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Journal of General Physiology
Volumn 141, Issue 4, 2013, Pages 467-478
Loop C and the mechanism of acetylcholine receptor-channel gating
Author keywords

[No Author keywords available]
Indexed keywords

NICOTINIC AGENT; NICOTINIC RECEPTOR;
EID: 84878637061     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210946     Document Type: Article
Times cited : (60)
References (50)
  • 1
    • 0026711051 scopus 로고
    • Kinetic behavior of cloned mouse acetylcholine receptors. A semi-autonomous, stepwise model of gating
    • Auerbach, A. 1992. Kinetic behavior of cloned mouse acetylcholine receptors. A semi-autonomous, stepwise model of gating. Biophys. J. 62:72-73. http://dx.doi.org/10.1016/S0006-3495(92)81783-6
    • (1992) Biophys. J. , vol.62 , pp. 72-73
    • Auerbach, A.1
  • 2
    • 0027410307 scopus 로고
    • A statistical analysis of acetylcholine receptor activation in Xenopus myocytes: stepwise versus concerted models of gating
    • Auerbach, A. 1993. A statistical analysis of acetylcholine receptor activation in Xenopus myocytes: stepwise versus concerted models of gating. J. Physiol. 461:339-378.
    • (1993) J. Physiol. , vol.461 , pp. 339-378
    • Auerbach, A.1
  • 3
    • 13444274310 scopus 로고    scopus 로고
    • Gating of acetylcholine receptor channels: Brownian motion across a broad transition state
    • USA
    • Auerbach, A. 2005. Gating of acetylcholine receptor channels: Brownian motion across a broad transition state. Proc. Natl. Acad. Sci. USA. 102:1408-1412. http://dx.doi.org/10.1073/pnas.0406787102
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 1408-1412
    • Auerbach, A.1
  • 4
    • 77949497067 scopus 로고    scopus 로고
    • The gating isomerization of neuromuscular acetylcholine receptors
    • Auerbach, A. 2010. The gating isomerization of neuromuscular acetylcholine receptors. J. Physiol. 588:573-586. http://dx.doi.org/10 .1113/jphysiol.2009.182774
    • (2010) J. Physiol. , vol.588 , pp. 573-586
    • Auerbach, A.1
  • 5
    • 84876411224 scopus 로고    scopus 로고
    • The energy and work of a ligand-gated ion channel
    • Auerbach, A. 2013. The energy and work of a ligand-gated ion channel. J. Mol. Biol. In press.
    • (2013) J. Mol. Biol. In press.
    • Auerbach, A.1
  • 6
    • 49649099967 scopus 로고    scopus 로고
    • Gating at the mouth of the acetylcholine receptor channel: energetic consequences of mutations in the alphaM2-cap
    • Bafna, P.A., P.G. Purohit, and A. Auerbach. 2008. Gating at the mouth of the acetylcholine receptor channel: energetic consequences of mutations in the alphaM2-cap. PLoS ONE. 3:e2515. http://dx.doi.org/ 10.1371/journal.pone.0002515
    • (2008) PLoS ONE. , vol.3
    • Bafna, P.A.1    Purohit, P.G.2    Auerbach, A.3
  • 7
    • 79953684899 scopus 로고    scopus 로고
    • A structural and mutagenic blueprint for molecular recognition of strychnine and d-tubocurarine by different cys-loop receptors
    • Brams, M., A. Pandya, D. Kuzmin, R. van Elk, L. Krijnen, J.L. Yakel, V. Tsetlin, A.B. Smit, and C. Ulens. 2011. A structural and mutagenic blueprint for molecular recognition of strychnine and d-tubocurarine by different cys-loop receptors. PLoS Biol. 9:e1001034. http:// dx.doi.org/10.1371/journal.pbio.1001034
    • (2011) PLoS Biol. , vol.9
    • 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
  • 8
    • 34547691116 scopus 로고    scopus 로고
    • Conformational dynamics of the alphaM3 transmembrane helix during acetylcholine receptor channel gating
    • Cadugan, D.J., and A. Auerbach. 2007. Conformational dynamics of the alphaM3 transmembrane helix during acetylcholine receptor channel gating. Biophys. J. 93:859-865. http://dx.doi.org/10.1529/ biophysj.107.105171
    • (2007) Biophys. J. , vol.93 , pp. 859-865
    • Cadugan, D.J.1    Auerbach, A.2
  • 9
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie, P.H., S.E. van Rossum-Fikkert, W.J. van Dijk, K. Brejc, A.B. Smit, and T.K. Sixma. 2004. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron. 41:907-914. http://dx.doi.org/10.1016/ S0896-6273(04)00115-1
    • (2004) Neuron. , vol.41 , pp. 907-914
    • Celie, P.H.1    van Rossum-Fikkert, S.E.2    van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 10
    • 0029153305 scopus 로고
    • Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of alpha-subunit tyrosine 190 affect both binding and gating
    • Chen, J., Y. Zhang, G. Akk, S. Sine, and A. Auerbach. 1995. Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of alpha-subunit tyrosine 190 affect both binding and gating. Biophys. J. 69:849-859. http://dx.doi.org/10.1016/ S0006-3495(95)79959-3
    • (1995) Biophys. J. , vol.69 , pp. 849-859
    • Chen, J.1    Zhang, Y.2    Akk, G.3    Sine, S.4    Auerbach, A.5
  • 11
    • 70449143838 scopus 로고
    • Interaction at end-plate receptors between different choline derivatives
    • Del Castillo, J., and B. Katz. 1957. Interaction at end-plate receptors between different choline derivatives. Proc. R. Soc. Lond. B Biol. Sci. 146:369-381. http://dx.doi.org/10.1098/rspb.1957.0018
    • (1957) Proc. R. Soc. Lond. B Biol. Sci. , vol.146 , pp. 369-381
    • Del Castillo, J.1    Katz, B.2
  • 12
    • 0034100847 scopus 로고    scopus 로고
    • Kinetic, mechanistic, and structural aspects of unliganded gating of acetylcholine receptor channels: A single-channel study of second transmembrane segment 12? mutants
    • Grosman, C., and A. Auerbach. 2000. Kinetic, mechanistic, and structural aspects of unliganded gating of acetylcholine receptor channels: A single-channel study of second transmembrane segment 12? mutants. J. Gen. Physiol. 115:621-635. http://dx.doi
    • (2000) J. Gen. Physiol. , vol.115 , pp. 621-635
    • Grosman, C.1    Auerbach, A.2
  • 13
    • 0035923695 scopus 로고    scopus 로고
    • The dissociation of acetylcholine from open nicotinic receptor channels
    • Grosman, C., and A. Auerbach. 2001. The dissociation of acetylcholine from open nicotinic receptor channels. Proc. Natl. Acad. Sci. USA. 98:14102-14107. http://dx.doi.org/10.1073/pnas.251402498
    • (2001) Proc. Natl. Acad. Sci. USA. , vol.98 , pp. 14102-14107
    • Grosman, C.1    Auerbach, A.2
  • 14
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • Grosman, C., M. Zhou, and A. Auerbach. 2000. Mapping the conformational wave of acetylcholine receptor channel gating. Nature. 403:773-776. http://dx.doi.org/10.1038/35001586
    • (2000) Nature. , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 15
    • 79951834831 scopus 로고    scopus 로고
    • Temperature dependence of acetylcholine receptor channels activated by different agonists
    • Gupta, S., and A. Auerbach. 2011. Temperature dependence of acetylcholine receptor channels activated by different agonists. Biophys. J. 100:895-903. http://dx.doi.org/10.1016/j.bpj.2010.12.3727
    • (2011) Biophys. J. , vol.100 , pp. 895-903
    • Gupta, S.1    Auerbach, A.2
  • 16
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen, S.B., G. Sulzenbacher, T. Huxford, P. Marchot, P. Taylor, and Y. Bourne. 2005. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J. 24:3635-3646. http://dx .doi.org/10.1038/sj.emboj.7600828
    • (2005) EMBO J. , vol.24 , pp. 3635-3646
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 17
    • 0022628717 scopus 로고
    • Kinetics of unliganded acetylcholine receptor channel gating
    • Jackson, M.B. 1986. Kinetics of unliganded acetylcholine receptor channel gating. Biophys. J. 49:663-672. http://dx.doi.org/10 .1016/S0006-3495(86)83693-1
    • (1986) Biophys. J. , vol.49 , pp. 663-672
    • Jackson, M.B.1
  • 18
    • 84864009008 scopus 로고    scopus 로고
    • An integrated catch-and-hold mechanism activates nicotinic acetylcholine receptors
    • Jadey, S., and A. Auerbach. 2012. An integrated catch-and-hold mechanism activates nicotinic acetylcholine receptors. J. Gen. Physiol. 140:17-28. http://dx.doi.org/10.1085/jgp.201210801
    • (2012) J. Gen. Physiol. , vol.140 , pp. 17-28
    • Jadey, S.1    Auerbach, A.2
  • 19
    • 79951824109 scopus 로고    scopus 로고
    • Design and control of acetylcholine receptor conformational change
    • USA
    • Jadey, S.V., P. Purohit, I. Bruhova, T.M. Gregg, and A. Auerbach. 2011. Design and control of acetylcholine receptor conformational change. Proc. Natl. Acad. Sci. USA. 108:4328-4333. http:// dx.doi.org/10.1073/pnas.1016617108
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 4328-4333
    • Jadey, S.V.1    Purohit, P.2    Bruhova, I.3    Gregg, T.M.4    Auerbach, A.5
  • 20
    • 77950248091 scopus 로고    scopus 로고
    • Acetylcholine receptor channels activated by a single agonist molecule
    • Jha, A., and A. Auerbach. 2010. Acetylcholine receptor channels activated by a single agonist molecule. Biophys. J. 98:1840-1846. http://dx.doi.org/10.1016/j.bpj.2010.01.025
    • (2010) Biophys. J. , vol.98 , pp. 1840-1846
    • Jha, A.1    Auerbach, A.2
  • 21
    • 36549043834 scopus 로고    scopus 로고
    • Acetylcholine receptor gating at extracellular transmembrane domain interface: The cys-loop and M2-M3 linker
    • Jha, A., D.J. Cadugan, P. Purohit, and A. Auerbach. 2007. Acetylcholine receptor gating at extracellular transmembrane domain interface: The cys-loop and M2-M3 linker. J. Gen. Physiol. 130:547-558. http://dx.doi.org/10.1085/jgp.200709856
    • (2007) J. Gen. Physiol. , vol.130 , pp. 547-558
    • Jha, A.1    Cadugan, D.J.2    Purohit, P.3    Auerbach, A.4
  • 22
    • 68049143193 scopus 로고    scopus 로고
    • Energy and structure of the M2 helix in acetylcholine receptor-channel gating
    • Jha, A., P. Purohit, and A. Auerbach. 2009. Energy and structure of the M2 helix in acetylcholine receptor-channel gating. Biophys. J. 96:4075-4084. http://dx.doi.org/10.1016/j.bpj.2009.02.030
    • (2009) Biophys. J. , vol.96 , pp. 4075-4084
    • Jha, A.1    Purohit, P.2    Auerbach, A.3
  • 23
    • 0014115893 scopus 로고
    • On the application of "a plausible model" of allosteric proteins to the receptor for acetylcholine
    • Karlin, A. 1967. On the application of "a plausible model" of allosteric proteins to the receptor for acetylcholine. J. Theor. Biol. 16:306-320. http://dx.doi.org/10.1016/0022-5193(67)90011-2
    • (1967) J. Theor. Biol. , vol.16 , pp. 306-320
    • Karlin, A.1
  • 24
    • 85021531015 scopus 로고
    • Chemical modification of the active site of the acetylcholine receptor
    • Karlin, A. 1969. Chemical modification of the active site of the acetylcholine receptor. J. Gen. Physiol. 54:245-264.
    • (1969) J. Gen. Physiol. , vol.54 , pp. 245-264
    • Karlin, A.1
  • 25
    • 49649102025 scopus 로고    scopus 로고
    • On the nature of partial agonism in the nicotinic receptor superfamily
    • Lape, R., D. Colquhoun, and L.G. Sivilotti. 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
  • 26
    • 27744438169 scopus 로고    scopus 로고
    • Principal pathway coupling agonist binding to channel gating in nicotinic receptors
    • Lee, W.Y., and S.M. Sine. 2005. Principal pathway coupling agonist binding to channel gating in nicotinic receptors. Nature. 438:243-247. http://dx.doi.org/10.1038/nature04156
    • (2005) Nature. , vol.438 , pp. 243-247
    • Lee, W.Y.1    Sine, S.M.2
  • 27
    • 48649097534 scopus 로고    scopus 로고
    • Nicotinic receptor interloop proline anchors β1-β2 and Cys loops in coupling agonist binding to channel gating
    • Lee, W.Y., C.R. Free, and S.M. Sine. 2008. Nicotinic receptor interloop proline anchors β1-β2 and Cys loops in coupling agonist binding to channel gating. J. Gen. Physiol. 132:265-278. http:// dx.doi.org/10.1085/jgp.200810014
    • (2008) J. Gen. Physiol. , vol.132 , pp. 265-278
    • Lee, W.Y.1    Free, C.R.2    Sine, S.M.3
  • 28
    • 63849179080 scopus 로고    scopus 로고
    • Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2-M3 regions
    • Lee, W.Y., C.R. Free, and S.M. Sine. 2009. Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2-M3 regions. J. Neurosci. 29:3189-3199. http:// dx.doi.org/10.1523/JNEUROSCI.6185-08.2009
    • (2009) J. Neurosci. , vol.29 , pp. 3189-3199
    • Lee, W.Y.1    Free, C.R.2    Sine, S.M.3
  • 29
    • 27744608733 scopus 로고    scopus 로고
    • Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
    • Lummis, S.C., D.L. Beene, L.W. Lee, H.A. Lester, R.W. Broadhurst, and D.A. Dougherty. 2005. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature. 438:248-252. http://dx.doi.org/10.1038/nature04130
    • (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
  • 30
    • 4644289077 scopus 로고    scopus 로고
    • Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating
    • Mitra, A., T.D. Bailey, and A.L. Auerbach. 2004. Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating. Structure. 12:1909-1918. http://dx.doi.org/10.1016/j.str.2004.08.004
    • (2004) Structure. , vol.12 , pp. 1909-1918
    • Mitra, A.1    Bailey, T.D.2    Auerbach, A.L.3
  • 31
    • 27244454364 scopus 로고    scopus 로고
    • Dynamics of the acetylcholine receptor pore at the gating transition state
    • USA
    • Mitra, A., G.D. Cymes, and A. Auerbach. 2005. Dynamics of the acetylcholine receptor pore at the gating transition state. Proc. Natl. Acad. Sci. USA. 102:15069-15074. http://dx.doi.org/10.1073/ pnas.0505090102
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 15069-15074
    • Mitra, A.1    Cymes, G.D.2    Auerbach, A.3
  • 32
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., J. Wyman, and J.P. Changeux. 1965. On the nature of allosteric transitions: A plausible model. J. Mol. Biol. 12:88-118. http:// dx.doi.org/10.1016/S0022-2836(65)80285-6
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 33
    • 84872804983 scopus 로고    scopus 로고
    • Nicotinic receptor transduction zone: invariant arginine couples to multiple electron-rich residues
    • Mukhtasimova, N., and S.M. Sine. 2013. Nicotinic receptor transduction zone: invariant arginine couples to multiple electron-rich residues. Biophys. J. 104:355-367. http://dx.doi.org/10.1016/j.bpj .2012.12.013
    • (2013) Biophys. J. , vol.104 , pp. 355-367
    • Mukhtasimova, N.1    Sine, S.M.2
  • 34
    • 67349279395 scopus 로고    scopus 로고
    • Detection and trapping of intermediate states priming nicotinic receptor channel opening
    • Mukhtasimova, N., W.Y. Lee, H.L. Wang, and S.M. Sine. 2009. Detection and trapping of intermediate states priming nicotinic receptor channel opening. Nature. 459:451-454. http://dx.doi.org/ 10.1038/nature07923
    • (2009) Nature. , vol.459 , pp. 451-454
    • Mukhtasimova, N.1    Lee, W.Y.2    Wang, H.L.3    Sine, S.M.4
  • 35
    • 84861145025 scopus 로고    scopus 로고
    • The intrinsic energy of the gating isomerization of a neuromuscular acetylcholine receptor channel
    • Nayak, T.K., P.G. Purohit, and A. Auerbach. 2012. The intrinsic energy of the gating isomerization of a neuromuscular acetylcholine receptor channel. J. Gen. Physiol. 139:349-358. http://dx.doi .org/10.1085/jgp.201110752
    • (2012) J. Gen. Physiol. , vol.139 , pp. 349-358
    • Nayak, T.K.1    Purohit, P.G.2    Auerbach, A.3
  • 36
    • 67650470848 scopus 로고    scopus 로고
    • Isomerization of the proline in the M2-M3 linker is not required for activation of the human 5-HT3A receptor
    • Paulsen, I.M., I.L. Martin, and S.M. Dunn. 2009. Isomerization of the proline in the M2-M3 linker is not required for activation of the human 5-HT3A receptor. J. Neurochem. 110:870-878. http://dx.doi .org/10.1111/j.1471-4159.2009.06180.x
    • (2009) J. Neurochem. , vol.110 , pp. 870-878
    • Paulsen, I.M.1    Martin, I.L.2    Dunn, S.M.3
  • 37
    • 36549039473 scopus 로고    scopus 로고
    • Acetylcholine receptor gating at extracellular transmembrane domain interface: The "pre-M1" linker
    • Purohit, P., and A. Auerbach. 2007. Acetylcholine receptor gating at extracellular transmembrane domain interface: The "pre-M1" linker. J. Gen. Physiol. 130:559-568. http://dx.doi.org/10.1085/jgp .200709857
    • (2007) J. Gen. Physiol. , vol.130 , pp. 559-568
    • Purohit, P.1    Auerbach, A.2
  • 38
    • 58549118250 scopus 로고    scopus 로고
    • Unliganded gating of acetylcholine receptor channels
    • USA
    • Purohit, P., and A. Auerbach. 2009. Unliganded gating of acetylcholine receptor channels. Proc. Natl. Acad. Sci. USA. 106:115-120. http://dx.doi.org/10.1073/pnas.0809272106
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 115-120
    • Purohit, P.1    Auerbach, A.2
  • 39
    • 77950282036 scopus 로고    scopus 로고
    • Energetics of gating at the apoacetylcholine receptor transmitter binding site
    • Purohit, P., and A. Auerbach. 2010. Energetics of gating at the apoacetylcholine receptor transmitter binding site. J. Gen. Physiol. 135:321-331. http://dx.doi.org/10.1085/jgp.200910384
    • (2010) J. Gen. Physiol. , vol.135 , pp. 321-331
    • Purohit, P.1    Auerbach, A.2
  • 40
    • 84862162118 scopus 로고    scopus 로고
    • Sources of energy for gating by neurotransmitters in acetylcholine receptor channels
    • Purohit, P., I. Bruhova, and A. Auerbach. 2012. Sources of energy for gating by neurotransmitters in acetylcholine receptor channels. Proc. Natl. Acad. Sci. USA. 109:9384-9389. http://dx.doi.org/ 10.1073/pnas.1203633109
    • (2012) Proc. Natl. Acad. Sci. USA. , vol.109 , pp. 9384-9389
    • Purohit, P.1    Bruhova, I.2    Auerbach, A.3
  • 41
    • 1542285356 scopus 로고    scopus 로고
    • Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling
    • Qin, F. 2004. Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling. Biophys. J. 86:1488-1501. http://dx.doi.org/10.1016/S0006-3495(04)74217-4
    • (2004) Biophys. J. , vol.86 , pp. 1488-1501
    • Qin, F.1
  • 42
    • 0030956174 scopus 로고    scopus 로고
    • Maximum likelihood estimation of aggregated Markov processes
    • Qin, F., A. Auerbach, and F. Sachs. 1997. Maximum likelihood estimation of aggregated Markov processes. Proc. Biol. Sci. 264:375- 383. http://dx.doi.org/10.1098/rspb.1997.0054
    • (1997) Proc. Biol. Sci. , vol.264
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 43
    • 84864060207 scopus 로고    scopus 로고
    • End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease
    • Sine, S.M. 2012. End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease. Physiol. Rev. 92:1189-1234. http://dx.doi.org/10.1152/physrev.00015.2011
    • (2012) Physiol. Rev. , vol.92 , pp. 1189-1234
    • Sine, S.M.1
  • 44
    • 22244438519 scopus 로고    scopus 로고
    • Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism
    • Taly, A., M. Delarue, T. Grutter, M. Nilges, N. Le Novère, P.J. Corringer, and J.P. Changeux. 2005. Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism. Biophys. J. 88:3954-3965. http://dx.doi.org/10.1529/ biophysj.104.050229
    • (2005) Biophys. J. , vol.88 , pp. 3954-3965
    • Taly, A.1    Delarue, M.2    Grutter, T.3    Nilges, M.4    Le Novère, N.5    Corringer, P.J.6    Changeux, J.P.7
  • 45
    • 0028839461 scopus 로고
    • Mutations in the M1 region of the nicotinic acetylcholine receptor alter the sensitivity to inhibition by quinacrine
    • Tamamizu, S., A.P. Todd, and M.G. McNamee. 1995. Mutations in the M1 region of the nicotinic acetylcholine receptor alter the sensitivity to inhibition by quinacrine. Cell. Mol. Neurobiol. 15:427-438. http://dx.doi.org/10.1007/BF02071878
    • (1995) Cell. Mol. Neurobiol. , vol.15 , pp. 427-438
    • Tamamizu, S.1    Todd, A.P.2    McNamee, M.G.3
  • 46
    • 0026004411 scopus 로고
    • Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor
    • Tomaselli, G.F., J.T. McLaughlin, M.E. Jurman, E. Hawrot, and G. Yellen. 1991. Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor. Biophys. J. 60:721-727. http://dx.doi.org/ 10.1016/S0006-3495(91)82102-6
    • (1991) Biophys. J. , vol.60 , pp. 721-727
    • Tomaselli, G.F.1    McLaughlin, J.T.2    Jurman, M.E.3    Hawrot, E.4    Yellen, G.5
  • 47
    • 41149104308 scopus 로고    scopus 로고
    • Allostery: absence of a change in shape does not imply that allostery is not at play
    • Tsai, C.J., A. del Sol, and R. Nussinov. 2008. Allostery: absence of a change in shape does not imply that allostery is not at play. J. Mol. Biol. 378:1-11. http://dx.doi.org/10.1016/j.jmb.2008.02.034
    • (2008) J. Mol. Biol. , vol.378 , pp. 1-11
    • Tsai, C.J.1    del Sol, A.2    Nussinov, R.3
  • 48
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin, N. 2005. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346:967-989. http://dx.doi .org/10.1016/j.jmb.2004.12.031
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 49
    • 84865696393 scopus 로고    scopus 로고
    • Gating movement of acetylcholine receptor caught by plunge-freezing
    • Unwin, N., and Y. Fujiyoshi. 2012. Gating movement of acetylcholine receptor caught by plunge-freezing. J. Mol. Biol. 422:617-634. http://dx.doi.org/10.1016/j.jmb.2012.07.010
    • (2012) J. Mol. Biol. , vol.422 , pp. 617-634
    • Unwin, N.1    Fujiyoshi, Y.2
  • 50
    • 79551615831 scopus 로고    scopus 로고
    • Decrypting the sequence of structural events during the gating transition of pentameric ligand-gated ion channels based on an interpolated elastic network model
    • Zheng, W., and A. Auerbach. 2011. Decrypting the sequence of structural events during the gating transition of pentameric ligand-gated ion channels based on an interpolated elastic network model. PLOS Comput. Biol. 7:e1001046. http://dx.doi.org/ 10.1371/journal.pcbi.1001046
    • (2011) PLOS Comput. Biol , vol.7
    • Zheng, W.1    Auerbach, A.2

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