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Volumn 32, Issue , 2003, Pages 311-334

Acetylcholine binding protein (AChBP): A secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels

Author keywords

5HT3; Cys loop; GABAA; Glycine receptor; Nicotinic acetylcholine receptor

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; ACETYLCHOLINE BINDING PROTEIN; BINDING PROTEIN; CYSTEINE; GLYCINE RECEPTOR; ION CHANNEL; NICOTINIC RECEPTOR; SEROTONIN 3 RECEPTOR; UNCLASSIFIED DRUG;

EID: 0041352143     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.32.110601.142536     Document Type: Review
Times cited : (123)

References (135)
  • 1
    • 0005994352 scopus 로고    scopus 로고
    • Properties of neuronal nicotinic acetylcholine receptors: Pharmacological characterization and modulation of synaptic function
    • Albuquerque EX, Alkondon M, Pereira EF, Castro NG, Schrattenholz A, et al. 1997. Properties of neuronal nicotinic acetylcholine receptors: pharmacological characterization and modulation of synaptic function. J. Pharmacol. Exp. Ther. 280:1117-36
    • (1997) J. Pharmacol. Exp. Ther. , vol.280 , pp. 1117-1136
    • Albuquerque, E.X.1    Alkondon, M.2    Pereira, E.F.3    Castro, N.G.4    Schrattenholz, A.5
  • 2
    • 0027787023 scopus 로고
    • GABAA receptor needs two homologous domains of the beta-subunit for activation by GABA but not by pentobarbital
    • Amin J, Weiss DS. 1993. GABAA receptor needs two homologous domains of the beta-subunit for activation by GABA but not by pentobarbital. Nature 366:565-69
    • (1993) Nature , vol.366 , pp. 565-569
    • Amin, J.1    Weiss, D.S.2
  • 3
    • 0027508383 scopus 로고
    • Reporter epitopes: A novel approach to examine transmembrane topology of integral membrane proteins applied to the alpha 1 subunit of the nicotinic acetylcholine receptor
    • Anand R, Bason L, Saedi MS, Gerzanich V, Peng X, Lindstrom J. 1993. Reporter epitopes: a novel approach to examine transmembrane topology of integral membrane proteins applied to the alpha 1 subunit of the nicotinic acetylcholine receptor. Biochemistry 32:9975-84
    • (1993) Biochemistry , vol.32 , pp. 9975-9984
    • Anand, R.1    Bason, L.2    Saedi, M.S.3    Gerzanich, V.4    Peng, X.5    Lindstrom, J.6
  • 4
    • 0034703102 scopus 로고    scopus 로고
    • Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal alpha 7-nicotinic acetylcholine receptor
    • Antil-Delbeke S, Gaillard C, Tamiya T, Corringer PJ, Changeux JP, et al. 2000. Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal alpha 7-nicotinic acetylcholine receptor. J. Biol. Chem. 275:29594-601
    • (2000) J. Biol. Chem. , vol.275 , pp. 29594-29601
    • Antil-Delbeke, S.1    Gaillard, C.2    Tamiya, T.3    Corringer, P.J.4    Changeux, J.P.5
  • 6
    • 0034212292 scopus 로고    scopus 로고
    • Localization of agonist and competitive antagonist binding sites on nicotinic acetylcholine receptors
    • Arias HR. 2000. Localization of agonist and competitive antagonist binding sites on nicotinic acetylcholine receptors. Neurochem. Int. 36:595-645
    • (2000) Neurochem. Int. , vol.36 , pp. 595-645
    • Arias, H.R.1
  • 7
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • Armstrong N, Gouaux E. 2000. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28:165-81
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 8
    • 0030912541 scopus 로고    scopus 로고
    • The alpha-bungarotoxin binding site on the nicotinic acetylcholine receptor: Analysis using a phage-epitope library
    • Balass M, Katchalski-Katzir E, Fuchs S. 1997. The alpha-bungarotoxin binding site on the nicotinic acetylcholine receptor: analysis using a phage-epitope library. Proc. Natl. Acad. Sci. USA 94:6054-58
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6054-6058
    • Balass, M.1    Katchalski-Katzir, E.2    Fuchs, S.3
  • 9
    • 0034636493 scopus 로고    scopus 로고
    • Glutamatergic synapses on oligodendrocyte precursor cells in the hippocampus
    • Bergles DE, Roberts JD, Somogyi P, Jahr CE. 2000. Glutamatergic synapses on oligodendrocyte precursor cells in the hippocampus. Nature 405:187-91
    • (2000) Nature , vol.405 , pp. 187-191
    • Bergles, D.E.1    Roberts, J.D.2    Somogyi, P.3    Jahr, C.E.4
  • 10
    • 0029143458 scopus 로고
    • Three-dimensional location of the main immunogenic region of the acetylcholine receptor
    • Beroukhim R, Unwin N. 1995. Three-dimensional location of the main immunogenic region of the acetylcholine receptor. Neuron 15:323-31
    • (1995) Neuron , vol.15 , pp. 323-331
    • Beroukhim, R.1    Unwin, N.2
  • 12
    • 0032518514 scopus 로고    scopus 로고
    • Prostaglandins stimulate calcium-dependent glutamate release in astrocytes
    • Bezzi P, Carmignoto G, Pasti L, Vesce S, Rossi D, et al. 1998. Prostaglandins stimulate calcium-dependent glutamate release in astrocytes. Nature 391:281-85
    • (1998) Nature , vol.391 , pp. 281-285
    • Bezzi, P.1    Carmignoto, G.2    Pasti, L.3    Vesce, S.4    Rossi, D.5
  • 13
    • 0035369037 scopus 로고    scopus 로고
    • A neuron-glia signalling network in the active brain
    • Bezzi P, Volterra A. 2001. A neuron-glia signalling network in the active brain. Curr. Opin. Neurobiol. 11:387-94
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 387-394
    • Bezzi, P.1    Volterra, A.2
  • 14
    • 0024725677 scopus 로고
    • Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor
    • Blount P, Merlie JP. 1989. Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor. Neuron 3:349-57
    • (1989) Neuron , vol.3 , pp. 349-357
    • Blount, P.1    Merlie, J.P.2
  • 15
    • 0030992581 scopus 로고    scopus 로고
    • Analysis of the ligand binding site of the 5-HT3 receptor using site directed mutagenesis: Importance of glutamate 106
    • Boess FG, Steward LJ, Steele JA, Liu D, Reid J, et al. 1997. Analysis of the ligand binding site of the 5-HT3 receptor using site directed mutagenesis: importance of glutamate 106. Neuropharmacology 36:637-47
    • (1997) Neuropharmacology , vol.36 , pp. 637-647
    • Boess, F.G.1    Steward, L.J.2    Steele, J.A.3    Liu, D.4    Reid, J.5
  • 16
    • 0033564411 scopus 로고    scopus 로고
    • Mapping the agonist binding site of the GABAA receptor: Evidence for a beta-strand
    • Boileau AJ, Evers AR, Davis AF, Czajkowski C. 1999. Mapping the agonist binding site of the GABAA receptor: evidence for a beta-strand. J. Neurosci. 19:4847-54
    • (1999) J. Neurosci. , vol.19 , pp. 4847-4854
    • Boileau, A.J.1    Evers, A.R.2    Davis, A.F.3    Czajkowski, C.4
  • 17
    • 0037169532 scopus 로고    scopus 로고
    • GABA(A) receptor beta 2 Tyr97 and Leu99 line the GABA-binding site. Insights into mechanisms of agonist and antagonist actions
    • Boileau AJ, Newell JG, Czajkowski C. 2002. GABA(A) receptor beta 2 Tyr97 and Leu99 line the GABA-binding site. Insights into mechanisms of agonist and antagonist actions. J. Biol. Chem. 277:2931-37
    • (2002) J. Biol. Chem. , vol.277 , pp. 2931-2937
    • Boileau, A.J.1    Newell, J.G.2    Czajkowski, C.3
  • 18
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc K, van Dijk WJ, Klaassen RV, Schuurmans M, van Der Oost J, et al. 2001. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411:269-76
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    Van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    Van Der Oost, J.5
  • 19
    • 0034724745 scopus 로고    scopus 로고
    • Hydrophobic pairwise interactions stabilize alpha-conotoxin MI in the muscle acetylcholine receptor binding site
    • Bren N, Sine SM. 2000. Hydrophobic pairwise interactions stabilize alpha-conotoxin MI in the muscle acetylcholine receptor binding site. J. Biol. Chem. 275:12692-700
    • (2000) J. Biol. Chem. , vol.275 , pp. 12692-12700
    • Bren, N.1    Sine, S.M.2
  • 20
    • 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 DC, Cohen JB. 1997. Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the Torpedo nicotinic acetylcholine receptor. J. Biol. Chem. 272:32940-50
    • (1997) J. Biol. Chem. , vol.272 , pp. 32940-32950
    • Chiara, D.C.1    Cohen, J.B.2
  • 21
    • 0033580614 scopus 로고    scopus 로고
    • Structure of the agonist-binding sites of the Torpedo nicotinic acetylcholine receptor: Affinity-labeling and mutational analyses identify gamma Tyr-111/delta Arg-113 as antagonist affinity determinants
    • Chiara DC, Xie Y, Cohen JB. 1999. Structure of the agonist-binding sites of the Torpedo nicotinic acetylcholine receptor: affinity-labeling and mutational analyses identify gamma Tyr-111/delta Arg-113 as antagonist affinity determinants. Biochemistry 38:6689-98
    • (1999) Biochemistry , vol.38 , pp. 6689-6698
    • Chiara, D.C.1    Xie, Y.2    Cohen, J.B.3
  • 22
    • 0025615542 scopus 로고
    • Modelling of binding sites of the nicotinic acetylcholine receptor and their relation to models of the whole receptor
    • Cockcroft VB, Lunt GG, Osguthorpe DJ. 1990. Modelling of binding sites of the nicotinic acetylcholine receptor and their relation to models of the whole receptor. Biochem. Soc. Symp. 57:65-79
    • (1990) Biochem. Soc. Symp. , vol.57 , pp. 65-79
    • Cockcroft, V.B.1    Lunt, G.G.2    Osguthorpe, D.J.3
  • 24
    • 0035915357 scopus 로고    scopus 로고
    • Conformational analysis of the eight-membered ring of the oxidized cysteinyl-cysteine unit implicated in nicotinic acetylcholine receptor ligand recognition
    • Creighton CJ, Reynolds CH, Lee DH, Leo GC, Reitz AB. 2001. Conformational analysis of the eight-membered ring of the oxidized cysteinyl-cysteine unit implicated in nicotinic acetylcholine receptor ligand recognition. J. Am. Chem. Soc. 123:12664-69
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12664-12669
    • Creighton, C.J.1    Reynolds, C.H.2    Lee, D.H.3    Leo, G.C.4    Reitz, A.B.5
  • 25
    • 0036607862 scopus 로고    scopus 로고
    • Anxiety over GABA(A) receptor structure relieved by AChBP
    • Cromer BA, Morton CJ, Parker MW. 2002. Anxiety over GABA(A) receptor structure relieved by AChBP. Trends Biochem. Sci. 27:280-87
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 280-287
    • Cromer, B.A.1    Morton, C.J.2    Parker, M.W.3
  • 26
    • 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, et al. 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. Genet. 6:767-74
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 767-774
    • Croxen, R.1    Newland, C.2    Beeson, D.3    Oosterhuis, H.4    Chauplannaz, G.5
  • 27
    • 0028036881 scopus 로고
    • Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans
    • Cully DF, Vassilatis DK, Liu KK, Paress PS, Van der Ploeg LH, et al. 1994. Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans. Nature 371:707-11
    • (1994) Nature , vol.371 , pp. 707-711
    • Cully, D.F.1    Vassilatis, D.K.2    Liu, K.K.3    Paress, P.S.4    Van Der Ploeg, L.H.5
  • 28
    • 0028852622 scopus 로고
    • Structure of the nicotinic receptor acetylcholine-binding site. Identification of acidic residues in the delta subunit within 0.9 nm of the 5 alpha subunit-binding
    • Czajkowski C, Karlin A. 1995. Structure of the nicotinic receptor acetylcholine-binding site. Identification of acidic residues in the delta subunit within 0.9 nm of the 5 alpha subunit-binding. J. Biol. Chem. 270:3160-64
    • (1995) J. Biol. Chem. , vol.270 , pp. 3160-3164
    • Czajkowski, C.1    Karlin, A.2
  • 29
    • 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, et al. 1988. Amino acids of the Torpedo marmorata acetylcholine receptor alpha subunit labeled by a photoaffinity ligand for the acetylcholine binding site. Biochemistry 27:2346-57
    • (1988) Biochemistry , vol.27 , pp. 2346-2357
    • Dennis, M.1    Giraudat, J.2    Kotzyba-Hibert, F.3    Goeldner, M.4    Hirth, C.5
  • 30
    • 0025675821 scopus 로고
    • Acetylcholine binding by a synthetic receptor: Implications for biological recognition
    • Dougherty DA, Stauffer DA. 1990. Acetylcholine binding by a synthetic receptor: implications for biological recognition. Science 250:1558-60
    • (1990) Science , vol.250 , pp. 1558-1560
    • Dougherty, D.A.1    Stauffer, D.A.2
  • 31
    • 0033168351 scopus 로고    scopus 로고
    • The concentration of synaptically released glutamate outside of the climbing fiber-Purkinje cell synaptic cleft
    • Dzubay JA, Jahr CE. 1999. The concentration of synaptically released glutamate outside of the climbing fiber-Purkinje cell synaptic cleft. J. Neurosci. 19:5265-74
    • (1999) J. Neurosci. , vol.19 , pp. 5265-5274
    • Dzubay, J.A.1    Jahr, C.E.2
  • 32
    • 0027772476 scopus 로고
    • Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities
    • Eisele JL, Bertrand S, Galzi JL, Devillers-Thiery A, Changeux JP, Bertrand D. 1993. Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities. Nature 366:479-83
    • (1993) Nature , vol.366 , pp. 479-483
    • Eisele, J.L.1    Bertrand, S.2    Galzi, J.L.3    Devillers-Thiery, A.4    Changeux, J.P.5    Bertrand, D.6
  • 33
    • 0028171296 scopus 로고
    • Alpha 9: An acetylcholine receptor with novel pharmacological properties expressed in rat cochlear hair cells
    • Elgoyhen AB, Johnson DS, Boulter J, Vetter DE, Heinemann S. 1994. Alpha 9: an acetylcholine receptor with novel pharmacological properties expressed in rat cochlear hair cells. Cell 79:705-15
    • (1994) Cell , vol.79 , pp. 705-715
    • Elgoyhen, A.B.1    Johnson, D.S.2    Boulter, J.3    Vetter, D.E.4    Heinemann, S.5
  • 34
    • 0033027785 scopus 로고    scopus 로고
    • Congenital myasthenic syndromes: Recent advances
    • Engel AG, Ohno K, Sine SM. 1999. Congenital myasthenic syndromes: recent advances. Arch. Neurol. 56:163-67
    • (1999) Arch. Neurol. , vol.56 , pp. 163-167
    • Engel, A.G.1    Ohno, K.2    Sine, S.M.3
  • 35
    • 0034820138 scopus 로고    scopus 로고
    • GABA(C) receptors: A molecular view
    • Enz R. 2001. GABA(C) receptors: a molecular view. Biol. Chem. 382:1111-22
    • (2001) Biol. Chem. , vol.382 , pp. 1111-1122
    • Enz, R.1
  • 36
    • 0030848730 scopus 로고    scopus 로고
    • In vitro synaptogenesis between the somata of identified Lymnaea neurons requires protein synthesis but not extrinsic growth factors or substrate adhesion molecules
    • Feng ZP, Klumperman J, Lukowiak K, Syed NI. 1997. In vitro synaptogenesis between the somata of identified Lymnaea neurons requires protein synthesis but not extrinsic growth factors or substrate adhesion molecules. J. Neurosci. 17:7839-49
    • (1997) J. Neurosci. , vol.17 , pp. 7839-7849
    • Feng, Z.P.1    Klumperman, J.2    Lukowiak, K.3    Syed, N.I.4
  • 38
    • 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 JL, Revah F, Black D, Goeldner M, Hirth C, Changeux JP. 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. 265:10430-37
    • (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
  • 39
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. 1999. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15:305-8
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 41
    • 0033811476 scopus 로고    scopus 로고
    • The extracellular linker of muscle acetylcholine receptor channels is a gating control element
    • Grosman C, Salamone FN, Sine SM, Auerbach A. 2000. The extracellular linker of muscle acetylcholine receptor channels is a gating control element. J. Gen. Physiol. 116:327-40
    • (2000) J. Gen. Physiol. , vol.116 , pp. 327-340
    • Grosman, C.1    Salamone, F.N.2    Sine, S.M.3    Auerbach, A.4
  • 42
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • Grosman C, Zhou M, Auerbach-A. 2000. Mapping the conformational wave of acetylcholine receptor channel gating. Nature 403:773-76
    • (2000) Nature , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 44
    • 0033232536 scopus 로고    scopus 로고
    • Excitatory synaptogenesis between identified Lymnaea neurons requires extrinsic trophic factors and is mediated by receptor tyrosine kinases
    • Hamakawa T, Woodin MA, Bjorgum MC, Painter SD, Takasaki M, et al. 1999. Excitatory synaptogenesis between identified Lymnaea neurons requires extrinsic trophic factors and is mediated by receptor tyrosine kinases. J. Neurosci. 19:9306-12
    • (1999) J. Neurosci. , vol.19 , pp. 9306-9312
    • Hamakawa, T.1    Woodin, M.A.2    Bjorgum, M.C.3    Painter, S.D.4    Takasaki, M.5
  • 45
    • 0034695407 scopus 로고    scopus 로고
    • Conservation of folding and stability within a protein family: The tyrosine comer as an evolutionary cul-de-sac
    • Hamill SJ, Cota E, Chothia C, Clarke J. 2000. Conservation of folding and stability within a protein family: the tyrosine comer as an evolutionary cul-de-sac. J. Mol. Biol. 295:641-49
    • (2000) J. Mol. Biol. , vol.295 , pp. 641-649
    • Hamill, S.J.1    Cota, E.2    Chothia, C.3    Clarke, J.4
  • 46
    • 0036830585 scopus 로고    scopus 로고
    • Tryptophan fluorescence reveals conformational changes in the acetylcholine binding protein
    • Hansen SB, Radic Z, Talley TT, Molles BE, Deerinck T, et al. 2002. Tryptophan fluorescence reveals conformational changes in the acetylcholine binding protein. J. Biol. Chem. 277:41299-302
    • (2002) J. Biol. Chem. , vol.277 , pp. 41299-41302
    • Hansen, S.B.1    Radic, Z.2    Talley, T.T.3    Molles, B.E.4    Deerinck, T.5
  • 47
    • 17944368301 scopus 로고    scopus 로고
    • The binding site of acetylcholine receptor as visualized in the X-ray structure of a complex between alpha-bungarotoxin and a mimotope peptide
    • Harel M, Kasher R, Nicolas A, Guss JM, Balass M, et al. 2001. The binding site of acetylcholine receptor as visualized in the X-ray structure of a complex between alpha-bungarotoxin and a mimotope peptide. Neuron 32:265-75
    • (2001) Neuron , vol.32 , pp. 265-275
    • Harel, M.1    Kasher, R.2    Nicolas, A.3    Guss, J.M.4    Balass, M.5
  • 48
    • 0027368530 scopus 로고
    • Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase
    • Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, et al. 1993. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc. Natl. Acad. Sci. USA 90:9031-35
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9031-9035
    • Harel, M.1    Schalk, I.2    Ehret-Sabatier, L.3    Bouet, F.4    Goeldner, M.5
  • 49
    • 0033812369 scopus 로고    scopus 로고
    • Two conserved arginines in the extracellular N-terminal domain of the GABA(A) receptor alpha(5) subunit are crucial for receptor function
    • Hartvig L, Lukensmejer B, Liljefors T, Dekermendjian K. 2000. Two conserved arginines in the extracellular N-terminal domain of the GABA(A) receptor alpha(5) subunit are crucial for receptor function. J. Neurochem. 75:1746-53
    • (2000) J. Neurochem. , vol.75 , pp. 1746-1753
    • Hartvig, L.1    Lukensmejer, B.2    Liljefors, T.3    Dekermendjian, K.4
  • 51
    • 0032977303 scopus 로고    scopus 로고
    • Molecular determinants of (+)-tubocurarine binding at recombinant 5-hydroxytryptamine3A receptor subunits
    • Hope AG, Belelli D, Mair ID, Lambert JJ, Peters JA. 1999. Molecular determinants of (+)-tubocurarine binding at recombinant 5-hydroxytryptamine3A receptor subunits. Mol. Pharmacol. 55:1037-43
    • (1999) Mol. Pharmacol. , vol.55 , pp. 1037-1043
    • Hope, A.G.1    Belelli, D.2    Mair, I.D.3    Lambert, J.J.4    Peters, J.A.5
  • 52
    • 2542510054 scopus 로고    scopus 로고
    • Histochemical and electrophysiological evidence for estrogen receptors on cultured astrocytes: Colocalization with cholinergic receptors
    • Hosli E, Ruhl W, Hosli L. 2000. Histochemical and electrophysiological evidence for estrogen receptors on cultured astrocytes: colocalization with cholinergic receptors. Int. J. Dev. Neurosci. 18:101-11
    • (2000) Int. J. Dev. Neurosci. , vol.18 , pp. 101-111
    • Hosli, E.1    Ruhl, W.2    Hosli, L.3
  • 53
    • 0037075542 scopus 로고    scopus 로고
    • Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynxl
    • Ibanez-Tallon I, Miwa JM, Wang HL, Adams NC, Crabtree GW, et al. 2002. Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynxl. Neuron 33:893-903
    • (2002) Neuron , vol.33 , pp. 893-903
    • Ibanez-Tallon, I.1    Miwa, J.M.2    Wang, H.L.3    Adams, N.C.4    Crabtree, G.W.5
  • 54
    • 0026628322 scopus 로고
    • Transmitter release increases intracellular calcium in perisynaptic Schwann cells in situ
    • Jahromi BS, Robitaille R, Charlton MP. 1992. Transmitter release increases intracellular calcium in perisynaptic Schwann cells in situ. Neuron 8:1069-77
    • (1992) Neuron , vol.8 , pp. 1069-1077
    • Jahromi, B.S.1    Robitaille, R.2    Charlton, M.P.3
  • 55
    • 0032247897 scopus 로고    scopus 로고
    • Astrocyte-mediated potentiation of inhibitory synaptic transmission
    • Kang J, Jiang L, Goldman SA, Nedergaard M, 1998. Astrocyte-mediated potentiation of inhibitory synaptic transmission. Nat. Neurosci. 1:683-92
    • (1998) Nat. Neurosci. , vol.1 , pp. 683-692
    • Kang, J.1    Jiang, L.2    Goldman, S.A.3    Nedergaard, M.4
  • 56
    • 0021132711 scopus 로고
    • Identification of the alpha subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site
    • Kao PN, Dwork AJ, Kaldany RR, Silver ML, Wideman J, 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. 259:11662-65
    • (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
  • 57
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • Karlin A. 2002. Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci. 3:102-14
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 58
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin A, Akabas MH. 1998. Substituted-cysteine accessibility method. Methods Enzymol. 293:123-45
    • (1998) Methods Enzymol. , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 60
    • 0015795705 scopus 로고
    • The binding of acetylcholine to receptors and its removal from the synaptic cleft
    • Katz B, Miledi R. 1973. The binding of acetylcholine to receptors and its removal from the synaptic cleft. J. Physiol. 231:549-74
    • (1973) J. Physiol. , vol.231 , pp. 549-574
    • Katz, B.1    Miledi, R.2
  • 61
    • 0019518371 scopus 로고
    • Crystalline arrays of membrane-bound acetylcholine receptor
    • Kistler J, Stroud RM. 1981. Crystalline arrays of membrane-bound acetylcholine receptor. Proc. Natl. Acad. Sci. USA 78:3678-82
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3678-3682
    • Kistler, J.1    Stroud, R.M.2
  • 62
    • 0033963862 scopus 로고    scopus 로고
    • The third-dimensional structure of the complex between an Fv antibody fragment and an analogue of the main immunogenic region of the acetylcholine receptor: A combined two-dimensional NMR, homology, and molecular modeling approach
    • Kleinjung J, Petit MC, Orlewski P, Mamalaki A, Tzartos SJ, et al. 2000. The third-dimensional structure of the complex between an Fv antibody fragment and an analogue of the main immunogenic region of the acetylcholine receptor: a combined two-dimensional NMR, homology, and molecular modeling approach. Biopolymers 53:113-28
    • (2000) Biopolymers , vol.53 , pp. 113-128
    • Kleinjung, J.1    Petit, M.C.2    Orlewski, P.3    Mamalaki, A.4    Tzartos, S.J.5
  • 63
    • 0018781849 scopus 로고
    • Immunospecific identification and three-dimensional structure of a membrane-bound acetylcholine receptor from Torpedo californica
    • Klymkowsky MW, Stroud RM. 1979. Immunospecific identification and three-dimensional structure of a membrane-bound acetylcholine receptor from Torpedo californica. J. Mol. Biol. 128:319-34
    • (1979) J. Mol. Biol. , vol.128 , pp. 319-334
    • Klymkowsky, M.W.1    Stroud, R.M.2
  • 64
    • 0016773820 scopus 로고
    • The number of transmitter molecules in a quantum: An estimate from iontophoretic application of acetylcholine at the neuromuscular synapse
    • Kuffler SW, Yoshikami D. 1975. The number of transmitter molecules in a quantum: an estimate from iontophoretic application of acetylcholine at the neuromuscular synapse. J. Physiol. 251:465-82
    • (1975) J. Physiol. , vol.251 , pp. 465-482
    • Kuffler, S.W.1    Yoshikami, D.2
  • 65
    • 0027716526 scopus 로고
    • Assembly of the inhibitory glycine receptor: Identification of amino acid sequence motifs governing subunit stoichiometry
    • Kuhse J, Lanbe B, Magalei D, Betz H. 1993. Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry. Neuron 11:1049-56
    • (1993) Neuron , vol.11 , pp. 1049-1056
    • Kuhse, J.1    Lanbe, B.2    Magalei, D.3    Betz, H.4
  • 66
    • 0033216110 scopus 로고    scopus 로고
    • Neuron-glia signaling via alpha(1) adrenoceptor-mediated Ca(2+) release in Bergmann glial cells in situ
    • Kulik A, Haentzsch A, Luckermann M, Reichelt W, Ballanyi K. 1999. Neuron-glia signaling via alpha(1) adrenoceptor-mediated Ca(2+) release in Bergmann glial cells in situ. J. Neurosci. 19:8401-8
    • (1999) J. Neurosci. , vol.19 , pp. 8401-8408
    • Kulik, A.1    Haentzsch, A.2    Luckermann, M.3    Reichelt, W.4    Ballanyi, K.5
  • 67
    • 0019643274 scopus 로고
    • Kinetic parameters for acetylcholine interaction in intact neuromuscular junction
    • Land BR, Salpeter EE, Salpeter MM. 1981. Kinetic parameters for acetylcholine interaction in intact neuromuscular junction. Proc. Natl. Acad. Sci. USA 78:7200-4
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7200-7204
    • Land, B.R.1    Salpeter, E.E.2    Salpeter, M.M.3
  • 68
    • 0035172258 scopus 로고    scopus 로고
    • LGICdb: The ligand-gated ion channel database
    • Le Novere N, Changeux JP. 2001. LGICdb: the ligand-gated ion channel database. Nucleic Acids Res. 29:294-95
    • (2001) Nucleic Acids Res. , vol.29 , pp. 294-295
    • Le Novere, N.1    Changeux, J.P.2
  • 69
    • 0037022640 scopus 로고    scopus 로고
    • Models of the extracellular domain of the nicotinic receptors and of agonist- and Ca2+-binding sites
    • Le Novere N, Grutter T, Changeux JP. 2002. Models of the extracellular domain of the nicotinic receptors and of agonist- and Ca2+-binding sites. Proc. Natl. Acad. Sci. USA 99:3210-15
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3210-3215
    • Le Novere, N.1    Grutter, T.2    Changeux, J.P.3
  • 70
    • 0034973097 scopus 로고    scopus 로고
    • The glycinergic inhibitory synapse
    • Legendre P. 2001. The glycinergic inhibitory synapse. Cell Mol. Life Sci. 58:760-93
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 760-793
    • Legendre, P.1
  • 71
    • 0034065330 scopus 로고    scopus 로고
    • Acetylcholine receptors and myasthenia
    • Lindstrom JM. 2000. Acetylcholine receptors and myasthenia. Muscle Nerve 23:453-77
    • (2000) Muscle Nerve , vol.23 , pp. 453-477
    • Lindstrom, J.M.1
  • 72
    • 0022943266 scopus 로고
    • The crystal structure of α-bungarotoxin and its relation to solution structure and binding to AcCh receptor
    • Lover RA, Stroud RM. 1986. The crystal structure of α-bungarotoxin and its relation to solution structure and binding to AcCh receptor. Protein Eng. 1:37-46
    • (1986) Protein Eng. , vol.1 , pp. 37-46
    • Lover, R.A.1    Stroud, R.M.2
  • 74
    • 0029114531 scopus 로고
    • Photolabeling reveals the proximity of the alpha-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor
    • Macbold J, Utkin Y, Kirscb D, Kaufmann R, Tsetlin V, Hucho F. 1995. Photolabeling reveals the proximity of the alpha-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. USA 92:7282-86
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7282-7286
    • Macbold, J.1    Utkin, Y.2    Kirscb, D.3    Kaufmann, R.4    Tsetlin, V.5    Hucho, F.6
  • 75
    • 0028807762 scopus 로고
    • The bandedness of the subunit arrangement of the nicotinic acetylcholine receptor from Torpedo californica
    • Macbold J, Weise C, Utkin Y, Tsetlin V, Hucho F. 1995. The bandedness of the subunit arrangement of the nicotinic acetylcholine receptor from Torpedo californica. Eur. J. Biochem. 234:427-30
    • (1995) Eur. J. Biochem. , vol.234 , pp. 427-430
    • Macbold, J.1    Weise, C.2    Utkin, Y.3    Tsetlin, V.4    Hucho, F.5
  • 76
    • 0034732104 scopus 로고    scopus 로고
    • Allosteric modulation of nicotinic acetylcholine receptors as a treatment strategy for Alzheimer's disease
    • Maelicke A, Albuquerque EX. 2000. Allosteric modulation of nicotinic acetylcholine receptors as a treatment strategy for Alzheimer's disease. Eur. J. Pharmacol. 393:165-70
    • (2000) Eur. J. Pharmacol. , vol.393 , pp. 165-170
    • Maelicke, A.1    Albuquerque, E.X.2
  • 77
    • 0034687756 scopus 로고    scopus 로고
    • Orientation of alpba-neurotoxin at the subunit interfaces of the nicotinic acetylcholine receptor
    • Malany S, Osaka H, Sine SM, Taylor P. 2000. Orientation of alpba-neurotoxin at the subunit interfaces of the nicotinic acetylcholine receptor. Biochemistry 39:15388-98
    • (2000) Biochemistry , vol.39 , pp. 15388-15398
    • Malany, S.1    Osaka, H.2    Sine, S.M.3    Taylor, P.4
  • 78
    • 0032970572 scopus 로고    scopus 로고
    • Molecular diversity of neuronal nicotinic acetylcholine receptors
    • McGebee DS. 1999. Molecular diversity of neuronal nicotinic acetylcholine receptors. Ann. NY Acad. Sci. 868:565-77
    • (1999) Ann. NY Acad. Sci. , vol.868 , pp. 565-577
    • McGebee, D.S.1
  • 79
    • 0032881372 scopus 로고    scopus 로고
    • Conus peptides targeted to specific nicotinic acetylcholine receptor subtypes
    • McIntosb JM, Santos AD, Olivera BM. 1999. Conus peptides targeted to specific nicotinic acetylcholine receptor subtypes. Annu. Rev. Biochem. 68:59-88
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 59-88
    • McIntosb, J.M.1    Santos, A.D.2    Olivera, B.M.3
  • 80
    • 0033136270 scopus 로고    scopus 로고
    • lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS
    • Miwa JM, Ibanez-Tallon I, Crabtree GW, Sancbez R, Sali A, et al. 1999. lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS. Neuron 23:105-14
    • (1999) Neuron , vol.23 , pp. 105-114
    • Miwa, J.M.1    Ibanez-Tallon, I.2    Crabtree, G.W.3    Sancbez, R.4    Sali, A.5
  • 81
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 Å resolution: Transverse tunnels in the channel wall
    • Miyazawa A, Fujiyoshi Y, Stowell M, Unwin N. 1999. Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse tunnels in the channel wall. J. Mol. Biol. 288:765-86
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 82
    • 0032990485 scopus 로고    scopus 로고
    • Identification of a domain affecting agonist potency of meta-chlorophenylbiguanide in 5-HT3 receptors
    • Mochizuki S, Miyake A, Furuichi K. 1999. Identification of a domain affecting agonist potency of meta-chlorophenylbiguanide in 5-HT3 receptors. Eur. J. Pharmacol. 369:125-32
    • (1999) Eur. J. Pharmacol. , vol.369 , pp. 125-132
    • Mochizuki, S.1    Miyake, A.2    Furuichi, K.3
  • 83
    • 0037023750 scopus 로고    scopus 로고
    • NMR structural analysis of alpha-bungarotoxin and its complex with the principal alpha-neurotoxin-binding sequence on the alpha 7 subunit of a neuronal nicotinic acetylcholine receptor
    • Moise L, Piserchio A, Basus VJ, Hawrot E. 2002. NMR structural analysis of alpha-bungarotoxin and its complex with the principal alpha-neurotoxin-binding sequence on the alpha 7 subunit of a neuronal nicotinic acetylcholine receptor. J. Biol. Chem. 277:12406-17
    • (2002) J. Biol. Chem. , vol.277 , pp. 12406-12417
    • Moise, L.1    Piserchio, A.2    Basus, V.J.3    Hawrot, E.4
  • 84
    • 0037085479 scopus 로고    scopus 로고
    • Identification of residues at the alpha and epsilon subunit interfaces mediating species selectivity of Waglerin-1 for nicotinic acetylcholine receptors
    • Molles BE, Rezai P, Kline EF, McArdle JJ, Sine SM, Taylor P. 2002. Identification of residues at the alpha and epsilon subunit interfaces mediating species selectivity of Waglerin-1 for nicotinic acetylcholine receptors. J. Biol. Chem. 277:5433-40
    • (2002) J. Biol. Chem. , vol.277 , pp. 5433-5440
    • Molles, B.E.1    Rezai, P.2    Kline, E.F.3    McArdle, J.J.4    Sine, S.M.5    Taylor, P.6
  • 85
    • 0037172669 scopus 로고    scopus 로고
    • Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site
    • Molles BE, Tsigelny I, Nguyen PD, Gao SX, Sine SM, Taylor P. 2002. Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site. Biochemistry 41:7895-906
    • (2002) Biochemistry , vol.41 , pp. 7895-7906
    • Molles, B.E.1    Tsigelny, I.2    Nguyen, P.D.3    Gao, S.X.4    Sine, S.M.5    Taylor, P.6
  • 86
    • 0343203033 scopus 로고
    • Analysis of ligand binding to the synthetic dodecapeptide 185-196 of the acetylcholine receptor alpha subunit
    • Neumann D, Barchan D, Fridkin M, Fuchs S. 1986. Analysis of ligand binding to the synthetic dodecapeptide 185-196 of the acetylcholine receptor alpha subunit. Proc. Natl. Acad. Sci. USA 83:9250-53
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9250-9253
    • Neumann, D.1    Barchan, D.2    Fridkin, M.3    Fuchs, S.4
  • 87
    • 0030272707 scopus 로고    scopus 로고
    • Interactions of glycine and strychnine with their receptor recognition sites in mouse spinal cord
    • O'Connor V, Phelan PP, Fry JP. 1996. Interactions of glycine and strychnine with their receptor recognition sites in mouse spinal cord. Neurochem. Int. 29:423-34
    • (1996) Neurochem. Int. , vol.29 , pp. 423-434
    • O'Connor, V.1    Phelan, P.P.2    Fry, J.P.3
  • 88
    • 15844429136 scopus 로고    scopus 로고
    • Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor epsilon subunit
    • Ohno K, Wang HL, Milone M, Bren N, Brengman JM, et al. 1996. Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor epsilon subunit. Neuron 17:157-70
    • (1996) Neuron , vol.17 , pp. 157-170
    • Ohno, K.1    Wang, H.L.2    Milone, M.3    Bren, N.4    Brengman, J.M.5
  • 89
    • 0030424262 scopus 로고    scopus 로고
    • Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (M/R) decapeptide and the antibody-bound [A76]MIR analogue: A molecular dynamics simulation from two-dimensional NMR data
    • Orlewski P, Marraud M, Cung MT, Tsikaris V, Sakarellos-Daitsiotis M, et al. 1996. Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (M/R) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data. Biopolymers 40:419-32
    • (1996) Biopolymers , vol.40 , pp. 419-432
    • Orlewski, P.1    Marraud, M.2    Cung, M.T.3    Tsikaris, V.4    Sakarellos-Daitsiotis, M.5
  • 90
    • 0028796049 scopus 로고
    • Evolutionary history of the ligand-gated ion-channel superfamily of receptors
    • Ortells MO, Lunt GG. 1995. Evolutionary history of the ligand-gated ion-channel superfamily of receptors. Trends Neurosci. 18:121-27
    • (1995) Trends Neurosci. , vol.18 , pp. 121-127
    • Ortells, M.O.1    Lunt, G.G.2
  • 91
    • 0033515532 scopus 로고    scopus 로고
    • Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor
    • Osaka H, Malany S, Kanter JR, Sine SM, Taylor P. 1999. Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor. J. Biol. Chem. 274:9581-86
    • (1999) J. Biol. Chem. , vol.274 , pp. 9581-9586
    • Osaka, H.1    Malany, S.2    Kanter, J.R.3    Sine, S.M.4    Taylor, P.5
  • 93
    • 0025308169 scopus 로고
    • d-Tubocurarine binding sites are located at alpha-gamma and alpha-delta subunit interfaces of the nicotinic acetylcholine receptor
    • Pedersen SE, Cohen JB. 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 87:2785-89
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2785-2789
    • Pedersen, S.E.1    Cohen, J.B.2
  • 94
    • 0034826222 scopus 로고    scopus 로고
    • Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies
    • Poulas K, Eliopoulos E, Vatzaki E, Navaza J, Kontou M, et al. 2001. Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies. Eur. J. Biochem. 268:3685-93
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3685-3693
    • Poulas, K.1    Eliopoulos, E.2    Vatzaki, E.3    Navaza, J.4    Kontou, M.5
  • 95
    • 0029958548 scopus 로고    scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor. Identification of residues that determine agonist selectivity
    • Prince RJ, Sine SM. 1996. Molecular dissection of subunit interfaces in the acetylcholine receptor. Identification of residues that determine agonist selectivity. J. Biol. Chem. 271:25770-77
    • (1996) J. Biol. Chem. , vol.271 , pp. 25770-25777
    • Prince, R.J.1    Sine, S.M.2
  • 96
    • 0033538459 scopus 로고    scopus 로고
    • Pairwise interactions between neuronal alpha7 acetylcholine receptors and alpha-conotoxin ImI
    • Quiram PA, Jones JJ, Sine SM. 1999. Pairwise interactions between neuronal alpha7 acetylcholine receptors and alpha-conotoxin ImI. J. Biol. Chem. 274:19517-24
    • (1999) J. Biol. Chem. , vol.274 , pp. 19517-19524
    • Quiram, P.A.1    Jones, J.J.2    Sine, S.M.3
  • 97
    • 0036117729 scopus 로고    scopus 로고
    • The molecular basis of the structure and function of the 5-HT3 receptor: A model ligand-gated ion channel
    • Reeves DC, Lummis SC. 2002. The molecular basis of the structure and function of the 5-HT3 receptor: a model ligand-gated ion channel (review). Mol. Membr. Biol. 19:11-26
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 11-26
    • Reeves, D.C.1    Lummis, S.C.2
  • 98
    • 0032191867 scopus 로고    scopus 로고
    • Modulation of synaptic efficacy and synaptic depression by glial cells at the frog neuromuscular junction
    • Robitaille R. 1998. Modulation of synaptic efficacy and synaptic depression by glial cells at the frog neuromuscular junction. Neuron 21:847-55
    • (1998) Neuron , vol.21 , pp. 847-855
    • Robitaille, R.1
  • 99
    • 0030702069 scopus 로고    scopus 로고
    • Muscarinic Ca2+ responses resistant to muscarinic antagonists at perisynaptic Schwann cells of the frog neuromuscular junction
    • Robitaille R, Jahromi BS, Charlton MP. 1997. Muscarinic Ca2+ responses resistant to muscarinic antagonists at perisynaptic Schwann cells of the frog neuromuscular junction. J. Physiol. 504:337-47
    • (1997) J. Physiol. , vol.504 , pp. 337-347
    • Robitaille, R.1    Jahromi, B.S.2    Charlton, M.P.3
  • 100
    • 0035071458 scopus 로고    scopus 로고
    • Neuronal nicotinic acetylcholine receptor expression by O2A/oligodendrocyte progenitor cells
    • Rogers SW, Gregori NZ, Carlson N, Gahring LC, Noble M. 2001. Neuronal nicotinic acetylcholine receptor expression by O2A/oligodendrocyte progenitor cells. Glia 33:306-13
    • (2001) Glia , vol.33 , pp. 306-313
    • Rogers, S.W.1    Gregori, N.Z.2    Carlson, N.3    Gahring, L.C.4    Noble, M.5
  • 101
    • 0028333002 scopus 로고
    • A missense mutation in the gene encoding the alpha 1 subunit of the inhibitory glycine receptor in the spasmodic mouse
    • Ryan SG, Buckwalter MS, Lynch JW, Handford CA, Segura L, et al. 1994. A missense mutation in the gene encoding the alpha 1 subunit of the inhibitory glycine receptor in the spasmodic mouse. Nat. Genet. 7:131-35
    • (1994) Nat. Genet. , vol.7 , pp. 131-135
    • Ryan, S.G.1    Buckwalter, M.S.2    Lynch, J.W.3    Handford, C.A.4    Segura, L.5
  • 102
    • 0033227472 scopus 로고    scopus 로고
    • A protein from the salivary glands of the giant Amazon leech with high sequence homology to a nicotinic acetylcholine receptor subunit
    • Salgueiro S, Potts S, McIlgorm EA, Ansell KH, Hemberger J, Gussow D. 1999. A protein from the salivary glands of the giant Amazon leech with high sequence homology to a nicotinic acetylcholine receptor subunit. Z. Naturforsch. 54:963-71
    • (1999) Z. Naturforsch. , vol.54 , pp. 963-971
    • Salgueiro, S.1    Potts, S.2    McIlgorm, E.A.3    Ansell, K.H.4    Hemberger, J.5    Gussow, D.6
  • 103
    • 0002315013 scopus 로고    scopus 로고
    • Structural model of nicotinic acetylcholine receptor isotypes bound to acetylcholine and nicotine
    • Schapira M, Abagyan R, Totrov M. 2002. Structural model of nicotinic acetylcholine receptor isotypes bound to acetylcholine and nicotine. BMC Struct. Biol. 2:1
    • (2002) BMC Struct. Biol. , vol.2 , pp. 1
    • Schapira, M.1    Abagyan, R.2    Totrov, M.3
  • 104
    • 0027424165 scopus 로고
    • Mutation of glycine receptor subunit creates beta-alanine receptor responsive to GABA
    • Schmieden V, Kuhse J, Betz H. 1993. Mutation of glycine receptor subunit creates beta-alanine receptor responsive to GABA. Science 262:256-58
    • (1993) Science , vol.262 , pp. 256-258
    • Schmieden, V.1    Kuhse, J.2    Betz, H.3
  • 105
    • 0032868182 scopus 로고    scopus 로고
    • A novel domain of the inhibitory glycine receptor determining antagonist efficacies: Further evidence for partial agonism resuiting from self-inhibition
    • Schmieden V, Kuhse J, Betz H. 1999. A novel domain of the inhibitory glycine receptor determining antagonist efficacies: further evidence for partial agonism resuiting from self-inhibition. Mol. Pharmacol. 56:464-72
    • (1999) Mol. Pharmacol. , vol.56 , pp. 464-472
    • Schmieden, V.1    Kuhse, J.2    Betz, H.3
  • 106
    • 0027418871 scopus 로고
    • Biochemical characterization of a novel channel-activating site on nicotinic acetylcholine receptors
    • Schrattenholz A, Coban T, Schroder B, Okonjo KO, Kuhlmann J, et al. 1993. Biochemical characterization of a novel channel-activating site on nicotinic acetylcholine receptors. J. Recept. Res. 13:393-412
    • (1993) J. Recept. Res. , vol.13 , pp. 393-412
    • Schrattenholz, A.1    Coban, T.2    Schroder, B.3    Okonjo, K.O.4    Kuhlmann, J.5
  • 108
    • 0026607902 scopus 로고
    • Point mutations affecting antagonist affinity and agonist dependent gating of GABAA receptor channels
    • Sigel E, Baur R, Kellenberger S, Malherbe P. 1992. Point mutations affecting antagonist affinity and agonist dependent gating of GABAA receptor channels. EMBO J. 11:2017-23
    • (1992) EMBO J. , vol.11 , pp. 2017-2023
    • Sigel, E.1    Baur, R.2    Kellenberger, S.3    Malherbe, P.4
  • 109
    • 0030813536 scopus 로고    scopus 로고
    • Identification of equivalent residues in the gamma, delta, and epsilon subunits of the nicotinic receptor that contribute to alpha-bungarotoxin binding
    • Sine SM. 1997. Identification of equivalent residues in the gamma, delta, and epsilon subunits of the nicotinic receptor that contribute to alpha-bungarotoxin binding. J. Biol. Chem. 272:23521-27
    • (1997) J. Biol. Chem. , vol.272 , pp. 23521-23527
    • Sine, S.M.1
  • 110
    • 0026045588 scopus 로고
    • Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor
    • Sine SM, Claudio T. 1991. Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor. J. Biol. Chem. 266:19369-77
    • (1991) J. Biol. Chem. , vol.266 , pp. 19369-19377
    • Sine, S.M.1    Claudio, T.2
  • 111
    • 0029085766 scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of determinants of alpha-conotoxin M1 selectivity
    • Sine SM, Kreienkamp HJ, Bren N, Maeda R, Taylor P. 1995. Molecular dissection of subunit interfaces in the acetylcholine receptor: identification of determinants of alpha-conotoxin M1 selectivity. Neuron 15:205-11
    • (1995) Neuron , vol.15 , pp. 205-211
    • Sine, S.M.1    Kreienkamp, H.J.2    Bren, N.3    Maeda, R.4    Taylor, P.5
  • 112
    • 0029087136 scopus 로고
    • Mutation of the acetylcholine receptor alpha subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity
    • Sine SM, Ohno K, Bouzat C, Auerbach A, Milone M, et al. 1995. Mutation of the acetylcholine receptor alpha subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity. Neuron 15:229-39
    • (1995) Neuron , vol.15 , pp. 229-239
    • Sine, S.M.1    Ohno, K.2    Bouzat, C.3    Auerbach, A.4    Milone, M.5
  • 113
    • 0028292368 scopus 로고
    • Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists
    • Sine SM, Quiram P, Papanikolaou F, Kreienkamp HJ, 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. 269:8808-16
    • (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
  • 114
    • 0037047296 scopus 로고    scopus 로고
    • Lysine scanning mutagenesis delineates structural model of the nicotinic receptor ligand binding domain
    • Sine SM, Wang HL, Bren ND. 2002. Lysine scanning mutagenesis delineates structural model of the nicotinic receptor ligand binding domain. J. Biol. Chem. 277:29210-23
    • (2002) J. Biol. Chem. , vol.277 , pp. 29210-29223
    • Sine, S.M.1    Wang, H.L.2    Bren, N.D.3
  • 115
    • 0035902187 scopus 로고    scopus 로고
    • A glia-derived acetylcholine-binding protein that modulates synaptic transmission
    • Smit AB, Syed NI, Schaap D, van Minnen J, Klumperman J, et al. 2001. A glia-derived acetylcholine-binding protein that modulates synaptic transmission. Nature 411:261-68
    • (2001) Nature , vol.411 , pp. 261-268
    • Smit, A.B.1    Syed, N.I.2    Schaap, D.3    Van Minnen, J.4    Klumperman, J.5
  • 116
    • 0034102071 scopus 로고    scopus 로고
    • The role of tryptophan residues in the 5-hydroxytryptamine(3) receptor ligand binding domain
    • Spier AD, Lummis SC. 2000. The role of tryptophan residues in the 5-hydroxytryptamine(3) receptor ligand binding domain. J. Biol. Chem. 275:5620-25
    • (2000) J. Biol. Chem. , vol.275 , pp. 5620-5625
    • Spier, A.D.1    Lummis, S.C.2
  • 117
    • 0034084247 scopus 로고    scopus 로고
    • Importance of phenylalanine 107 in agonist recognition by the 5-hydroxytryptamine(3A) receptor
    • Steward LJ, Boess FG, Steele JA, Liu D, Wong N, Martin IL. 2000. Importance of phenylalanine 107 in agonist recognition by the 5-hydroxytryptamine(3A) receptor. Mol. Pharmacol. 57:1249-55
    • (2000) Mol. Pharmacol. , vol.57 , pp. 1249-1255
    • Steward, L.J.1    Boess, F.G.2    Steele, J.A.3    Liu, D.4    Wong, N.5    Martin, I.L.6
  • 118
    • 0036151496 scopus 로고    scopus 로고
    • Mapping the agonist binding site of the nicotinic acetylcholine receptor by cysteine scanning mutagenesis: Antagonist footprint and secondary structure prediction
    • Sullivan D, Chiara DC, Cohen JB. 2002. Mapping the agonist binding site of the nicotinic acetylcholine receptor by cysteine scanning mutagenesis: antagonist footprint and secondary structure prediction. Mol. Pharmacol. 61:463-72
    • (2002) Mol. Pharmacol. , vol.61 , pp. 463-472
    • Sullivan, D.1    Chiara, D.C.2    Cohen, J.B.3
  • 119
    • 0027370656 scopus 로고
    • Activity-dependent neuronal-glial and synaptic plasticity in the adult mammalian hypothalamus
    • Theodosis DT, Poulain DA. 1993. Activity-dependent neuronal-glial and synaptic plasticity in the adult mammalian hypothalamus. Neuroscience 57:501-35
    • (1993) Neuroscience , vol.57 , pp. 501-535
    • Theodosis, D.T.1    Poulain, D.A.2
  • 120
    • 0021092912 scopus 로고
    • High affinity binding of alpha-bungarotoxin to the purified alpha-subunit and to its 27,000-dalton proteolytic peptide from Torpedo marmorata acetylcholine receptor. Requirement for sodium dodecyl sulfate
    • Tzartos SJ, Changeux JP. 1983. High affinity binding of alpha-bungarotoxin to the purified alpha-subunit and to its 27,000-dalton proteolytic peptide from Torpedo marmorata acetylcholine receptor. Requirement for sodium dodecyl sulfate. EMBO J. 2:381-87
    • (1983) EMBO J. , vol.2 , pp. 381-387
    • Tzartos, S.J.1    Changeux, J.P.2
  • 121
    • 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
  • 122
    • 0036304564 scopus 로고    scopus 로고
    • Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the alpha subunits
    • Unwin N, Miyazawa A, Li J, Fujiyoshi Y. 2002. Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the alpha subunits. J. Mol. Biol. 319:1165-76
    • (2002) J. Mol. Biol. , vol.319 , pp. 1165-1176
    • Unwin, N.1    Miyazawa, A.2    Li, J.3    Fujiyoshi, Y.4
  • 123
    • 0032692626 scopus 로고    scopus 로고
    • Identification of a new ligand binding domain in the alphal subunit of the inhibitory glycine receptor
    • Vafa B, Lewis TM, Cunningham AM, Jacques P, Lynch JW, Schofield PR. 1999. Identification of a new ligand binding domain in the alphal subunit of the inhibitory glycine receptor. J. Neurochem. 73:2158-66
    • (1999) J. Neurochem. , vol.73 , pp. 2158-2166
    • Vafa, B.1    Lewis, T.M.2    Cunningham, A.M.3    Jacques, P.4    Lynch, J.W.5    Schofield, P.R.6
  • 124
    • 0031613616 scopus 로고    scopus 로고
    • Heritable mutations in the glycine, GABAA, and nicotinic acetylcholine receptors provide new insights into the ligand-gated ion channel receptor superfamily
    • Vafa B, Schofield PR. 1998. Heritable mutations in the glycine, GABAA, and nicotinic acetylcholine receptors provide new insights into the ligand-gated ion channel receptor superfamily. Int. Rev. Neurobiol. 42:285-32
    • (1998) Int. Rev. Neurobiol. , vol.42 , pp. 285-332
    • Vafa, B.1    Schofield, P.R.2
  • 125
    • 0026536645 scopus 로고
    • Antagonism of ligand-gated ion channel receptors: Two domains of the glycine receptor alpha subunit form the strychnine-binding site
    • Vandenberg RJ, French CR, Barry PH, Shine J, Schofield PR. 1992. Antagonism of ligand-gated ion channel receptors: two domains of the glycine receptor alpha subunit form the strychnine-binding site. Proc. Natl. Acad. Sci. USA 89:1765-69
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1765-1769
    • Vandenberg, R.J.1    French, C.R.2    Barry, P.H.3    Shine, J.4    Schofield, P.R.5
  • 126
    • 0026787189 scopus 로고
    • Distinct agonist- and antagonist-binding sites on the glycine receptor
    • Vandenberg RJ, Handford CA, Schofield PR. 1992. Distinct agonist- and antagonist-binding sites on the glycine receptor. Neuron 9:491-96
    • (1992) Neuron , vol.9 , pp. 491-496
    • Vandenberg, R.J.1    Handford, C.A.2    Schofield, P.R.3
  • 129
    • 0035141668 scopus 로고    scopus 로고
    • Structure and dynamics of the ABA binding pocket: A narrowing cleft that constricts during activation
    • Wagner DA, Czajkowski C. 2001. Structure and dynamics of the ABA binding pocket: a narrowing cleft that constricts during activation. J. Neurosci. 21:67-74
    • (2001) J. Neurosci. , vol.21 , pp. 67-74
    • Wagner, D.A.1    Czajkowski, C.2
  • 130
    • 0018772249 scopus 로고
    • Numerical reconstruction of the quantal event at nicotinic synapses
    • Wathey JC, Nass MM, Lester HA. 1979. Numerical reconstruction of the quantal event at nicotinic synapses. Biophys. J. 27:145-64
    • (1979) Biophys. J. , vol.27 , pp. 145-164
    • Wathey, J.C.1    Nass, M.M.2    Lester, H.A.3
  • 131
    • 0032865776 scopus 로고    scopus 로고
    • Trophic factor-induced plasticity of synaptic connections between identified Lymnaea neurons
    • Woodin MA, Hamakawa T, Takasaki M, Lukowiak K, Syed NI. 1999. Trophic factor-induced plasticity of synaptic connections between identified Lymnaea neurons. Learn Mem. 6:307-16
    • (1999) Learn Mem. , vol.6 , pp. 307-316
    • Woodin, M.A.1    Hamakawa, T.2    Takasaki, M.3    Lukowiak, K.4    Syed, N.I.5
  • 132
    • 0037080004 scopus 로고    scopus 로고
    • Trophic factor-induced excitatory synaptogenesis involves postsynaptic modulation of nicotinic acetylcholine receptors
    • Woodin MA, Munno DW, Syed NI. 2002. Trophic factor-induced excitatory synaptogenesis involves postsynaptic modulation of nicotinic acetylcholine receptors. J. Neurosci. 22:505-14
    • (2002) J. Neurosci. , vol.22 , pp. 505-514
    • Woodin, M.A.1    Munno, D.W.2    Syed, N.I.3
  • 133
    • 0032004243 scopus 로고    scopus 로고
    • Interaction of D-tubocurarine analogs with the 5HT3 receptor
    • Yan D, Pedersen SE, White MM. 1998. Interaction of D-tubocurarine analogs with the 5HT3 receptor. Neuropharmacology 37:251-57
    • (1998) Neuropharmacology , vol.37 , pp. 251-257
    • Yan, D.1    Pedersen, S.E.2    White, M.M.3
  • 134
    • 0037127296 scopus 로고    scopus 로고
    • Identification of two novel Drosophila melanogaster histamine-gated chloride channel subunits expressed in the eye
    • Zheng Y, Hirschberg B, Yuan J, Wang AP, Hunt DC, et al. 2002. Identification of two novel Drosophila melanogaster histamine-gated chloride channel subunits expressed in the eye. J. Biol. Chem. 277:2000-5
    • (2002) J. Biol. Chem. , vol.277 , pp. 2000-2005
    • Zheng, Y.1    Hirschberg, B.2    Yuan, J.3    Wang, A.P.4    Hunt, D.C.5
  • 135
    • 0032514762 scopus 로고    scopus 로고
    • From ab initio quantum mechanics to molecular neurobiology: A cation-pi binding site in the nicotinic receptor
    • Zhong W, Gallivan JP, Zhang Y, Li L, Lester HA, Dougherty DA. 1998. From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor. Proc. Natl. Acad. Sci. USA 95:12088-93
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12088-12093
    • Zhong, W.1    Gallivan, J.P.2    Zhang, Y.3    Li, L.4    Lester, H.A.5    Dougherty, D.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.