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Volumn 6, Issue 5, 1997, Pages 767-774

Mutations in different functional domains of the human muscle acetylcholine receptor α subunit in patients with the slow-channel congenital myasthenic syndrome

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; CHOLINERGIC RECEPTOR; ION CHANNEL; RECEPTOR SUBUNIT;

EID: 0030987817     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/6.5.767     Document Type: Article
Times cited : (121)

References (38)
  • 1
    • 0031060063 scopus 로고    scopus 로고
    • Genes at the junction - Candidates for congenital myasthenic syndromes
    • Vincent, A., Newland, C., Croxen, R. and Beeson, D. (1997) Genes at the junction - candidates for congenital myasthenic syndromes. Trends Neurosci., 20, 15-22.
    • (1997) Trends Neurosci. , vol.20 , pp. 15-22
    • Vincent, A.1    Newland, C.2    Croxen, R.3    Beeson, D.4
  • 2
    • 0028821376 scopus 로고
    • Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the ε subunit
    • Ohno, K., Hutchinson, D.O., Milone, M., Brengman, J.M., Bouzat, C., Sine, S.M. and Engel, A.G. (1995) Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the ε subunit. Proc. Natl Acad. Sci. USA, 92, 758-762.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 758-762
    • Ohno, K.1    Hutchinson, D.O.2    Milone, M.3    Brengman, J.M.4    Bouzat, C.5    Sine, S.M.6    Engel, A.G.7
  • 3
    • 0029077770 scopus 로고
    • A leucine-to-phenylalanine substitution in the acetylcholine receptor ion channel in a family with slow-channel syndrome
    • Gomez, C.M. and Gammack, J.T. (1995) A leucine-to-phenylalanine substitution in the acetylcholine receptor ion channel in a family with slow-channel syndrome. Neurology, 45, 982-985.
    • (1995) Neurology , vol.45 , pp. 982-985
    • Gomez, C.M.1    Gammack, J.T.2
  • 4
    • 0029087136 scopus 로고
    • Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity
    • Sine, S.M., Ohno, K., Bouzat, C., Auerbach, A., Milone, M., Pruitt, J.N. and Engel, A.G. (1995) Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenic 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
  • 7
    • 0028210663 scopus 로고
    • Syndromes myasthéniques héréditaires a revelation tardive
    • Chauplannaz, G. and Bady, B. (1994) Syndromes myasthéniques héréditaires a revelation tardive. Rev. Neurol. (Paris), 150, 142-148.
    • (1994) Rev. Neurol. (Paris) , vol.150 , pp. 142-148
    • Chauplannaz, G.1    Bady, B.2
  • 9
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin, A. and Akabas, M.H. (1995) Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron, 15, 1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 10
    • 0030011258 scopus 로고    scopus 로고
    • The emerging three-dimensional structure of a receptor: The nicotinic acetylcholine receptor
    • Hucho, F., Tsetlin, V.I. and Machold, J. (1996) The emerging three-dimensional structure of a receptor: the nicotinic acetylcholine receptor. Eur. J. Biochem., 239, 539-557.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 539-557
    • Hucho, F.1    Tsetlin, V.I.2    Machold, J.3
  • 11
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9Å resolution
    • Unwin, N. (1993) Nicotinic acetylcholine receptor at 9Å resolution. J. Mol. Biol., 229, 1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 12
    • 0022628717 scopus 로고
    • Kinetics of unliganded acetylcholine receptor channel gating
    • Jackson, M.B. (1986) Kinetics of unliganded acetylcholine receptor channel gating. Biophys J., 49, 663-672.
    • (1986) Biophys J. , vol.49 , pp. 663-672
    • Jackson, M.B.1
  • 13
    • 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
  • 14
    • 0029859799 scopus 로고    scopus 로고
    • Binding sites contribute unequally to the gating of mouse nicotinic αD200N acetylcholine receptors
    • Akk, G., Sine, S. and Auerbach, A. (1996) Binding sites contribute unequally to the gating of mouse nicotinic αD200N acetylcholine receptors. J. Physiol. (Lond.), 496, 185-196.
    • (1996) J. Physiol. (Lond.) , vol.496 , pp. 185-196
    • Akk, G.1    Sine, S.2    Auerbach, A.3
  • 15
    • 0029586515 scopus 로고
    • Functional and non-functional isoforms of the human muscle acetylcholine receptor
    • Newland, C.F., Beeson, D., Vincent, A. and Newsom-Davis, J. (1995) Functional and non-functional isoforms of the human muscle acetylcholine receptor. J. Physiol. (Lond.), 489, 767-778.
    • (1995) J. Physiol. (Lond.) , vol.489 , pp. 767-778
    • Newland, C.F.1    Beeson, D.2    Vincent, A.3    Newsom-Davis, J.4
  • 16
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetycholine receptor a subunit labeled by a photoaffinity ligand for the acetylcholine binding site
    • Dennis, M., Giraudat, J., Kotzyba-Hibert, F., Goeldner, M., Hirth, C., Chang, J.-Y., Lazure, C., Chrétien, M., and Changeux, J.-P. (1988) Amino acids of the Torpedo marmorata acetycholine receptor a subunit labeled by a photoaffinity ligand for the acetylcholine binding site. Biochemistry, 27, 2346-2357.
    • (1988) Biochemistry , vol.27 , pp. 2346-2357
    • Dennis, M.1    Giraudat, J.2    Kotzyba-Hibert, F.3    Goeldner, M.4    Hirth, C.5    Chang, J.-Y.6    Lazure, C.7    Chrétien, M.8    Changeux, J.-P.9
  • 17
    • 0029153305 scopus 로고
    • Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: Mutations of α-subunit tyrosine 190 affect both binding and gating
    • Chen, J., Zhang, Y., Akk, G., Sine, S. and Auerbach, A. (1995) Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of α-subunit tyrosine 190 affect both binding and gating. Biophys. J., 69, 849-859.
    • (1995) Biophys. J. , vol.69 , pp. 849-859
    • Chen, J.1    Zhang, Y.2    Akk, G.3    Sine, S.4    Auerbach, A.5
  • 18
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the a subunit
    • Akabas, M.H., Kaufmann, C., Archdeacon, P. and Karlin, A. (1994) Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the a subunit. Neuron, 13, 919-927.
    • (1994) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 19
    • 0028268955 scopus 로고
    • Transverse distance between the membrane and the agonist binding site on the Torpedo acetylcholine receptor: A fluorescence study
    • Valenzuela, C., Weign, P., Yguerabide, J. and Johnson, D. (1994) Transverse distance between the membrane and the agonist binding site on the Torpedo acetylcholine receptor: a fluorescence study. Biophys. J., 66, 674-682.
    • (1994) Biophys. J. , vol.66 , pp. 674-682
    • Valenzuela, C.1    Weign, P.2    Yguerabide, J.3    Johnson, D.4
  • 20
    • 0025678678 scopus 로고
    • Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction
    • Toyoshima, C. and Unwin, N. (1990) Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction. J. Cell Biol., 111, 2623-2635.
    • (1990) J. Cell Biol. , vol.111 , pp. 2623-2635
    • Toyoshima, C.1    Unwin, N.2
  • 22
    • 0028016521 scopus 로고
    • Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia
    • Langosch, D., Laube, B., Rundström, N., Schmieden, V., Bormann, J. and Betz, H. (1994) Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia. EMBO J., 13, 4223-4228.
    • (1994) EMBO J. , vol.13 , pp. 4223-4228
    • Langosch, D.1    Laube, B.2    Rundström, N.3    Schmieden, V.4    Bormann, J.5    Betz, H.6
  • 23
    • 0028831226 scopus 로고
    • Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists
    • Rajendra, S., Lynch, J.W., Pierce, K.D., French, C.R., Barry, P.H. and Schofield, P.R. (1995) Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists. Neuron, 14, 169-175.
    • (1995) Neuron , vol.14 , pp. 169-175
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 24
    • 0029018726 scopus 로고
    • Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator
    • Lynch, J., Rajendra, S., Barry, P. and Schofield, P. (1995) Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator. J. Biol. Chem., 270, 13799-13806.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13799-13806
    • Lynch, J.1    Rajendra, S.2    Barry, P.3    Schofield, P.4
  • 25
    • 0028966653 scopus 로고
    • Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for β-amino-acids
    • Laube, B., Langosch, D., Beiz, H. and Schmieden, V. (1995) Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for β-amino-acids Neuroreport, 6, 897-900.
    • (1995) Neuroreport , vol.6 , pp. 897-900
    • Laube, B.1    Langosch, D.2    Beiz, H.3    Schmieden, V.4
  • 26
    • 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-Agulló, F., Criado, M. and 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-Agulló, F.4    Criado, M.5    Sala, F.6
  • 27
    • 0029803994 scopus 로고    scopus 로고
    • Calcium permeability increase of endplate channels in rat muscle during postnatal development
    • Villarroel, A. and Sakmann, B. (1996) Calcium permeability increase of endplate channels in rat muscle during postnatal development. J. Physiol. (Lond.), 496, 331-338.
    • (1996) J. Physiol. (Lond.) , vol.496 , pp. 331-338
    • Villarroel, A.1    Sakmann, B.2
  • 28
    • 0020047892 scopus 로고
    • A newly recognised congenital myasthenic syndrome attributed to a prolonged open time of the acetylcholine-induced ion channel
    • Engel, A.G., Lambert, E.H., Mulder, D.M., Torres, C.F., Sahashi, K., Bertorini, T.E. and Whitaker, J.N. (1982) A newly recognised congenital myasthenic syndrome attributed to a prolonged open time of the acetylcholine-induced ion channel. Ann. Neurol., 11, 553-569.
    • (1982) Ann. Neurol. , vol.11 , pp. 553-569
    • Engel, A.G.1    Lambert, E.H.2    Mulder, D.M.3    Torres, C.F.4    Sahashi, K.5    Bertorini, T.E.6    Whitaker, J.N.7
  • 29
    • 15844429136 scopus 로고    scopus 로고
    • Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor ε subunit
    • Ohno, K., Wang, H.-L., Milone, M., Brenn N., Brengman, J.M., Nakano, S., Quiram, P., Pruitt, J.N., Sine, S.M. and Engel, A.G. (1996) Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor ε subunit. Neuron, 17, 157-170.
    • (1996) Neuron , vol.17 , pp. 157-170
    • Ohno, K.1    Wang, H.-L.2    Milone, M.3    Brenn, N.4    Brengman, J.M.5    Nakano, S.6    Quiram, P.7    Pruitt, J.N.8    Sine, S.M.9    Engel, A.G.10
  • 30
    • 0028980028 scopus 로고
    • A missense mutation in the neuronal nicotinic acetylcholine receptor α4 subunit is associated with autosomal dominant nocturnal frontal lobe epilepsy
    • Steinlein, O.K., Mulley, J.C., Propping, P., Wallace, R.H., Phillips, H.A., Sutherland, G.R., Scheffer, I.E. and Berkovic, S.F. (1995) A missense mutation in the neuronal nicotinic acetylcholine receptor α4 subunit is associated with autosomal dominant nocturnal frontal lobe epilepsy. Nature Genet., 11, 201-203.
    • (1995) Nature Genet. , vol.11 , pp. 201-203
    • Steinlein, O.K.1    Mulley, J.C.2    Propping, P.3    Wallace, R.H.4    Phillips, H.A.5    Sutherland, G.R.6    Scheffer, I.E.7    Berkovic, S.F.8
  • 31
    • 0028944389 scopus 로고
    • A mutated acetylcholine receptor subunit causes neuronal degeneration in C.elegans
    • Treinin, M. and Chalfie, M. (1995) A mutated acetylcholine receptor subunit causes neuronal degeneration in C.elegans. Neuron, 14, 871-877.
    • (1995) Neuron , vol.14 , pp. 871-877
    • Treinin, M.1    Chalfie, M.2
  • 32
    • 0027177625 scopus 로고
    • Primary structure of the human muscle acetylcholine receptor: cDNA cloning of the γ and ε subunits
    • Beeson, D., Brydson, M., Betty, M., Jeremiah, S., Povey, S., Vincent, A. and Newsom-Davis, J. (1993) Primary structure of the human muscle acetylcholine receptor: cDNA cloning of the γ and ε subunits. Eur. J. Biochem., 215, 229-238.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 229-238
    • Beeson, D.1    Brydson, M.2    Betty, M.3    Jeremiah, S.4    Povey, S.5    Vincent, A.6    Newsom-Davis, J.7
  • 34
    • 0024316438 scopus 로고
    • Nucleotide sequence of human muscle acetylcholine receptor β-subunit
    • Beeson, D., Brydson, M. and Newsom-Davis, J. (1989) Nucleotide sequence of human muscle acetylcholine receptor β-subunit. Nucleic Acids Res., 17, 4391.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4391
    • Beeson, D.1    Brydson, M.2    Newsom-Davis, J.3
  • 36
    • 0026485457 scopus 로고
    • + channel determined by construction of multimeric cDNAs
    • + channel determined by construction of multimeric cDNAs. Neuron, 9, 861-871.
    • (1992) Neuron , vol.9 , pp. 861-871
    • Liman, E.R.1    Tytgat, J.2    Hess, P.3
  • 37
    • 0022272338 scopus 로고
    • Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate
    • Colquhoun, D. and Sakmann, B. (1985) Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate. J. Physiol. (Lond.), 369, 501-557.
    • (1985) J. Physiol. (Lond.) , vol.369 , pp. 501-557
    • Colquhoun, D.1    Sakmann, B.2
  • 38
    • 0028809730 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α subunit
    • Akabas, M.H. and Karlin, A. (1995) Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α subunit. Biochemistry, 34, 12496-12500.
    • (1995) Biochemistry , vol.34 , pp. 12496-12500
    • Akabas, M.H.1    Karlin, A.2


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