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Volumn 19, Issue 4, 2002, Pages 277-284

Lipid matters: Nicotinic acetylcholine receptor-lipid interactions (review)

Author keywords

Cholinergic receptor; Fluorescence; Ion channels; Lipid protein interactions; Membrane

Indexed keywords

ION CHANNEL; LIPID; NICOTINIC RECEPTOR;

EID: 0036821982     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/09687680210166226     Document Type: Review
Times cited : (49)

References (59)
  • 1
    • 0019135697 scopus 로고
    • Inhibition of ion permeability control properties of acetylcholine receptor from Torpedo californica by long-chain fatty acids
    • Andreasen, T.J. and McNamee, M.G., 1980, Inhibition of ion permeability control properties of acetylcholine receptor from Torpedo californica by long-chain fatty acids. Biochemistry, 19, 4719-4726.
    • (1980) Biochemistry , vol.19 , pp. 4719-4726
    • Andreasen, T.J.1    McNamee, M.G.2
  • 3
    • 0032564372 scopus 로고    scopus 로고
    • Disclosure of discrete sites for different lipids at the protein-lipid interface in native acetylcholine receptor-rich membrane
    • Antollini, S.S. and Barrantes, F.J., 1998, Disclosure of discrete sites for different lipids at the protein-lipid interface in native acetylcholine receptor-rich membrane. Biochemistry, 37, 16653-16662.
    • (1998) Biochemistry , vol.37 , pp. 16653-16662
    • Antollini, S.S.1    Barrantes, F.J.2
  • 4
    • 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
    • Antollini, S.S., Soto, M.A., Bonini de Romanelli, I., Gutierrez-Merino, C., Sotomayor, P. and Barrantes, F.J., 1996, Physical state of bulk and protein-associated lipid in nicotinic acetylcholine receptor-rich membrane studied by Laurdan generalized polarization and fluorescence energy transfer. Biophysics Journal, 70, 1275-1284.
    • (1996) Biophysics Journal , vol.70 , pp. 1275-1284
    • Antollini, S.S.1    Soto, M.A.2    Bonini de Romanelli, I.3    Gutierrez-Merino, C.4    Sotomayor, P.5    Barrantes, F.J.6
  • 5
    • 0028800463 scopus 로고    scopus 로고
    • Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of α-helical peptide hydrogens in the nicotinic acetylcholine receptor
    • Baenziger, J. E. and Méthot, N., 1996, Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of α-helical peptide hydrogens in the nicotinic acetylcholine receptor. Journal of Biological Chemistry, 270, 29129-29137.
    • (1996) Journal of Biological Chemistry , vol.270 , pp. 29129-29137
    • Baenziger, J.E.1    Méthot, N.2
  • 7
    • 0001193946 scopus 로고    scopus 로고
    • Fluorescence studies of the acetylcholine receptor: Structure and dynamics in the membrane environment
    • Barrantes, F. J., 2001, Fluorescence studies of the acetylcholine receptor: Structure and dynamics in the membrane environment. Journal of Fluorescence, 11, 273-285.
    • (2001) Journal of Fluorescence , vol.11 , pp. 273-285
    • Barrantes, F.J.1
  • 10
    • 0026654217 scopus 로고
    • Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor
    • Blanton, M.P. and Cohen, J.B., 1992, Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor. Biochemistry, 31, 3738-3750.
    • (1992) Biochemistry , vol.31 , pp. 3738-3750
    • Blanton, M.P.1    Cohen, J.B.2
  • 11
    • 0028326435 scopus 로고
    • Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: Secondary structure implications
    • Blanton, M.P. and Cohen. J.B., 1994, Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: secondary structure implications. Biochemistry, 33, 2859-2872.
    • (1994) Biochemistry , vol.33 , pp. 2859-2872
    • Blanton, M.P.1    Cohen, J.B.2
  • 12
    • 0025850892 scopus 로고
    • Localization of regions of the Torpedo californica nicotinic acetylcholine receptor labeled with an aryl azide derivative of phosphatidylserine
    • Blanton, M.P. and Wang, H.H., 1991, Localization of regions of the Torpedo californica nicotinic acetylcholine receptor labeled with an aryl azide derivative of phosphatidylserine. Biochimica et Biophysica Acta, 1067, 1-8.
    • (1991) Biochimica et Biophysica Acta , vol.1067 , pp. 1-8
    • Blanton, M.P.1    Wang, H.H.2
  • 14
    • 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
    • Blanton, M.P., Xie, Y., Dangott, L.J. and Cohen, J.B., 1999, The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface. Molecular Pharmacology, 55, 269-278.
    • (1999) Molecular Pharmacology , vol.55 , pp. 269-278
    • Blanton, M.P.1    Xie, Y.2    Dangott, L.J.3    Cohen, J.B.4
  • 15
    • 0024548732 scopus 로고
    • An unusual β-spectrin associated with clustered acetylcholine receptors
    • Bloch, R.J. and Morrow, J.S., 1989, An unusual β-spectrin associated with clustered acetylcholine receptors. Journal of Cell Biology, 108, 481-494.
    • (1989) Journal of Cell Biology , vol.108 , pp. 481-494
    • Bloch, R.J.1    Morrow, J.S.2
  • 16
    • 0027141153 scopus 로고
    • Effects of long-chain fatty acids on the channel activity of the nicotinic acetylcholine receptor
    • Bouzat, C.B. and Barrantes, F.J., 1993a, Effects of long-chain fatty acids on the channel activity of the nicotinic acetylcholine receptor. Receptors and Channels, 1, 251-258.
    • (1993) Receptors and Channels , vol.1 , pp. 251-258
    • Bouzat, C.B.1    Barrantes, F.J.2
  • 17
    • 0027339530 scopus 로고
    • Hydrocortisone and 11-desoxycortisone modify acetylcholine receptor channel gating
    • Bouzat, C.B. and Barrantes, F.J., 1993b, Hydrocortisone and 11-desoxycortisone modify acetylcholine receptor channel gating. NeuroReport, 4, 143-146.
    • (1993) NeuroReport , vol.4 , pp. 143-146
    • Bouzat, C.B.1    Barrantes, F.J.2
  • 18
    • 0027296434 scopus 로고
    • Acute exposure of nicotinic acetylcholine receptor to the synthetic glucocorticoid dexamethasone alters single-channel gating properties
    • Bouzat, C.B. and Barrantes, F.J., 1993c, Acute exposure of nicotinic acetylcholine receptor to the synthetic glucocorticoid dexamethasone alters single-channel gating properties. Molecular Neuropharmacy, 3, 109-116.
    • (1993) Molecular Neuropharmacy , vol.3 , pp. 109-116
    • Bouzat, C.B.1    Barrantes, F.J.2
  • 19
    • 0029995665 scopus 로고    scopus 로고
    • Modulation of muscle nicotinic acetylcholine receptors by the glucocorticoid hydrocortisone. Possible allosteric mechanism of channel blockade
    • Bouzat, C.B. and Barrantes, F.J., 1996, Modulation of muscle nicotinic acetylcholine receptors by the glucocorticoid hydrocortisone. Possible allosteric mechanism of channel blockade. Journal of Biological Chemistry, 271, 25835-25841.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 25835-25841
    • Bouzat, C.B.1    Barrantes, F.J.2
  • 20
    • 0026068852 scopus 로고
    • The effects of short-chain phospholipids on the acetylcholine-activated ion channel
    • Braun, M.S. and Haydon, D.A., 1991, The effects of short-chain phospholipids on the acetylcholine-activated ion channel. Pflugers Archives, 418, 62-67.
    • (1991) Pflugers Archives , vol.418 , pp. 62-67
    • Braun, M.S.1    Haydon, D.A.2
  • 21
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc, K., van Dijk, W.J., Klaassen, R.V., Schuurmans, M., van der Oost, J., Smit, A.B. and Sixma, T.K., 2001, Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature, 411, 269-276.
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    Van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    Van der Oost, J.5    Smit, A.B.6    Sixma, T.K.7
  • 22
    • 0032215090 scopus 로고    scopus 로고
    • Allosteric receptors after 30 years
    • Changeux, J.-P. and Edelstein, S.J., 1998, Allosteric receptors after 30 years. Neuron, 21, 959-980.
    • (1998) Neuron , vol.21 , pp. 959-980
    • Changeux, J.-P.1    Edelstein, S.J.2
  • 23
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay, A. and London, E., 1987, Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry, 26, 39-45.
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 24
    • 0026513830 scopus 로고
    • Expression of fusion proteins of the nicotinic acetylcholine receptor from mammalian muscle identifies the membrane-spanning regions in the α and δ subunits
    • Chavez, R.A. and Hall, Z.W., 1992, Expression of fusion proteins of the nicotinic acetylcholine receptor from mammalian muscle identifies the membrane-spanning regions in the α and δ subunits. Journal of Cell Biology, 116, 385-393.
    • (1992) Journal of Cell Biology , vol.116 , pp. 385-393
    • Chavez, R.A.1    Hall, Z.W.2
  • 25
    • 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
    • Corbin, J., Méthot, N., Wang, H.H., Baenziger, J.E. and Blanton, M.P., 1998a, Secondary structure analysis of individual transmembrane segments of the nicotinic acetylcholine receptor by circular dichroism and fourier transform infrared spectroscopy. Journal of Biological Chemistry, 273, 771-777.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 771-777
    • Corbin, J.1    Méthot, N.2    Wang, H.H.3    Baenziger, J.E.4    Blanton, M.P.5
  • 27
    • 0020376564 scopus 로고
    • Effects of lipids on acetylcholine receptor. Essential need of cholesterol for the maintenance of agonist-induced state transitions in lipid vesicles
    • Criado, M., Eibl, H. and Barrantes, F.J., 1982, Effects of lipids on acetylcholine receptor. Essential need of cholesterol for the maintenance of agonist-induced state transitions in lipid vesicles. Biochemistry, 21, 3622-3629.
    • (1982) Biochemistry , vol.21 , pp. 3622-3629
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 28
    • 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 receptormediated ion translocation
    • Criado, M., Eibl, H. and Barrantes, F.J., 1984, 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 receptormediated ion translocation. Journal of Biological Chemistry, 259, 9188-9198.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 9188-9198
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 30
    • 0021110283 scopus 로고
    • Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor
    • Ellena, J.F., Blazing, M.A. and McNamee. M.G., 1983, Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor. Biochemistry, 22, 5523-5535.
    • (1983) Biochemistry , vol.22 , pp. 5523-5535
    • Ellena, J.F.1    Blazing, M.A.2    McNamee, M.G.3
  • 31
    • 0018120101 scopus 로고
    • Reconstitution of carbamylcholinedependent sodium ion flux and desensitization of the acetylcholine receptor from Torpedo californica
    • Epstein, M. and Racker, E., 1978, Reconstitution of carbamylcholinedependent sodium ion flux and desensitization of the acetylcholine receptor from Torpedo californica. Journal of Biological Chemistry, 253, 6660-6662.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 6660-6662
    • Epstein, M.1    Racker, E.2
  • 32
    • 0023193779 scopus 로고
    • Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes
    • Fong, T.M. and McNamee, M.G., 1987, Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes. Biochemistry, 26, 3871-3880.
    • (1987) Biochemistry , vol.26 , pp. 3871-3880
    • Fong, T.M.1    McNamee, M.G.2
  • 33
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Förster, Th., 1948, Intermolecular energy migration and fluorescence. Annals of Physics (Leipzig), 2, 55-75.
    • (1948) Annals of Physics (Leipzig) , vol.2 , pp. 55-75
    • Förster, Th.1
  • 34
    • 0035847596 scopus 로고    scopus 로고
    • Steroids differentially inhibit the nicotinic acetylcholine receptor
    • Garbus, I., Bouzat, C. and Barrantes, F.J., 2001, Steroids differentially inhibit the nicotinic acetylcholine receptor. Neuro-Report, 12, 227-231.
    • (2001) Neuro-Report , vol.12 , pp. 227-231
    • Garbus, I.1    Bouzat, C.2    Barrantes, F.J.3
  • 35
    • 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
    • Garbus, I., Roccamo, A.M. and Barrantes, F. J., 2002, Identification of threonine 422 in transmembrane domain αM4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone. Neuropharmacology, 43, 65-73.
    • (2002) Neuropharmacology , vol.43 , pp. 65-73
    • Garbus, I.1    Roccamo, A.M.2    Barrantes, F.J.3
  • 36
    • 0021881226 scopus 로고
    • Transmembrane topology of acetylcholine receptor subunits probed with photoreactive phospholipids
    • Giraudat, J., Montecucco, C., Brisson, R. and Changeux, J.-P. 1985, Transmembrane topology of acetylcholine receptor subunits probed with photoreactive phospholipids. Biochemistry, 24, 3121-3127.
    • (1985) Biochemistry , vol.24 , pp. 3121-3127
    • Giraudat, J.1    Montecucco, C.2    Brisson, R.3    Changeux, J.-P.4
  • 37
    • 0024278441 scopus 로고
    • Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor
    • Jones, O.T. and McNamee, M.G., 1988, Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor. Biochemistry, 27, 2364-2374.
    • (1988) Biochemistry , vol.27 , pp. 2364-2374
    • Jones, O.T.1    McNamee, M.G.2
  • 38
    • 0023941416 scopus 로고
    • A minimum number of lipids are required to support the functional properties of the nicotinic acetylcholine receptor
    • Jones, O.T., Eubanks, J.H., Earnest, J.P. and McNamee, M.G., 1988, A minimum number of lipids are required to support the functional properties of the nicotinic acetylcholine receptor. Biochemistry, 27, 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
  • 39
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • Karlin, A., 2002, Emerging structure of the nicotinic acetylcholine receptors. Nature Reviews in Neuroscience, 3, 102-114.
    • (2002) Nature Reviews in Neuroscience , vol.3 , pp. 102-114
    • Karlin, A.1
  • 40
    • 0018655548 scopus 로고
    • Biochemical properties of acteylcholine receptor subunits from Torpedo californica
    • Lindstrom, J., Merlie, J. P. and Yogeeswaram, G., 1979, Biochemical properties of acteylcholine receptor subunits from Torpedo californica. Biochemistry, 18, 4465-4470.
    • (1979) Biochemistry , vol.18 , pp. 4465-4470
    • Lindstrom, J.1    Merlie, J.P.2    Yogeeswaram, G.3
  • 43
    • 0019404213 scopus 로고
    • Phospholipid chain immobilization and steroid rotational immobilization in acetylcholine receptor-rich membranes from Torpedo marmorata
    • Marsh, D., Watts, A. and Barrantes, F.J., 1981, Phospholipid chain immobilization and steroid rotational immobilization in acetylcholine receptor-rich membranes from Torpedo marmorata. Biochimica et Biophysica Acta, 645, 97-101.
    • (1981) Biochimica et Biophysica Acta , vol.645 , pp. 97-101
    • Marsh, D.1    Watts, A.2    Barrantes, F.J.3
  • 44
    • 0027441795 scopus 로고
    • Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 2. Membrane fluidity and ligand-mediated alteration in the accessibility of gamma subunit cysteine residues to cholesterol
    • Narayanaswami, V. and McNamee, M.G., 1993, Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 2. Membrane fluidity and ligand-mediated alteration in the accessibility of gamma subunit cysteine residues to cholesterol. Biochemistry, 32, 12420-12427.
    • (1993) Biochemistry , vol.32 , pp. 12420-12427
    • Narayanaswami, V.1    McNamee, M.G.2
  • 46
    • 0020665176 scopus 로고
    • Reconstitution of acetylcholine receptor function in lipid vesicles of defined composition
    • Ochoa, E.L., Dalziel, A.W. and McNamee, M.G., 1983, Reconstitution of acetylcholine receptor function in lipid vesicles of defined composition. Biochimica et Biophysica Acta, 727, 151-162.
    • (1983) Biochimica et Biophysica Acta , vol.727 , pp. 151-162
    • Ochoa, E.L.1    Dalziel, A.W.2    McNamee, M.G.3
  • 48
    • 0029936679 scopus 로고    scopus 로고
    • A mixed helix-β-sheet model for the transmembrane region of the nicotinic acetylcholine receptor
    • Ortells, M.O. and Lunt, G.G., 1996, A mixed helix-β-sheet model for the transmembrane region of the nicotinic acetylcholine receptor. Protein Engineering., 9, 51-59.
    • (1996) Protein Engineering , vol.9 , pp. 51-59
    • Ortells, M.O.1    Lunt, G.G.2
  • 49
    • 0002640943 scopus 로고    scopus 로고
    • Molecular modelling of the nicotinic acetylcholine receptor
    • F.J. Barrantes, ed. (Berlin/Heidelberg: Springer Verlag and Georgetown: Landes Publishing Co.)
    • Ortells, M.O., Barrantes, G.E. and Barrantes, F.J., 1998, Molecular modelling of the nicotinic acetylcholine receptor. In The nicotinic acetylcholine receptor: Current views and future trends, F.J. Barrantes, ed. (Berlin/Heidelberg: Springer Verlag and Georgetown: Landes Publishing Co.), pp. 85-108.
    • (1998) The Nicotinic Acetylcholine Receptor: Current Views and Future Trends , pp. 85-108
    • Ortells, M.O.1    Barrantes, G.E.2    Barrantes, F.J.3
  • 50
    • 0030912140 scopus 로고    scopus 로고
    • Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state
    • Ortells, M.O., Barrantes, G.E., Wood, C., Lunt, G.G. and Barrantes, F.J., 1997, Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state. Protein Engineering, 10, 511-517.
    • (1997) Protein Engineering , vol.10 , pp. 511-517
    • Ortells, M.O.1    Barrantes, G.E.2    Wood, C.3    Lunt, G.G.4    Barrantes, F.J.5
  • 51
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • Parasassi, T., De Stasio, G., Ravagnan, G., Rusch, R.M. and Gratton,E., 1991, Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence. Biophysics Journal, 60, 179-189.
    • (1991) Biophysics Journal , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 52
    • 0032811126 scopus 로고    scopus 로고
    • Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit
    • Pashkov, V.S., Maslenikov, I.V., Tchikin, L.D., Efremov, R.G., Ivanov, V.T. and Arseniev, A.S., 1999, Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit. FEBS Letters, 457, 117-121.
    • (1999) FEBS Letters , vol.457 , pp. 117-121
    • Pashkov, V.S.1    Maslenikov, I.V.2    Tchikin, L.D.3    Efremov, R.G.4    Ivanov, V.T.5    Arseniev, A.S.6
  • 53
    • 0019311334 scopus 로고
    • Acetylcholine receptor: Complex of homologous subunits
    • Raftery, M. A., Hunkapiller, M. W., Strader, C. D. and Hood, L. E. 1980, Acetylcholine receptor: complex of homologous subunits. Science, 208, 1454-1457.
    • (1980) Science , vol.208 , pp. 1454-1457
    • Raftery, M.A.1    Hunkapiller, M.W.2    Strader, C.D.3    Hood, L.E.4
  • 54
    • 0018788915 scopus 로고
    • Free fatty acids and esters can be immobilized by receptor rich membranes from Torpedo marmorata but not phospholipid acyl chains
    • Rousselet, A., Devaux, P.F. and Wirtz, K.W., 1979, Free fatty acids and esters can be immobilized by receptor rich membranes from Torpedo marmorata but not phospholipid acyl chains. Biochemical and Biophysical Research Communications, 90, 871-877.
    • (1979) Biochemical and Biophysical Research Communications , vol.90 , pp. 871-877
    • Rousselet, A.1    Devaux, P.F.2    Wirtz, K.W.3
  • 55
    • 0028345212 scopus 로고
    • Lipid modulation of nicotinic acetylcholine receptor function: The role of membrane lipid composition and fluidity
    • Sunshine, C. and McNamee, M.G., 1994, Lipid modulation of nicotinic acetylcholine receptor function: the role of membrane lipid composition and fluidity. Biochimica et Biophysica Acta, 1191, 59-64.
    • (1994) Biochimica et Biophysica Acta , vol.1191 , pp. 59-64
    • Sunshine, C.1    McNamee, M.G.2
  • 57
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N., 1995, Acetylcholine receptor channel imaged in the open state. Nature, 373, 37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 58
    • 0000166649 scopus 로고    scopus 로고
    • Structural characterization of the M4 transmembrane domain of the acetylcholine receptor: An NMR study
    • Williamson, P.F., Bonev, B., Barrantes, F.J. and Watts, A., 2000, Structural characterization of the M4 transmembrane domain of the acetylcholine receptor: an NMR study. Biophysics Journal, 78, 147A.
    • (2000) Biophysics Journal , vol.78
    • Williamson, P.F.1    Bonev, B.2    Barrantes, F.J.3    Watts, A.4
  • 59
    • 0029968851 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment
    • Zanello, L.P., Aztiria, E., Antollini, S.S. and Barrantes, F.J., 1996, Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment. Biophysical Journal, 70, 2155-2164.
    • (1996) Biophysical Journal , vol.70 , pp. 2155-2164
    • Zanello, L.P.1    Aztiria, E.2    Antollini, S.S.3    Barrantes, F.J.4


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