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Volumn 158, Issue 1, 1997, Pages 17-30

Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing

Author keywords

Burst analysis; Ion channel gating; Single channel electrophysiology; Site directed mutagenesis; Torpedo californica

Indexed keywords

ION CHANNEL; NICOTINIC RECEPTOR;

EID: 0030873046     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900240     Document Type: Article
Times cited : (47)

References (67)
  • 1
    • 0025856536 scopus 로고
    • Neuronal nicotinic acelylcholine receptors expressed in Xenopus oocytes have a pentameric quarternary structure
    • Anand, R., Conroy, W.G., Schoepfer, R., Whiting, P., Lindstrom, J. 1991. Neuronal nicotinic acelylcholine receptors expressed in Xenopus oocytes have a pentameric quarternary structure. J. Biol. Chem. 266:11192-11198
    • (1991) J. Biol. Chem. , vol.266 , pp. 11192-11198
    • Anand, R.1    Conroy, W.G.2    Schoepfer, R.3    Whiting, P.4    Lindstrom, J.5
  • 2
    • 0019954907 scopus 로고
    • Incorporation of acetylcholine receptors into liposomes. Vesicle structure and acetylcholine receptor function
    • Anholt R., Fredkin, D.R., Deerink, T., Ellisman, M., Montal, M., Lindstrom, J. 1982. Incorporation of acetylcholine receptors into liposomes. Vesicle structure and acetylcholine receptor function. J. Biol. Chem. 257:7122-7134
    • (1982) J. Biol. Chem. , vol.257 , pp. 7122-7134
    • Anholt, R.1    Fredkin, D.R.2    Deerink, T.3    Ellisman, M.4    Montal, M.5    Lindstrom, J.6
  • 3
    • 0027410307 scopus 로고
    • A Statistical analysis of acetylcholine receptor activation in Xenopus myocytes: Stepwise versus concerted models of gating
    • Auerbach, A. 1993. A Statistical analysis of acetylcholine receptor activation in Xenopus myocytes: Stepwise versus concerted models of gating. J. Physiol. 461:339-378
    • (1993) J. Physiol. , vol.461 , pp. 339-378
    • Auerbach, A.1
  • 4
    • 0022558275 scopus 로고
    • Heterogeneous kinetic properties of acetylcholine receptor channels in Xenopus myocytes
    • Auerbach, A., Lingle, C.J. 1986. Heterogeneous kinetic properties of acetylcholine receptor channels in Xenopus myocytes. J. Physiol. 378:119-140
    • (1986) J. Physiol. , vol.378 , pp. 119-140
    • Auerbach, A.1    Lingle, C.J.2
  • 5
    • 0026654217 scopus 로고
    • Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor
    • Blanton M.P., 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
  • 6
    • 0028326435 scopus 로고
    • Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: Secondary structure implications
    • Blanton M.P., 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
  • 8
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia, C. 1975. Structural invariants in protein folding. Nature 254:304-308
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 9
    • 0022838313 scopus 로고
    • Labeling of functional sensitive sulfhydryl-containing domains of acetylcholine receptor from Torpedo californica membranes
    • Clarke, J.H., Martinez-Carrion, M. 1986. Labeling of functional sensitive sulfhydryl-containing domains of acetylcholine receptor from Torpedo californica membranes. J. Biol. Chem. 261:10063-10072
    • (1986) J. Biol. Chem. , vol.261 , pp. 10063-10072
    • Clarke, J.H.1    Martinez-Carrion, M.2
  • 10
    • 0016246242 scopus 로고
    • Effects of local anesthetics and calcium on the interaction of cholinergic ligands with the nicotinic receptor protein from Torpedo marmorata
    • Cohen, J.B., Weber, M., Changeux, J.-P. 1974. Effects of local anesthetics and calcium on the interaction of cholinergic ligands with the nicotinic receptor protein from Torpedo marmorata. Mol. Pharmacol. 10:904-932
    • (1974) Mol. Pharmacol. , vol.10 , pp. 904-932
    • Cohen, J.B.1    Weber, M.2    Changeux, J.-P.3
  • 11
    • 0019522622 scopus 로고
    • On the stochastic properties of single ion channels
    • Colquhoun, D., Hawkes, A.G. 1981. On the stochastic properties of single ion channels. Proc. R. Soc. Land. B. 211:205-235
    • (1981) Proc. R. Soc. Land. B. , vol.211 , pp. 205-235
    • Colquhoun, D.1    Hawkes, A.G.2
  • 12
    • 0023856335 scopus 로고
    • Activation of ion channels in the frog endplate by high concentrations of acetylcholine
    • Colquhoun, D., Ogden, D.C. 1988. Activation of ion channels in the frog endplate by high concentrations of acetylcholine. J Physiol. 395:131-159
    • (1988) J Physiol. , vol.395 , pp. 131-159
    • Colquhoun, D.1    Ogden, D.C.2
  • 13
    • 0019856889 scopus 로고
    • Fluctuations in the microsecond time range of the current through single acetylcholine receptor ion channels
    • Colquhoun, D., Sakmann, B. 1981. Fluctuations in the microsecond time range of the current through single acetylcholine receptor ion channels. Nature 294:464-466
    • (1981) Nature , vol.294 , pp. 464-466
    • Colquhoun, D.1    Sakmann, B.2
  • 14
    • 0001908198 scopus 로고
    • Fitting and statistical analysis of single-channel records
    • B. Sakmann, and E. Neher, editors. Plenum Press, New York
    • Colquhoun, D., Sigworth, F.J. 1983. Fitting and statistical analysis of single-channel records. In: Single-Channel Recording. Second edition. B. Sakmann, and E. Neher, editors. pp. 254-257. Plenum Press, New York
    • (1983) Single-Channel Recording. Second Edition , pp. 254-257
    • Colquhoun, D.1    Sigworth, F.J.2
  • 15
    • 0025828670 scopus 로고
    • Pentameric structure and subunit stoichiometry of a neuronal nicotinic acetylcholine receptor
    • Cooper, E., Couturier, S., Ballivet, M. 1991. Pentameric structure and subunit stoichiometry of a neuronal nicotinic acetylcholine receptor. Nature. 350:235-238
    • (1991) Nature , vol.350 , pp. 235-238
    • Cooper, E.1    Couturier, S.2    Ballivet, M.3
  • 16
    • 8544236239 scopus 로고
    • Physical forces that determine the properties of properties
    • W.H. Freeman, New York
    • Creighton, T.E. 1983. Physical forces that determine the properties of properties. In: Proteins; Structure and Molecular Properties. pp. 133-157. W.H. Freeman, New York
    • (1983) Proteins; Structure and Molecular Properties , pp. 133-157
    • Creighton, T.E.1
  • 17
    • 0020478350 scopus 로고
    • Effects of lipids on acetylcholine receptor. Essential need of cholesterol for maintenance of agonist-induced state transitions in lipid vesicles
    • Criado, M., Eibl, H., Barrantes, F.J. 1982. Effects of lipids on acetylcholine receptor. Essential need of cholesterol for maintenance of agonist-induced state transitions in lipid vesicles. Biochemistry. 21:5750-5755
    • (1982) Biochemistry , vol.21 , pp. 5750-5755
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 18
    • 0000631357 scopus 로고
    • Complete mRNA coding sequence of the acetylcholine binding a-subunit of Torpedo marmorata acetylcholine receptor: A model for transmembrane organization of the polypeptide chain
    • Devillers-Thiery, A., Giraudat, J., Bentaboulet, M., Changeux, J.-P. 1983. Complete mRNA coding sequence of the acetylcholine binding a-subunit of Torpedo marmorata acetylcholine receptor: a model for transmembrane organization of the polypeptide chain. Proc. Natt. Acad. Sci. USA. 80:2067-2071
    • (1983) Proc. Natt. Acad. Sci. USA , vol.80 , pp. 2067-2071
    • Devillers-Thiery, A.1    Giraudat, J.2    Bentaboulet, M.3    Changeux, J.-P.4
  • 19
    • 0026028283 scopus 로고
    • The temperature dependence of some kinetic and conductance properties of acetylcholine receptor channels
    • Dilger, J.P., Brett, R.S., Poppers, D.M., Liu, Y. 1991. The temperature dependence of some kinetic and conductance properties of acetylcholine receptor channels. Biochim. et Biophys. Acta 1063:253-258
    • (1991) Biochim. et Biophys. Acta , vol.1063 , pp. 253-258
    • Dilger, J.P.1    Brett, R.S.2    Poppers, D.M.3    Liu, Y.4
  • 20
    • 0022979927 scopus 로고
    • Binding of local anesthetics to reconstituted acetylcholine receptors: Effect of protein surface potential
    • Earnest, J.P., Limbacher, Jr., H.P., McNamee, M.G., Wang, H.H. 1986. Binding of local anesthetics to reconstituted acetylcholine receptors: effect of protein surface potential. Biochemistry. 25:5809-5818
    • (1986) Biochemistry , vol.25 , pp. 5809-5818
    • Earnest, J.P.1    Limbacher Jr., H.P.2    McNamee, M.G.3    Wang, H.H.4
  • 21
    • 0021221779 scopus 로고
    • Multiple binding sites for local anesthetics on reconstituted acetylcholine receptor membranes
    • Earnest, J.P., Wang, H.H., McNamee, M.G. 1984. Multiple binding sites for local anesthetics on reconstituted acetylcholine receptor membranes. Biochem. Biophys. Res. Commun. 123:862-868
    • (1984) Biochem. Biophys. Res. Commun. , vol.123 , pp. 862-868
    • Earnest, J.P.1    Wang, H.H.2    McNamee, M.G.3
  • 22
    • 0029123899 scopus 로고
    • The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating
    • Filatov, G.N., White, M.M. 1995. The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating. Molec. Pharmacol. 48:379-384
    • (1995) Molec. Pharmacol. , vol.48 , pp. 379-384
    • Filatov, G.N.1    White, M.M.2
  • 23
    • 0022552318 scopus 로고
    • Correlation between acetylcholine receptor function and structural properties of membranes
    • Fong, T.M., McNamee, M.G. 1986. Correlation between acetylcholine receptor function and structural properties of membranes. Biochemistry. 25:830-840
    • (1986) Biochemistry , vol.25 , pp. 830-840
    • Fong, T.M.1    McNamee, M.G.2
  • 24
    • 0023193779 scopus 로고
    • Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes
    • Fong, T.M., 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
  • 25
    • 0025884565 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: From electric organ to brain
    • Galzi, J.-L., Revah, F., Bessis, A., Changeux, J.-P. 1991. Functional architecture of the nicotinic acetylcholine receptor: from electric organ to brain. Annu. Rev. Pharmacol. 31:37-72
    • (1991) Annu. Rev. Pharmacol. , vol.31 , pp. 37-72
    • Galzi, J.-L.1    Revah, F.2    Bessis, A.3    Changeux, J.-P.4
  • 27
    • 0021881226 scopus 로고
    • Transmembrane topology of acetylcholine receptor subunits probed with photoreactive phospholipids
    • Giraudat, J., Montecucco, C., Bisson, R., 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    Bisson, R.3    Changeux, J.-P.4
  • 28
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O.P., Marty, A., Neher, E., Sakmann, B., Sigworth, F.J. 1981. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pfluegers Arch. 391:85-100
    • (1981) Pfluegers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 29
    • 0020621092 scopus 로고
    • Multiple sites of action for noncompetitive blockers on acetylcholine receptor rich membrane fragments from Torpedo marmorata
    • Heidmann, T., Oswald, R.E., Changeux, J.-P. 1983. Multiple sites of action for noncompetitive blockers on acetylcholine receptor rich membrane fragments from Torpedo marmorata. Biochemistry. 22:3112-3127
    • (1983) Biochemistry , vol.22 , pp. 3112-3127
    • Heidmann, T.1    Oswald, R.E.2    Changeux, J.-P.3
  • 30
    • 0024328738 scopus 로고
    • Distance between the agonist and noncompetitive inhibitor sites on the nicotinic acetylcholine receptor
    • Hertz, J.M., Johnson, D.A., Taylor, P. 1989. Distance between the agonist and noncompetitive inhibitor sites on the nicotinic acetylcholine receptor. J. Biol. Chem. 264:12439-12448
    • (1989) J. Biol. Chem. , vol.264 , pp. 12439-12448
    • Hertz, J.M.1    Johnson, D.A.2    Taylor, P.3
  • 31
    • 0000210446 scopus 로고
    • Elementary properties of ions in solution
    • Sinauer Associates, Sunderland, MA
    • Hille, B. 1992. Elementary properties of ions in solution. In Ionic Channels of Excitable Membranes. Second edition. pp. 259-290. Sinauer Associates, Sunderland, MA
    • (1992) Ionic Channels of Excitable Membranes. Second Edition , pp. 259-290
    • Hille, B.1
  • 32
    • 0002447044 scopus 로고
    • Recombination and mutagenesis of DNA sequence using PCR
    • M.J. McPherson, editor. IRL Press, New York
    • Horton, R.M., Pease, L.R. 1991. Recombination and mutagenesis of DNA sequence using PCR. In: Directed Mutagenesis. M.J. McPherson, editor. pp. 217-246. IRL Press, New York
    • (1991) Directed Mutagenesis , pp. 217-246
    • Horton, R.M.1    Pease, L.R.2
  • 33
    • 0022458822 scopus 로고
    • The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices MII of the receptor subunits
    • Hucho, F., Oherthur, W., Lottspeich, F. 1986. The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices MII of the receptor subunits. FEBS Lett. 205:137-142
    • (1986) FEBS Lett. , vol.205 , pp. 137-142
    • Hucho, F.1    Oherthur, W.2    Lottspeich, F.3
  • 34
    • 0020491047 scopus 로고
    • Properties of proteoliposomes reconstituted with acetylcholine receptor from Torpedo californica
    • Huganir, R.L., Racker, E. 1982. Properties of proteoliposomes reconstituted with acetylcholine receptor from Torpedo californica. J. Biol. Chem. 257:9372-9378
    • (1982) J. Biol. Chem. , vol.257 , pp. 9372-9378
    • Huganir, R.L.1    Racker, E.2
  • 37
    • 0021132711 scopus 로고
    • Identification of a subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site
    • Kao, P.N., Dwork, A.J., Kaldany, R.J., Silver, M.L., Wideman, J., Stein, S., Karlin, A. 1984. Identification of a subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site. J. Biol. Chem. 259:11662-11665
    • (1984) J. Biol. Chem. , vol.259 , pp. 11662-11665
    • Kao, P.N.1    Dwork, A.J.2    Kaldany, R.J.3    Silver, M.L.4    Wideman, J.5    Stein, S.6    Karlin, A.7
  • 38
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of the nicotinic acetylcholine receptors and their cousins
    • Karlin, A., Akabas, M.H. 1995. Toward a structural basis for the function of the nicotinic acetylcholine receptors and their cousins. Neuron. 15:1231-1244
    • (1995) Neuron. , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 39
    • 0029163027 scopus 로고
    • Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors
    • Labarca, C., Nowak, M.W., Zhang, H., Tang, L., Deshpande, P., Lester, H.A. 1995. Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors. Nature. 376:514-516
    • (1995) Nature , vol.376 , pp. 514-516
    • Labarca, C.1    Nowak, M.W.2    Zhang, H.3    Tang, L.4    Deshpande, P.5    Lester, H.A.6
  • 40
    • 0028989869 scopus 로고
    • Heterogeneous distributions of acetylcholine receptors in chick myocytes induced by cholesterol enrichment
    • Lasalde, J.A., Colom, A., Resto, E., Zuazaga, C. 1995. Heterogeneous distributions of acetylcholine receptors in chick myocytes induced by cholesterol enrichment. Biochim. Biophys. Acta 1235:361-368
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 361-368
    • Lasalde, J.A.1    Colom, A.2    Resto, E.3    Zuazaga, C.4
  • 41
    • 0029849201 scopus 로고    scopus 로고
    • Tryptophan substitutions at the lipid exposed transmembrane segment M4 of the Torpedo AChR governs channel gating
    • In press
    • Lasalde, J.A., Tamamizu, S., Butler, D.H., Vibat, C.R.T., McNamee, M.G. 1996. Tryptophan substitutions at the lipid exposed transmembrane segment M4 of the Torpedo AChR governs channel gating. In press, Biochemistry
    • (1996) Biochemistry
    • Lasalde, J.A.1    Tamamizu, S.2    Butler, D.H.3    Vibat, C.R.T.4    McNamee, M.G.5
  • 42
    • 0028219505 scopus 로고
    • Mutations in the M4 domain of Torpedo californica acetylcholine receptor dramatically alter ion channel function
    • Lee Y-H., Li, L., Lasalde, J., Rojas, L., McNamee, M.G., OrtizMiranda, S.I., Pappone, P. 1994. Mutations in the M4 domain of Torpedo californica acetylcholine receptor dramatically alter ion channel function. Biophys. J. 66:646-653
    • (1994) Biophys. J. , vol.66 , pp. 646-653
    • Lee, Y.-H.1    Li, L.2    Lasalde, J.3    Rojas, L.4    McNamee, M.G.5    Ortizmiranda, S.I.6    Pappone, P.7
  • 43
    • 0027536977 scopus 로고
    • Allosteric modulations of the nicotinic acetylcholine receptor
    • Lena, C., Changeux, J.-P. 1993. Allosteric modulations of the nicotinic acetylcholine receptor. Trends in Neurosc. 5:181-186
    • (1993) Trends in Neurosc. , vol.5 , pp. 181-186
    • Lena, C.1    Changeux, J.-P.2
  • 44
    • 0026704565 scopus 로고
    • Site-specific mutations of the nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating
    • Li, L., Lee, Y.-H., Pappone, P., Palma, A., McNamee, M.G. 1992. Site-specific mutations of the nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating. Biophys. J. 62:61-63
    • (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
  • 45
    • 0025358006 scopus 로고
    • Functional Role of the cysteine 451 thiol group in the M4 helix of the γ-subunit of Torpedo californica acetylcholine receptor
    • Li, L., Schuchard, M., Palma, A., Pradier, L., McNamee, M.G. 1990. Functional Role of the cysteine 451 thiol group in the M4 helix of the γ-subunit of Torpedo californica acetylcholine receptor. Biochemistry. 29:5428-5436
    • (1990) Biochemistry , vol.29 , pp. 5428-5436
    • Li, L.1    Schuchard, M.2    Palma, A.3    Pradier, L.4    McNamee, M.G.5
  • 46
    • 0026027519 scopus 로고
    • Role of a key cysteine residue in the gating of the acetylcholine receptor
    • Lo, D.C., Pinkham, J.L., Stevens, C.F. 1991. Role of a key cysteine residue in the gating of the acetylcholine receptor. Neuron 6:31-40
    • (1991) Neuron , vol.6 , pp. 31-40
    • Lo, D.C.1    Pinkham, J.L.2    Stevens, C.F.3
  • 47
    • 0019937045 scopus 로고
    • Reconstitution of acetylcholine receptor function in model membranes
    • McNamee, M.G., Ochoa, E.L.M. 1982. Reconstitution of acetylcholine receptor function in model membranes. Neurosc. 7:2305-2319
    • (1982) Neurosc. , vol.7 , pp. 2305-2319
    • McNamee, M.G.1    Ochoa, E.L.M.2
  • 48
    • 0022911410 scopus 로고
    • Patch clamp measurements on Xenopus laevis oocytes: Currents through endogenous channels and implanted acetylcholine receptors and sodium channels
    • Methfessel, C., Witzemann, V., Takahashi, T., Mishina, M., Numa, S., Sakmann, B. 1986. Patch clamp measurements on Xenopus laevis oocytes: currents through endogenous channels and implanted acetylcholine receptors and sodium channels. Pfluegers Arch. 407:577-588
    • (1986) Pfluegers Arch. , vol.407 , pp. 577-588
    • Methfessel, C.1    Witzemann, V.2    Takahashi, T.3    Mishina, M.4    Numa, S.5    Sakmann, B.6
  • 49
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod, J., Changeux, J.-P., Jacob, F. 1963. Allosteric proteins and cellular control systems. J. Mol. Biol. 6:306-329
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.-P.2    Jacob, F.3
  • 50
  • 52
    • 0024319944 scopus 로고
    • Desensitization of the nicotinic acetylcholine receptor: Molecular mechanisms and effect of modulators
    • Ochoa, E.L.M., Chattopadhyay, A., McNamee, M.G. 1989. Desensitization of the nicotinic acetylcholine receptor: Molecular mechanisms and effect of modulators. Cellular and Molec. Neurobiol. 9:141-178
    • (1989) Cellular and Molec. Neurobiol. , vol.9 , pp. 141-178
    • Ochoa, E.L.M.1    Chattopadhyay, A.2    McNamee, M.G.3
  • 53
    • 0021934164 scopus 로고
    • Ion channel block by acetylcholine, carbachol and suberyldicholine at the frog neuromuscular junction
    • Ogden, D.C., Colquhoun, D. 1985. Ion channel block by acetylcholine, carbachol and suberyldicholine at the frog neuromuscular junction. Proc. R. Soc London B. 225:329-355
    • (1985) Proc. R. Soc London B. , vol.225 , pp. 329-355
    • Ogden, D.C.1    Colquhoun, D.2
  • 54
    • 0020560273 scopus 로고
    • 3H]phencyclidine binding to acetylcholine receptor rich membrane fragments from Torpedo marmorata
    • 3H]phencyclidine binding to acetylcholine receptor rich membrane fragments from Torpedo marmorata. Biochemistry 22:3128-3136
    • (1983) Biochemistry , vol.22 , pp. 3128-3136
    • Oswald, R.E.1    Heidmann, T.2    Changeux, J.-P.3
  • 55
    • 0009611964 scopus 로고
    • The nicotinic acetylcholine receptor
    • P. Yeagle, editor. Telford, Caldwell, New Jersey
    • Pradier, L., McNamee, M.G. 1992. The nicotinic acetylcholine receptor. In: The Structure of Biological Membranes. P. Yeagle, editor. pp. 1047-1106. Telford, Caldwell, New Jersey
    • (1992) The Structure of Biological Membranes , pp. 1047-1106
    • Pradier, L.1    McNamee, M.G.2
  • 56
    • 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
    • Pradier, L., Yee, A.S., McNamee, M.G. 1989. 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 28:6562-6571
    • (1989) Biochemistry , vol.28 , pp. 6562-6571
    • Pradier, L.1    Yee, A.S.2    McNamee, M.G.3
  • 57
    • 0020998370 scopus 로고
    • Single channel electrophysiology: Use of the patch clamp
    • Sachs, F., Auerbach, A. 1983. Single channel electrophysiology: use of the patch clamp. Methods in Enzymology 103:147-176
    • (1983) Methods in Enzymology , vol.103 , pp. 147-176
    • Sachs, F.1    Auerbach, A.2
  • 58
    • 0020346538 scopus 로고
    • The automated analysis of data from single ionic channels
    • Sachs, F., Neil, J., Barkakati, N. 1982. The automated analysis of data from single ionic channels. Pfluegers Arch. 395:331-340
    • (1982) Pfluegers Arch. , vol.395 , pp. 331-340
    • Sachs, F.1    Neil, J.2    Barkakati, N.3
  • 59
    • 0019215162 scopus 로고
    • Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist
    • Sakmann, B., Patlak, J., Neher, E. 1980. Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist. Nature 286:71-73
    • (1980) Nature , vol.286 , pp. 71-73
    • Sakmann, B.1    Patlak, J.2    Neher, E.3
  • 60
    • 0025123090 scopus 로고
    • Activation of Torpedo acelylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities
    • Sine, S.M., Claudio, T., Sigworth, F.J. 1990. Activation of Torpedo acelylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities. J. Gen. Physiol. 96:395-437
    • (1990) J. Gen. Physiol. , vol.96 , pp. 395-437
    • Sine, S.M.1    Claudio, T.2    Sigworth, F.J.3
  • 61
    • 0021150988 scopus 로고
    • Agonists block currents through acetylcholine receptor channels
    • Sine, S.M., Steinbach, J.H. 1984. Agonists block currents through acetylcholine receptor channels. Biophys. J. 46:277-284
    • (1984) Biophys. J. , vol.46 , pp. 277-284
    • Sine, S.M.1    Steinbach, J.H.2
  • 62
    • 0026631606 scopus 로고
    • Lipid modulation of acetylcholine receptor function: The role of neutral and negatively charged lipids
    • Sunshine, C., McNamee, M.G. 1992. Lipid modulation of acetylcholine receptor function: the role of neutral and negatively charged lipids. Biochim. et Biophys. Acta 1108:240-246
    • (1992) Biochim. et Biophys. Acta , vol.1108 , pp. 240-246
    • Sunshine, C.1    McNamee, M.G.2
  • 63
    • 0028345212 scopus 로고
    • Lipid modulation of nicotinic acetylcholine receptor function: The role of membrane lipid composition and fluidity
    • Sunshine, C., McNamee, M.G. 1994. Lipid modulation of nicotinic acetylcholine receptor function: The role of membrane lipid composition and fluidity. Biochim. Biophys. Acta 1191:59-64
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 59-64
    • Sunshine, C.1    McNamee, M.G.2
  • 64
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin, N. 1993. Nicotinic acetylcholine receptor at 9 Å resolution. J. Molecular Biol. 229:1101-1124
    • (1993) J. Molecular Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 65
    • 0021238290 scopus 로고
    • Effects of thiol-group modifications of Torpedo californica acetylcholine receptor on ion flux activation and inactivation kinetics
    • Walker, J.W., Richardson, C.A., McNamee, M.G. 1984. Effects of thiol-group modifications of Torpedo californica acetylcholine receptor on ion flux activation and inactivation kinetics. Biochemistry 23:2329-2338
    • (1984) Biochemistry , vol.23 , pp. 2329-2338
    • Walker, J.W.1    Richardson, C.A.2    McNamee, M.G.3
  • 66
    • 0022456566 scopus 로고
    • Thiol-group modification of Torpedo californica acetylcholine receptor: Subunit localization and effects on function
    • Yee, A.S., Corley, D.E., McNamee, M.G. 1986. Thiol-group modification of Torpedo californica acetylcholine receptor: subunit localization and effects on function. Biochemistry 25:2110-2119
    • (1986) Biochemistry , vol.25 , pp. 2110-2119
    • Yee, A.S.1    Corley, D.E.2    McNamee, M.G.3
  • 67
    • 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., Barrantes, F.J. 1996. Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment. Biophys. J. 70:2155-2164
    • (1996) Biophys. J. , vol.70 , pp. 2155-2164
    • Zanello, L.P.1    Aztiria, E.2    Antollini, S.3    Barrantes, F.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.