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Volumn 47, Issue 1-3, 2004, Pages 71-95

Structural basis for lipid modulation of nicotinic acetylcholine receptor function

Author keywords

Ligand gated ion channels; Lipid modulation; Nicotinic acetylcholine receptor function

Indexed keywords

ANDROSTANE DERIVATIVE; ANESTHETIC AGENT; BENZOCAINE; BENZYL ALCOHOL; CHLORPROMAZINE; CHOLESTANE DERIVATIVE; CHOLESTEROL; DEXAMETHASONE; ENFLURANE; FATTY ACID DERIVATIVE; HYDROCORTISONE; ISOFLURANE; LIPID; LOCAL ANESTHETIC AGENT; MEMBRANE PROTEIN; N [(2,6 DIMETHYLPHENYL)CARBAMOYLMETHYL]TRIMETHYLAMMONIUM; NICOTINIC AGENT; NICOTINIC RECEPTOR; PHENCYCLIDINE; PHOSPHATIDYLINOSITOL; PHOSPHOLIPID; PROCAINE; STEROL DERIVATIVE; TETRACAINE;

EID: 9644294471     PISSN: 01650173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainresrev.2004.06.008     Document Type: Conference Paper
Times cited : (157)

References (198)
  • 1
    • 0028088573 scopus 로고
    • Lipid-protein interactions and protein dynamics in vesicles containing the nicotinic acetylcholine receptor: A study with ethanol
    • V.C. Abadji, D.E. Reines, L.A. Dalton, and K.M. Miller Lipid-protein interactions and protein dynamics in vesicles containing the nicotinic acetylcholine receptor: a study with ethanol Biochim. Biophys. Acta 1194 1994 25 34
    • (1994) Biochim. Biophys. Acta , vol.1194 , pp. 25-34
    • Abadji, V.C.1    Reines, D.E.2    Dalton, L.A.3    Miller, K.M.4
  • 3
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • M.H. Akabas, D.A. Stauffer, M. Xu, and A. Karlin Acetylcholine receptor channel structure probed in cysteine-substitution mutants Science 258 1992 307 310
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 4
    • 0019135697 scopus 로고
    • Inhibition of ion permeability control properties of acetylcholine receptor from Torpedo californica by long-chain fatty acids
    • T.J. Andreasen, and M.G. McNamee Inhibition of ion permeability control properties of acetylcholine receptor from Torpedo californica by long-chain fatty acids Biochemistry 19 1980 4719 4726
    • (1980) Biochemistry , vol.19 , pp. 4719-4726
    • Andreasen, T.J.1    McNamee, M.G.2
  • 5
    • 0032564372 scopus 로고    scopus 로고
    • Disclosure of discrete sites for phospholipid and sterols at the protein-lipid interface in native acetylcholine receptor-rich membrane
    • S.S. Antollini, and F.J. Barrantes Disclosure of discrete sites for phospholipid and sterols at the protein-lipid interface in native acetylcholine receptor-rich membrane Biochemistry 37 1998 16653 16662
    • (1998) Biochemistry , vol.37 , pp. 16653-16662
    • Antollini, S.S.1    Barrantes, F.J.2
  • 6
    • 0037059803 scopus 로고    scopus 로고
    • Unique effects of different fatty acid species on the physical properties of the torpedo acetylcholine receptor membrane
    • S.S. Antollini, and F.J. Barrantes Unique effects of different fatty acid species on the physical properties of the torpedo acetylcholine receptor membrane J. Biol. Chem. 277 2002 1249 1254
    • (2002) J. Biol. Chem. , vol.277 , pp. 1249-1254
    • Antollini, S.S.1    Barrantes, F.J.2
  • 7
    • 0030032803 scopus 로고    scopus 로고
    • Physical state of bulk and protein-associated lipid in nicotinic acetylcholine receptor-rich membrane studied by Laurdan generalized polarization and fluorescence energy transfer
    • S.S. Antollini, M.A. Soto, I.C. Bonini de Romanelli, C. Gutierrez-Merino, P. Sotomayor, and F.J. Barrantes Physical state of bulk and protein-associated lipid in nicotinic acetylcholine receptor-rich membrane studied by Laurdan generalized polarization and fluorescence energy transfer Biophys. J. 70 1996 1275 1284
    • (1996) Biophys. J. , vol.70 , pp. 1275-1284
    • Antollini, S.S.1    Soto, M.A.2    Bonini De Romanelli, I.C.3    Gutierrez-Merino, C.4    Sotomayor, P.5    Barrantes, F.J.6
  • 8
    • 0024992914 scopus 로고
    • Effect of local anaesthetics on steroid-nicotinic acetylcholine receptor interactions in native membranes of Torpedo marmorata electric organ
    • H.R. Arias, M.B. Sankaram, D. Marsh, and F.J. Barrantes Effect of local anaesthetics on steroid-nicotinic acetylcholine receptor interactions in native membranes of Torpedo marmorata electric organ Biochim. Biophys. Acta 1027 1990 287 294
    • (1990) Biochim. Biophys. Acta , vol.1027 , pp. 287-294
    • Arias, H.R.1    Sankaram, M.B.2    Marsh, D.3    Barrantes, F.J.4
  • 9
    • 0024457025 scopus 로고
    • Cholesterol stabilizes the structure of the nicotinic acetylcholine receptor reconstituted in lipid vesicles
    • A. Artigues, M.T. Villar, A.M. Fernandez, J.A. Ferragut, and J.M. Gonzalez-Ros Cholesterol stabilizes the structure of the nicotinic acetylcholine receptor reconstituted in lipid vesicles Biochim. Biophys. Acta 985 1989 325 330
    • (1989) Biochim. Biophys. Acta , vol.985 , pp. 325-330
    • Artigues, A.1    Villar, M.T.2    Fernandez, A.M.3    Ferragut, J.A.4    Gonzalez-Ros, J.M.5
  • 10
    • 0027308749 scopus 로고
    • A Raman spectroscopic study of acetylcholine receptor-rich membranes from Torpedo marmorata. Interaction of the receptor with carbamylcholine and (+)-tubocurarine
    • D. Aslanian, P. Grof, J.-L. Galzi, and J.-P. Changeux A Raman spectroscopic study of acetylcholine receptor-rich membranes from Torpedo marmorata. Interaction of the receptor with carbamylcholine and (+)-tubocurarine Biochim. Biophys. Acta 1148 1993 291 302
    • (1993) Biochim. Biophys. Acta , vol.1148 , pp. 291-302
    • Aslanian, D.1    Grof, P.2    Galzi, J.-L.3    Changeux, J.-P.4
  • 11
    • 0028800463 scopus 로고    scopus 로고
    • Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of a-helical peptide hydrogens in the nicotinic acetylcholine receptor
    • J.E. Baenziger, and N. Methot Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of a-helical peptide hydrogens in the nicotinic acetylcholine receptor J. Biol. Chem. 270 1996 29129 29137
    • (1996) J. Biol. Chem. , vol.270 , pp. 29129-29137
    • Baenziger, J.E.1    Methot, N.2
  • 12
    • 18544393335 scopus 로고    scopus 로고
    • Internal dynamics of the nicotinic acetylcholine receptor in reconstituted membranes
    • J.E. Baenziger, T.E. Darsaut, and M.L. Morris Internal dynamics of the nicotinic acetylcholine receptor in reconstituted membranes Biochemistry 38 1999 4905 4911
    • (1999) Biochemistry , vol.38 , pp. 4905-4911
    • Baenziger, J.E.1    Darsaut, T.E.2    Morris, M.L.3
  • 13
    • 0033954766 scopus 로고    scopus 로고
    • Effect of membrane lipid composition on the conformational equilibria of the nicotinic acetylcholine receptor
    • J.E. Baenziger, M.L. Morris, T.E. Darsaut, and S.E. Ryan Effect of membrane lipid composition on the conformational equilibria of the nicotinic acetylcholine receptor J. Biol. Chem. 275 2000 777 784
    • (2000) J. Biol. Chem. , vol.275 , pp. 777-784
    • Baenziger, J.E.1    Morris, M.L.2    Darsaut, T.E.3    Ryan, S.E.4
  • 14
    • 0018082157 scopus 로고
    • Agonist-mediated changes of the acetylcholine receptor in its membrane environment
    • F.J. Barrantes Agonist-mediated changes of the acetylcholine receptor in its membrane environment J. Mol. Biol. 124 1978 1 26
    • (1978) J. Mol. Biol. , vol.124 , pp. 1-26
    • Barrantes, F.J.1
  • 15
    • 0020992167 scopus 로고
    • Recent developments in the structure and function of the acetylcholine receptor
    • F.J. Barrantes Recent developments in the structure and function of the acetylcholine receptor Int. Rev. Neurobiol. 24 1983 259 341
    • (1983) Int. Rev. Neurobiol. , vol.24 , pp. 259-341
    • Barrantes, F.J.1
  • 16
    • 0024330573 scopus 로고
    • The lipid environment of the nicotinic acetylcholine receptor in native and reconstituted membranes
    • F.J. Barrantes The lipid environment of the nicotinic acetylcholine receptor in native and reconstituted membranes Crit. Rev. Biochem. Mol. Biol. 24 1989 437 478
    • (1989) Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 437-478
    • Barrantes, F.J.1
  • 17
    • 0027021365 scopus 로고
    • Structural and functional crosstalk between acetylcholine receptor and its membrane environment
    • F.J. Barrantes Structural and functional crosstalk between acetylcholine receptor and its membrane environment Mol. Neurobiol. 6 1992 463 482
    • (1992) Mol. Neurobiol. , vol.6 , pp. 463-482
    • Barrantes, F.J.1
  • 18
    • 0027143944 scopus 로고
    • Structural-functional correlates of the nicotinic acetylcholine receptor and its lipid microenvironment
    • F.J. Barrantes Structural-functional correlates of the nicotinic acetylcholine receptor and its lipid microenvironment FASEB J. 7 1993 1460 1467
    • (1993) FASEB J. , vol.7 , pp. 1460-1467
    • Barrantes, F.J.1
  • 19
    • 77956833553 scopus 로고
    • The lipid annulus of the nicotinic acetylcholine receptor as a locus of structural-functional interactions
    • A. Watts Elsevier Amsterdam
    • F.J. Barrantes The lipid annulus of the nicotinic acetylcholine receptor as a locus of structural-functional interactions A. Watts New Comprehensive Biochemistry 1993 Elsevier Amsterdam 231 257
    • (1993) New Comprehensive Biochemistry , pp. 231-257
    • Barrantes, F.J.1
  • 20
  • 22
    • 0001193946 scopus 로고    scopus 로고
    • Fluorescence studies of the acetylcholine receptor: Structure and dynamics in the membramne environment
    • F.J. Barrantes Fluorescence studies of the acetylcholine receptor: structure and dynamics in the membramne environment J. Fluoresc. 11 2001 273 285
    • (2001) J. Fluoresc. , vol.11 , pp. 273-285
    • Barrantes, F.J.1
  • 23
    • 0142027322 scopus 로고    scopus 로고
    • Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains
    • F.J. Barrantes Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains Curr. Opin. Drug Discov. Dev. 6 2003 620 632
    • (2003) Curr. Opin. Drug Discov. Dev. , vol.6 , pp. 620-632
    • Barrantes, F.J.1
  • 24
    • 0034532112 scopus 로고    scopus 로고
    • Topography of nicotinic acetylcholine receptor membrane-embedded domains
    • F.J. Barrantes, S.S. Antollini, M.P. Blanton, and M. Prieto Topography of nicotinic acetylcholine receptor membrane-embedded domains J. Biol. Chem. 275 2000 37333 37339
    • (2000) J. Biol. Chem. , vol.275 , pp. 37333-37339
    • Barrantes, F.J.1    Antollini, S.S.2    Blanton, M.P.3    Prieto, M.4
  • 28
    • 0027270304 scopus 로고
    • Correlation of phospholipid structure with functional effects on the nicotinic acetylcholine receptor. A modulatory role for phosphatidic acid
    • A. Bhushan, and M.G. McNamee Correlation of phospholipid structure with functional effects on the nicotinic acetylcholine receptor. A modulatory role for phosphatidic acid Biophys. J. 64 1993 716 723
    • (1993) Biophys. J. , vol.64 , pp. 716-723
    • Bhushan, A.1    McNamee, M.G.2
  • 29
    • 0026654217 scopus 로고
    • Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor
    • M.P. Blanton, and J.B. Cohen Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor Biochemistry 31 1992 3738 3750
    • (1992) Biochemistry , vol.31 , pp. 3738-3750
    • Blanton, M.P.1    Cohen, J.B.2
  • 30
    • 0028326435 scopus 로고
    • Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: Secondary structure implications
    • M.P. Blanton, and J.B. Cohen Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: secondary structure implications Biochemistry 33 1994 2859 2872
    • (1994) Biochemistry , vol.33 , pp. 2859-2872
    • Blanton, M.P.1    Cohen, J.B.2
  • 31
    • 0025044562 scopus 로고
    • Photoaffinity labeling of the Torpedo californica nicotinic acetylcholine receptor with an aryl azide derivative of phosphatidylserine
    • M.P. Blanton, and H.H. Wang Photoaffinity labeling of the Torpedo californica nicotinic acetylcholine receptor with an aryl azide derivative of phosphatidylserine Biochemistry 29 1990 1186 1194
    • (1990) Biochemistry , vol.29 , pp. 1186-1194
    • Blanton, M.P.1    Wang, H.H.2
  • 32
    • 0025850892 scopus 로고
    • Localization of regions of the Torpedo californica nicotinic acetylcholine receptor labeled with an aryl azide derivative of phosphatidylserine
    • M.P. Blanton, and H.H. Wang Localization of regions of the Torpedo californica nicotinic acetylcholine receptor labeled with an aryl azide derivative of phosphatidylserine Biochim. Biophys. Acta 1067 1991 1 8
    • (1991) Biochim. Biophys. Acta , vol.1067 , pp. 1-8
    • Blanton, M.P.1    Wang, H.H.2
  • 34
    • 0033046008 scopus 로고    scopus 로고
    • The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface
    • M.P. Blanton, Y. Xie, L.J. Dangott, and J.B. Cohen The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface Mol. Pharmacol. 55 1999 269 278
    • (1999) Mol. Pharmacol. , vol.55 , pp. 269-278
    • Blanton, M.P.1    Xie, Y.2    Dangott, L.J.3    Cohen, J.B.4
  • 36
    • 0023370310 scopus 로고
    • Extraction of peripheral proteins is accompanied by selective depletion of certain glycerophospholipid classes and changes in the phosphorylation pattern of acetylcholine-receptor-rich-membrane proteins
    • I.C. Bonini de Romanelli, A.M. Roccamo de Fernandez, and F.J. Barrantes Extraction of peripheral proteins is accompanied by selective depletion of certain glycerophospholipid classes and changes in the phosphorylation pattern of acetylcholine-receptor-rich-membrane proteins Biochem. J. 245 1987 111 118
    • (1987) Biochem. J. , vol.245 , pp. 111-118
    • Bonini De Romanelli, I.C.1    Roccamo De Fernandez, A.M.2    Barrantes, F.J.3
  • 37
    • 0036823480 scopus 로고    scopus 로고
    • Sphingomyelin composition and physical asymmetries in native acetylcholine receptor-rich membranes
    • I.C. Bonini, S.S. Antollini, C. Gutierrez-Merino, and F.J. Barrantes Sphingomyelin composition and physical asymmetries in native acetylcholine receptor-rich membranes Eur. Biophys. J. 31 2002 417 427
    • (2002) Eur. Biophys. J. , vol.31 , pp. 417-427
    • Bonini, I.C.1    Antollini, S.S.2    Gutierrez-Merino, C.3    Barrantes, F.J.4
  • 38
    • 0025999524 scopus 로고
    • Acetylcholine receptor channel properties are modified by benzyl alcohol
    • C. Bouzat, and F.J. Barrantes Acetylcholine receptor channel properties are modified by benzyl alcohol NeuroReport 2 1991 681 684
    • (1991) NeuroReport , vol.2 , pp. 681-684
    • Bouzat, C.1    Barrantes, F.J.2
  • 39
    • 0027296434 scopus 로고
    • Acute exposure of nicotinic acetylcholine receptors to the synthetic glucocorticoid dexamethasone alters single-channel gating properties
    • C. Bouzat, and F.J. Barrantes Acute exposure of nicotinic acetylcholine receptors to the synthetic glucocorticoid dexamethasone alters single-channel gating properties Mol. Neuropharmacol. 3 1993 109 116
    • (1993) Mol. Neuropharmacol. , vol.3 , pp. 109-116
    • Bouzat, C.1    Barrantes, F.J.2
  • 40
    • 0027339530 scopus 로고
    • Hydrocortisone and 11-desoxycortisone modify acetylcholine receptor channel gating
    • C. Bouzat, and F.J. Barrantes Hydrocortisone and 11-desoxycortisone modify acetylcholine receptor channel gating NeuroReport 4 1993 143 146
    • (1993) NeuroReport , vol.4 , pp. 143-146
    • Bouzat, C.1    Barrantes, F.J.2
  • 41
    • 0027141153 scopus 로고
    • Effects of long-chain fatty acids on the channel activity of the nicotinic acetylcholine receptor
    • C.B. Bouzat, and F.J. Barrantes Effects of long-chain fatty acids on the channel activity of the nicotinic acetylcholine receptor Recept. Channels 1 1993 251 258
    • (1993) Recept. Channels , vol.1 , pp. 251-258
    • Bouzat, C.B.1    Barrantes, F.J.2
  • 42
    • 0029995665 scopus 로고    scopus 로고
    • Modulation of muscle nicotinic acetylcholine receptors by the glucocorticoid hydrocortisone. Possible allosteric mechanism of channel blockade
    • C. Bouzat, and F.J. Barrantes Modulation of muscle nicotinic acetylcholine receptors by the glucocorticoid hydrocortisone. Possible allosteric mechanism of channel blockade J. Biol. Chem. 271 1996 25835 25841
    • (1996) J. Biol. Chem. , vol.271 , pp. 25835-25841
    • Bouzat, C.1    Barrantes, F.J.2
  • 43
    • 0028600111 scopus 로고
    • Structural basis of the different gating kinetics of fetal and adult nicotinic acetylcholine receptors
    • C.B. Bouzat, N. Bren, and S.M. Sine Structural basis of the different gating kinetics of fetal and adult nicotinic acetylcholine receptors Neuron 13 1994 1395 1402
    • (1994) Neuron , vol.13 , pp. 1395-1402
    • Bouzat, C.B.1    Bren, N.2    Sine, S.M.3
  • 44
    • 0031595748 scopus 로고    scopus 로고
    • Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics
    • C. Bouzat, A.M. Roccamo, I. Garbus, and F.J. Barrantes Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics Mol. Pharmacol. 54 1998 146 153
    • (1998) Mol. Pharmacol. , vol.54 , pp. 146-153
    • Bouzat, C.1    Roccamo, A.M.2    Garbus, I.3    Barrantes, F.J.4
  • 45
    • 0034059664 scopus 로고    scopus 로고
    • Nicotinic receptor fourth transmembrane domain. Hydrogen bonding by conserved threonine contributes to channel gating kinetics
    • C. Bouzat, F.J. Barrantes, and S. Sine Nicotinic receptor fourth transmembrane domain. Hydrogen bonding by conserved threonine contributes to channel gating kinetics J. Gen. Physiol. 115 2000 663 672
    • (2000) J. Gen. Physiol. , vol.115 , pp. 663-672
    • Bouzat, C.1    Barrantes, F.J.2    Sine, S.3
  • 46
    • 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, O.J. van Der, A.B. Smit, and T.K. Sixma Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors Nature 411 2001 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, O.J.5    Smit, A.B.6    Sixma, T.K.7
  • 47
    • 0028567824 scopus 로고
    • Differential effects of eicosapentaenoic acid and docosahexaenoic acid on human skin fibroblasts
    • E.R. Brown, and P.V. Subbaiah Differential effects of eicosapentaenoic acid and docosahexaenoic acid on human skin fibroblasts Lipids 29 1994 825 829
    • (1994) Lipids , vol.29 , pp. 825-829
    • Brown, E.R.1    Subbaiah, P.V.2
  • 48
    • 0027202225 scopus 로고
    • FTIR analysis of nicotinic acetylcholine receptor secondary structure in reconstituted membranes
    • D.H. Butler, and M.G. McNamee FTIR analysis of nicotinic acetylcholine receptor secondary structure in reconstituted membranes Biochim. Biophys. Acta, Biomembr. 1150 1993 17 24
    • (1993) Biochim. Biophys. Acta, Biomembr. , vol.1150 , pp. 17-24
    • Butler, D.H.1    McNamee, M.G.2
  • 51
    • 0032215090 scopus 로고    scopus 로고
    • Allosteric receptors after 30 years
    • J.P. Changeux, and S.J. Edelstein Allosteric receptors after 30 years Neuron 21 1998 959 980
    • (1998) Neuron , vol.21 , pp. 959-980
    • Changeux, J.P.1    Edelstein, S.J.2
  • 52
    • 0022558294 scopus 로고
    • Effects of chlorpromazine and phencyclidine on mouse C2 acetylcholine receptor kinetics
    • J.-P. Changeux, C. Pinset, and A.B. Ribera Effects of chlorpromazine and phencyclidine on mouse C2 acetylcholine receptor kinetics J. Physiol. 378 1986 497 513
    • (1986) J. Physiol. , vol.378 , pp. 497-513
    • Changeux, J.-P.1    Pinset, C.2    Ribera, A.B.3
  • 53
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • A. Chattopadhyay, and E. London Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids Biochemistry 26 1987 39 45
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 54
    • 0025748666 scopus 로고
    • Average membrane penetration depth of tryptophan residues of the nicotinic acetylcholine receptor by the parallax method
    • A. Chattopadhyay, and M.G. McNamee Average membrane penetration depth of tryptophan residues of the nicotinic acetylcholine receptor by the parallax method Biochemistry 30 1991 7159 7164
    • (1991) Biochemistry , vol.30 , pp. 7159-7164
    • Chattopadhyay, A.1    McNamee, M.G.2
  • 55
    • 0026513830 scopus 로고
    • Expression of fusion proteins of the nicotinic acetylcholine receptor from mammalian muscle identifies the membrane-spanning regions in the alpha and delta subunits
    • R.A. Chavez, and Z.W. Hall Expression of fusion proteins of the nicotinic acetylcholine receptor from mammalian muscle identifies the membrane-spanning regions in the alpha and delta subunits J. Cell Biol. 116 1992 385 393
    • (1992) J. Cell Biol. , vol.116 , pp. 385-393
    • Chavez, R.A.1    Hall, Z.W.2
  • 56
    • 0010665535 scopus 로고
    • Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor τ subunit
    • T. Claudio, M. Ballivet, J. Patrick, and S. Heinemann Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor τ subunit Proc. Natl. Acad. Sci. U. S. A. 80 1983 1111 1115
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 1111-1115
    • Claudio, T.1    Ballivet, M.2    Patrick, J.3    Heinemann, S.4
  • 58
    • 2642642114 scopus 로고    scopus 로고
    • Secondary structure analysis of individual transmembrane segments of the nicotinic acetylcholine receptor by circular dichroism and Fourier transform infrared spectroscopy
    • J. Corbin, N. Methot, H.H. Wang, J.E. Baenziger, and M.P. Blanton Secondary structure analysis of individual transmembrane segments of the nicotinic acetylcholine receptor by circular dichroism and Fourier transform infrared spectroscopy J. Biol. Chem. 273 1998 771 777
    • (1998) J. Biol. Chem. , vol.273 , pp. 771-777
    • Corbin, J.1    Methot, N.2    Wang, H.H.3    Baenziger, J.E.4    Blanton, M.P.5
  • 61
    • 0020376564 scopus 로고
    • Effects of lipids on acetylcholine receptor. Essential need of cholesterol for maintenance of agonist-induced state transitions in lipid vesicles
    • M. Criado, H. Eibl, and F.J. Barrantes Effects of lipids on acetylcholine receptor. Essential need of cholesterol for maintenance of agonist-induced state transitions in lipid vesicles Biochemistry 21 1982 3622 3629
    • (1982) Biochemistry , vol.21 , pp. 3622-3629
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 62
    • 0020478350 scopus 로고
    • Translational diffusion of acetylcholine receptor (monomeric and dimeric forms) of Torpedo marmorata reconstituted into phospholipid bilayers studied by fluorescence recovery after photobleaching
    • M. Criado, W.L. Vaz, F.J. Barrantes, and T.M. Jovin Translational diffusion of acetylcholine receptor (monomeric and dimeric forms) of Torpedo marmorata reconstituted into phospholipid bilayers studied by fluorescence recovery after photobleaching Biochemistry 21 1982 5750 5755
    • (1982) Biochemistry , vol.21 , pp. 5750-5755
    • Criado, M.1    Vaz, W.L.2    Barrantes, F.J.3    Jovin, T.M.4
  • 63
    • 0021152857 scopus 로고
    • Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptor-mediated ion translocation
    • M. Criado, H. Eibl, and F.J. Barrantes Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptor-mediated ion translocation J. Biol. Chem. 259 1984 9188 9198
    • (1984) J. Biol. Chem. , vol.259 , pp. 9188-9198
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 64
    • 0035449159 scopus 로고    scopus 로고
    • Tryptophan substitutions at lipid-exposed positions of the gamma M3 transmembrane domain increase the macroscopic ionic current response of the Torpedo californica nicotinic acetylcholine receptor
    • A. Cruz-Martin, J.L. Mercado, L.V. Rojas, M.G. McNamee, and J.A. Lasalde-Dominicci Tryptophan substitutions at lipid-exposed positions of the gamma M3 transmembrane domain increase the macroscopic ionic current response of the Torpedo californica nicotinic acetylcholine receptor J. Membr. Biol. 183 2001 61 70
    • (2001) J. Membr. Biol. , vol.183 , pp. 61-70
    • Cruz-Martin, A.1    Mercado, J.L.2    Rojas, L.V.3    McNamee, M.G.4    Lasalde-Dominicci, J.A.5
  • 65
    • 0036006697 scopus 로고    scopus 로고
    • Potentiation of human alpha4beta2 neuronal nicotinic acetylcholine receptor by estradiol
    • L. Curtis, B. Buisson, S. Bertrand, and D. Bertrand Potentiation of human alpha4beta2 neuronal nicotinic acetylcholine receptor by estradiol Mol. Pharmacol. 61 2002 127 135
    • (2002) Mol. Pharmacol. , vol.61 , pp. 127-135
    • Curtis, L.1    Buisson, B.2    Bertrand, S.3    Bertrand, D.4
  • 66
    • 0037016745 scopus 로고    scopus 로고
    • Lipid-protein interactions at the nicotinic acetylcholine receptor. A functional coupling between nicotinic receptors and phosphatidic acid-containing lipid bilayers
    • C.J. daCosta, A.A. Ogrel, E.A. McCardy, M.P. Blanton, and J.E. Baenziger Lipid-protein interactions at the nicotinic acetylcholine receptor. A functional coupling between nicotinic receptors and phosphatidic acid-containing lipid bilayers J. Biol. Chem. 277 2002 201 208
    • (2002) J. Biol. Chem. , vol.277 , pp. 201-208
    • Dacosta, C.J.1    Ogrel, A.A.2    McCardy, E.A.3    Blanton, M.P.4    Baenziger, J.E.5
  • 67
    • 0019137281 scopus 로고
    • The effect of cholesterol on agonist-induced flux reconstituted acetylcholine receptor vesicles
    • A.W. Dalziel, E.S. Rollins, and M.G. McNamee The effect of cholesterol on agonist-induced flux reconstituted acetylcholine receptor vesicles FEBS Lett. 122 1980 193 196
    • (1980) FEBS Lett. , vol.122 , pp. 193-196
    • Dalziel, A.W.1    Rollins, E.S.2    McNamee, M.G.3
  • 68
    • 1942519443 scopus 로고    scopus 로고
    • Cholesterol modulates the organization of the gammaM4 transmembrane domain of the muscle nicotinic acetylcholine receptor
    • R.F. De Almeida, L.M. Loura, M. Prieto, A. Watts, A. Fedorov, and F.J. Barrantes Cholesterol modulates the organization of the gammaM4 transmembrane domain of the muscle nicotinic acetylcholine receptor Biophys. J. 86 2004 2261 2272
    • (2004) Biophys. J. , vol.86 , pp. 2261-2272
    • De Almeida, R.F.1    Loura, L.M.2    Prieto, M.3    Watts, A.4    Fedorov, A.5    Barrantes, F.J.6
  • 69
    • 0036074066 scopus 로고    scopus 로고
    • Nicotinic receptor M3 transmembrane domain: Position 8′ contributes to channel gating
    • M.J.d. De Rosa, D. Rayes, G. Spitzmaul, and C. Bouzat Nicotinic receptor M3 transmembrane domain: position 8′ contributes to channel gating Mol. Pharmacol. 62 2003 406 414
    • (2003) Mol. Pharmacol. , vol.62 , pp. 406-414
    • D.rosa, D.J.M.1    Rayes, D.2    Spitzmaul, G.3    Bouzat, C.4
  • 70
    • 0034688285 scopus 로고    scopus 로고
    • Blocker protection in the pore of a voltage-gated K+ channel and its structural implications
    • D. del Camino, M. Holmgren, Y. Liu, and G. Yellen Blocker protection in the pore of a voltage-gated K+ channel and its structural implications Nature 403 2000 321 325
    • (2000) Nature , vol.403 , pp. 321-325
    • Del Camino, D.1    Holmgren, M.2    Liu, Y.3    Yellen, G.4
  • 71
    • 0026636418 scopus 로고
    • Protein involvement in transmembrane lipid asymmetry
    • P.F. Devaux Protein involvement in transmembrane lipid asymmetry Annu. Rev. Biophys. Biomol. Struct. 21 1992 417 439
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 417-439
    • Devaux, P.F.1
  • 73
    • 0025859786 scopus 로고
    • Actions of volatile anesthetics and alcohols on cholinergic receptor channels
    • J.P. Dilger, and R.S. Brett Actions of volatile anesthetics and alcohols on cholinergic receptor channels Ann. N.Y. Acad. Sci. 625 1991 616 627
    • (1991) Ann. N.Y. Acad. Sci. , vol.625 , pp. 616-627
    • Dilger, J.P.1    Brett, R.S.2
  • 74
    • 0026532751 scopus 로고
    • Effects of isoflurane on acetylcholine receptor channels: 1. Single-channel currents
    • J.P. Dilger, R.S. Brett, and L.A. Lesko Effects of isoflurane on acetylcholine receptor channels: 1. Single-channel currents Mol. Pharmacol. 41 1992 127 133
    • (1992) Mol. Pharmacol. , vol.41 , pp. 127-133
    • Dilger, J.P.1    Brett, R.S.2    Lesko, L.A.3
  • 75
    • 0024362248 scopus 로고
    • An analysis of the periodicity of conserved residues in sequence alignments of G-protein coupled receptors. Implications for the three-dimensional structure
    • D. Donnelly, M.S. Johnson, T.L. Blundell, and J. Saunders An analysis of the periodicity of conserved residues in sequence alignments of G-protein coupled receptors. Implications for the three-dimensional structure FEBS Lett. 251 1989 109 116
    • (1989) FEBS Lett. , vol.251 , pp. 109-116
    • Donnelly, D.1    Johnson, M.S.2    Blundell, T.L.3    Saunders, J.4
  • 76
    • 0001091926 scopus 로고    scopus 로고
    • Interactions of the nicotinic acetylcholine receptor transmembrane segments with the lipid bilayer in native receptor-rich membranes
    • M. Dreger, M. Krauss, A. Herrmann, and F. Hucho Interactions of the nicotinic acetylcholine receptor transmembrane segments with the lipid bilayer in native receptor-rich membranes Biochemistry 36 1997 839 847
    • (1997) Biochemistry , vol.36 , pp. 839-847
    • Dreger, M.1    Krauss, M.2    Herrmann, A.3    Hucho, F.4
  • 77
    • 0021110283 scopus 로고
    • Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor
    • J.F. Ellena, M.A. Blazing, and M.G. McNamee Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor Biochemistry 22 1983 5523 5535
    • (1983) Biochemistry , vol.22 , pp. 5523-5535
    • Ellena, J.F.1    Blazing, M.A.2    McNamee, M.G.3
  • 78
    • 0032458176 scopus 로고    scopus 로고
    • Congenital myasthenic syndromes: Experiments of nature
    • A.G. Engel, K. Ohno, and S.M. Sine Congenital myasthenic syndromes: experiments of nature J. Physiol. 92 1998 117
    • (1998) J. Physiol. , vol.92 , pp. 117
    • Engel, A.G.1    Ohno, K.2    Sine, S.M.3
  • 79
    • 0018120101 scopus 로고
    • Reconstitution of carbamylcholine-dependent sodium ion flux and desensitization of the acetylcholine receptor from Torpedo californica
    • M. Epstein, and E. Racker Reconstitution of carbamylcholine-dependent sodium ion flux and desensitization of the acetylcholine receptor from Torpedo californica J. Biol. Chem. 253 1978 6660 6662
    • (1978) J. Biol. Chem. , vol.253 , pp. 6660-6662
    • Epstein, M.1    Racker, E.2
  • 80
    • 0024523690 scopus 로고
    • 5 alpha-dihydrotestosterone has nonspecific effects on membrane channels and possible genomic effects on ACh-activated channels
    • S.D. Erulkar, and D.M. Wetzel 5 alpha-dihydrotestosterone has nonspecific effects on membrane channels and possible genomic effects on ACh-activated channels J. Neurophysiol. 61 1989 1036 1052
    • (1989) J. Neurophysiol. , vol.61 , pp. 1036-1052
    • Erulkar, S.D.1    Wetzel, D.M.2
  • 81
    • 0027273911 scopus 로고
    • Labeling of the nicotinic acetylcholine receptor by a photoactivatable steroid probe: Effects of cholesterol and cholinergic ligands
    • A.M. Fernandez, G. Fernandez-Ballester, J.A. Ferragut, and J.M. Gonzalez-Ros Labeling of the nicotinic acetylcholine receptor by a photoactivatable steroid probe: effects of cholesterol and cholinergic ligands Biochim. Biophys. Acta 1149 1993 135 144
    • (1993) Biochim. Biophys. Acta , vol.1149 , pp. 135-144
    • Fernandez, A.M.1    Fernandez-Ballester, G.2    Ferragut, J.A.3    Gonzalez-Ros, J.M.4
  • 82
    • 0026443750 scopus 로고
    • Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy
    • G. Fernandez-Ballester, J. Castresana, J.-L.R. Arrondo, J.A. Ferragut, and J.M. Gonzalez-Ros Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy Biochem. J. 288 1992 421 426
    • (1992) Biochem. J. , vol.288 , pp. 421-426
    • Fernandez-Ballester, G.1    Castresana, J.2    Arrondo, J.-L.R.3    Ferragut, J.A.4    Gonzalez-Ros, J.M.5
  • 84
    • 0026523827 scopus 로고
    • Lysophosphatidic acid induces inward currents in Xenopus laevis oocytes; Evidence for an extracellular site of action
    • B.J. Fernhout, F.A. Dijcks, W.H. Moolenaar, and G.S. Ruigt Lysophosphatidic acid induces inward currents in Xenopus laevis oocytes; evidence for an extracellular site of action Eur. J. Pharmacol. 213 1992 313 315
    • (1992) Eur. J. Pharmacol. , vol.213 , pp. 313-315
    • Fernhout, B.J.1    Dijcks, F.A.2    Moolenaar, W.H.3    Ruigt, G.S.4
  • 86
    • 0010214174 scopus 로고
    • Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor
    • J. Finer-Moore, and R.M. Stroud Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor Proc. Natl. Acad. Sci. U. S. A. 81 1984 155 159
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 155-159
    • Finer-Moore, J.1    Stroud, R.M.2
  • 87
    • 0023193779 scopus 로고
    • Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes
    • T.M. Fong, and M.G. McNamee Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes Biochemistry 26 1987 3871 3880
    • (1987) Biochemistry , vol.26 , pp. 3871-3880
    • Fong, T.M.1    McNamee, M.G.2
  • 88
    • 0027370953 scopus 로고
    • Arachidonic acid inhibits sodium currents and synaptic transmission in cultured striatal neurons
    • D.D. Fraser, K. Hoehn, S. Weiss, and B.A. MacVicar Arachidonic acid inhibits sodium currents and synaptic transmission in cultured striatal neurons Neuron 11 1993 633 644
    • (1993) Neuron , vol.11 , pp. 633-644
    • Fraser, D.D.1    Hoehn, K.2    Weiss, S.3    MacVicar, B.A.4
  • 90
    • 0025753149 scopus 로고
    • Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand
    • J.-L. Galzi, F. Revah, F. Bouet, A. Ménez, M. Goeldner, C. Hirth, and J.-P. Changeux Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand Proc. Natl. Acad. Sci. U. S. A. 88 1991 5051 5055
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5051-5055
    • Galzi, J.-L.1    Revah, F.2    Bouet, F.3    Ménez, A.4    Goeldner, M.5    Hirth, C.6    Changeux, J.-P.7
  • 91
    • 0035847596 scopus 로고    scopus 로고
    • Steroids differentially inhibit the nicotinic acetylcholine receptor
    • I. Garbus, C. Bouzat, and F.J. Barrantes Steroids differentially inhibit the nicotinic acetylcholine receptor NeuroReport 12 2001 227 231
    • (2001) NeuroReport , vol.12 , pp. 227-231
    • Garbus, I.1    Bouzat, C.2    Barrantes, F.J.3
  • 92
    • 0036629771 scopus 로고    scopus 로고
    • Identification of threonine 422 in transmembrane domain αm4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone
    • I. Garbus, A.M. Roccamo, and F.J. Barrantes Identification of threonine 422 in transmembrane domain αM4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone. Neuropharmacology 43 2002 65 73
    • (2002) Neuropharmacology , vol.43 , pp. 65-73
    • Garbus, I.1    Roccamo, A.M.2    Barrantes, F.J.3
  • 93
    • 0021881226 scopus 로고
    • Transmembrane topology of acetylcholine receptor subunits probed with photoreactive phospholipids
    • J. Giraudat, C. Montecucco, R. Bisson, and J.-P. Changeux Transmembrane topology of acetylcholine receptor subunits probed with photoreactive phospholipids Biochemistry 24 1985 3121 3127
    • (1985) Biochemistry , vol.24 , pp. 3121-3127
    • Giraudat, J.1    Montecucco, C.2    Bisson, R.3    Changeux, J.-P.4
  • 95
    • 0027954627 scopus 로고
    • The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β structures
    • U. Görne-Tschelnokow, A. Strecker, C. Kaduk, D. Naumann, and F. Hucho The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β structures EMBO J. 13 1994 338 341
    • (1994) EMBO J. , vol.13 , pp. 338-341
    • Görne-Tschelnokow, U.1    Strecker, A.2    Kaduk, C.3    Naumann, D.4    Hucho, F.5
  • 97
    • 0033578392 scopus 로고    scopus 로고
    • Expression and spectroscopic analysis of soluble nicotinic acetylcholine receptor fragments derived from the extracellular domain of the alpha-subunit
    • M.A. Grant, L.N. Gentile, Q.L. Shi, M. Pellegrini, and E. Hawrot Expression and spectroscopic analysis of soluble nicotinic acetylcholine receptor fragments derived from the extracellular domain of the alpha-subunit Biochemistry 38 1999 10730 10742
    • (1999) Biochemistry , vol.38 , pp. 10730-10742
    • Grant, M.A.1    Gentile, L.N.2    Shi, Q.L.3    Pellegrini, M.4    Hawrot, E.5
  • 98
    • 0028841402 scopus 로고
    • The desensitization of the embryonic mouse muscle acetylcholine receptor depends on the cellular environment
    • F. Grassi, E. Palma, A.M. Mileo, and F. Eusebi The desensitization of the embryonic mouse muscle acetylcholine receptor depends on the cellular environment. Pflügers Arch. 430 1995 787 794
    • (1995) Pflügers Arch. , vol.430 , pp. 787-794
    • Grassi, F.1    Palma, E.2    Mileo, A.M.3    Eusebi, F.4
  • 99
    • 0019363342 scopus 로고
    • Glycosphingolipids in cellular interaction, differentiation, and oncogenesis
    • S. Hakomori Glycosphingolipids in cellular interaction, differentiation, and oncogenesis Ann. Rev. Biochem. 50 1981 733 764
    • (1981) Ann. Rev. Biochem. , vol.50 , pp. 733-764
    • Hakomori, S.1
  • 100
    • 0025687373 scopus 로고
    • A temperature-sensitive mammalian cell mutant with thermolabile serine palmitoyltransferase for the sphingolipid biosynthesis
    • K. Hanada, M. Nishijima, and Y. Akamatsu A temperature-sensitive mammalian cell mutant with thermolabile serine palmitoyltransferase for the sphingolipid biosynthesis J. Biol. Chem. 265 1990 22137 22142
    • (1990) J. Biol. Chem. , vol.265 , pp. 22137-22142
    • Hanada, K.1    Nishijima, M.2    Akamatsu, Y.3
  • 101
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Y.A. Hannun Functions of ceramide in coordinating cellular responses to stress Science 274 1996 1805 1976
    • (1996) Science , vol.274 , pp. 1805-1976
    • Hannun, Y.A.1
  • 102
    • 0024989939 scopus 로고
    • Association of spin-labeled local anesthetics at the hydrophobic surface of acetylcholine receptor in native membranes from Torpedo marmorata
    • L.I. Horváth, H.R. Arias, H.O. Hankovszky, K. Hideg, F.J. Barrantes, and D. Marsh Association of spin-labeled local anesthetics at the hydrophobic surface of acetylcholine receptor in native membranes from Torpedo marmorata Biochemistry 29 1990 8707 8713
    • (1990) Biochemistry , vol.29 , pp. 8707-8713
    • Horváth, L.I.1    Arias, H.R.2    Hankovszky, H.O.3    Hideg, K.4    Barrantes, F.J.5    Marsh, D.6
  • 103
    • 0029935694 scopus 로고    scopus 로고
    • Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes of mice
    • U. Igbavboa, N.A. Avdulov, F. Schroeder, and W.G. Wood Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes of mice J. Neurochem. 66 1996 1717 1725
    • (1996) J. Neurochem. , vol.66 , pp. 1717-1725
    • Igbavboa, U.1    Avdulov, N.A.2    Schroeder, F.3    Wood, W.G.4
  • 104
    • 0024308769 scopus 로고
    • Glucocorticoids inhibit acetylcholine-induced current in chromaffin cells
    • M. Inoue, and H. Kuriyama Glucocorticoids inhibit acetylcholine-induced current in chromaffin cells Am. J. Physiol. 257 1989 C906 C912
    • (1989) Am. J. Physiol. , vol.257
    • Inoue, M.1    Kuriyama, H.2
  • 106
    • 0024278441 scopus 로고
    • Annular and nonannular binding sites for cholesterol associated with the nicotinic aceytlcholine receptor
    • O.T. Jones, and M.G. McNamee Annular and nonannular binding sites for cholesterol associated with the nicotinic aceytlcholine receptor Biochemistry 27 1988 2364 2374
    • (1988) Biochemistry , vol.27 , pp. 2364-2374
    • Jones, O.T.1    McNamee, M.G.2
  • 107
    • 0023941416 scopus 로고
    • A minimum number of lipids are required to support the functional properties of the nicotinic acetylcholine receptor
    • O.T. Jones, J.H. Eubanks, J.P. Earnest, and M.G. McNamee A minimum number of lipids are required to support the functional properties of the nicotinic acetylcholine receptor Biochemistry 27 1988 3733 3742
    • (1988) Biochemistry , vol.27 , pp. 3733-3742
    • Jones, O.T.1    Eubanks, J.H.2    Earnest, J.P.3    McNamee, M.G.4
  • 108
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • A. Karlin Emerging structure of the nicotinic acetylcholine receptors Nat. Rev., Neurosci. 3 2002 102 114
    • (2002) Nat. Rev., Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 109
    • 0029825054 scopus 로고    scopus 로고
    • Effects of steroid exposure on ligand binding and functional activities of diverse nicotinic acetylcholine receptor subtypes
    • L. Ke, and R.J. Lukas Effects of steroid exposure on ligand binding and functional activities of diverse nicotinic acetylcholine receptor subtypes J. Neurochem. 67 1996 1100 1112
    • (1996) J. Neurochem. , vol.67 , pp. 1100-1112
    • Ke, L.1    Lukas, R.J.2
  • 110
    • 0032584318 scopus 로고    scopus 로고
    • Topological disposition of Cys 222 in the alpha-subunit of nicotinic acetylcholine receptor analyzed by fluorescence-quenching and electron paramagnetic resonance measurements
    • J. Kim, and M.G. McNamee Topological disposition of Cys 222 in the alpha-subunit of nicotinic acetylcholine receptor analyzed by fluorescence-quenching and electron paramagnetic resonance measurements Biochemistry 37 1998 4680 4686
    • (1998) Biochemistry , vol.37 , pp. 4680-4686
    • Kim, J.1    McNamee, M.G.2
  • 111
    • 0026016879 scopus 로고
    • Intracellular transport and metabolism of sphingomyelin
    • M. Koval, and R.E. Pagano Intracellular transport and metabolism of sphingomyelin Biochim. Biophys. Acta 1082 1991 113 125
    • (1991) Biochim. Biophys. Acta , vol.1082 , pp. 113-125
    • Koval, M.1    Pagano, R.E.2
  • 112
    • 0029849201 scopus 로고    scopus 로고
    • Tryptophan substitutions at the lipid-exposed transmembrane segment M4 of Torpedo californica acetylcholine receptor govern channel gating
    • J.A. Lasalde-Dominicci, S. Tamamizu, D.H. Butler, R.T. Vibat, B. Hung, and M.G. McNamee Tryptophan substitutions at the lipid-exposed transmembrane segment M4 of Torpedo californica acetylcholine receptor govern channel gating Biochemistry 35 1996 14139 14148
    • (1996) Biochemistry , vol.35 , pp. 14139-14148
    • Lasalde-Dominicci, J.A.1    Tamamizu, S.2    Butler, D.H.3    Vibat, R.T.4    Hung, B.5    McNamee, M.G.6
  • 113
  • 114
    • 0033032332 scopus 로고    scopus 로고
    • Improved secondary structure predictions for a nicotinic receptor subunit: Incorporation of solvent accessibility and experimental data into a two-dimensional representation
    • N. Le Novère, P.J. Corringer, and J.P. Changeux Improved secondary structure predictions for a nicotinic receptor subunit: incorporation of solvent accessibility and experimental data into a two-dimensional representation Biophys. J. 76 1999 2329 2345
    • (1999) Biophys. J. , vol.76 , pp. 2329-2345
    • Le Novère, N.1    Corringer, P.J.2    Changeux, J.P.3
  • 115
    • 0025358006 scopus 로고
    • Functional role of the cysteine 451 thiol group in the M4 helix of the γ subunit of Torpedo californica acetylcholine receptor
    • L. Li, M. Schuchard, A. Palma, L. Pradier, and M.G. McNamee Functional role of the cysteine 451 thiol group in the M4 helix of the γ subunit of Torpedo californica acetylcholine receptor Biochemistry 29 1990 5428 5436
    • (1990) Biochemistry , vol.29 , pp. 5428-5436
    • Li, L.1    Schuchard, M.2    Palma, A.3    Pradier, L.4    McNamee, M.G.5
  • 116
    • 0026704565 scopus 로고
    • Site-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating
    • L. Li, Y.-H. Lee, P. Pappone, A. Palma, and M.G. McNamee Site-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating Biophys. J. 62 1992 61 63
    • (1992) Biophys. J. , vol.62 , pp. 61-63
    • Li, L.1    Lee, Y.-H.2    Pappone, P.3    Palma, A.4    McNamee, M.G.5
  • 118
    • 0018655548 scopus 로고
    • Biochemical properties of acteylcholine receptor subunits from Torpedo californica
    • J. Lindstrom, J. Merlie, and G. Yogeeswaran Biochemical properties of acteylcholine receptor subunits from Torpedo californica Biochemistry 18 1979 4465 4470
    • (1979) Biochemistry , vol.18 , pp. 4465-4470
    • Lindstrom, J.1    Merlie, J.2    Yogeeswaran, G.3
  • 119
    • 0019891907 scopus 로고
    • Fluorescence quenching in model membranes: 2. Determination of the local lipid environment of the calcium adenosinetriphosphatase from sarcoplasmic reticulum
    • E. London, and G.W. Feigenson Fluorescence quenching in model membranes: 2. Determination of the local lipid environment of the calcium adenosinetriphosphatase from sarcoplasmic reticulum Biochemistry 20 1981 1939 1948
    • (1981) Biochemistry , vol.20 , pp. 1939-1948
    • London, E.1    Feigenson, G.W.2
  • 121
    • 0043166978 scopus 로고    scopus 로고
    • Lipid-protein interactions and effect of local anesthetics in acetylcholine receptor-rich membranes from Torpedo marmorata electric organ
    • S.B. Mantipragada, L.I. Horvath, H.R. Arias, G. Schwarzmann, K. Sandhoff, F.J. Barrantes, and D. Marsh Lipid-protein interactions and effect of local anesthetics in acetylcholine receptor-rich membranes from Torpedo marmorata electric organ Biochemistry 42 2003 9167 9175
    • (2003) Biochemistry , vol.42 , pp. 9167-9175
    • Mantipragada, S.B.1    Horvath, L.I.2    Arias, H.R.3    Schwarzmann, G.4    Sandhoff, K.5    Barrantes, F.J.6    Marsh, D.7
  • 122
    • 0001145625 scopus 로고
    • ESR spin label studies of lipid-protein interactions
    • A. Watts J.J.H.H.M. De Pont Elsevier Amsterdam
    • D. Marsh ESR spin label studies of lipid-protein interactions A. Watts J.J.H.H.M. De Pont Progress in Protein-lipid Interactions 1985 Elsevier Amsterdam 143 172
    • (1985) Progress in Protein-lipid Interactions , pp. 143-172
    • Marsh, D.1
  • 123
    • 0018083022 scopus 로고
    • Immobilized lipid in acetylcholine receptor-rich membranes from Torpedo marmorata
    • D. Marsh, and F.J. Barrantes Immobilized lipid in acetylcholine receptor-rich membranes from Torpedo marmorata Proc. Natl. Acad. Sci. U. S. A. 75 1978 4329 4333
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 4329-4333
    • Marsh, D.1    Barrantes, F.J.2
  • 124
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • D. Marsh, and L.I. Horváth Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling Biochim. Biophys. Acta 1376 1998 267 296
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 267-296
    • Marsh, D.1    Horváth, L.I.2
  • 125
    • 0002316753 scopus 로고
    • Spin labeling and lipid-protein interactions in membranes
    • P. Jost O. Hayes John Wiley and Sons
    • D. Marsh, and A. Watts Spin labeling and lipid-protein interactions in membranes P. Jost O. Hayes Lipid-protein Interactions vol. 2 1982 John Wiley and Sons 53 126
    • (1982) Lipid-protein Interactions , vol.2 , pp. 53-126
    • Marsh, D.1    Watts, A.2
  • 126
    • 0019404213 scopus 로고
    • Phospholipid chain immobilization and steroid rotational immobilization in acetylcholine receptor-rich membranes from Torpedo marmorata
    • D. Marsh, A. Watts, and F.J. Barrantes Phospholipid chain immobilization and steroid rotational immobilization in acetylcholine receptor-rich membranes from Torpedo marmorata Biochim. Biophys. Acta 645 1981 97 101
    • (1981) Biochim. Biophys. Acta , vol.645 , pp. 97-101
    • Marsh, D.1    Watts, A.2    Barrantes, F.J.3
  • 127
    • 0024579187 scopus 로고
    • Conformational states of the nicotinic acetylcholine receptor from Torpedo californica induced by the binding of agonists, antagonists, and local anesthetics. Equilibrium measurements using tritium-hydrogen exchange
    • M.P. McCarthy, and R.M. Stroud Conformational states of the nicotinic acetylcholine receptor from Torpedo californica induced by the binding of agonists, antagonists, and local anesthetics. Equilibrium measurements using tritium-hydrogen exchange Biochemistry 28 1989 40 48
    • (1989) Biochemistry , vol.28 , pp. 40-48
    • McCarthy, M.P.1    Stroud, R.M.2
  • 128
    • 85021552613 scopus 로고
    • Lipid-protein interactions in membranes containing the acetylcholine receptor
    • M.G. McNamee, J.F. Ellena, and A.W. Dalziel Lipid-protein interactions in membranes containing the acetylcholine receptor Biophys. J. 37 1982 103 104
    • (1982) Biophys. J. , vol.37 , pp. 103-104
    • McNamee, M.G.1    Ellena, J.F.2    Dalziel, A.W.3
  • 129
    • 0028361585 scopus 로고
    • Secondary structure of the nicotinic acetylcholine receptor: Implications for structural models of a ligand-gated ion channel
    • N. Méthot, M.P. McCarthy, and J.E. Baenziger Secondary structure of the nicotinic acetylcholine receptor: implications for structural models of a ligand-gated ion channel Biochemistry 33 1994 7709 7717
    • (1994) Biochemistry , vol.33 , pp. 7709-7717
    • Méthot, N.1    McCarthy, M.P.2    Baenziger, J.E.3
  • 130
    • 0028825381 scopus 로고
    • Structure of both the ligand- and lipid-dependent channel-inactive states of the nicotinic acetylcholine receptor probed by FTIR spectroscopy and hydrogen exchange
    • N. Méthot, C.N. Demers, and J.E. Baenziger Structure of both the ligand- and lipid-dependent channel-inactive states of the nicotinic acetylcholine receptor probed by FTIR spectroscopy and hydrogen exchange Biochemistry 34 1995 15142 15149
    • (1995) Biochemistry , vol.34 , pp. 15142-15149
    • Méthot, N.1    Demers, C.N.2    Baenziger, J.E.3
  • 131
    • 0035968206 scopus 로고    scopus 로고
    • Structure of the pore-forming transmembrane domain of a ligand-gated ion channel
    • N. Méthot, B.D. Ritchie, M.P. Blanton, and J.E. Baenziger Structure of the pore-forming transmembrane domain of a ligand-gated ion channel J. Biol. Chem. 276 2001 23726 23732
    • (2001) J. Biol. Chem. , vol.276 , pp. 23726-23732
    • Méthot, N.1    Ritchie, B.D.2    Blanton, M.P.3    Baenziger, J.E.4
  • 132
    • 0023124272 scopus 로고
    • Identification of subunits of acetylcholine receptor that interact with a cholesterol photoaffinity probe
    • D.S. Middlemas, and M.A. Raftery Identification of subunits of acetylcholine receptor that interact with a cholesterol photoaffinity probe Biochemistry 26 1987 1219 1223
    • (1987) Biochemistry , vol.26 , pp. 1219-1223
    • Middlemas, D.S.1    Raftery, M.A.2
  • 133
    • 0023834873 scopus 로고
    • Secondary structural analyses of the nicotinic acetylcholine receptor as a test of molecular models
    • D.L. Mielke, and B.A. Wallace Secondary structural analyses of the nicotinic acetylcholine receptor as a test of molecular models J. Biol. Chem. 263 1988 3177 3182
    • (1988) J. Biol. Chem. , vol.263 , pp. 3177-3182
    • Mielke, D.L.1    Wallace, B.A.2
  • 134
    • 9644263556 scopus 로고
    • Effector-induced changes in the secondary structure of the nicotinic acetylcholine receptor
    • D.L. Mielke, R.-R. Kaldany, A. Karlin, and B.A. Wallace Effector-induced changes in the secondary structure of the nicotinic acetylcholine receptor Biophys. J. 45 1984 205a
    • (1984) Biophys. J. , vol.45
    • Mielke, D.L.1    Kaldany, R.-R.2    Karlin, A.3    Wallace, B.A.4
  • 135
    • 0026570085 scopus 로고
    • Potentiation of NMDA receptor currents by arachidonic acid
    • B. Miller, M. Sarantis, S.F. Traynelis, and D. Attwell Potentiation of NMDA receptor currents by arachidonic acid Nature 355 1992 722 725
    • (1992) Nature , vol.355 , pp. 722-725
    • Miller, B.1    Sarantis, M.2    Traynelis, S.F.3    Attwell, D.4
  • 136
    • 0024382038 scopus 로고
    • Three-dimensional structure of the nicotinic acetylcholine receptor and location of the major associated 43-kD cytoskeletal protein, determined at 22 Å by low dose electron microscopy and X-ray diffraction to 12.5 Å
    • A.K. Mitra, M.P. McCarthy, and R.M. Stroud Three-dimensional structure of the nicotinic acetylcholine receptor and location of the major associated 43-kD cytoskeletal protein, determined at 22 Å by low dose electron microscopy and X-ray diffraction to 12.5 Å J. Cell Biol. 109 1989 755 774
    • (1989) J. Cell Biol. , vol.109 , pp. 755-774
    • Mitra, A.K.1    McCarthy, M.P.2    Stroud, R.M.3
  • 137
    • 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 423 2003 949 955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 138
    • 0016239175 scopus 로고
    • On the conformation of the acetylcholine receptor protein from Torpedo nobiliana
    • W.M. Moore, L.A. Holladay, D. Puett, and R.N. Brady On the conformation of the acetylcholine receptor protein from Torpedo nobiliana FEBS Lett. 45 1974 145 149
    • (1974) FEBS Lett. , vol.45 , pp. 145-149
    • Moore, W.M.1    Holladay, L.A.2    Puett, D.3    Brady, R.N.4
  • 139
    • 0025731038 scopus 로고
    • Actions of n-alcohols on nicotinic acetylcholine receptor channels in cultured rat myotubes
    • R.D. Murrell, M.S. Braun, and D.A. Haydon Actions of n-alcohols on nicotinic acetylcholine receptor channels in cultured rat myotubes J. Physiol. 437 1991 431 448
    • (1991) J. Physiol. , vol.437 , pp. 431-448
    • Murrell, R.D.1    Braun, M.S.2    Haydon, D.A.3
  • 140
    • 84862477804 scopus 로고    scopus 로고
    • Tryptophan substitutions reveal role of nicotinic acetylcholine receptor α-TM3 domain in channel gating
    • M. Navedo, M. Nieves, L. Rojas, and J.A. Lasalde-Dominicci Tryptophan substitutions reveal role of nicotinic acetylcholine receptor α-TM3 domain in channel gating Biochemistry 2003
    • (2003) Biochemistry
    • Navedo, M.1    Nieves, M.2    Rojas, L.3    Lasalde-Dominicci, J.A.4
  • 142
    • 0030979047 scopus 로고    scopus 로고
    • Corticosterone modifies the murine muscle acetylcholine receptor channel kinetics
    • E. Nurowska, and F. Ruzzier Corticosterone modifies the murine muscle acetylcholine receptor channel kinetics NeuroReport 8 1996 77 80
    • (1996) NeuroReport , vol.8 , pp. 77-80
    • Nurowska, E.1    Ruzzier, F.2
  • 143
    • 0020665176 scopus 로고
    • Reconstitution of acetylcholine receptor function in lipid vesicles of defined composition
    • E.L. Ochoa, A.W. Dalziel, and M.G. McNamee Reconstitution of acetylcholine receptor function in lipid vesicles of defined composition Biochim. Biophys. Acta 727 1983 151 162
    • (1983) Biochim. Biophys. Acta , vol.727 , pp. 151-162
    • Ochoa, E.L.1    Dalziel, A.W.2    McNamee, M.G.3
  • 145
    • 0024411914 scopus 로고
    • Arachidonic acid and other fatty acids directly activate potassium channels in smooth muscle cells
    • R.W. Ordway, J.V. Walsh, and J.J. Singer Arachidonic acid and other fatty acids directly activate potassium channels in smooth muscle cells Science 244 1989 1176 1179
    • (1989) Science , vol.244 , pp. 1176-1179
    • Ordway, R.W.1    Walsh, J.V.2    Singer, J.J.3
  • 146
    • 0026016095 scopus 로고
    • Direct regulation of ion channels by fatty acids
    • R.W. Ordway, J.J. Singer, and J.V.J. Walsh Direct regulation of ion channels by fatty acids TINS 14 1991 96 100
    • (1991) TINS , vol.14 , pp. 96-100
    • Ordway, R.W.1    Singer, J.J.2    Walsh, J.V.J.3
  • 147
    • 0029936679 scopus 로고    scopus 로고
    • A mixed helix-beta-sheet model of the transmembrane region of the nicotinic acetylcholine receptor
    • M.O. Ortells, and G.G. Lunt A mixed helix-beta-sheet model of the transmembrane region of the nicotinic acetylcholine receptor Protein Eng. 9 1996 51 59
    • (1996) Protein Eng. , vol.9 , pp. 51-59
    • Ortells, M.O.1    Lunt, G.G.2
  • 150
    • 0030873046 scopus 로고    scopus 로고
    • Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing
    • S.I. Ortiz-Miranda, J.A. Lasalde-Dominicci, P.A. Pappone, and M.G. McNamee Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing J. Membr. Biol. 158 1997 17 30
    • (1997) J. Membr. Biol. , vol.158 , pp. 17-30
    • Ortiz-Miranda, S.I.1    Lasalde-Dominicci, J.A.2    Pappone, P.A.3    McNamee, M.G.4
  • 151
  • 152
    • 0035449919 scopus 로고    scopus 로고
    • The C terminus of the human nicotinic alpha4beta2 receptor forms a binding site required for potentiation by an estrogenic steroid
    • K. Paradiso, J. Zhang, and J.H. Steinbach The C terminus of the human nicotinic alpha4beta2 receptor forms a binding site required for potentiation by an estrogenic steroid J. Neurosci. 21 2001 6561 6568
    • (2001) J. Neurosci. , vol.21 , pp. 6561-6568
    • Paradiso, K.1    Zhang, J.2    Steinbach, J.H.3
  • 153
    • 0025295884 scopus 로고
    • Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence
    • T. Parasassi, G. De Stasio, A. d'Ubaldo, and E. Gratton Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence Biophys. J. 57 1990 1179 1186
    • (1990) Biophys. J. , vol.57 , pp. 1179-1186
    • Parasassi, T.1    De Stasio, G.2    D'Ubaldo, A.3    Gratton, E.4
  • 154
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • T. Parasassi, G. De Stasio, G. Ravagnan, R.M. Rusch, and E. Gratton Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence Biophys. J. 60 1991 179 189
    • (1991) Biophys. J. , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 155
    • 0032811126 scopus 로고    scopus 로고
    • Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit
    • V.S. Pashkov, I.V. Maslennikov, L.D. Tchikin, R.G. Efremov, V.T. Ivanov, and A.S. Arseniev Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit FEBS Lett. 457 1999 117 121
    • (1999) FEBS Lett. , vol.457 , pp. 117-121
    • Pashkov, V.S.1    Maslennikov, I.V.2    Tchikin, L.D.3    Efremov, R.G.4    Ivanov, V.T.5    Arseniev, A.S.6
  • 156
    • 0021740393 scopus 로고
    • Nicotinic receptor of acetylcholine: Structure of an oligomeric integral membrane protein
    • J.L. Popot, and J.-P. Changeux Nicotinic receptor of acetylcholine: structure of an oligomeric integral membrane protein Physiol. Rev. 64 1984 1162 1239
    • (1984) Physiol. Rev. , vol.64 , pp. 1162-1239
    • Popot, J.L.1    Changeux, J.-P.2
  • 157
    • 0018147538 scopus 로고
    • Interaction of the acetylcholine (nicotinic) receptor protein from Torpedo marmorata electric organ with monolayers of pure lipids
    • J.L. Popot, R.A. Demel, A. Sobel, L.L. van Deenen, and J.P. Changeux Interaction of the acetylcholine (nicotinic) receptor protein from Torpedo marmorata electric organ with monolayers of pure lipids Eur. J. Biochem. 85 1978 27 42
    • (1978) Eur. J. Biochem. , vol.85 , pp. 27-42
    • Popot, J.L.1    Demel, R.A.2    Sobel, A.3    Van Deenen, L.L.4    Changeux, J.P.5
  • 158
    • 0024964940 scopus 로고
    • Use of chemical modifications and site-directed mutagenesis to probe the functional role of thiol groups on the gamma subunit of Torpedo californica acetylcholine receptor
    • L. Pradier, A.S. Yee, and M.G. McNamee Use of chemical modifications and site-directed mutagenesis to probe the functional role of thiol groups on the gamma subunit of Torpedo californica acetylcholine receptor Biochemistry 28 1989 6562 6571
    • (1989) Biochemistry , vol.28 , pp. 6562-6571
    • Pradier, L.1    Yee, A.S.2    McNamee, M.G.3
  • 159
  • 160
    • 0030734157 scopus 로고    scopus 로고
    • The cholesterol dependence of activation and fast desensitization of the nicotinic acetylcholine receptor
    • S.E. Rankin, G.H. Addona, M.A. Kloczewiak, B. Bugge, and K.W. Miller The cholesterol dependence of activation and fast desensitization of the nicotinic acetylcholine receptor Biophys. J. 73 1997 2446 2455
    • (1997) Biophys. J. , vol.73 , pp. 2446-2455
    • Rankin, S.E.1    Addona, G.H.2    Kloczewiak, M.A.3    Bugge, B.4    Miller, K.W.5
  • 161
    • 0017826395 scopus 로고
    • Molecular weight in detergent solution of acetylcholine receptor from Torpedo californica
    • J.A. Reynolds, and A. Karlin Molecular weight in detergent solution of acetylcholine receptor from Torpedo californica Biochemistry 17 1978 2035 2038
    • (1978) Biochemistry , vol.17 , pp. 2035-2038
    • Reynolds, J.A.1    Karlin, A.2
  • 162
    • 0023200637 scopus 로고
    • Composition of lipids in elasmobranch electric organ and acetylcholine receptor membranes
    • N.P. Rotstein, H.R. Arias, F.J. Barrantes, and M.I. Aveldano Composition of lipids in elasmobranch electric organ and acetylcholine receptor membranes J. Neurochem. 49 1987 1333 1340
    • (1987) J. Neurochem. , vol.49 , pp. 1333-1340
    • Rotstein, N.P.1    Arias, H.R.2    Barrantes, F.J.3    Aveldano, M.I.4
  • 163
    • 0018788915 scopus 로고
    • Free fatty acids and esters can be immobilized by receptor rich membranes from Torpedo marmorata but not phospholipid acyl chains
    • A. Rousselet, P.F. Devaux, and K.W. Wirtz Free fatty acids and esters can be immobilized by receptor rich membranes from Torpedo marmorata but not phospholipid acyl chains Biochem. Biophys. Res. Commun. 90 1979 871 877
    • (1979) Biochem. Biophys. Res. Commun. , vol.90 , pp. 871-877
    • Rousselet, A.1    Devaux, P.F.2    Wirtz, K.W.3
  • 164
    • 0035824639 scopus 로고    scopus 로고
    • Probing the effects of membrane cholesterol in the Torpedo californica acetylcholine receptor and the novel lipid-exposed mutation aC418W in Xenopus oocytes
    • J. Santiago, G.R. Guzman, L.V. Rojas, R. Marti, G.A. Asmar-Rovira, L.F. Santana, M.G. McNamee, and J.A. Lasalde-Dominicci Probing the effects of membrane cholesterol in the Torpedo californica acetylcholine receptor and the novel lipid-exposed mutation aC418W in Xenopus oocytes J. Biol. Chem. 276 2001 46523 46532
    • (2001) J. Biol. Chem. , vol.276 , pp. 46523-46532
    • Santiago, J.1    Guzman, G.R.2    Rojas, L.V.3    Marti, R.4    Asmar-Rovira, G.A.5    Santana, L.F.6    McNamee, M.G.7    Lasalde-Dominicci, J.A.8
  • 165
    • 0027364559 scopus 로고
    • Phospholipid asymmetry in acetylcholine receptor clusters
    • M.G. Scher, and R.J. Bloch Phospholipid asymmetry in acetylcholine receptor clusters Exp. Cell Res. 208 1993 485 491
    • (1993) Exp. Cell Res. , vol.208 , pp. 485-491
    • Scher, M.G.1    Bloch, R.J.2
  • 166
    • 0017811657 scopus 로고
    • Membranes rich in acetylcholine receptor: Characterization and reconstitution to excitable membranes from exogenus lipids
    • W. Schiebler, and F. Hucho Membranes rich in acetylcholine receptor: characterization and reconstitution to excitable membranes from exogenus lipids Eur. J. Biochem. 85 1978 55 63
    • (1978) Eur. J. Biochem. , vol.85 , pp. 55-63
    • Schiebler, W.1    Hucho, F.2
  • 167
    • 0024272090 scopus 로고
    • Transbilayer effects of ethanol on fluidity of brain membrane leaflets
    • F. Schroeder, W.J. Morrison, C. Gorka, and W.G. Wood Transbilayer effects of ethanol on fluidity of brain membrane leaflets Biochim. Biophys. Acta 946 1988 85 94
    • (1988) Biochim. Biophys. Acta , vol.946 , pp. 85-94
    • Schroeder, F.1    Morrison, W.J.2    Gorka, C.3    Wood, W.G.4
  • 168
    • 0026688978 scopus 로고
    • Modulation of voltage-dependent Ca channel current by arachidonic acid and other long-chain fatty acids in rabbit intestinal smooth muscle
    • T. Shimada, and A.P. Somlyo Modulation of voltage-dependent Ca channel current by arachidonic acid and other long-chain fatty acids in rabbit intestinal smooth muscle J. Gen. Physiol. 100 1992 27 44
    • (1992) J. Gen. Physiol. , vol.100 , pp. 27-44
    • Shimada, T.1    Somlyo, A.P.2
  • 169
    • 0032491439 scopus 로고    scopus 로고
    • Membrane phospholipid control of nucleotide sensitivity of KATP channels
    • S.L. Shyng, and C.G. Nichols Membrane phospholipid control of nucleotide sensitivity of KATP channels Science 282 1998 1138 1141
    • (1998) Science , vol.282 , pp. 1138-1141
    • Shyng, S.L.1    Nichols, C.G.2
  • 171
    • 9244222121 scopus 로고
    • Function of mammalian nicotinic acetylcholine receptors: Agonist concentration dependence of single channel current kinetics
    • Academic Press
    • S.M. Sine, and J.H. Steinbach Function of mammalian nicotinic acetylcholine receptors: agonist concentration dependence of single channel current kinetics Current Topics in Membranes and Transport vol. 33 1988 Academic Press 133 145
    • (1988) Current Topics in Membranes and Transport , vol.33 , pp. 133-145
    • Sine, S.M.1    Steinbach, J.H.2
  • 172
    • 0025999108 scopus 로고
    • The neurosteroids pregnenolone and pregnenolone-sulfate but not progesterone, block Ca2+ currents in acutely isolated hippocampal CA1 neurons
    • K.T. Spence, C.R. Plata-Salaman, and J.M. Ffrench-Mullen The neurosteroids pregnenolone and pregnenolone-sulfate but not progesterone, block Ca2+ currents in acutely isolated hippocampal CA1 neurons Life Sci. 49 1991 L235 L239
    • (1991) Life Sci. , vol.49
    • Spence, K.T.1    Plata-Salaman, C.R.2    Ffrench-Mullen, J.M.3
  • 173
    • 0028345212 scopus 로고
    • Lipid modulation of nicotinic acetylcholine receptor function: The role of membrane lipid composition and fluidity
    • C. Sunshine, and M.G. McNamee Lipid modulation of nicotinic acetylcholine receptor function: The role of membrane lipid composition and fluidity Biochim. Biophys. Acta, Biomembr. 1191 1994 59 64
    • (1994) Biochim. Biophys. Acta, Biomembr. , vol.1191 , pp. 59-64
    • Sunshine, C.1    McNamee, M.G.2
  • 174
    • 0032772075 scopus 로고    scopus 로고
    • Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain
    • S. Tamamizu, Y. Lee, B. Hung, M.G. McNamee, and J.A. Lasalde-Dominicci Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain [published erratum appears in J Membr Biol 1999 Nov 1;172(1):89] J. Membr. Biol. 170 1999 157 164
    • (1999) J. Membr. Biol. , vol.170 , pp. 157-164
    • Tamamizu, S.1    Lee, Y.2    Hung, B.3    McNamee, M.G.4    Lasalde-Dominicci, J.A.5
  • 175
    • 0034712698 scopus 로고    scopus 로고
    • Functional effects of periodic tryptophan substitutions in the alpha M4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor
    • S. Tamamizu, G.R. Guzman, J. Santiago, L.V. Rojas, M.G. McNamee, and J.A. Lasalde-Dominicci Functional effects of periodic tryptophan substitutions in the alpha M4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor Biochemistry 39 2000 4666 4673
    • (2000) Biochemistry , vol.39 , pp. 4666-4673
    • Tamamizu, S.1    Guzman, G.R.2    Santiago, J.3    Rojas, L.V.4    McNamee, M.G.5    Lasalde-Dominicci, J.A.6
  • 177
    • 0025678678 scopus 로고
    • Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction
    • C. Toyoshima, and N. Unwin Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction J. Cell Biol. 111 1990 2623 2635
    • (1990) J. Cell Biol. , vol.111 , pp. 2623-2635
    • Toyoshima, C.1    Unwin, N.2
  • 178
    • 0027348041 scopus 로고
    • Neurotransmitter action: Opening of ligand-gated ion channels
    • N. Unwin Neurotransmitter action: opening of ligand-gated ion channels Cell 72 1993 31 41
    • (1993) Cell , vol.72 , pp. 31-41
    • Unwin, N.1
  • 179
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • N. Unwin Nicotinic acetylcholine receptor at 9 Å resolution J. Mol. Biol. 229 1993 1101 1124
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 180
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • N. Unwin Acetylcholine receptor channel imaged in the open state Nature 373 1995 37 43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 181
    • 0034731271 scopus 로고    scopus 로고
    • The Croonian Lecture 2000. Nicotinic acetylcholine receptor and the structural basis of fast synaptic transmission
    • N. Unwin The Croonian Lecture 2000. Nicotinic acetylcholine receptor and the structural basis of fast synaptic transmission Philos. Trans. R. Soc. Lond., B Biol. Sci. 355 2000 1813 1829
    • (2000) Philos. Trans. R. Soc. Lond., B Biol. Sci. , vol.355 , pp. 1813-1829
    • Unwin, N.1
  • 182
    • 0028268955 scopus 로고
    • Transverse distance between the membrane and the agonist binding sites on the Torpedo acetylcholine receptor: A fluorescence study
    • C.F. Valenzuela, P. Weign, J. Yguerabide, and D.A. Johnson Transverse distance between the membrane and the agonist binding sites on the Torpedo acetylcholine receptor: a fluorescence study Biophys. J. 66 1994 674 682
    • (1994) Biophys. J. , vol.66 , pp. 674-682
    • Valenzuela, C.F.1    Weign, P.2    Yguerabide, J.3    Johnson, D.A.4
  • 183
    • 0026738827 scopus 로고
    • Progesterone modulates a neuronal nicotinic acetylcholine receptor
    • S. Valera, M. Ballivet, and D. Bertrand Progesterone modulates a neuronal nicotinic acetylcholine receptor Proc. Natl. Acad. Sci. U. S. A. 89 1992 9949 9953
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 9949-9953
    • Valera, S.1    Ballivet, M.2    Bertrand, D.3
  • 184
    • 0020491932 scopus 로고
    • Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. A study using fluorescence recovery after photobleaching
    • W.L. Vaz, M. Criado, V.M.C. Madeira, G. Schoellmann, and T.M. Jovin Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. A study using fluorescence recovery after photobleaching Biochemistry 21 1982 5608 5612
    • (1982) Biochemistry , vol.21 , pp. 5608-5612
    • Vaz, W.L.1    Criado, M.2    Madeira, V.M.C.3    Schoellmann, G.4    Jovin, T.M.5
  • 185
    • 0029052360 scopus 로고
    • Arachidonic acid as a possible negative feedback inhibitor of nicotinic acetylcholine receptors on neurons
    • S. Vijayaraghavan, B. Huang, E.M. Blumental, and D.K. Berg Arachidonic acid as a possible negative feedback inhibitor of nicotinic acetylcholine receptors on neurons J. Neurosci. 15 1995 3679 3687
    • (1995) J. Neurosci. , vol.15 , pp. 3679-3687
    • Vijayaraghavan, S.1    Huang, B.2    Blumental, E.M.3    Berg, D.K.4
  • 186
    • 0024281190 scopus 로고
    • Phospholipase A2 hydrolysis of membrane phospholipids causes structural alteration of the nicotinic acetylcholine receptor
    • M.T. Villar, A. Artigues, J.A. Ferragut, and J.M. Gonzalez-Ros Phospholipase A2 hydrolysis of membrane phospholipids causes structural alteration of the nicotinic acetylcholine receptor Biochim. Biophys. Acta 938 1988 35 43
    • (1988) Biochim. Biophys. Acta , vol.938 , pp. 35-43
    • Villar, M.T.1    Artigues, A.2    Ferragut, J.A.3    Gonzalez-Ros, J.M.4
  • 188
    • 0017145336 scopus 로고
    • Stimulation of guanylate cyclase of fibroblasts by free fatty acids
    • D. Wallach, and I. Pastan Stimulation of guanylate cyclase of fibroblasts by free fatty acids J. Biol. Chem. 251 1976 5802 5809
    • (1976) J. Biol. Chem. , vol.251 , pp. 5802-5809
    • Wallach, D.1    Pastan, I.2
  • 189
    • 0030906795 scopus 로고    scopus 로고
    • Mutation in the M1 domain of the acetylcholine receptor α subunit decreases the rate of agonist dissociation
    • H.-L. Wang, A. Auerbach, N. Bren, K. Ohno, A.G. Engel, and S.M. Sine Mutation in the M1 domain of the acetylcholine receptor α subunit decreases the rate of agonist dissociation J. Gen. Physiol. 109 1997 757 766
    • (1997) J. Gen. Physiol. , vol.109 , pp. 757-766
    • Wang, H.-L.1    Auerbach, A.2    Bren, N.3    Ohno, K.4    Engel, A.G.5    Sine, S.M.6
  • 192
    • 0024434701 scopus 로고
    • Arachidonic acid induces a long term activity-dependent enhancement of synaptic transmission in the hippocampus
    • J.H. Williams, M.L. Errington, M.A. Lynch, and T.V.P. Bliss Arachidonic acid induces a long term activity-dependent enhancement of synaptic transmission in the hippocampus Nature 341 1989 739 742
    • (1989) Nature , vol.341 , pp. 739-742
    • Williams, J.H.1    Errington, M.L.2    Lynch, M.A.3    Bliss, T.V.P.4
  • 193
    • 0000166649 scopus 로고    scopus 로고
    • Structural characterization of the M4 transmembrane domain of the acetylcholine receptor: An NMR study
    • P.F. Williamson, B. Bonev, and F.J. Barrantes Structural characterization of the M4 transmembrane domain of the acetylcholine receptor: an NMR study Biophys. J. 147A 2000 (New Orleans)
    • (2000) Biophys. J. , vol.147
    • Williamson, P.F.1    Bonev, B.2    Barrantes, F.J.3
  • 194
    • 0025333463 scopus 로고
    • Conformation of acetylcholine receptor in the presence of agonists and antagonists
    • C.-S.C. Wu, X.H. Sun, and J.T. Yang Conformation of acetylcholine receptor in the presence of agonists and antagonists J. Protein Chem. 9 1990 119 126
    • (1990) J. Protein Chem. , vol.9 , pp. 119-126
    • Wu, C.-S.C.1    Sun, X.H.2    Yang, J.T.3
  • 195
    • 84916319138 scopus 로고
    • The secondary structure of acetylcholine receptor reconstituted in a single lipid component as determined by Raman spectroscopy
    • P. Yager, E.L. Chang, R.W. Williams, and A.W. Dalziel The secondary structure of acetylcholine receptor reconstituted in a single lipid component as determined by Raman spectroscopy Biophys. J. 45 1984 26 28
    • (1984) Biophys. J. , vol.45 , pp. 26-28
    • Yager, P.1    Chang, E.L.2    Williams, R.W.3    Dalziel, A.W.4
  • 196
    • 0029968851 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment
    • L.P. Zanello, E. Aztiria, S. Antollini, and F.J. Barrantes Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment Biophys. J. 70 1996 2155 2164
    • (1996) Biophys. J. , vol.70 , pp. 2155-2164
    • Zanello, L.P.1    Aztiria, E.2    Antollini, S.3    Barrantes, F.J.4
  • 197
    • 0019947925 scopus 로고
    • Direct structural localization of two toxin-recognition sites on an ACh receptor protein
    • H.P. Zingsheim, F.J. Barrantes, J. Frank, W. Hanicke, and D.C. Neugebauer Direct structural localization of two toxin-recognition sites on an ACh receptor protein Nature 299 1982 81 84
    • (1982) Nature , vol.299 , pp. 81-84
    • Zingsheim, H.P.1    Barrantes, F.J.2    Frank, J.3    Hanicke, W.4    Neugebauer, D.C.5
  • 198
    • 0020339121 scopus 로고
    • Dimeric arrangement and structure of the membrane-bound acetylcholine receptor studied by electron microscopy
    • H.P. Zingsheim, D.C. Neugebauer, J. Frank, W. Hanicke, and F.J. Barrantes Dimeric arrangement and structure of the membrane-bound acetylcholine receptor studied by electron microscopy EMBO J. 1 1982 541 547
    • (1982) EMBO J. , vol.1 , pp. 541-547
    • Zingsheim, H.P.1    Neugebauer, D.C.2    Frank, J.3    Hanicke, W.4    Barrantes, F.J.5


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