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Volumn 4, Issue 1, 2005, Pages 70-80

Ligand-gated channels

Author keywords

Acetylcholine receptor channel; Channel gating; Glycine receptor channel; Ion permeation

Indexed keywords

BIOLOGICAL MEMBRANES; ELECTRIC CONDUCTANCE; IONS; MOLECULAR DYNAMICS; NEUROLOGY; PROTEINS; SIGNAL PROCESSING;

EID: 15244363737     PISSN: 15361241     EISSN: None     Source Type: Journal    
DOI: 10.1109/TNB.2004.842497     Document Type: Article
Times cited : (40)

References (61)
  • 8
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 A resolution
    • N. Unwin, "Nicotinic acetylcholine receptor at 9 A resolution," J. Mol. Biol., vol. 229, pp. 1101-1124, 1993.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 9
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 A resolution: Transverse tunnels in the channel wall
    • A. Miyazawa, Y. Fujiyoshi, M. Stowell, and N. Unwin, "Nicotinic acetylcholine receptor at 4.6 A resolution: transverse tunnels in the channel wall," J. Mol. Biol., vol. 288, pp. 765-786, 1999.
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 10
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • K. Brejc, W. J. van Dijk, R. V. Klaassen, M. Schuurmans, J. van der Oost, A. B. Smit, and T. K. Sixma, "Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors," Nature, vol. 411, pp. 269-276, 2001.
    • (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    Smit, A.B.6    Sixma, T.K.7
  • 11
  • 12
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • A. Miyazawa, Y. Fujiyoshi, and N. Unwin, "Structure and gating mechanism of the acetylcholine receptor pore," Nature, vol. 423, pp. 949-955, 2003.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 13
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
    • N. Unwin, "Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy," FEBS Lett., vol. 555, pp. 91-95, 2003.
    • (2003) FEBS Lett. , vol.555 , pp. 91-95
    • Unwin, N.1
  • 14
    • 0034731271 scopus 로고    scopus 로고
    • The Croonian lecture 2000. Nicotinic acetylcholine receptor and the structural basis of fast synaptic transmission
    • _, "The Croonian lecture 2000. Nicotinic acetylcholine receptor and the structural basis of fast synaptic transmission," Philos. Trans. R. Soc. London B, Biol. Sci., vol. 355, pp. 1813-1829, 2000.
    • (2000) Philos. Trans. R. Soc. London B, Biol. Sci. , vol.355 , pp. 1813-1829
  • 15
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel
    • C. Bouzat, F. Gumilar, G. Spitzmaul, H. L. Wang, D. Rayes, S. B. Hansen, P. Taylor, and S. M. Sine, "Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel," Nature, vol. 430, pp. 896-900, 2004.
    • (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
  • 17
    • 4644265039 scopus 로고    scopus 로고
    • Molecular structure and function of the glycine receptor chloride channel
    • J. W. Lynch, "Molecular structure and function of the glycine receptor chloride channel," Physiol. Rev., vol. 84, pp. 1051-1095, 2004.
    • (2004) Physiol. Rev. , vol.84 , pp. 1051-1095
    • Lynch, J.W.1
  • 18
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • O. P. Hamill, A. Marty, E. Neher, B. Sakmann, and F. J. Sigworth, "Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches," Pflugers Arch., vol. 391, pp. 85-100, 1981.
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 19
    • 15244355046 scopus 로고    scopus 로고
    • Fifty years of progress in ion channel research
    • Mar.
    • P. C. Jordan, "Fifty years of progress in ion channel research," IEEE Trans. Nanobiosci., vol. 4, no. 1, pp. 1-9, Mar. 2005.
    • (2005) IEEE Trans. Nanobiosci. , vol.4 , Issue.1 , pp. 1-9
    • Jordan, P.C.1
  • 20
    • 0027224010 scopus 로고
    • Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers
    • J. Bormann, N. Rundstrom, H. Betz, and D. Langosch, "Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers," EMBO J., vol. 12, pp. 3729-3737, 1993.
    • (1993) EMBO J. , vol.12 , pp. 3729-3737
    • Bormann, J.1    Rundstrom, N.2    Betz, H.3    Langosch, D.4
  • 21
    • 0028831226 scopus 로고
    • Mutation of an arginine residue in the human glycine receptor transforms beta-alanine and taurine from agonists into competitive antagonists
    • S. Rajendra, J. W. Lynch, K. D. Pierce, C. R. French, P. H. Barry, and P. R. Schofield, "Mutation of an arginine residue in the human glycine receptor transforms beta-alanine and taurine from agonists into competitive antagonists," Neuron, vol. 14, pp. 169-175, 1995.
    • (1995) Neuron , vol.14 , pp. 169-175
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 22
    • 0001802726 scopus 로고
    • Ionic selectivity of channels at the end plate
    • P. H. Barry and P. W. Gage, "Ionic selectivity of channels at the end plate," Curr. Top. Membr. Transport, vol. 21, pp. 1-51, 1984.
    • (1984) Curr. Top. Membr. Transport , vol.21 , pp. 1-51
    • Barry, P.H.1    Gage, P.W.2
  • 23
  • 24
    • 0028016521 scopus 로고
    • Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia
    • D. Langosch, B. Laube, N. Rundstrom, V. Schmieden, J. Bormann, and H. Betz, "Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia," EMBO J., vol. 13, pp. 4223-4228, 1994.
    • (1994) EMBO J. , vol.13 , pp. 4223-4228
    • Langosch, D.1    Laube, B.2    Rundstrom, N.3    Schmieden, V.4    Bormann, J.5    Betz, H.6
  • 25
    • 0035999832 scopus 로고    scopus 로고
    • Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels
    • A. J. Moorhouse, A. Keramidas, A. Zaykin, P. R. Schofield, and P. H. Barry, "Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels," J. Gen. Physiol., vol. 119, pp. 411-425, 2002.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 411-425
    • Moorhouse, A.J.1    Keramidas, A.2    Zaykin, A.3    Schofield, P.R.4    Barry, P.H.5
  • 26
    • 0041806486 scopus 로고    scopus 로고
    • A cytoplasmic region determines single-channel conductance in 5-HT3 receptors
    • S. P. Kelley, J. I. Dunlop, E. F. Kirkness, J. J. Lambert, and J. A. Peters, "A cytoplasmic region determines single-channel conductance in 5-HT3 receptors," Nature, vol. 424, pp. 321-324, 2003.
    • (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
  • 27
    • 0030848203 scopus 로고    scopus 로고
    • Hippocampal GABA(A) channel conductance increased by diazepam
    • M. Eghbali, J. P. Curmi, B. Birnir, and P. W. Gage, "Hippocampal GABA(A) channel conductance increased by diazepam," Nature, vol. 388, pp. 71-75, 1997.
    • (1997) Nature , vol.388 , pp. 71-75
    • Eghbali, M.1    Curmi, J.P.2    Birnir, B.3    Gage, P.W.4
  • 28
    • 0026082583 scopus 로고
    • Location of a threonine residue in the alpha-subunit M2 transmembrane segment that determines the ion flow through the acetylcholine receptor channel
    • A. Villarroel, S. Herlitze, M. Koenen, and B. Sakmann, "Location of a threonine residue in the alpha-subunit M2 transmembrane segment that determines the ion flow through the acetylcholine receptor channel," Proc. R. Soc. London B, Biol. Sci., vol. 243, pp. 69-74, 1991.
    • (1991) Proc. R. Soc. London B, Biol. Sci. , vol.243 , pp. 69-74
    • Villarroel, A.1    Herlitze, S.2    Koenen, M.3    Sakmann, B.4
  • 29
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • J.-L. Galzi, A. Devillers-Thiery, N. Hussy, S. Bertrand, J. P. Changeux, and D. Bertrand, "Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic," Nature, vol. 359, pp. 500-505, 1992.
    • (1992) Nature , vol.359 , pp. 500-505
    • Galzi, J.-L.1    Devillers-Thiery, A.2    Hussy, N.3    Bertrand, S.4    Changeux, J.P.5    Bertrand, D.6
  • 30
    • 0033119869 scopus 로고    scopus 로고
    • Mutational analysis of the charge selectivity filter of the alpha7 nicotinic acetylcholine receptor
    • P. J. Corringer, S. Bertrand, J.-L. Galzi, A. Devillers-Thiery, J. P. Changeux, and D. Bertrand, "Mutational analysis of the charge selectivity filter of the alpha7 nicotinic acetylcholine receptor," Neuron, vol. 22, pp. 831-843, 1999.
    • (1999) Neuron , vol.22 , pp. 831-843
    • Corringer, P.J.1    Bertrand, S.2    Galzi, J.-L.3    Devillers-Thiery, A.4    Changeux, J.P.5    Bertrand, D.6
  • 31
    • 0033916254 scopus 로고    scopus 로고
    • M2 pore mutations convert the glycine receptor channel from being anion- To cation-selective
    • A. Keramidas, A. J. Moorhouse, C. R. French, P. R. Schofield, and P. H. Barry, "M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective," Biophys. J., vol. 79, pp. 247-259, 2000.
    • (2000) Biophys. J. , vol.79 , pp. 247-259
    • Keramidas, A.1    Moorhouse, A.J.2    French, C.R.3    Schofield, P.R.4    Barry, P.H.5
  • 32
    • 0035999831 scopus 로고    scopus 로고
    • Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity
    • A. Keramidas, A. J. Moorhouse, K. D. Pierce, P. R. Schofield, and P. H. Barry, "Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity," J. Gen. Physiol., vol. 119, pp. 393-410, 2002.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 393-410
    • Keramidas, A.1    Moorhouse, A.J.2    Pierce, K.D.3    Schofield, P.R.4    Barry, P.H.5
  • 33
    • 0242416182 scopus 로고    scopus 로고
    • The contribution of proline 250 (P-2′) to pore diameter and ion selectivity in the human glycine receptor channel
    • D. J.-S. Lee, A. Keramidas, A. J. Moorhouse, P. R. Schofield, and P. H. Barry, "The contribution of proline 250 (P-2′) to pore diameter and ion selectivity in the human glycine receptor channel," Neurosci. Lett., vol. 351, pp. 196-200, 2003.
    • (2003) Neurosci. Lett. , vol.351 , pp. 196-200
    • Lee, D.J.-S.1    Keramidas, A.2    Moorhouse, A.J.3    Schofield, P.R.4    Barry, P.H.5
  • 34
    • 0035815730 scopus 로고    scopus 로고
    • Conversion of the ion selectivity of the 5-HT(3A) receptor from cationic to anionic reveals a conserved feature of the ligand-gated ion channel superfamily
    • M. J. Gunthorpe and S. C. Lummis, "Conversion of the ion selectivity of the 5-HT(3A) receptor from cationic to anionic reveals a conserved feature of the ligand-gated ion channel superfamily," J. Biol. Chem., vol. 276, pp. 10977-10983, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10977-10983
    • Gunthorpe, M.J.1    Lummis, S.C.2
  • 35
    • 0038069026 scopus 로고    scopus 로고
    • Mutations at the GABA receptor selectivity filter: A possible role for effective charges
    • V. E. Wotring, T. S. Miller, and D. S. Weiss, "Mutations at the GABA receptor selectivity filter: a possible role for effective charges," J. Physiol., vol. 548, pp. 527-540, 2003.
    • (2003) J. Physiol. , vol.548 , pp. 527-540
    • Wotring, V.E.1    Miller, T.S.2    Weiss, D.S.3
  • 36
    • 11144230053 scopus 로고    scopus 로고
    • Charged residues at the 2′ position of human GABAC rho 1 receptors invert ion selectivity and influence open state probability
    • J. E. Carland, A. J. Moorhouse, P. H. Barry, G. A. Johnston, and M. Chebib, "Charged residues at the 2′ position of human GABAC rho 1 receptors invert ion selectivity and influence open state probability," J. Biol. Chem., vol. 279, pp. 54 153-54 160, 2004.
    • (2004) J. Biol. Chem. , vol.279
    • Carland, J.E.1    Moorhouse, A.J.2    Barry, P.H.3    Johnston, G.A.4    Chebib, M.5
  • 37
    • 0242349200 scopus 로고    scopus 로고
    • A model of the glycine receptor deduced from Brownian dynamics studies
    • M. O'Mara, P. H. Barry, and S. H. Chung, "A model of the glycine receptor deduced from Brownian dynamics studies," Proc. Nat. Acad. Sci. USA, vol. 100, pp. 4310-4315, 2003.
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , pp. 4310-4315
    • O'Mara, M.1    Barry, P.H.2    Chung, S.H.3
  • 38
    • 0032215090 scopus 로고    scopus 로고
    • Allosteric receptors after 30 years
    • J. P. Changeux and S. J. Edelstein, "Allosteric receptors after 30 years," Neuron, vol. 21, pp. 959-980, 1998.
    • (1998) Neuron , vol.21 , pp. 959-980
    • Changeux, J.P.1    Edelstein, S.J.2
  • 39
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • D. E. Koshland Jr., G. Nemethy, and D. Filmer, "Comparison of experimental binding data and theoretical models in proteins containing subunits," Biochemistry, vol. 5, pp. 365-385, 1966.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 40
    • 0038149197 scopus 로고    scopus 로고
    • Life at the top: The transition state of AChR gating
    • A. Auerbach, "Life at the top: the transition state of AChR gating," Sci. STKE, vol. 2003, p. re11, 2003.
    • (2003) Sci. STKE , vol.2003
    • Auerbach, A.1
  • 42
    • 0032514762 scopus 로고    scopus 로고
    • From ab initio quantum mechanics to molecular neurobiology: A cation-pi binding site in the nicotinic receptor
    • W. Zhong, J. P. Gallivan, Y. Zhang, L. Li, H. A. Lester, and D. A. Dougherty, "From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor," Proc. Nat. Acad. Sci. USA, vol. 95, pp. 12088-12093, 1998.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 12088-12093
    • Zhong, W.1    Gallivan, J.P.2    Zhang, Y.3    Li, L.4    Lester, H.A.5    Dougherty, D.A.6
  • 43
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • P. H. Celie, S. E. van Rossum-Fikkert, W. J. van Dijk, K. Brejc, A. B. Smit, and T. K. Sixma, "Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures," Neuron, vol. 41, pp. 907-914, 2004.
    • (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
  • 44
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • N. Unwin, "Acetylcholine receptor channel imaged in the open state," Nature, vol. 373, pp. 37-43, 1995.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 45
    • 0036304564 scopus 로고    scopus 로고
    • Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the alpha subunits
    • N. Unwin, A. Miyazawa, J. Li, and Y. Fujiyoshi, "Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the alpha subunits," J. Mol. Biol., vol. 319, pp. 1165-1176, 2002.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1165-1176
    • Unwin, N.1    Miyazawa, A.2    Li, J.3    Fujiyoshi, Y.4
  • 46
    • 0035141668 scopus 로고    scopus 로고
    • Structure and dynamics of the GABA binding pocket: A narrowing cleft that constricts during activation
    • D. A. Wagner and C. Czajkowski, "Structure and dynamics of the GABA binding pocket: a narrowing cleft that constricts during activation," J. Neurosci., vol. 21, pp. 67-74, 2001.
    • (2001) J. Neurosci. , vol.21 , pp. 67-74
    • Wagner, D.A.1    Czajkowski, C.2
  • 47
    • 0037544107 scopus 로고    scopus 로고
    • An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors
    • T. Grutter, L. Prado de Carvalho, N. Le Novere, P. J. Corringer, S. Edelstein, and J. P. Changeux, "An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors," EMBO J., vol. 22, pp. 1990-2003, 2003.
    • (2003) EMBO J. , vol.22 , pp. 1990-2003
    • Grutter, T.1    Prado De Carvalho, L.2    Le Novere, N.3    Corringer, P.J.4    Edelstein, S.5    Changeux, J.P.6
  • 48
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • J. W. Lynch, S. Rajendra, K. D. Pierce, C. A. Handford, P. H. Barry, and P. R. Schofield, "Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel," EMBO J., vol. 16, pp. 110-120, 1997.
    • (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
  • 49
    • 0347379903 scopus 로고    scopus 로고
    • Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor
    • N. L. Absalom, T. M. Lewis, W. Kaplan, K. D. Pierce, and P. R. Schofield, "Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor," J. Biol Chem., vol. 278, pp. 50151-50157, 2003.
    • (2003) J. Biol Chem. , vol.278 , pp. 50151-50157
    • Absalom, N.L.1    Lewis, T.M.2    Kaplan, W.3    Pierce, K.D.4    Schofield, P.R.5
  • 50
    • 0037448581 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in the GABA(A) receptor
    • T. L. Kash, A. Jenkins, J. C. Kelley, J. R. Trudell, and N. L. Harrison, "Coupling of agonist binding to channel gating in the GABA(A) receptor," Nature, vol. 421, pp. 272-275, 2003.
    • (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
    • 1042301377 scopus 로고    scopus 로고
    • Charged residues in the beta2 subunit involved in GABAA receptor activation
    • T. L. Kash, M. J. Dizon, J. R. Trudell, and N. L. Harrison, "Charged residues in the beta2 subunit involved in GABAA receptor activation," J. Biol. Chem., vol. 279, pp. 4887-4893, 2004.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4887-4893
    • Kash, T.L.1    Dizon, M.J.2    Trudell, J.R.3    Harrison, N.L.4
  • 52
    • 0029163027 scopus 로고
    • Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors
    • C. Labarca, M. W. Nowak, H. Zhang, L. Tang, P. Deshpande, and H. A. Lester, "Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors," Nature, vol. 376, pp. 514-516, 1995.
    • (1995) Nature , vol.376 , pp. 514-516
    • Labarca, C.1    Nowak, M.W.2    Zhang, H.3    Tang, L.4    Deshpande, P.5    Lester, H.A.6
  • 53
    • 1642565156 scopus 로고    scopus 로고
    • Loose protein packing around the extracellular half of the GABA(A) receptor beta1 subunit M2 channel-lining segment
    • E. N. Goren, D. C. Reeves, and M. H. Akabas, "Loose protein packing around the extracellular half of the GABA(A) receptor beta1 subunit M2 channel-lining segment," J. Biol. Chem., vol. 279, pp. 11198-11205, 2004.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11198-11205
    • Goren, E.N.1    Reeves, D.C.2    Akabas, M.H.3
  • 54
    • 0035042719 scopus 로고    scopus 로고
    • Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment
    • J. Horenstein, D. A. Wagner, C. Czajkowski, and M. H. Akabas, "Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment," Nature Neurosci., vol. 4, pp. 477-485, 2001.
    • (2001) Nature Neurosci. , vol.4 , pp. 477-485
    • Horenstein, J.1    Wagner, D.A.2    Czajkowski, C.3    Akabas, M.H.4
  • 55
    • 4143126482 scopus 로고    scopus 로고
    • A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore
    • S. Kim, A. K. Chamberlain, and J. U. Bowie, "A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore," Biophys. J., vol. 87, pp. 792-799, 2004.
    • (2004) Biophys. J. , vol.87 , pp. 792-799
    • Kim, S.1    Chamberlain, A.K.2    Bowie, J.U.3
  • 56
    • 0036522962 scopus 로고    scopus 로고
    • Evidence for a centrally located gate in the pore of a serotonin-gated ion channel
    • S. Panicker, H. Cruz, C. Arrabit, and P. A. Slesinger, "Evidence for a centrally located gate in the pore of a serotonin-gated ion channel," J. Neurosci., vol. 22, pp. 1629-1639, 2002.
    • (2002) J. Neurosci. , vol.22 , pp. 1629-1639
    • Panicker, S.1    Cruz, H.2    Arrabit, C.3    Slesinger, P.A.4
  • 57
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit
    • M. H. Akabas, C. Kaufmann, P. Archdeacon, and A. Karlin, "Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit," Neuron, vol. 13, pp. 919-927, 1994.
    • (1994) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 58
    • 2442682764 scopus 로고    scopus 로고
    • Evidence that the TM1-TM2 to the rho1 GABA receptor pore
    • N. Filippova, V. E. Wotring, and D. S. Weiss, "Evidence that the TM1-TM2 to the rho1 GABA receptor pore," J. Biol. Chem., vol. 279, pp. 20906-20914, 2004.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20906-20914
    • Filippova, N.1    Wotring, V.E.2    Weiss, D.S.3
  • 59
    • 0029865892 scopus 로고    scopus 로고
    • Identification of channel-lining residues in the M2 membrane-spanning segment of the GABA(A) receptor alpha1 subunit
    • M. Xu and M. H. Akabas, "Identification of channel-lining residues in the M2 membrane-spanning segment of the GABA(A) receptor alpha1 subunit," J. Gen. Physiol., vol. 107, pp. 195-205, 1996.
    • (1996) J. Gen. Physiol. , vol.107 , pp. 195-205
    • Xu, M.1    Akabas, M.H.2
  • 60
    • 0032102496 scopus 로고    scopus 로고
    • The location of the gate in the acetylcholine receptor channel
    • G. G. Wilson and A. Karlin, "The location of the gate in the acetylcholine receptor channel," Neuron, vol. 20, pp. 1269-1281, 1998.
    • (1998) Neuron , vol.20 , pp. 1269-1281
    • Wilson, G.G.1    Karlin, A.2
  • 61
    • 0037389775 scopus 로고    scopus 로고
    • Structural effects of quinacrine binding in the open channel of the acetylcholine receptor
    • Y. Yu, L. Shi, and A. Karlin, "Structural effects of quinacrine binding in the open channel of the acetylcholine receptor," Proc. Nat. Acad. Sci. USA, vol. 100, pp. 3907-3912, 2003.
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , pp. 3907-3912
    • Yu, Y.1    Shi, L.2    Karlin, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.