopus 로고    scopus 로고
    • Allosteric activation mechanism of the alpha 1 beta 2 gamma 2 gamma-aminobutyric acid type A receptor revealed by mutation of the conserved M2 leucine
    • 10545355 10.1016/S0006-3495(99)77089-X 1:CAS:528:DyaK1MXnt1Wktb8%3D
    • Chang Y, Weiss DS (1999) Allosteric activation mechanism of the alpha 1 beta 2 gamma 2 gamma-aminobutyric acid type A receptor revealed by mutation of the conserved M2 leucine. Biophys J 77:2542-2551
    • (1999) Biophys J , vol.77 , pp. 2542-2551
    • Chang, Y.1    Weiss, D.S.2
  • 75
    • 29244442919 scopus 로고    scopus 로고
    • A unified view of the role of electrostatic interactions in modulating the gating of cys loop receptors
    • 16216879 10.1074/jbc.M508635200 1:CAS:528:DC%2BD2MXhtlShsbnO
    • Xiu X, Hanek AP, Wang J, Lester HA, Dougherty DA (2005) A unified view of the role of electrostatic interactions in modulating the gating of cys loop receptors. J Biol Chem 280:41655-41666
    • (2005) J Biol Chem , vol.280 , pp. 41655-41666
    • Xiu, X.1    Hanek, A.P.2    Wang, J.3    Lester, H.A.4    Dougherty, D.A.5
  • 76
    • 14844295746 scopus 로고    scopus 로고
    • Charged amino acids of the N-terminal domain are involved in coupling binding and gating in alpha7 nicotinic receptors
    • 15611071 10.1074/jbc.M411048200 1:CAS:528:DC%2BD2MXhsV2qsbs%3D
    • Sala F, Mulet J, Sala S, Gerber S, Criado M (2005) Charged amino acids of the N-terminal domain are involved in coupling binding and gating in alpha7 nicotinic receptors. J Biol Chem 280:6642-6647
    • (2005) J Biol Chem , vol.280 , pp. 6642-6647
    • Sala, F.1    Mulet, J.2    Sala, S.3    Gerber, S.4    Criado, M.5
  • 77
    • 0037124034 scopus 로고    scopus 로고
    • Point mutation in the first transmembrane region of the beta 2 subunit of the gamma-aminobutyric acid type A receptor alters desensitization kinetics of gamma-aminobutyric acid- and anesthetic-induced channel gating
    • 11877425 10.1074/jbc.M111215200 1:CAS:528:DC%2BD38XktVCgtrY%3D
    • Engblom AC, Carlson BX, Olsen RW, Schousboe A, Kristiansen U (2002) Point mutation in the first transmembrane region of the beta 2 subunit of the gamma-aminobutyric acid type A receptor alters desensitization kinetics of gamma-aminobutyric acid- and anesthetic-induced channel gating. J Biol Chem 277:17438-17447
    • (2002) J Biol Chem , vol.277 , pp. 17438-17447
    • Engblom, A.C.1    Carlson, B.X.2    Olsen, R.W.3    Schousboe, A.4    Kristiansen, U.5
  • 78
    • 0035866070 scopus 로고    scopus 로고
    • Structural determinants of fast desensitization and desensitization- deactivation coupling in GABAa receptors
    • 11160383 1:CAS:528:DC%2BD3MXhtFers7o%3D
    • Bianchi MT, Haas KF, Macdonald RL (2001) Structural determinants of fast desensitization and desensitization-deactivation coupling in GABAa receptors. J Neurosci 21:1127-1136
    • (2001) J Neurosci , vol.21 , pp. 1127-1136
    • Bianchi, M.T.1    Haas, K.F.2    MacDonald, R.L.3
  • 79
    • 0032527959 scopus 로고    scopus 로고
    • Separate domains for desensitization of GABA rho 1 and beta 2 subunits expressed in Xenopus oocytes
    • 9662556 10.1007/s002329900398 1:CAS:528:DyaK1cXks1KltLY%3D
    • Lu L, Huang Y (1998) Separate domains for desensitization of GABA rho 1 and beta 2 subunits expressed in Xenopus oocytes. J Membr Biol 164:115-124
    • (1998) J Membr Biol , vol.164 , pp. 115-124
    • Lu, L.1    Huang, Y.2
  • 80
    • 78449248065 scopus 로고    scopus 로고
    • Rapid desensitization of the rat alpha7 nAChR is facilitated by the presence of a proline residue in the outer beta-sheet
    • 20837638 10.1113/jphysiol.2010.195495 1:CAS:528:DC%2BC3cXhsFaqs7rF
    • McCormack TJ, Melis C, Colon J, Gay EA, Mike A, Karoly R, Lamb PW, Molteni C, Yakel JL (2010) Rapid desensitization of the rat alpha7 nAChR is facilitated by the presence of a proline residue in the outer beta-sheet. J Physiol 588:4415-4429
    • (2010) J Physiol , vol.588 , pp. 4415-4429
    • McCormack, T.J.1    Melis, C.2    Colon, J.3    Gay, E.A.4    Mike, A.5    Karoly, R.6    Lamb, P.W.7    Molteni, C.8    Yakel, J.L.9
  • 81
    • 77949509797 scopus 로고    scopus 로고
    • Gating of nicotinic ACh receptors: Latest insights into ligand binding and function
    • 19917567 10.1113/jphysiol.2009.182691 1:CAS:528:DC%2BC3cXisVeksLg%3D
    • Yakel JL (2010) Gating of nicotinic ACh receptors: latest insights into ligand binding and function. J Physiol 588:597-602
    • (2010) J Physiol , vol.588 , pp. 597-602
    • Yakel, J.L.1
  • 82
    • 0035916261 scopus 로고    scopus 로고
    • Desensitization of neuronal nicotinic acetylcholine receptors conferred by N-terminal segments of the beta 2 subunit
    • 11329274 10.1021/bi0020022 1:CAS:528:DC%2BD3MXlsFGitg%3D%3D
    • Bohler S, Gay S, Bertrand S, Corringer PJ, Edelstein SJ, Changeux JP, Bertrand D (2001) Desensitization of neuronal nicotinic acetylcholine receptors conferred by N-terminal segments of the beta 2 subunit. Biochemistry 40:2066-2074
    • (2001) Biochemistry , vol.40 , pp. 2066-2074
    • Bohler, S.1    Gay, S.2    Bertrand, S.3    Corringer, P.J.4    Edelstein, S.J.5    Changeux, J.P.6    Bertrand, D.7
  • 83
    • 4644265039 scopus 로고    scopus 로고
    • Molecular structure and function of the glycine receptor chloride channel
    • 15383648 10.1152/physrev.00042.2003 1:CAS:528:DC%2BD2cXovVyltLk%3D
    • Lynch JW (2004) Molecular structure and function of the glycine receptor chloride channel. Physiol Rev 84:1051-1095
    • (2004) Physiol Rev , vol.84 , pp. 1051-1095
    • Lynch, J.W.1
  • 84
    • 0033080914 scopus 로고    scopus 로고
    • Novel GLRA1 missense mutation (P250T) in dominant hyperekplexia defines an intracellular determinant of glycine receptor channel gating
    • 9920650 1:CAS:528:DyaK1MXpsl2mtQ%3D%3D
    • Saul B, Kuner T, Sobetzko D, Brune W, Hanefeld F, Meinck HM, Becker CM (1999) Novel GLRA1 missense mutation (P250T) in dominant hyperekplexia defines an intracellular determinant of glycine receptor channel gating. J Neurosci 19:869-877
    • (1999) J Neurosci , vol.19 , pp. 869-877
    • Saul, B.1    Kuner, T.2    Sobetzko, D.3    Brune, W.4    Hanefeld, F.5    Meinck, H.M.6    Becker, C.M.7
  • 85
    • 0035839433 scopus 로고    scopus 로고
    • Opposing effects of molecular volume and charge at the hyperekplexia site alpha 1(P250) govern glycine receptor activation and desensitization
    • 11395484 10.1074/jbc.M100446200 1:CAS:528:DC%2BD3MXmtFeitbg%3D
    • Breitinger HG, Villmann C, Becker K, Becker CM (2001) Opposing effects of molecular volume and charge at the hyperekplexia site alpha 1(P250) govern glycine receptor activation and desensitization. J Biol Chem 276:29657-29663
    • (2001) J Biol Chem , vol.276 , pp. 29657-29663
    • Breitinger, H.G.1    Villmann, C.2    Becker, K.3    Becker, C.M.4
  • 86
    • 33746788525 scopus 로고    scopus 로고
    • An interaction involving an arginine residue in the cytoplasmic domain of the 5-HT3A receptor contributes to receptor desensitization mechanism
    • 16754678 10.1074/jbc.M600676200 1:CAS:528:DC%2BD28XnsVOntbY%3D
    • Hu XQ, Sun H, Peoples RW, Hong R, Zhang L (2006) An interaction involving an arginine residue in the cytoplasmic domain of the 5-HT3A receptor contributes to receptor desensitization mechanism. J Biol Chem 281:21781-21788
    • (2006) J Biol Chem , vol.281 , pp. 21781-21788
    • Hu, X.Q.1    Sun, H.2    Peoples, R.W.3    Hong, R.4    Zhang, L.5
  • 87
    • 33344468020 scopus 로고    scopus 로고
    • Ligand binding transmits conformational changes across the membrane-spanning region to the intracellular side of the 5-HT3 serotonin receptor
    • 16254942 10.1002/cbic.200500191 1:CAS:528:DC%2BD2MXhtlalu7fP
    • Ilegems E, Pick H, Deluz C, Kellenberger S, Vogel H (2005) Ligand binding transmits conformational changes across the membrane-spanning region to the intracellular side of the 5-HT3 serotonin receptor. ChemBioChem 6:2180-2185
    • (2005) ChemBioChem , vol.6 , pp. 2180-2185
    • Ilegems, E.1    Pick, H.2    Deluz, C.3    Kellenberger, S.4    Vogel, H.5


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