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Volumn 320, Issue 12, 1997, Pages 953-961

Myasthenic nicotinic receptor mutant interpreted in terms of the allosteric model

Author keywords

Allosteric model; Myasthenic channel mutant; Nicotinic acetylcholine receptor; Single channel open times

Indexed keywords

MUTANT PROTEIN; NICOTINIC RECEPTOR;

EID: 0031456294     PISSN: 07644469     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0764-4469(97)82468-7     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0027467469 scopus 로고
    • Neurotransmitter action: Opening of the ligandgated ion channels
    • Unwin N. 1993. Neurotransmitter action: opening of the ligandgated ion channels. Neuron 10, 31-41
    • (1993) Neuron , vol.10 , pp. 31-41
    • Unwin, N.1
  • 2
    • 0028031541 scopus 로고
    • Neurotransmitter-gated ion channels as unconventional allosteric proteins
    • Galzi J.-L., Changeux J.-P. 1994. Neurotransmitter-gated ion channels as unconventional allosteric proteins. Curr. Opin. Struct Biol. 4, 554-565
    • (1994) Curr. Opin. Struct Biol. , vol.4 , pp. 554-565
    • Galzi, J.-L.1    Changeux, J.-P.2
  • 3
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors
    • Karlin A., Akabas M.H. 1995. Toward a structural basis for the function of nicotinic acetylcholine receptors. Neuron 15, 1231-1244
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 4
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J., Wyman J., Changeux J.-P. 1965. On the nature of allosteric transitions: A plausible model. J. Mol. Biol. 12, 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 5
    • 0030281174 scopus 로고    scopus 로고
    • A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions
    • Edelstein S.J., Schaad O., Henry E., Bertrand D., Changeux J.-P. 1996. A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions. Biol. Cybern. 75, 361-380
    • (1996) Biol. Cybern. , vol.75 , pp. 361-380
    • Edelstein, S.J.1    Schaad, O.2    Henry, E.3    Bertrand, D.4    Changeux, J.-P.5
  • 6
    • 0030481333 scopus 로고    scopus 로고
    • Allosteric proteins after thirty years: The binding and state functions of the neuronal 7 nicotinic acetylcholine receptor
    • Edelstein S.J., Changeux J.-P. 1996. Allosteric proteins after thirty years: the binding and state functions of the neuronal (7 nicotinic acetylcholine receptor. Experientia 52, 1083-1090
    • (1996) Experientia , vol.52 , pp. 1083-1090
    • Edelstein, S.J.1    Changeux, J.-P.2
  • 7
    • 0010518490 scopus 로고
    • Spontaneous openings of the acetylcholine receptor channel
    • Jackson M.B. 1984. Spontaneous openings of the acetylcholine receptor channel. Proc. Natl. Acad. Sci. USA 81, 3901-3904
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3901-3904
    • Jackson, M.B.1
  • 8
    • 0025173684 scopus 로고
    • Spontaneous and agonist-induced openings of an acetylcholine receptor channel composed of bovine α, β-and δsubunits
    • Jackson M.B., Imoto K., Mishina M., Konno T., Numa S.,Sakmann B. 1990. Spontaneous and agonist-induced openings of an acetylcholine receptor channel composed of bovine α, β-and δsubunits. Pflügers Arch. Eur. J. Physiol. 417, 129-135
    • (1990) Pflügers Arch. Eur. J. Physiol. , vol.417 , pp. 129-135
    • Jackson, M.B.1    Imoto, K.2    Mishina, M.3    Konno, T.4    Numa, S.5    Sakmann, B.6
  • 9
    • 0029934560 scopus 로고    scopus 로고
    • Voltage dependence of mouse acetylcholine receptor gating: Different charge movements in di-, mono-, and unliganded receptors
    • Auerbach A., Sigurdson W., Chen J., Akk G. 1996. Voltage dependence of mouse acetylcholine receptor gating: different charge movements in di-, mono-, and unliganded receptors. J. Physiol. 494, 155-179
    • (1996) J. Physiol. , vol.494 , pp. 155-179
    • Auerbach, A.1    Sigurdson, W.2    Chen, J.3    Akk, G.4
  • 10
    • 70449143838 scopus 로고
    • Interaction at endplate receptors between different choline derivatives
    • Del Castillo J., Katz B. 1957. Interaction at endplate receptors between different choline derivatives. J. Physiol. 146, 369-381
    • (1957) J. Physiol. , vol.146 , pp. 369-381
    • Del Castillo, J.1    Katz, B.2
  • 11
    • 0022272338 scopus 로고
    • Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate
    • Colquhoun D., Sakmann B. 1985. Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate. J. Physiol. 369, 501-557
    • (1985) J. Physiol. , vol.369 , pp. 501-557
    • Colquhoun, D.1    Sakmann, B.2
  • 12
    • 0026536073 scopus 로고
    • Activation of skeletal muscle nicotinic acetylcholine receptors
    • Lingle C.J., Maconochie D.,Steinbach J.H. 1992. Activation of skeletal muscle nicotinic acetylcholine receptors. J. Membrane Biol. 126. 195-217
    • (1992) J. Membrane Biol. , vol.126 , pp. 195-217
    • Lingle, C.J.1    Maconochie, D.2    Steinbach, J.H.3
  • 13
    • 0028902550 scopus 로고
    • Mechanisms of activation of muscle nicotinic acetylcholine receptors and the time course of endplate currents
    • Edmonds B., Gibb A.J., Colquhoun D. 1995. Mechanisms of activation of muscle nicotinic acetylcholine receptors and the time course of endplate currents. Annu. Rev. Physiol. 57, 469-493
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 469-493
    • Edmonds, B.1    Gibb, A.J.2    Colquhoun, D.3
  • 14
    • 0030906795 scopus 로고    scopus 로고
    • Mutation in the M l domain of the acetylcholine receptor alpha subunit decreases the rate of agonist dissociation
    • Wang H.-L., Auerbach A., Bren N., Ohno K., Engel A.G., Sine S.M. 1997. Mutation in the M l domain of the acetylcholine receptor alpha subunit decreases the rate of agonist dissociation. J. Gen. Physiol. 109, 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
  • 15
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D.E., Némethy G., Filmer D. 1966. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365-385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Némethy, G.2    Filmer, D.3
  • 16
    • 0023875658 scopus 로고
    • Dependence of acetylcholine receptor channel kinetics on agonist concentration in cultured mouse muscle fibers
    • Jackson M.B. 1988. Dependence of acetylcholine receptor channel kinetics on agonist concentration in cultured mouse muscle fibers. J. Physiol. 397, 555-583
    • (1988) J. Physiol. , vol.397 , pp. 555-583
    • Jackson, M.B.1
  • 17
    • 0025123090 scopus 로고
    • Activation of Torpedo acetylcholine 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 acetylcholine 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
  • 18
    • 0029041254 scopus 로고
    • Activation of recombinant mouse acetylcholine receptors by acetylcholine, carbamylcholine and tetramethylammonium
    • Zhang Y., Chen J., Auerbach A. 1995. Activation of recombinant mouse acetylcholine receptors by acetylcholine, carbamylcholine and tetramethylammonium. J. Physiol. 486, 189-206
    • (1995) J. Physiol. , vol.486 , pp. 189-206
    • Zhang, Y.1    Chen, J.2    Auerbach, A.3
  • 19
    • 0029087136 scopus 로고
    • Mutation of the acetylcholine receptor a subunit causes a slow-channel myasthenie syndrome by enhancing agonist binding affinity
    • Sine S.M., Ohno K., Bouzat C., Auerbach A., Milone M., Pruitt J.N., Engel A.G. 1995. Mutation of the acetylcholine receptor a subunit causes a slow-channel myasthenie syndrome by enhancing agonist binding affinity. Neuron 15, 229-239
    • (1995) Neuron , vol.15 , pp. 229-239
    • Sine, S.M.1    Ohno, K.2    Bouzat, C.3    Auerbach, A.4    Milone, M.5    Pruitt, J.N.6    Engel, A.G.7
  • 20
    • 15844429136 scopus 로고    scopus 로고
    • Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine e subunit
    • Ohno K., Wang H.-L., Milone M., Bren N., Brengman J.M., Nakano S., Quiram P., Pruitt J.N., Sine S.M., Engel A.G. 1996. Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine e subunit. Neuron 17, 157-170
    • (1996) Neuron , vol.17 , pp. 157-170
    • Ohno, K.1    Wang, H.-L.2    Milone, M.3    Bren, N.4    Brengman, J.M.5    Nakano, S.6    Quiram, P.7    Pruitt, J.N.8    Sine, S.M.9    Engel, A.G.10
  • 21
    • 0030757151 scopus 로고    scopus 로고
    • Slow-channel myasthenic syndrome caused by enhanced activation, desensitization, and agonist binding affinity attributable to mutation in the M2 domain of the acetylcholine receptor a subunit
    • Milone M., Wang H.-L, Ohno K., Fukudome T., Pruitt J.N., Bren N., Sine S.M., Engel A.G. 1997. Slow-channel myasthenic syndrome caused by enhanced activation, desensitization, and agonist binding affinity attributable to mutation in the M2 domain of the acetylcholine receptor a subunit. J. Neurosci, 17, 5651-5665
    • (1997) J. Neurosci , vol.17 , pp. 5651-5665
    • Milone, M.1    Wang, H.-L.2    Ohno, K.3    Fukudome, T.4    Pruitt, J.N.5    Bren, N.6    Sine, S.M.7    Engel, A.G.8
  • 22
    • 0028821376 scopus 로고
    • Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the e subunit
    • Ohno K., Hutchison D.O., Milone M., Brengman J.M., Bouzat C., Sine S.M., Engel A.G. 1995. Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the e subunit. Proc. Natl. Acad. Sci. USA 92, 758-762
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 758-762
    • Ohno, K.1    Hutchison, D.O.2    Milone, M.3    Brengman, J.M.4    Bouzat, C.5    Sine, S.M.6    Engel, A.G.7
  • 25
    • 0030987817 scopus 로고    scopus 로고
    • Mutations in different functional domains of the human muscle acetylcholine receptor alpha subunit in patients with the slow-channel congenital myasthenic syndrome
    • Croxen R., Newland C., Beeson D., Oosterhuis H., Chauplannaz G., Vincent A., Newsom-Davis J. 1997. Mutations in different functional domains of the human muscle acetylcholine receptor alpha subunit in patients with the slow-channel congenital myasthenic syndrome. Hum. Mol. Gen. 6. 767-774
    • (1997) Hum. Mol. Gen. , vol.6 , pp. 767-774
    • Croxen, R.1    Newland, C.2    Beeson, D.3    Oosterhuis, H.4    Chauplannaz, G.5    Vincent, A.6    Newsom-Davis, J.7
  • 26
    • 8244225989 scopus 로고    scopus 로고
    • Congenital myasthenic syndromes due to heteroallelic nonsense/missense mutations in the acetylcholine receptor epsilon subunit gene: Identification and functional characterization of six new mutations
    • Ohno K., Quiram P., Milone M., Wang H.-L., Harper M.C., Pruitt II J.N., Brengman J.M., Pao L., Fischbeck K.H., Crawford T.O., Sine S.M., Engel A.G. 1997. Congenital myasthenic syndromes due to heteroallelic nonsense/missense mutations in the acetylcholine receptor epsilon subunit gene: identification and functional characterization of six new mutations. Hum. Mol. Gen. 6, 753-767
    • (1997) Hum. Mol. Gen. , vol.6 , pp. 753-767
    • Ohno, K.1    Quiram, P.2    Milone, M.3    Wang, H.-L.4    Harper, M.C.5    Pruitt J.N. II6    Brengman, J.M.7    Pao, L.8    Fischbeck, K.H.9    Crawford, T.O.10    Sine, S.M.11    Engel, A.G.12
  • 27
    • 0023478292 scopus 로고
    • Data transformations for improved display and fitting of single-channel dwell time histograms
    • Sigworth F.J., Sine S.M. 1987. Data transformations for improved display and fitting of single-channel dwell time histograms. Biophys. J. 52, 1047-1054
    • (1987) Biophys. J. , vol.52 , pp. 1047-1054
    • Sigworth, F.J.1    Sine, S.M.2
  • 28
    • 0000410893 scopus 로고
    • The principles of the stochastic interpretation of ion-channel mechanisms
    • (Sakmann, B., Neher, E. eds.), Second Edition, Plenum Press, New York
    • Colquhoun D., Hawkes A.G. 1995. The principles of the stochastic interpretation of ion-channel mechanisms. In: Single-Channel Recording (Sakmann, B., Neher, E. eds.), Second Edition, Plenum Press, New York, 397-482
    • (1995) Single-Channel Recording , pp. 397-482
    • Colquhoun, D.1    Hawkes, A.G.2
  • 29
    • 0030656992 scopus 로고    scopus 로고
    • Single bindings versus single channel recordings: A new approach to ionotropic receptors
    • Edelstein SJ.,Schaad O., Changeux J.-P. 1997. Single bindings versus single channel recordings: a new approach to ionotropic receptors. Biochemistry 36, 13755-13760
    • (1997) Biochemistry , vol.36 , pp. 13755-13760
    • Edelstein, S.J.1    Schaad, O.2    Changeux, J.-P.3
  • 33
    • 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, Desphande 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    Desphande, P.5    Lester, H.A.6
  • 34
    • 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. Mol. Pharmacol. 48, 379-384
    • (1995) Mol. Pharmacol. , vol.48 , pp. 379-384
    • Filatov, G.N.1    White, M.M.2
  • 35
    • 0027194134 scopus 로고
    • Single amino acid substitution affects desensitization of the 5-hydroxytryptamine type 3 receptor expressed in Xenopus oocytes
    • Yakel J.L., Lagrutta A., Adelman J.P., North R.A. 1993. Single amino acid substitution affects desensitization of the 5-hydroxytryptamine type 3 receptor expressed in Xenopus oocytes. Proc. Natl. Acad. Sci. USA 90, 5030-5033
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5030-5033
    • Yakel, J.L.1    Lagrutta, A.2    Adelman, J.P.3    North, R.A.4
  • 39
    • 0029954238 scopus 로고    scopus 로고
    • A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors
    • Campos-Caro A., Sala S., Ballesta J.J., Vicente-Aguilló F., Criado M., Sala F. 1996. A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors. Proc. Natl. Acad. Sci. USA 93,6118-6123
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6118-6123
    • Campos-Caro, A.1    Sala, S.2    Ballesta, J.J.3    Vicente-Aguilló, F.4    Criado, M.5    Sala, F.6
  • 41
    • 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


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