메뉴 건너뛰기




Volumn 9, Issue 6, 2011, Pages

Ligand activation of the Prokaryotic Pentameric ligand-gated ion channel ELIC

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; AMIDE; ELIC PROTEIN; LIGAND GATED ION CHANNEL; NICOTINIC RECEPTOR; UNCLASSIFIED DRUG; LIGAND;

EID: 79959775185     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001101     Document Type: Article
Times cited : (93)

References (61)
  • 2
    • 77950494200 scopus 로고    scopus 로고
    • Binding, activation and modulation of Cys-loop receptors
    • Miller P. S, Smart T. G, (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
  • 3
    • 79951674390 scopus 로고    scopus 로고
    • The structural basis of function in Cys-loop receptors
    • Thompson A. J, Lester H. A, Lummis S. C, (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
  • 4
    • 33645302360 scopus 로고    scopus 로고
    • Recent advances in Cys-loop receptor structure and function
    • Sine S. M, Engel A. G, (2006) Recent advances in Cys-loop receptor structure and function. Nature 440: 448-455.
    • (2006) Nature , vol.440 , pp. 448-455
    • Sine, S.M.1    Engel, A.G.2
  • 5
    • 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
  • 7
    • 69249088472 scopus 로고    scopus 로고
    • A prokaryotic perspective on pentameric ligand-gated ion channel structure
    • Hilf R. J, 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
  • 8
    • 26944443142 scopus 로고    scopus 로고
    • Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels
    • Tasneem A, Iyer L. M, Jakobsson E, Aravind L, (2005) Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels. Genome Biol 6: R4.
    • (2005) Genome Biol , vol.6
    • Tasneem, A.1    Iyer, L.M.2    Jakobsson, E.3    Aravind, L.4
  • 9
    • 77949538692 scopus 로고    scopus 로고
    • Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues
    • Corringer P. J, Baaden M, Bocquet N, Delarue M, Dufresne V, et al. (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
  • 10
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf R. J, 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
  • 11
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf R. J, 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
  • 12
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux J. P, et al. (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
  • 13
    • 33846106078 scopus 로고    scopus 로고
    • A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family
    • Bocquet N, Prado de Carvalho L, Cartaud J, Neyton J, Le Poupon C, 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.P.2    Cartaud, J.3    Neyton, J.4    Le Poupon, C.5
  • 14
    • 0020003862 scopus 로고
    • Desensitization at the frog neuromuscular junction: a biphasic process
    • Feltz A, Trautmann A, (1982) Desensitization at the frog neuromuscular junction: a biphasic process. J Physiol 322: 257-272.
    • (1982) J Physiol , vol.322 , pp. 257-272
    • Feltz, A.1    Trautmann, A.2
  • 15
    • 0031870973 scopus 로고    scopus 로고
    • Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism
    • 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
  • 16
    • 0019215162 scopus 로고
    • Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist
    • Sakmann B, Patlak J, Neher E, (1980) Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist. Nature 286: 71-73.
    • (1980) Nature , vol.286 , pp. 71-73
    • Sakmann, B.1    Patlak, J.2    Neher, E.3
  • 17
    • 78549271990 scopus 로고    scopus 로고
    • Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel
    • Hilf R. J, Bertozzi C, Zimmermann I, Reiter A, Trauner D, et al. (2010) Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel. Nat Struct Mol Biol 17: 1330-1336.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1330-1336
    • Hilf, R.J.1    Bertozzi, C.2    Zimmermann, I.3    Reiter, A.4    Trauner, D.5
  • 18
    • 68949105566 scopus 로고    scopus 로고
    • Molecular-dynamics simulations of ELIC-a prokaryotic homologue of the nicotinic acetylcholine receptor
    • Cheng X, Ivanov I, Wang H, Sine S. M, McCammon J. A, (2009) Molecular-dynamics simulations of ELIC-a prokaryotic homologue of the nicotinic acetylcholine receptor. Biophys J 96: 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
  • 19
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • 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
  • 20
    • 0041352143 scopus 로고    scopus 로고
    • Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels
    • Sixma T. K, Smit A. B, (2003) Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels. Annu Rev Biophys Biomol Struct 32: 311-334.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 311-334
    • Sixma, T.K.1    Smit, A.B.2
  • 21
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc K, van Dijk W. J, Klaassen R. V, Schuurmans M, van Der Oost J, 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.J.2    Klaassen, R.V.3    Schuurmans, M.4    van der Oost, J.5
  • 22
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie P. H, van Rossum-Fikkert S. E, van Dijk W. J, Brejc K, Smit A. B, 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.H.1    van Rossum-Fikkert, S.E.2    van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5
  • 23
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen S. B, Sulzenbacher G, Huxford T, Marchot P, Taylor P, 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.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5
  • 24
    • 0036891560 scopus 로고    scopus 로고
    • The nicotinic receptor ligand binding domain
    • Sine S. M, (2002) The nicotinic receptor ligand binding domain. J Neurobiol 53: 431-446.
    • (2002) J Neurobiol , vol.53 , pp. 431-446
    • Sine, S.M.1
  • 25
    • 0032514762 scopus 로고    scopus 로고
    • From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor
    • Zhong W, Gallivan J. P, Zhang Y, Li L, Lester H. A, et al. (1998) From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor. Proc Natl Acad Sci U S A 95: 12088-12093.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12088-12093
    • Zhong, W.1    Gallivan, J.P.2    Zhang, Y.3    Li, L.4    Lester, H.A.5
  • 26
    • 0025675821 scopus 로고
    • Acetylcholine binding by a synthetic receptor: implications for biological recognition
    • Dougherty D. A, Stauffer D. A, (1990) Acetylcholine binding by a synthetic receptor: implications for biological recognition. Science 250: 1558-1560.
    • (1990) Science , vol.250 , pp. 1558-1560
    • Dougherty, D.A.1    Stauffer, D.A.2
  • 27
    • 0036607862 scopus 로고    scopus 로고
    • Anxiety over GABA(A) receptor structure relieved by AChBP
    • Cromer B. A, Morton C. J, Parker M. W, (2002) Anxiety over GABA(A) receptor structure relieved by AChBP. Trends Biochem Sci 27: 280-287.
    • (2002) Trends Biochem Sci , vol.27 , pp. 280-287
    • Cromer, B.A.1    Morton, C.J.2    Parker, M.W.3
  • 28
    • 0026607902 scopus 로고
    • Point mutations affecting antagonist affinity and agonist dependent gating of GABAA receptor channels
    • Sigel E, Baur R, Kellenberger S, Malherbe P, (1992) Point mutations affecting antagonist affinity and agonist dependent gating of GABAA receptor channels. EMBO J 11: 2017-2023.
    • (1992) EMBO J , vol.11 , pp. 2017-2023
    • Sigel, E.1    Baur, R.2    Kellenberger, S.3    Malherbe, P.4
  • 29
    • 70450208914 scopus 로고    scopus 로고
    • Locating GABA in GABA receptor binding sites
    • Lummis S. C, (2009) Locating GABA in GABA receptor binding sites. Biochem Soc Trans 37: 1343-1346.
    • (2009) Biochem Soc Trans , vol.37 , pp. 1343-1346
    • Lummis, S.C.1
  • 30
    • 0022975736 scopus 로고
    • Location of a delta-subunit region determining ion transport through the acetylcholine receptor channel
    • Imoto K, Methfessel C, Sakmann B, Mishina M, Mori Y, et al. (1986) Location of a delta-subunit region determining ion transport through the acetylcholine receptor channel. Nature 324: 670-674.
    • (1986) Nature , vol.324 , pp. 670-674
    • Imoto, K.1    Methfessel, C.2    Sakmann, B.3    Mishina, M.4    Mori, Y.5
  • 31
    • 77958509782 scopus 로고    scopus 로고
    • Bridging the gap between structural models of nicotinic receptor superfamily ion channels and their corresponding functional states
    • Gonzalez-Gutierrez G, Grosman C, (2010) Bridging the gap between structural models of nicotinic receptor superfamily ion channels and their corresponding functional states. J Mol Biol 403: 693-705.
    • (2010) J Mol Biol , vol.403 , pp. 693-705
    • Gonzalez-Gutierrez, G.1    Grosman, C.2
  • 32
    • 0020490146 scopus 로고
    • On the stochastic properties of bursts of single ion channel openings and of clusters of bursts
    • Colquhoun D, Hawkes A. G, (1982) On the stochastic properties of bursts of single ion channel openings and of clusters of bursts. Philos Trans R Soc Lond B Biol Sci 300: 1-59.
    • (1982) Philos Trans R Soc Lond B Biol Sci , vol.300 , pp. 1-59
    • Colquhoun, D.1    Hawkes, A.G.2
  • 33
    • 0022272338 scopus 로고
    • Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate
    • Colquhoun D, Sakmann B, (1985) Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate. J Physiol 369: 501-557.
    • (1985) J Physiol , vol.369 , pp. 501-557
    • Colquhoun, D.1    Sakmann, B.2
  • 34
    • 0018894860 scopus 로고
    • The permeability of endplate channels to monovalent and divalent metal cations
    • Adams D. J, Dwyer T. M, Hille B, (1980) The permeability of endplate channels to monovalent and divalent metal cations. J Gen Physiol 75: 493-510.
    • (1980) J Gen Physiol , vol.75 , pp. 493-510
    • Adams, D.J.1    Dwyer, T.M.2    Hille, B.3
  • 35
    • 0021063982 scopus 로고
    • Acetylcholine receptor channel ionic selectivity: ions experience an aqueous environment
    • Lewis C. A, Stevens C. F, (1983) Acetylcholine receptor channel ionic selectivity: ions experience an aqueous environment. Proc Natl Acad Sci U S A 80: 6110-6113.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 6110-6113
    • Lewis, C.A.1    Stevens, C.F.2
  • 36
    • 0029065764 scopus 로고
    • Monovalent and divalent cation permeability and block of neuronal nicotinic receptor channels in rat parasympathetic ganglia
    • Nutter T. J, Adams D. J, (1995) Monovalent and divalent cation permeability and block of neuronal nicotinic receptor channels in rat parasympathetic ganglia. J Gen Physiol 105: 701-723.
    • (1995) J Gen Physiol , vol.105 , pp. 701-723
    • Nutter, T.J.1    Adams, D.J.2
  • 37
    • 0027214596 scopus 로고
    • Mutations at two distinct sites within the channel domain M2 alter calcium permeability of neuronal alpha 7 nicotinic receptor
    • Bertrand D, Galzi J. L, Devillers-Thiery A, Bertrand S, Changeux J. P, (1993) Mutations at two distinct sites within the channel domain M2 alter calcium permeability of neuronal alpha 7 nicotinic receptor. Proc Natl Acad Sci U S A 90: 6971-6975.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 6971-6975
    • Bertrand, D.1    Galzi, J.L.2    Devillers-Thiery, A.3    Bertrand, S.4    Changeux, J.P.5
  • 38
    • 0023237915 scopus 로고
    • Monovalent and divalent cation permeation in acetylcholine receptor channels. Ion transport related to structure
    • Dani J. A, Eisenman G, (1987) Monovalent and divalent cation permeation in acetylcholine receptor channels. Ion transport related to structure. J Gen Physiol 89: 959-983.
    • (1987) J Gen Physiol , vol.89 , pp. 959-983
    • Dani, J.A.1    Eisenman, G.2
  • 39
    • 0023748825 scopus 로고
    • Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance
    • Imoto K, Busch C, Sakmann B, Mishina M, Konno T, 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
  • 40
    • 0025802063 scopus 로고
    • Rings of anionic amino acids as structural determinants of ion selectivity in the acetylcholine receptor channel
    • Konno T, Busch C, Von Kitzing E, Imoto K, Wang F, et al. (1991) Rings of anionic amino acids as structural determinants of ion selectivity in the acetylcholine receptor channel. Proc Biol Sci 244: 69-79.
    • (1991) Proc Biol Sci , vol.244 , pp. 69-79
    • Konno, T.1    Busch, C.2    Von Kitzing, E.3    Imoto, K.4    Wang, F.5
  • 41
    • 0016784460 scopus 로고
    • Conductance increases produced by bath application of cholinergic agonists to Electrophorus electroplaques
    • Lester H. A, Changeux J. P, Sheridan R. E, (1975) Conductance increases produced by bath application of cholinergic agonists to Electrophorus electroplaques. J Gen Physiol 65: 797-816.
    • (1975) J Gen Physiol , vol.65 , pp. 797-816
    • Lester, H.A.1    Changeux, J.P.2    Sheridan, R.E.3
  • 42
    • 65949085351 scopus 로고    scopus 로고
    • Number and locations of agonist binding sites required to activate homomeric Cys-loop receptors
    • Rayes D, De Rosa M. J, Sine S. M, 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
  • 43
    • 0029859799 scopus 로고    scopus 로고
    • Binding sites contribute unequally to the gating of mouse nicotinic alpha D200N acetylcholine receptors
    • Akk G, Sine S, Auerbach A, (1996) Binding sites contribute unequally to the gating of mouse nicotinic alpha D200N acetylcholine receptors. J Physiol 496 (Pt 1): 185-196.
    • (1996) J Physiol , vol.496 , Issue.Pt 1 , pp. 185-196
    • Akk, G.1    Sine, S.2    Auerbach, A.3
  • 45
    • 70349584397 scopus 로고    scopus 로고
    • Single-channel kinetic analysis for activation and desensitization of homomeric 5-HT(3)A receptors
    • 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
  • 46
    • 49649102025 scopus 로고    scopus 로고
    • On the nature of partial agonism in the nicotinic receptor superfamily
    • Lape R, Colquhoun D, Sivilotti L. G, (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
  • 47
    • 0035970016 scopus 로고    scopus 로고
    • Acetylcholine receptor channel structure in the resting, open, and desensitized states probed with the substituted-cysteine-accessibility method
    • Wilson G, Karlin A, (2001) Acetylcholine receptor channel structure in the resting, open, and desensitized states probed with the substituted-cysteine-accessibility method. Proc Natl Acad Sci U S A 98: 1241-1248.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1241-1248
    • Wilson, G.1    Karlin, A.2
  • 48
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun D, (1998) Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br J Pharmacol 125: 924-947.
    • (1998) Br J Pharmacol , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 50
    • 0141888445 scopus 로고    scopus 로고
    • A single ring of charged amino acids at one end of the pore can control ion selectivity in the 5-HT3 receptor
    • Thompson A. J, Lummis S. C, (2003) A single ring of charged amino acids at one end of the pore can control ion selectivity in the 5-HT3 receptor. Br J Pharmacol 140: 359-365.
    • (2003) Br J Pharmacol , vol.140 , pp. 359-365
    • Thompson, A.J.1    Lummis, S.C.2
  • 51
    • 0032609297 scopus 로고    scopus 로고
    • Molecular basis of the charge selectivity of nicotinic acetylcholine receptor and related ligand-gated ion channels
    • discussion 224-230
    • Corringer P. J, Bertrand S, Galzi J. L, Devillers-Thiery A, Changeux J. P, et al. (1999) Molecular basis of the charge selectivity of nicotinic acetylcholine receptor and related ligand-gated ion channels. Novartis Found Symp 225: 215-224; discussion 224-230.
    • (1999) Novartis Found Symp , vol.225 , pp. 215-224
    • Corringer, P.J.1    Bertrand, S.2    Galzi, J.L.3    Devillers-Thiery, A.4    Changeux, J.P.5
  • 52
    • 61349137676 scopus 로고    scopus 로고
    • An ion selectivity filter in the extracellular domain of Cys-loop receptors reveals determinants for ion conductance
    • Hansen S. B, Wang H. L, Taylor P, Sine S. M, (2008) An ion selectivity filter in the extracellular domain of Cys-loop receptors reveals determinants for ion conductance. J Biol Chem 283: 36066-36070.
    • (2008) J Biol Chem , vol.283 , pp. 36066-36070
    • Hansen, S.B.1    Wang, H.L.2    Taylor, P.3    Sine, S.M.4
  • 53
    • 0027224010 scopus 로고
    • Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers
    • Bormann J, Rundstrom N, Betz H, Langosch D, (1993) Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers. EMBO J 12: 3729-3737.
    • (1993) EMBO J , vol.12 , pp. 3729-3737
    • Bormann, J.1    Rundstrom, N.2    Betz, H.3    Langosch, D.4
  • 54
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W, (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 55
    • 0028103275 scopus 로고
    • Collaborative computational project Nr. 4. The CCP4 suite: programs for X-ray crystallography
    • CCP4
    • CCP4 (1994) Collaborative computational project Nr. 4. The CCP4 suite: programs for X-ray crystallography. Acta Crystallogr D 50: 760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 56
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A, Zou J. Y, Cowan S. W, Kjeldgaard M, (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47 (Pt 2): 110-119.
    • (1991) Acta Crystallogr A , vol.47 , Issue.Pt 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 59
    • 0036714139 scopus 로고    scopus 로고
    • Na+ block and permeation in a K+ channel of known structure
    • Nimigean C. M, Miller C, (2002) Na+ block and permeation in a K+ channel of known structure. J Gen Physiol 120: 323-335.
    • (2002) J Gen Physiol , vol.120 , pp. 323-335
    • Nimigean, C.M.1    Miller, C.2
  • 60
    • 0029843417 scopus 로고    scopus 로고
    • Heteromultimeric CLC chloride channels with novel properties
    • Lorenz C, Pusch M, Jentsch T. J, (1996) Heteromultimeric CLC chloride channels with novel properties. Proc Natl Acad Sci U S A 93: 13362-13366.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13362-13366
    • Lorenz, C.1    Pusch, M.2    Jentsch, T.J.3
  • 61
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: a program for the analysis of the pore dimensions of ion channel structural models
    • Smart OS, Neduvelil J. G, Wang X, Wallace B. A, Sansom M. S, (1996) HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J Mol Graph 14: 354-360, 376.
    • (1996) J Mol Graph , vol.14
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.