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Volumn 96, Issue 11, 2009, Pages 4502-4513

Molecular-dynamics simulations of ELIC - A prokaryotic homologue of the nicotinic acetylcholine receptor

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE DERIVATIVE; NICOTINIC RECEPTOR; PROTEIN; ALPHA-BUNGAROTOXIN RECEPTOR; BACTERIAL PROTEIN; BUNGAROTOXIN RECEPTOR; ION CHANNEL; WATER;

EID: 68949105566     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.03.018     Document Type: Article
Times cited : (34)

References (60)
  • 1
    • 33645302360 scopus 로고    scopus 로고
    • Recent advances in Cys-loop receptor structure and function
    • Sine, S., and A. Engel. 2006. Recent advances in Cys-loop receptor structure and function. Nature. 440:448-455.
    • (2006) Nature , vol.440 , pp. 448-455
    • Sine, S.1    Engel, A.2
  • 3
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • 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
  • 4
    • 0029553116 scopus 로고
    • Acetylcholine: A neurotransmitter for learning and memory?
    • Blokland, A. 1995. Acetylcholine: a neurotransmitter for learning and memory? Brain Res. Brain Res. Rev. 21:285-300.
    • (1995) Brain Res. Brain Res. Rev , vol.21 , pp. 285-300
    • Blokland, A.1
  • 5
    • 0034732138 scopus 로고    scopus 로고
    • Neuronal nicotinic receptors, important newplayers in brain function
    • Clementi, F., D. Fornasari, and C. Gotti. 2000. Neuronal nicotinic receptors, important newplayers in brain function.Eur. J. Pharmacol. 393:3-10.
    • (2000) Eur. J. Pharmacol , vol.393 , pp. 3-10
    • Clementi, F.1    Fornasari, D.2    Gotti, C.3
  • 6
    • 0242367566 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptors: From structure to brain function
    • Hogg, R., M. Raggenbass, and D. Bertrand. 2003. Nicotinic acetylcholine receptors: from structure to brain function. Rev. Physiol. Biochem. Pharmacol. 147:1-46.
    • (2003) Rev. Physiol. Biochem. Pharmacol , vol.147 , pp. 1-46
    • Hogg, R.1    Raggenbass, M.2    Bertrand, D.3
  • 7
    • 2942657957 scopus 로고    scopus 로고
    • Rational understanding of nicotinic receptors drug binding
    • Grutter, T., N. Le Novere, and J. Changeux. 2004. Rational understanding of nicotinic receptors drug binding. Curr. Top. Med. Chem. 4:645-650.
    • (2004) Curr. Top. Med. Chem , vol.4 , pp. 645-650
    • Grutter, T.1    Le Novere, N.2    Changeux, J.3
  • 8
    • 29144435115 scopus 로고    scopus 로고
    • From ligand design to therapeutic efficacy: The challenge for nicotinic receptor research
    • Cassels, B., I. Bermudez, F. Dajas, J. Abin-Carriquiry, and S. Wonnacott. 2005. From ligand design to therapeutic efficacy: the challenge for nicotinic receptor research. Drug Discov. Today. 10:1657-1665.
    • (2005) Drug Discov. Today , vol.10 , pp. 1657-1665
    • Cassels, B.1    Bermudez, I.2    Dajas, F.3    Abin-Carriquiry, J.4    Wonnacott, S.5
  • 9
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin, A., and M. Akabas. 1995. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron. 15:1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.2
  • 10
    • 0036891560 scopus 로고    scopus 로고
    • The nicotinic receptor ligand binding domain
    • Sine, S. 2002. The nicotinic receptor ligand binding domain. J. Neurobiol. 53:431-446.
    • (2002) J. Neurobiol , vol.53 , pp. 431-446
    • Sine, S.1
  • 11
    • 0033119869 scopus 로고    scopus 로고
    • Mutational analysis of the charge selectivity filter of the α7 nicotinic acetylcholine receptor
    • Corringer, P., S. Bertrand, J. Galzi, A. Devillers-Thiery, J. Changeux, et al. 1999. Mutational analysis of the charge selectivity filter of the α7 nicotinic acetylcholine receptor. Neuron. 22:831-843.
    • (1999) Neuron , vol.22 , pp. 831-843
    • Corringer, P.1    Bertrand, S.2    Galzi, J.3    Devillers-Thiery, A.4    Changeux, J.5
  • 12
    • 0031870973 scopus 로고    scopus 로고
    • Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism
    • Auerbach, A., and G. Akk. 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
  • 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.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14102-14107
    • Grosman, C.1    Auerbach, A.2
  • 14
    • 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.
    • (2005) J. Mol. Biol , vol.346 , pp. 967-989
    • Unwin, N.1
  • 15
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A., Y. Fujiyoshi, and N. Unwin. 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
  • 16
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc, K., W. van Dijk, R. Klaassen, M. Schuurmans, J. van Der Oost, et al. 2001. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature. 411:269-276.
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    van Dijk, W.2    Klaassen, R.3    Schuurmans, M.4    van Der Oost, J.5
  • 17
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie, P., S. van Rossum-Fikkert, W. van Dijk, K. Brejc, A. Smit, et al. 2004. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron. 41:907-914.
    • (2004) Neuron , vol.41 , pp. 907-914
    • Celie, P.1    van Rossum-Fikkert, S.2    van Dijk, W.3    Brejc, K.4    Smit, A.5
  • 18
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen, S., G. Sulzenbacher, T. Huxford, P. Marchot, P. Taylor, et al. 2005. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J. 24:3635-3646.
    • (2005) EMBO J , vol.24 , pp. 3635-3646
    • Hansen, S.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5
  • 19
    • 18444411922 scopus 로고    scopus 로고
    • Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake α-neurotoxins and nicotinic receptors
    • Bourne, Y., T. Talley, S. Hansen, P. Taylor, and P. Marchot. 2005. Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake α-neurotoxins and nicotinic receptors. EMBO J. 24:1512-1522.
    • (2005) EMBO J , vol.24 , pp. 1512-1522
    • Bourne, Y.1    Talley, T.2    Hansen, S.3    Taylor, P.4    Marchot, P.5
  • 20
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR α1 bound to α-bungarotoxin at 1.94 A resolution
    • Dellisanti, C., Y. Yao, J. Stroud, Z. Wang, and L. Chen. 2007. Crystal structure of the extracellular domain of nAChR α1 bound to α-bungarotoxin at 1.94 A resolution. Nat. Neurosci. 10:953-962.
    • (2007) Nat. Neurosci , vol.10 , pp. 953-962
    • Dellisanti, C.1    Yao, Y.2    Stroud, J.3    Wang, Z.4    Chen, L.5
  • 21
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf, R., and R. Dutzler. 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.1    Dutzler, R.2
  • 22
    • 33846106078 scopus 로고    scopus 로고
    • A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family
    • Bocquet, N., L. de Carvalho, J. Cartaud, J. Neyton, C. Le Poupon, et al. 2007. A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family. Nature. 445:116-119.
    • (2007) Nature , vol.445 , pp. 116-119
    • Bocquet, N.1    de Carvalho, L.2    Cartaud, J.3    Neyton, J.4    Le Poupon, C.5
  • 23
    • 18744410192 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the {α}7 nicotinic receptor ligand binding domain
    • Henchman, R., H. Wang, S. Sine, P. Taylor, and J. McCammon. 2005. Ligand-induced conformational change in the {α}7 nicotinic receptor ligand binding domain. Biophys. J. 88:2564-2576.
    • (2005) Biophys. J , vol.88 , pp. 2564-2576
    • Henchman, R.1    Wang, H.2    Sine, S.3    Taylor, P.4    McCammon, J.5
  • 24
    • 0242385357 scopus 로고    scopus 로고
    • Asymmetric structural motions of the homomeric α7 nicotinic receptor ligand binding domain revealed by molecular dynamics simulation
    • Henchman, R., H. Wang, S. Sine, P. Taylor, and J. McCammon. 2003. Asymmetric structural motions of the homomeric α7 nicotinic receptor ligand binding domain revealed by molecular dynamics simulation. Biophys. J. 85:3007-3018.
    • (2003) Biophys. J , vol.85 , pp. 3007-3018
    • Henchman, R.1    Wang, H.2    Sine, S.3    Taylor, P.4    McCammon, J.5
  • 25
    • 17844364634 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: Structure and collective motions
    • Hung, A., K. Tai, and M. Sansom. 2005. Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: structure and collective motions. Biophys. J. 88:3321-3333.
    • (2005) Biophys. J , vol.88 , pp. 3321-3333
    • Hung, A.1    Tai, K.2    Sansom, M.3
  • 26
    • 21244436719 scopus 로고    scopus 로고
    • Homology modeling and molecular dynamics simulations of transmembrane domain structure of human neuronal nicotinic acetylcholine receptor
    • Saladino, A., Y. Xu, and P. Tang. 2005. Homology modeling and molecular dynamics simulations of transmembrane domain structure of human neuronal nicotinic acetylcholine receptor. Biophys. J. 88:1009-1017.
    • (2005) Biophys. J , vol.88 , pp. 1009-1017
    • Saladino, A.1    Xu, Y.2    Tang, P.3
  • 27
    • 13644270375 scopus 로고    scopus 로고
    • Conformational dynamics of the nicotinic acetylcholine receptor channel: A 35-ns molecular dynamics simulation study
    • Xu, Y., F. Barrantes, X. Luo, K. Chen, J. Shen, et al. 2005. Conformational dynamics of the nicotinic acetylcholine receptor channel: a 35-ns molecular dynamics simulation study. J. Am. Chem. Soc. 127:1291-1299.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 1291-1299
    • Xu, Y.1    Barrantes, F.2    Luo, X.3    Chen, K.4    Shen, J.5
  • 28
    • 46149085900 scopus 로고    scopus 로고
    • Spontaneous conformational change and toxin binding in α7 nicotinic acetylcholine receptor: Insight into channel activation and inhibition
    • Yi, M., H. Tjong, and H. Zhou. 2008. Spontaneous conformational change and toxin binding in α7 nicotinic acetylcholine receptor: insight into channel activation and inhibition. Proc. Natl. Acad. Sci. USA. 105:8280-8285.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8280-8285
    • Yi, M.1    Tjong, H.2    Zhou, H.3
  • 29
    • 18744363916 scopus 로고    scopus 로고
    • A gating mechanism proposed from a 15 nanosecond simulation of a complete human α7 nicotinic acetylcholine receptor model
    • Law, R., R. Henchman, and J. McCammon. 2005. A gating mechanism proposed from a 15 nanosecond simulation of a complete human α7 nicotinic acetylcholine receptor model. Proc. Natl. Acad. Sci. USA. 102:6813-6818.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6813-6818
    • Law, R.1    Henchman, R.2    McCammon, J.3
  • 30
    • 35348968348 scopus 로고    scopus 로고
    • Nanosecond-timescale conformational dynamics of the human α7 nicotinic acetylcholine receptor
    • Cheng, X., I. Ivanov, H. Wang, S. Sine, and J. McCammon. 2007. Nanosecond-timescale conformational dynamics of the human α7 nicotinic acetylcholine receptor. Biophys. J. 93:2622-2634.
    • (2007) Biophys. J , vol.93 , pp. 2622-2634
    • Cheng, X.1    Ivanov, I.2    Wang, H.3    Sine, S.4    McCammon, J.5
  • 31
    • 40149111452 scopus 로고    scopus 로고
    • Control of cation permeation through the nicotinic receptor channel
    • Wang, H., X. Cheng, P. Taylor, J. McCammon, and S. Sine. 2008. Control of cation permeation through the nicotinic receptor channel. PLoS Comput. Biol. 4:e41.
    • (2008) PLoS Comput. Biol , vol.4
    • Wang, H.1    Cheng, X.2    Taylor, P.3    McCammon, J.4    Sine, S.5
  • 32
    • 28844448877 scopus 로고    scopus 로고
    • Channel opening motion of α7 nicotinic acetylcholine receptor as suggested by normal mode analysis
    • Cheng, X., B. Lu, B. Grant, R. Law, and J. McCammon. 2006. Channel opening motion of α7 nicotinic acetylcholine receptor as suggested by normal mode analysis. J. Mol. Biol. 355:310-324.
    • (2006) J. Mol. Biol , vol.355 , pp. 310-324
    • Cheng, X.1    Lu, B.2    Grant, B.3    Law, R.4    McCammon, J.5
  • 33
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell, W., P. Cieplak, C. Bayly, I. Gould, K. Merz, et al. 1995. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117:5179-5197.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 5179-5197
    • Cornell, W.1    Cieplak, P.2    Bayly, C.3    Gould, I.4    Merz, K.5
  • 34
    • 85031352435 scopus 로고    scopus 로고
    • Case, D., T. Darden, T. Cheatham III, C. Simmerling, J. Wang, et al. 2004. AMBER8. University of California, San Francisco.
    • Case, D., T. Darden, T. Cheatham III, C. Simmerling, J. Wang, et al. 2004. AMBER8. University of California, San Francisco.
  • 35
    • 85031361793 scopus 로고    scopus 로고
    • http://agknapp.chemie.fu-berlin.de/karlsberg/.
  • 37
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerrell, A., D. Bashford, M. Bellott, R. Dunbrack, J. Evanseck, et al. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102:3586-3616.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerrell, A.1    Bashford, D.2    Bellott, M.3    Dunbrack, R.4    Evanseck, J.5
  • 38
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log (N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N log (N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 39
    • 33646650705 scopus 로고
    • Reversible multiple time scale molecular dynamics
    • Tuckerman, M., B. Berne, and G. Martyna. 1992. Reversible multiple time scale molecular dynamics. J. Chem. Phys. 97:1990-2001.
    • (1992) J. Chem. Phys , vol.97 , pp. 1990-2001
    • Tuckerman, M.1    Berne, B.2    Martyna, G.3
  • 40
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J., G. Ciccotti, and H. Berendsen. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23:327-341.
    • (1977) J. Comput. Phys , vol.23 , pp. 327-341
    • Ryckaert, J.1    Ciccotti, G.2    Berendsen, H.3
  • 42
    • 85031367377 scopus 로고    scopus 로고
    • MA
    • Origin 7.5, www.originlab.com: Northampton, MA.
    • Origin 7.5
  • 43
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and A. Szabo. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4559.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 44
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart, O., J. Neduvelil, X. Wang, B. Wallace, and M. Sansom. 1996. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14:354-360.
    • (1996) J. Mol. Graph , vol.14 , pp. 354-360
    • Smart, O.1    Neduvelil, J.2    Wang, X.3    Wallace, B.4    Sansom, M.5
  • 47
    • 14844300820 scopus 로고    scopus 로고
    • Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence
    • Gao, F., N. Bren, T. Burghardt, S. Hansen, R. Henchman, et al. 2005. Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence. J. Biol. Chem. 280:8443-8451.
    • (2005) J. Biol. Chem , vol.280 , pp. 8443-8451
    • Gao, F.1    Bren, N.2    Burghardt, T.3    Hansen, S.4    Henchman, R.5
  • 48
    • 4644289077 scopus 로고    scopus 로고
    • Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating
    • Mitra, A., T. Bailey, and A. Auerbach. 2004. Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating. Structure. 12:1909-1918.
    • (2004) Structure , vol.12 , pp. 1909-1918
    • Mitra, A.1    Bailey, T.2    Auerbach, A.3
  • 49
    • 12244294449 scopus 로고    scopus 로고
    • Pores formed by the nicotinic receptor m2δ peptide: A molecular dynamics simulation study
    • Law, R., D. Tieleman, and M. Sansom. 2003. Pores formed by the nicotinic receptor m2δ peptide: a molecular dynamics simulation study. Biophys. J. 84:14-27.
    • (2003) Biophys. J , vol.84 , pp. 14-27
    • Law, R.1    Tieleman, D.2    Sansom, M.3
  • 50
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • Henzler-Wildman, K., M. Lei, V. Thai, S. Kerns, M. Karplus, et al. 2007. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature. 450:913-916.
    • (2007) Nature , vol.450 , pp. 913-916
    • Henzler-Wildman, K.1    Lei, M.2    Thai, V.3    Kerns, S.4    Karplus, M.5
  • 51
    • 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 Novere, et al. 2005. Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism. Biophys. J. 88:3954-3965.
    • (2005) Biophys. J , vol.88 , pp. 3954-3965
    • Taly, A.1    Delarue, M.2    Grutter, T.3    Nilges, M.4    Le Novere, N.5
  • 52
    • 33750942341 scopus 로고    scopus 로고
    • Implications of the quaternary twist allosteric model for the physiology and pathology of nicotinic acetylcholine receptors
    • Taly, A., P. Corringer, T. Grutter, L. Prado de Carvalho, M. Karplus, et al. 2006. Implications of the quaternary twist allosteric model for the physiology and pathology of nicotinic acetylcholine receptors. Proc. Natl. Acad. Sci. USA. 103:16965-16970.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16965-16970
    • Taly, A.1    Corringer, P.2    Grutter, T.3    Prado de Carvalho, L.4    Karplus, M.5
  • 54
    • 30744470883 scopus 로고    scopus 로고
    • Probing ion-channel pores one proton at a time
    • Cymes, G., Y. Ni, and C. Grosman. 2005. Probing ion-channel pores one proton at a time. Nature. 438:975-980.
    • (2005) Nature , vol.438 , pp. 975-980
    • Cymes, G.1    Ni, Y.2    Grosman, C.3
  • 55
    • 41649119572 scopus 로고    scopus 로고
    • Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer
    • Cymes, G., and C. Grosman. 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.1    Grosman, C.2
  • 56
    • 34447131659 scopus 로고    scopus 로고
    • Barriers to ion translocation in cationic and anionic receptors from the Cys-loop family
    • Chem. Soc. n press
    • Ivanov, I., X. Cheng, S. Sine, and J. McCammon. 2007. Barriers to ion translocation in cationic and anionic receptors from the Cys-loop family. J. Am. Chem. Soc. n press.
    • (2007) J. Am
    • Ivanov, I.1    Cheng, X.2    Sine, S.3    McCammon, J.4
  • 57
    • 33745907550 scopus 로고    scopus 로고
    • A hydrophobic gate in an ion channel: The closed state of the nicotinic acetylcholine receptor
    • Beckstein, O., and M. Sansom. 2006. A hydrophobic gate in an ion channel: the closed state of the nicotinic acetylcholine receptor. Phys. Biol. 3:147-159.
    • (2006) Phys. Biol , vol.3 , pp. 147-159
    • Beckstein, O.1    Sansom, M.2
  • 58
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia, C. 1975. Structural invariants in protein folding. Nature. 254:304-308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 59
    • 0023748825 scopus 로고
    • Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance
    • Imoto, K., C. Busch, B. Sakmann, M. Mishina, T. Konno, et al. 1988. Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance. Nature. 335:645-648.
    • (1988) Nature , vol.335 , pp. 645-648
    • Imoto, K.1    Busch, C.2    Sakmann, B.3    Mishina, M.4    Konno, T.5
  • 60
    • 0028118783 scopus 로고
    • Conductance mutations of the nicotinic acetylcholine receptor do not act by a simple electrostatic mechanism
    • Kienker, P., G. Tomaselli, M. Jurman, and G. Yellen. 1994. Conductance mutations of the nicotinic acetylcholine receptor do not act by a simple electrostatic mechanism. Biophys. J. 66:325-334.
    • (1994) Biophys. J , vol.66 , pp. 325-334
    • Kienker, P.1    Tomaselli, G.2    Jurman, M.3    Yellen, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.