메뉴 건너뛰기




Volumn 20, Issue 1, 1999, Pages 45-59

Molecular investigations on the nicotinic acetylcholine receptor: Conformational mapping and dynamic exploration using photoaffinity labeling

Author keywords

Acetylcholine; Nicotinic receptors; Photosensitive agonists; Time resolved photoaffinity labeling

Indexed keywords

NICOTINIC RECEPTOR;

EID: 0032735643     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02741364     Document Type: Article
Times cited : (14)

References (83)
  • 1
    • 0029046913 scopus 로고
    • Neuronal nicotinic receptors: Molecular organization and regulations
    • Galzi J. L. and Changeux J. P. (1995) Neuronal nicotinic receptors: Molecular organization and regulations. Neuropharmacology 34, 563-582.
    • (1995) Neuropharmacology , vol.34 , pp. 563-582
    • Galzi, J.L.1    Changeux, J.P.2
  • 2
    • 0030175612 scopus 로고    scopus 로고
    • Nicotinic receptors in the development and modulation of CNS synapses
    • Role L. W. and Berg D. K. (1996) Nicotinic receptors in the development and modulation of CNS synapses. Neuron 16, 1077-1085.
    • (1996) Neuron , vol.16 , pp. 1077-1085
    • Role, L.W.1    Berg, D.K.2
  • 3
    • 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
  • 4
    • 0032458934 scopus 로고    scopus 로고
    • Allosteric nicotinic receptors, human pathologies
    • Lena C. and Changeux J. P. (1998) Allosteric nicotinic receptors, human pathologies. J. Physiol. Paris 92, 63-74.
    • (1998) J. Physiol. Paris , vol.92 , pp. 63-74
    • Lena, C.1    Changeux, J.P.2
  • 5
    • 0032458176 scopus 로고    scopus 로고
    • Congenital myasthenic syndromes: Experiments of nature
    • Engel A. G., Ohno K., and Sine S. M. (1998) Congenital myasthenic syndromes: Experiments of nature. J. Physiol. Paris 92, 113-117.
    • (1998) J. Physiol. Paris , vol.92 , pp. 113-117
    • Engel, A.G.1    Ohno, K.2    Sine, S.M.3
  • 6
    • 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
  • 7
    • 0018790793 scopus 로고
    • Fast kinetic studies on the interaction of a fluorescent agonist with the membrane-bound acetylcholine receptor from Torpedo marmorata
    • Heidmann T. and Changeux J. P. (1979) Fast kinetic studies on the interaction of a fluorescent agonist with the membrane-bound acetylcholine receptor from Torpedo marmorata. Eur. J. Biochem. 94, 255-279.
    • (1979) Eur. J. Biochem. , vol.94 , pp. 255-279
    • Heidmann, T.1    Changeux, J.P.2
  • 8
    • 0021041862 scopus 로고
    • Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata
    • Heidmann T., Bernhardt J., Neumann E., and Changeux J. P. (1983) Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata. Biochemistry 22, 5452-5459.
    • (1983) Biochemistry , vol.22 , pp. 5452-5459
    • Heidmann, T.1    Bernhardt, J.2    Neumann, E.3    Changeux, J.P.4
  • 9
    • 0020003862 scopus 로고
    • Desensitization at the frog neuromuscular junction: A biphasic process
    • Feltz A. and Trautmann A. (1982) Desensitization at the frog neuromuscular junction: A biphasic process. J. Physiol. 322, 257-272.
    • (1982) J. Physiol. , vol.322 , pp. 257-272
    • Feltz, A.1    Trautmann, A.2
  • 10
    • 0019225785 scopus 로고
    • Kinetics of binding of [3H]acetylcholine and [3H]carbamoylcholine to Torpedo postsynaptic membranes: Slow conformational transitions of the cholinergic receptor
    • Boyd N. D. and Cohen J. B. (1980) Kinetics of binding of [3H]acetylcholine and [3H]carbamoylcholine to Torpedo postsynaptic membranes: Slow conformational transitions of the cholinergic receptor. Biochemistry 19, 5344-5353.
    • (1980) Biochemistry , vol.19 , pp. 5344-5353
    • Boyd, N.D.1    Cohen, J.B.2
  • 11
    • 0018351106 scopus 로고
    • Identification of a local anesthetic binding site in nicotinic post-synaptic membranes isolated from Torpedo marmorata electric tissue
    • Krodel E. K., Beckman R. A., and Cohen J. B. (1979) Identification of a local anesthetic binding site in nicotinic post-synaptic membranes isolated from Torpedo marmorata electric tissue. Mol. Pharmacol. 15, 294-312.
    • (1979) Mol. Pharmacol. , vol.15 , pp. 294-312
    • Krodel, E.K.1    Beckman, R.A.2    Cohen, J.B.3
  • 12
    • 0020621092 scopus 로고
    • Multiple sites of action for noncompetitive blockers on acetylcholine receptor rich membrane fragments from torpedo marmorata
    • Heidmann T., Oswald R. E., and 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
  • 13
    • 0023585691 scopus 로고
    • A molecular view of neurotransmitter receptors and ionic channels
    • Numa S. (1989) A molecular view of neurotransmitter receptors and ionic channels. Harvey Lecture Series 83, 121-165.
    • (1989) Harvey Lecture Series , vol.83 , pp. 121-165
    • Numa, S.1
  • 14
    • 0024278375 scopus 로고
    • Photoaffinity labeling of the acetylcholine binding sites on the nicotinic receptor by an aryldiazonium derivative
    • Langenbuch-Cachat J., Bon C., Mulle C., Goeldner M., Hirth C., and Changeux J. P. (1988) Photoaffinity labeling of the acetylcholine binding sites on the nicotinic receptor by an aryldiazonium derivative. Biochemistry 27, 2337-2345.
    • (1988) Biochemistry , vol.27 , pp. 2337-2345
    • Langenbuch-Cachat, J.1    Bon, C.2    Mulle, C.3    Goeldner, M.4    Hirth, C.5    Changeux, J.P.6
  • 15
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetylcholine receptor alpha 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., et al. (1988) Amino acids of the Torpedo marmorata acetylcholine receptor alpha 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
  • 16
    • 0025346780 scopus 로고
    • Identification of a novel amino acid alpha-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-binding sites
    • Galzi J. L., Revah F., Black D., Goeldner M., Hirth C., and Changeux J. P. (1990) Identification of a novel amino acid alpha-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-binding sites. J. Biol. Chem. 265, 10,430-10,437.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10430-10437
    • Galzi, J.L.1    Revah, F.2    Black, D.3    Goeldner, M.4    Hirth, C.5    Changeux, J.P.6
  • 17
    • 0025753149 scopus 로고
    • Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand
    • Galzi J. L., Revah F., Bouet F., Menez A., Goeldner M., Hirth C., et al. (1991) Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand. Proc. Natl. Acad. Sci. USA 88, 5051-5055.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5051-5055
    • Galzi, J.L.1    Revah, F.2    Bouet, F.3    Menez, A.4    Goeldner, M.5    Hirth, C.6
  • 18
    • 0026625673 scopus 로고
    • Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist
    • White B. H. and Cohen J. B. (1992) Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist. J. Biol. Chem. 267, 15,770-15,783.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15770-15783
    • White, B.H.1    Cohen, J.B.2
  • 19
    • 0345363642 scopus 로고
    • Time-resolved photolabeling by the noncompetitive blocker chlorpromazine of the acetylcholine receptor in its transiently open and closed ion channel conformations
    • Heidmann T. and Changeux J. P. (1984) Time-resolved photolabeling by the noncompetitive blocker chlorpromazine of the acetylcholine receptor in its transiently open and closed ion channel conformations. Proc. Natl. Acad. Sci. USA 81, 1897-1901.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1897-1901
    • Heidmann, T.1    Changeux, J.P.2
  • 20
    • 0022998659 scopus 로고
    • Characterization of the transient agonist-triggered state of the acetylcholine receptor rapidly labeled by the noncompetitive blocker [3H]chlorpromazine: Additional evidence for the open channel conformation
    • Heidmann T. and Changeux J. P. (1986) Characterization of the transient agonist-triggered state of the acetylcholine receptor rapidly labeled by the noncompetitive blocker [3H]chlorpromazine: Additional evidence for the open channel conformation. Biochemistry 25, 6109-6113.
    • (1986) Biochemistry , vol.25 , pp. 6109-6113
    • Heidmann, T.1    Changeux, J.P.2
  • 21
    • 0021951294 scopus 로고
    • Covalent labeling of functional states of the acetylcholine receptor. Effects of antagonists on the receptor conformation
    • Fahr A., Lauffer L., Schmidt D., Heyn M. P., and Hucho F. (1985) Covalent labeling of functional states of the acetylcholine receptor. Effects of antagonists on the receptor conformation. Eur. J. Biochem. 147, 483-487.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 483-487
    • Fahr, A.1    Lauffer, L.2    Schmidt, D.3    Heyn, M.P.4    Hucho, F.5
  • 22
    • 0021755645 scopus 로고
    • Rapid laser flash photoaffinity labeling of binding sites for a noncompetitive inhibitor of the acetylcholine receptor
    • Muhn P., Fahr A., and Hucho F. (1984) Rapid laser flash photoaffinity labeling of binding sites for a noncompetitive inhibitor of the acetylcholine receptor. Biochemistry 23, 2725-2730.
    • (1984) Biochemistry , vol.23 , pp. 2725-2730
    • Muhn, P.1    Fahr, A.2    Hucho, F.3
  • 23
    • 0021806567 scopus 로고
    • Time-resolved photolabeling by quinacrine azide of a noncompetitive inhibitor site of the nicotinic acetylcholine receptor in a transient, agonist-induced state
    • Cox R. N., Kaldany R. R., DiPaola M., and Karlin A. (1985) Time-resolved photolabeling by quinacrine azide of a noncompetitive inhibitor site of the nicotinic acetylcholine receptor in a transient, agonist-induced state. J. Biol. Chem. 260, 7186-7193.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7186-7193
    • Cox, R.N.1    Kaldany, R.R.2    DiPaola, M.3    Karlin, A.4
  • 24
    • 0025291849 scopus 로고
    • Mapping the alpha-subunit site photolabeled by the noncompetitive inhibitor [3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor
    • DiPaola M., Kao P. N., and Karlin A. (1990) Mapping the alpha-subunit site photolabeled by the noncompetitive inhibitor [3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor. J. Biol. Chem. 265, 11,017-11,029.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11017-11029
    • DiPaola, M.1    Kao, P.N.2    Karlin, A.3
  • 25
    • 0024918350 scopus 로고
    • Explorations of the nicotinic acetylcholine receptor
    • Karlin A. (1991) Explorations of the nicotinic acetylcholine receptor. Harvey Lectures 71-107.
    • (1991) Harvey Lectures , pp. 71-107
    • Karlin, A.1
  • 27
    • 0023375835 scopus 로고
    • Location of subunits within the acetylcholine receptor by electron image analysis of tubular crystals from Torpedo marmorata
    • Kubalek E., Ralston S., Lindstrom J., and Unwin N. (1987) Location of subunits within the acetylcholine receptor by electron image analysis of tubular crystals from Torpedo marmorata. J. Cell. Biol. 105, 9-18.
    • (1987) J. Cell. Biol. , vol.105 , pp. 9-18
    • Kubalek, E.1    Ralston, S.2    Lindstrom, J.3    Unwin, N.4
  • 28
    • 0024725677 scopus 로고
    • Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor
    • Blount P. and Merlie J. P. (1989) Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor. Neuron 3, 349-357.
    • (1989) Neuron , vol.3 , pp. 349-357
    • Blount, P.1    Merlie, J.P.2
  • 29
    • 0026045588 scopus 로고
    • Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor
    • Sine S. M. and Claudio T. (1991) Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor. J. Biol. Chem. 266, 19,369-19,377.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19369-19377
    • Sine, S.M.1    Claudio, T.2
  • 30
    • 0028964767 scopus 로고
    • A new class of photoactivatable and cleavable derivatives of neurotoxin II from Naja maja oxiana
    • Machold J., Weise C., Utkin Y., Franke P., Tsetlin V., and Hucho F. (1995) A new class of photoactivatable and cleavable derivatives of neurotoxin II from Naja maja oxiana. Eur. J. Biochem. 228, 947-954.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 947-954
    • Machold, J.1    Weise, C.2    Utkin, Y.3    Franke, P.4    Tsetlin, V.5    Hucho, F.6
  • 31
    • 0025308169 scopus 로고
    • d-Tubocurarine binding sites are located at alpha-gamma and alpha-delta subunit interfaces of the nicotinic acetylcholine receptor
    • Pedersen S. E. and Cohen J. B. (1990) d-Tubocurarine binding sites are located at alpha-gamma and alpha-delta subunit interfaces of the nicotinic acetylcholine receptor. Proc Natl Acad Sci USA 87, 2785-2789.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2785-2789
    • Pedersen, S.E.1    Cohen, J.B.2
  • 33
    • 0029085766 scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of determinants of alpha-conotoxin M1 selectivity
    • Sine S. M., Kreienkamp H. J., Bren N., Maeda R., and Taylor P. (1995) Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of determinants of alpha-conotoxin M1 selectivity. Neuron 15, 205-211.
    • (1995) Neuron , vol.15 , pp. 205-211
    • Sine, S.M.1    Kreienkamp, H.J.2    Bren, N.3    Maeda, R.4    Taylor, P.5
  • 34
    • 0031468619 scopus 로고    scopus 로고
    • Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the Torpedo nicotinic acetylcholine receptor
    • Chiara D. C. and Cohen J. B. (1997) Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the Torpedo nicotinic acetylcholine receptor. J. Biol. Chem. 272, 32,940-32,950.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32940-32950
    • Chiara, D.C.1    Cohen, J.B.2
  • 35
    • 0025819979 scopus 로고
    • Mapping of the acetylcholine binding site of the nicotinic acetylcholine receptor: [3H]Nicotine as an agonist photoaffinity label
    • Middelton R. E. and Cohen B. C. (1991) Mapping of the acetylcholine binding site of the nicotinic acetylcholine receptor: [3H]Nicotine as an agonist photoaffinity label. Biochemistry 30, 6987-6997.
    • (1991) Biochemistry , vol.30 , pp. 6987-6997
    • Middelton, R.E.1    Cohen, B.C.2
  • 36
    • 0032548783 scopus 로고    scopus 로고
    • Identification of tryptophan 55 as the primary site of [3H]nicotine photoincorporation in the gamma-subunit of the Torpedo nicotinic acetylcholine receptor
    • Chiara D. C., Middleton R. E., and Cohen J. B. (1998) Identification of tryptophan 55 as the primary site of [3H]nicotine photoincorporation in the gamma-subunit of the Torpedo nicotinic acetylcholine receptor. FEBS Lett. 423, 223-226.
    • (1998) FEBS Lett. , vol.423 , pp. 223-226
    • Chiara, D.C.1    Middleton, R.E.2    Cohen, J.B.3
  • 37
    • 0021132711 scopus 로고
    • Identification of the alpha subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site
    • Kao P. N., Dwork A. J., Kaldany R. R., Silver M. L., Wideman J., Stein S., et al. (1984) Identification of the alpha subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site. J. Biol. Chem. 259, 11,662-11,665.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11662-11665
    • Kao, P.N.1    Dwork, A.J.2    Kaldany, R.R.3    Silver, M.L.4    Wideman, J.5    Stein, S.6
  • 38
    • 0024349141 scopus 로고
    • An analog of lophotoxin reacts covalently with Tyr190 in the alpha-subunit of the nicotinic acetylcholine receptor
    • Abramson S. N., Li Y., Culver P., and Taylor P. (1989) An analog of lophotoxin reacts covalently with Tyr190 in the alpha-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 264, 12,666-12,672.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12666-12672
    • Abramson, S.N.1    Li, Y.2    Culver, P.3    Taylor, P.4
  • 39
    • 0026344986 scopus 로고
    • Structure of the agonist-binding site of the nicotinic acetylcholine receptor. [3H]acetylcholine mustard identifies residues in the cation-binding subsite
    • Cohen J. B., Sharp S. D., and Liu W. S. (1991) Structure of the agonist-binding site of the nicotinic acetylcholine receptor. [3H]acetylcholine mustard identifies residues in the cation-binding subsite. J. Biol. Chem. 266, 23,354-23,364.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23354-23364
    • Cohen, J.B.1    Sharp, S.D.2    Liu, W.S.3
  • 40
    • 0025719155 scopus 로고
    • Agonist binding site of Torpedo electric tissue nicotinic acetylcholine receptor. A negatively charged region of the delta subunit within 0.9 nm of the alpha subunit binding site disulfide
    • Czajkowski C. and Karlin A. (1991) Agonist binding site of Torpedo electric tissue nicotinic acetylcholine receptor. A negatively charged region of the delta subunit within 0.9 nm of the alpha subunit binding site disulfide. J. Biol. Chem. 266, 22,603-22,612.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22603-22612
    • Czajkowski, C.1    Karlin, A.2
  • 41
    • 0029929234 scopus 로고    scopus 로고
    • The contributions of aspartyl residues in the acetylcholine receptor gamma and delta subunits to the binding of agonists and competitive antagonists
    • Martin M., Czajkowski C., and Karlin A. (1996) The contributions of aspartyl residues in the acetylcholine receptor gamma and delta subunits to the binding of agonists and competitive antagonists. J. Biol. Chem. 271, 13,497-13,503.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13497-13503
    • Martin, M.1    Czajkowski, C.2    Karlin, A.3
  • 42
    • 0030773018 scopus 로고    scopus 로고
    • Functional effects on the acetylcholine receptor of multiple mutations of gamma Asp174 and delta Asp180
    • Martin M. D. and Karlin A. (1997) Functional effects on the acetylcholine receptor of multiple mutations of gamma Asp174 and delta Asp180. Biochemistry 36, 10,742-10,750.
    • (1997) Biochemistry , vol.36 , pp. 10742-10750
    • Martin, M.D.1    Karlin, A.2
  • 43
    • 0029958548 scopus 로고    scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor. Identification of residues that determine agonist selectivity
    • Prince R. J. and Sine S. M. (1996) Molecular dissection of subunit interfaces in the acetylcholine receptor. Identification of residues that determine agonist selectivity. J. Biol. Chem. 271, 25,770-25,777.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25770-25777
    • Prince, R.J.1    Sine, S.M.2
  • 44
    • 0026758178 scopus 로고
    • Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor
    • O'Leary M. E. and White M. M. (1992) Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor. J. Biol. Chem. 267, 8360-8365.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8360-8365
    • O'Leary, M.E.1    White, M.M.2
  • 45
    • 0026004411 scopus 로고
    • Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor
    • Tomaselli G. F., McLaughlin J. T., Jurman M. E., Hawrot E., and Yellen G. (1991) Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor. Biophys. J. 60, 721-727.
    • (1991) Biophys. J. , vol.60 , pp. 721-727
    • Tomaselli, G.F.1    McLaughlin, J.T.2    Jurman, M.E.3    Hawrot, E.4    Yellen, G.5
  • 46
    • 0025985732 scopus 로고
    • Functional significance of aromatic amino acids from three peptide loops of the alpha 7 neuronal nicotinic receptor site investigated by site-directed mutagenesis
    • Galzi J. L., Bertrand D., Devillers-Thiery A., Revah F., Bertrand S., and Changeux J. P. (1991) Functional significance of aromatic amino acids from three peptide loops of the alpha 7 neuronal nicotinic receptor site investigated by site-directed mutagenesis. FEBS Lett. 294, 198-202.
    • (1991) FEBS Lett. , vol.294 , pp. 198-202
    • Galzi, J.L.1    Bertrand, D.2    Devillers-Thiery, A.3    Revah, F.4    Bertrand, S.5    Changeux, J.P.6
  • 47
    • 0028292368 scopus 로고
    • Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists
    • Sine S. M., Quiram P., Papanikolaou F., Kreienkamp H. J., and Taylor P. (1994) Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists. J. Biol. Chem. 269, 8808-8816.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8808-8816
    • Sine, S.M.1    Quiram, P.2    Papanikolaou, F.3    Kreienkamp, H.J.4    Taylor, P.5
  • 48
    • 0029078817 scopus 로고
    • Identification of a new component of the agonist binding site of the nicotinic alpha 7 homooligomeric receptor
    • Corringer P. J., Galzi J. L., Eisele J. L., Bertrand S., Changeux J. P., and Bertrand D. (1995) Identification of a new component of the agonist binding site of the nicotinic alpha 7 homooligomeric receptor. J. Biol. Chem. 270, 11,749-11,752.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11749-11752
    • Corringer, P.J.1    Galzi, J.L.2    Eisele, J.L.3    Bertrand, S.4    Changeux, J.P.5    Bertrand, D.6
  • 49
    • 0000631357 scopus 로고
    • Complete mRNA coding sequence of the acetylcholine binding alpha-subunit of Torpedo marmorata acetylcholine receptor: A model for the transmembrane organization of the polypeptide chain
    • Devillers-Thiery A., Giraudat J., Bentaboulet M., and Changeux J. P. (1983) Complete mRNA coding sequence of the acetylcholine binding alpha-subunit of Torpedo marmorata acetylcholine receptor: A model for the transmembrane organization of the polypeptide chain. Proc. Natl. Acad. Sci. USA 80, 2067-2071.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2067-2071
    • Devillers-Thiery, A.1    Giraudat, J.2    Bentaboulet, M.3    Changeux, J.P.4
  • 50
    • 0010665535 scopus 로고
    • Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor gamma subunit
    • Claudio T., Ballivet M., Patrick J., and Heinemann S. (1983) Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor gamma subunit. Proc. Natl. Acad. Sci. USA 80, 1111-1115.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1111-1115
    • Claudio, T.1    Ballivet, M.2    Patrick, J.3    Heinemann, S.4
  • 51
    • 0020583289 scopus 로고
    • Structural homology of Torpedo californica acetylcholine receptor subunits
    • Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Furutani Y., et al. (1983) Structural homology of Torpedo californica acetylcholine receptor subunits. Nature 302, 528-532.
    • (1983) Nature , vol.302 , pp. 528-532
    • Noda, M.1    Takahashi, H.2    Tanabe, T.3    Toyosato, M.4    Kikyotani, S.5    Furutani, Y.6
  • 53
    • 0000791015 scopus 로고
    • Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: Serine-262 of the delta subunit is labeled by [3H]chlorpromazine
    • Giraudat J., Dennis M., Heidmann T., Chang J. Y., and Changeux J. P. (1986) Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: Serine-262 of the delta subunit is labeled by [3H]chlorpromazine. Proc. Natl. Acad. Sci. USA 83, 2719-2723.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2719-2723
    • Giraudat, J.1    Dennis, M.2    Heidmann, T.3    Chang, J.Y.4    Changeux, J.P.5
  • 54
    • 0023277159 scopus 로고
    • Structure of the high-affinity binding site for non-competitive blockers of the acetylcholine receptor: [3H]chlorpromazine labels homologous residues in the beta and delta chains
    • Giraudat J., Dennis M., Heidmann T., Haumont P. Y., Lederer F., and Changeux J. P. (1987) Structure of the high-affinity binding site for non-competitive blockers of the acetylcholine receptor: [3H]chlorpromazine labels homologous residues in the beta and delta chains. Biochemistry 26, 2410-2418.
    • (1987) Biochemistry , vol.26 , pp. 2410-2418
    • Giraudat, J.1    Dennis, M.2    Heidmann, T.3    Haumont, P.Y.4    Lederer, F.5    Changeux, J.P.6
  • 55
    • 0025195179 scopus 로고
    • The non-competitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: Implications for the alpha-helical organization of regions MIJ and for the structure of the ion channel
    • Revah F., Galzi J. L., Giraudat J., Haumont P. Y., Lederer F., and Changeux J. P. (1990) The non-competitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: Implications for the alpha-helical organization of regions MIJ and for the structure of the ion channel. Proc. Natl. Acad. Sci. USA, 87, 4675-4679.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4675-4679
    • Revah, F.1    Galzi, J.L.2    Giraudat, J.3    Haumont, P.Y.4    Lederer, F.5    Changeux, J.P.6
  • 56
    • 0022458822 scopus 로고
    • The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits
    • Hucho F., Oberthur W., and Lottspeich F. (1986) The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits. FEBS Lett. 205, 137-142.
    • (1986) FEBS Lett. , vol.205 , pp. 137-142
    • Hucho, F.1    Oberthur, W.2    Lottspeich, F.3
  • 58
    • 0026079817 scopus 로고
    • Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor
    • Revah F., Bertrand D., Galzi J. L., Devillers-Thiery A., Mulle C., Hussy N., et al. (1991) Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor. Nature 353, 846-849.
    • (1991) Nature , vol.353 , pp. 846-849
    • Revah, F.1    Bertrand, D.2    Galzi, J.L.3    Devillers-Thiery, A.4    Mulle, C.5    Hussy, N.6
  • 60
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas M. H., Stauffer D. A., Xu M., and Karlin A. (1992) Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 258, 307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 62
    • 0028568234 scopus 로고
    • A hydrophobic inhibitor of the nicotinic acetylcholine receptor acts on the resting state
    • Wu G., Raines D. E., and Miller K. W. (1994) A hydrophobic inhibitor of the nicotinic acetylcholine receptor acts on the resting state. Biochemistry 33, 15,375-15,381.
    • (1994) Biochemistry , vol.33 , pp. 15375-15381
    • Wu, G.1    Raines, D.E.2    Miller, K.W.3
  • 63
    • 0032502674 scopus 로고    scopus 로고
    • Probing the structure of the nicotinic acetylcholine receptor ion channel with the uncharged photoactivable compound-3H-diazofluorene
    • Blanton M. P., Dangott L. J., Raja S. K., Lala A. K., and Cohen J. B. (1998) Probing the structure of the nicotinic acetylcholine receptor ion channel with the uncharged photoactivable compound-3H-diazofluorene. J. Biol. Chem. 273, 8659-8668.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8659-8668
    • Blanton, M.P.1    Dangott, L.J.2    Raja, S.K.3    Lala, A.K.4    Cohen, J.B.5
  • 64
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong N., Sun Y., Chen G. Q., and Gouaux E. (1998) Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395, 913-917.
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 65
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella S. J., Marassi F. M., Gesell J. J., Valente A. P., Kim Y., Oblatt-Montal M., et al. (1999) Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6, 374-379.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6
  • 66
    • 0027209828 scopus 로고
    • Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. I. Transmembrane segment M2 of the nicotinic cholinergic receptor channel is a key pore-lining structure
    • Oblatt-Montal M., Buhler L. K., Iwamoto T., Tomich J. M., and Montal M. (1993) Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. I. Transmembrane segment M2 of the nicotinic cholinergic receptor channel is a key pore-lining structure. J. Biol. Chem. 268, 14,601-14,607.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14601-14607
    • Oblatt-Montal, M.1    Buhler, L.K.2    Iwamoto, T.3    Tomich, J.M.4    Montal, M.5
  • 67
    • 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
  • 68
    • 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
  • 69
    • 0022634418 scopus 로고
    • A stopped-flow apparatus for photoaffinity labeling studies in the milliseconds time range. Application in investigations of the nicotinic acetylcholine receptor
    • Fahr A. and Hucho F. (1986) A stopped-flow apparatus for photoaffinity labeling studies in the milliseconds time range. Application in investigations of the nicotinic acetylcholine receptor. J. Neurosci. Methods 16, 29-38.
    • (1986) J. Neurosci. Methods , vol.16 , pp. 29-38
    • Fahr, A.1    Hucho, F.2
  • 70
    • 0029967067 scopus 로고    scopus 로고
    • Quinacrine noncompetitive inhibitor binding site localized on the Torpedo acetylcholine receptor in the open state
    • Johnson D. A. and Ayres S. (1996) Quinacrine noncompetitive inhibitor binding site localized on the Torpedo acetylcholine receptor in the open state. Biochemistry 35, 6330-6336.
    • (1996) Biochemistry , vol.35 , pp. 6330-6336
    • Johnson, D.A.1    Ayres, S.2
  • 71
    • 0031059313 scopus 로고    scopus 로고
    • Quinacrine and ethidium bromide bind the same locus on the nicotinic acetylcholine receptor from Torpedo californica
    • Lurtz M. M., Hareland M. L., and Pedersen S. E. (1997) Quinacrine and ethidium bromide bind the same locus on the nicotinic acetylcholine receptor from Torpedo californica. Biochemistry 36, 2068-2075.
    • (1997) Biochemistry , vol.36 , pp. 2068-2075
    • Lurtz, M.M.1    Hareland, M.L.2    Pedersen, S.E.3
  • 72
    • 0028809730 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the alpha-subunit
    • Akabas M. H. and Karlin A. (1995) Identification of acetylcholine receptor channel-lining residues in the M1 segment of the alpha-subunit. Biochemistry 34, 12,496-12,500.
    • (1995) Biochemistry , vol.34 , pp. 12496-12500
    • Akabas, M.H.1    Karlin, A.2
  • 73
    • 0031456382 scopus 로고    scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the beta-subunit
    • Zhang H. and Karlin A. (1997) Identification of acetylcholine receptor channel-lining residues in the M1 segment of the beta-subunit. Biochemistry 36, 15,856-15,864.
    • (1997) Biochemistry , vol.36 , pp. 15856-15864
    • Zhang, H.1    Karlin, A.2
  • 74
    • 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
    • Kim J. and McNamee M. G. (1998) Topological disposition of Cys 222 in the alpha-subunit of nicotinic acetylcholine receptor analyzed by fluorescence-quenching and electron paramagnetic resonance measurements. Biochemistry, 37, 4680-4686.
    • (1998) Biochemistry , vol.37 , pp. 4680-4686
    • Kim, J.1    McNamee, M.G.2
  • 75
    • 0028242326 scopus 로고
    • The transmembrane region of the nicotinic acetylcholine receptor: Is it an all-helix bundle?
    • Ortells M. O. and Lunt G. G. (1994) The transmembrane region of the nicotinic acetylcholine receptor: Is it an all-helix bundle? Receptors Channels 2, 53-59.
    • (1994) Receptors Channels , vol.2 , pp. 53-59
    • Ortells, M.O.1    Lunt, G.G.2
  • 76
    • 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 Eng 10, 511-517.
    • (1997) Protein Eng. , vol.10 , pp. 511-517
    • Ortells, M.O.1    Barrantes, G.E.2    Wood, C.3    Lunt, G.G.4    Barrantes, F.J.5
  • 78
    • 0027051415 scopus 로고
    • Photoactivatable agonist of the nicotinic acetylcholine receptor: Potential probe to characterize the structural transitions of the acetylcholine binding site in different states of the receptor
    • Chatrenet B., Kotzyba-Hibert F., Mulle C., Changeux J. P., Goeldner M. P., and Hirth C. (1992) Photoactivatable agonist of the nicotinic acetylcholine receptor: Potential probe to characterize the structural transitions of the acetylcholine binding site in different states of the receptor. Mol. Pharmacol. 41, 1100-1106.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 1100-1106
    • Chatrenet, B.1    Kotzyba-Hibert, F.2    Mulle, C.3    Changeux, J.P.4    Goeldner, M.P.5    Hirth, C.6
  • 79
    • 0029843324 scopus 로고    scopus 로고
    • Novel photoactivatable agonist of the nicotinic acetylcholine receptor of potential use for exploring the functional activated state
    • Kotzyba-Hibert F., Kessler P., Zerbib V., Bogen C., Snetkov V., Takeda K., et al. (1996) Novel photoactivatable agonist of the nicotinic acetylcholine receptor of potential use for exploring the functional activated state. J. Neurochem. 67, 2557-2565.
    • (1996) J. Neurochem. , vol.67 , pp. 2557-2565
    • Kotzyba-Hibert, F.1    Kessler, P.2    Zerbib, V.3    Bogen, C.4    Snetkov, V.5    Takeda, K.6
  • 80
    • 0030059778 scopus 로고    scopus 로고
    • Synthesis and properties of photoactivatable phospholipid derivatives designed to probe the membrane-associated domains of proteins
    • Alcaraz M. L., Peng L., Klotz P., and Goeldner M. (1996) Synthesis and properties of photoactivatable phospholipid derivatives designed to probe the membrane-associated domains of proteins. J. Org. Chem. 61, 192-201.
    • (1996) J. Org. Chem. , vol.61 , pp. 192-201
    • Alcaraz, M.L.1    Peng, L.2    Klotz, P.3    Goeldner, M.4
  • 81
    • 0031193837 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor labeled with a tritiated, photoactivatable agonist: A new tool for investigating the functional, activated state
    • Kotzyba-Hibert F., Kessler P., Zerbib V., Grutter T., Bogen C., Takeda K., et al. (1997) Nicotinic acetylcholine receptor labeled with a tritiated, photoactivatable agonist: A new tool for investigating the functional, activated state. Bioconjug. Chem. 8, 472-480.
    • (1997) Bioconjug. Chem. , vol.8 , pp. 472-480
    • Kotzyba-Hibert, F.1    Kessler, P.2    Zerbib, V.3    Grutter, T.4    Bogen, C.5    Takeda, K.6
  • 83
    • 0025202331 scopus 로고
    • Regulation of neurotransmitter receptor desensitization by protein phosphorylation
    • Huganir R. L. and Greengard P. (1990) Regulation of neurotransmitter receptor desensitization by protein phosphorylation. Neuron 5, 555-567.
    • (1990) Neuron , vol.5 , pp. 555-567
    • Huganir, R.L.1    Greengard, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.