메뉴 건너뛰기




Volumn 31, Issue 4, 1996, Pages 273-301

Nuclear magnetic resonance (NMR) analysis of ligand receptor interactions: The cholinergic system - A model

Author keywords

cholinergic system; ligand receptor interactions; nuclear magnetic resonance; pharmacological reagents

Indexed keywords

AMINO ACID SEQUENCE; CHOLINERGIC SYSTEM; DRUG STRUCTURE; HUMAN; LIGAND BINDING; MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; RECEPTOR BINDING; REVIEW; SPECIES DIFFERENCE;

EID: 0029742248     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.3109/10409239609106586     Document Type: Review
Times cited : (17)

References (150)
  • 1
    • 0024349141 scopus 로고
    • An analog of lophotoxin reacts covalently with Tyr-190 in the α-subunit of the nicotinic acetylcholine receptor
    • Abramson, S. N., Ying, L., Culver, P., and Taylor, P. 1989. An analog of lophotoxin reacts covalently with Tyr-190 in the α-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 264: 12666-12672.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12666-12672
    • Abramson, S.N.1    Ying, L.2    Culver, P.3    Taylor, P.4
  • 2
    • 0025885159 scopus 로고
    • Structure/activity and molecular modeling studies of the lophotoxin family of irreversible nicotinic receptor antagonists
    • Abramson, S. N., Trischman, J. A., Tapiolas, D. M., Harold, E. E., Fenical, W., and Taylor, P. 1991. Structure/activity and molecular modeling studies of the lophotoxin family of irreversible nicotinic receptor antagonists. J. Med. Chem. 34: 1798-1804.
    • (1991) J. Med. Chem. , vol.34 , pp. 1798-1804
    • Abramson, S.N.1    Trischman, J.A.2    Tapiolas, D.M.3    Harold, E.E.4    Fenical, W.5    Taylor, P.6
  • 3
    • 0002860359 scopus 로고
    • The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins
    • Albrand, J. P., Birdsall, B., Feeney, J., Roberts, G. C. K., and Burgen, A. S. V. 1979. The use of transferred nuclear Overhauser effects in the study of the conformations of small molecules bound to proteins. Int. J. Biol. Macromolecules 1: 37-41.
    • (1979) Int. J. Biol. Macromolecules , vol.1 , pp. 37-41
    • Albrand, J.P.1    Birdsall, B.2    Feeney, J.3    Roberts, G.C.K.4    Burgen, A.S.V.5
  • 4
    • 0024566913 scopus 로고
    • Interactions of antibody aromatic residues with a peptide of cholera toxin observed by two-dimensional transferred nuclear Overhauser effect difference spectroscopy
    • Anglister, J., Levy, R. H., and Scherf, T. 1990. Interactions of antibody aromatic residues with a peptide of cholera toxin observed by two-dimensional transferred nuclear Overhauser effect difference spectroscopy. Biochemistry 28: 3360-3365.
    • (1990) Biochemistry , vol.28 , pp. 3360-3365
    • Anglister, J.1    Levy, R.H.2    Scherf, T.3
  • 5
    • 0023710297 scopus 로고
    • Characterization of the binding site of α-bungarotoxin to bacterially expressed cholinergic binding sites
    • Aronheim, A., Eshel, Y., Mosckovitz, R., and Gershoni, J. M. 1988. Characterization of the binding site of α-bungarotoxin to bacterially expressed cholinergic binding sites. J. Biol. Chem. 263: 9933-9937.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9933-9937
    • Aronheim, A.1    Eshel, Y.2    Mosckovitz, R.3    Gershoni, J.M.4
  • 6
    • 0027308749 scopus 로고
    • A Raman spectroscopic study of acetylcholine receptor-rich membranes from Torpedo marmorata. Interaction of the receptor with carbamylcholine and (+)-tubocurarine
    • Aslanian, D., Grof, P., Galzi, J.-L., and Changeux, J.-P. 1993. A Raman spectroscopic study of acetylcholine receptor-rich membranes from Torpedo marmorata. Interaction of the receptor with carbamylcholine and (+)-tubocurarine. Biochim. Biophys. Acta 1148: 291-302.
    • (1993) Biochim. Biophys. Acta , vol.1148 , pp. 291-302
    • Aslanian, D.1    Grof, P.2    Galzi, J.-L.3    Changeux, J.-P.4
  • 7
    • 0028246033 scopus 로고
    • Ligand-receptor interactions in the nicotinic acetylcholine receptor probed using multiple substitutions at conserved tyrosines on the α subunit
    • Aylwin, M. L. and White, M. M. 1994. Ligand-receptor interactions in the nicotinic acetylcholine receptor probed using multiple substitutions at conserved tyrosines on the α subunit. FEBS Lett. 349: 99-103.
    • (1994) FEBS Lett. , vol.349 , pp. 99-103
    • Aylwin, M.L.1    White, M.M.2
  • 8
    • 0027190929 scopus 로고
    • Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: Evidence for specific protein structural changes upon desensitization
    • Baenziger, J. E., Miller, K. W., and Rothschild, K. J. 1993. Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: evidence for specific protein structural changes upon desensitization. Biochemistry 32: 5448-5454.
    • (1993) Biochemistry , vol.32 , pp. 5448-5454
    • Baenziger, J.E.1    Miller, K.W.2    Rothschild, K.J.3
  • 9
    • 0023931440 scopus 로고
    • Regulation of acetylcholine receptor transcript expression during development of enopus laevis
    • Baldwin, T. J., Yoshihara, C. M., Blackmer, K., Kinter, C. R., and Burden, S. J. 1988. Regulation of acetylcholine receptor transcript expression during development of enopus laevis. J. Cell Biol. 106: 469-478.
    • (1988) J. Cell Biol. , vol.106 , pp. 469-478
    • Baldwin, T.J.1    Yoshihara, C.M.2    Blackmer, K.3    Kinter, C.R.4    Burden, S.J.5
  • 10
    • 0020996120 scopus 로고
    • Genomic sequences encoding the α-subunit of acetylcholine receptor are conserved in evolution
    • Ballivet, M., Nef, P., Standler, R., and Fulpius, B. 1983. Genomic sequences encoding the α-subunit of acetylcholine receptor are conserved in evolution. Cold Spring Harbor Quant. Biol. 48: 83-87.
    • (1983) Cold Spring Harbor Quant. Biol. , vol.48 , pp. 83-87
    • Ballivet, M.1    Nef, P.2    Standler, R.3    Fulpius, B.4
  • 11
    • 0024459812 scopus 로고
    • Three-dimensional solution structure of a DNA duplex containing the Bcl I restriction sequence: Two-dimensional NMR studies, distance geometry calculations, and refinement by back-calculation of the NOESY spectrum
    • Banks, K. M., Hare, D. R., and Reid, B. R. 1989. Three-dimensional solution structure of a DNA duplex containing the Bcl I restriction sequence: two-dimensional NMR studies, distance geometry calculations, and refinement by back-calculation of the NOESY spectrum. Biochemistry 28: 6996-7010.
    • (1989) Biochemistry , vol.28 , pp. 6996-7010
    • Banks, K.M.1    Hare, D.R.2    Reid, B.R.3
  • 12
    • 0029111629 scopus 로고
    • The binding site of the nicotinic acetylcholine receptor in animal species resistant to α-bungarotoxin
    • Barchan, D., Ovadia, M., Kochva, E., and Fuchs, S. 1995. The binding site of the nicotinic acetylcholine receptor in animal species resistant to α-bungarotoxin. Biochemistry 34: 9172-9176.
    • (1995) Biochemistry , vol.34 , pp. 9172-9176
    • Barchan, D.1    Ovadia, M.2    Kochva, E.3    Fuchs, S.4
  • 13
    • 0023108720 scopus 로고
    • Mapping the main immunogenic region and toxin-binding site of the nicotinic acetylcholine receptor
    • Barkas, T., Mauron, A., Roth, B., Alliod, C., Tzartos, S. J., and Ballivet, M. 1987. Mapping the main immunogenic region and toxin-binding site of the nicotinic acetylcholine receptor. Science 235: 77-80.
    • (1987) Science , vol.235 , pp. 77-80
    • Barkas, T.1    Mauron, A.2    Roth, B.3    Alliod, C.4    Tzartos, S.J.5    Ballivet, M.6
  • 14
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax, A. and Davis, D. 1985. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63: 207-213.
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.2
  • 15
    • 0014934202 scopus 로고
    • Structure and activity of acetylcholine
    • Beers, W. H. and Reich, E. 1970. Structure and activity of acetylcholine. Nature 228: 917-922.
    • (1970) Nature , vol.228 , pp. 917-922
    • Beers, W.H.1    Reich, E.2
  • 16
    • 0023923826 scopus 로고
    • Measuring relative acetylcholine receptor agonist binding by selective proton nuclear magnetic resonance relaxation experiments
    • Behling, R. W., Yamane, T., Navon, G., Sammon, M. J., and Jelinski, L. W. 1988. Measuring relative acetylcholine receptor agonist binding by selective proton nuclear magnetic resonance relaxation experiments. Biophys. J. 53: 947-954.
    • (1988) Biophys. J. , vol.53 , pp. 947-954
    • Behling, R.W.1    Yamane, T.2    Navon, G.3    Sammon, M.J.4    Jelinski, L.W.5
  • 17
    • 0008007492 scopus 로고
    • Conformation of acetylcholine bound to the nicotinic acetylcholine receptor
    • Behling, R. W., Yamane, T., Navon, G., and Jelinski, L. W. 1988a. Conformation of acetylcholine bound to the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. U.S.A. 85: 6721-6725.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 6721-6725
    • Behling, R.W.1    Yamane, T.2    Navon, G.3    Jelinski, L.W.4
  • 18
    • 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
  • 19
    • 0017841471 scopus 로고
    • Inactivation of electric eel acetylcholine esterase by acylation with N-hydroxysucciinimide esters of amino acid derivatives
    • Blumberg, S. and Silman, I. 1978. Inactivation of electric eel acetylcholine esterase by acylation with N-hydroxysucciinimide esters of amino acid derivatives. Biochemistry 17: 1125-1130.
    • (1978) Biochemistry , vol.17 , pp. 1125-1130
    • Blumberg, S.1    Silman, I.2
  • 20
    • 0000434070 scopus 로고
    • A method for constrained refinement of macromolecular structure based on two-dimensional nuclear Overhauser effect spectra
    • Borgias, B. A. and James, T. L. 1988. A method for constrained refinement of macromolecular structure based on two-dimensional nuclear Overhauser effect spectra. J. Magn. Reson. 79: 493-512.
    • (1988) J. Magn. Reson. , vol.79 , pp. 493-512
    • Borgias, B.A.1    James, T.L.2
  • 21
    • 0000425457 scopus 로고
    • MARDIGRAS - A procedure for matrix analysis of relaxation for discerning geometry of an aqueous structure
    • Borgias, B. A. and James, T. L. 1990. MARDIGRAS - a procedure for matrix analysis of relaxation for discerning geometry of an aqueous structure. J. Magn. Reson. 87: 475-487.
    • (1990) J. Magn. Reson. , vol.87 , pp. 475-487
    • Borgias, B.A.1    James, T.L.2
  • 23
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-By, A. A., Stephens, R. L., and Lee, J. 1984. Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. J. Am. Chem. Soc. 106: 811-813.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.3
  • 25
    • 0026543476 scopus 로고
    • Hapten conformation in the combining site of antibodies that bind phenylphosphocholine
    • Bruderer, U., Peyton, D. H., Barber, E., Fellman, J. H., and Rittenberg, M. B. 1992. Hapten conformation in the combining site of antibodies that bind phenylphosphocholine. Biochemistry 31: 584-589.
    • (1992) Biochemistry , vol.31 , pp. 584-589
    • Bruderer, U.1    Peyton, D.H.2    Barber, E.3    Fellman, J.H.4    Rittenberg, M.B.5
  • 26
    • 0016744342 scopus 로고
    • Acetylcholine receptors at neuromuscular synapses. Phylogenetic differences detected by snake α-neurotoxins
    • Burden, S. J., Hartzell, H. C., and Yoshikami, D. 1975. Acetylcholine receptors at neuromuscular synapses. Phylogenetic differences detected by snake α-neurotoxins. Proc. Natl. Acad. Sci. U.S.A. 72: 3245-3249.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 3245-3249
    • Burden, S.J.1    Hartzell, H.C.2    Yoshikami, D.3
  • 27
    • 0001780788 scopus 로고
    • Theoretical evaluation of the two-dimensional transferred nuclear Overhauser effect
    • Campbell, A. P. and Sykes, B. D. 1991. Theoretical evaluation of the two-dimensional transferred nuclear Overhauser effect. J. Magn. Reson. 93: 77-92.
    • (1991) J. Magn. Reson. , vol.93 , pp. 77-92
    • Campbell, A.P.1    Sykes, B.D.2
  • 28
    • 0026410049 scopus 로고
    • Interaction of troponin I and troponin C: Use of the two-dimensional nuclear magnetic resonance transferred nuclear Overhauser effect to determine the structure of the inhibitory troponin I peptide when bound to skeletal troponin C
    • Campbell, A. P. and Sykes, B. D. 1991. Interaction of troponin I and troponin C: use of the two-dimensional nuclear magnetic resonance transferred nuclear Overhauser effect to determine the structure of the inhibitory troponin I peptide when bound to skeletal troponin C. J. Mol. Biol. 222: 405-421.
    • (1991) J. Mol. Biol. , vol.222 , pp. 405-421
    • Campbell, A.P.1    Sykes, B.D.2
  • 29
    • 0014030481 scopus 로고
    • Structure of acetylcholine and other substrates of cholinergic systems
    • Canepa, F. G., Pauling, P., and Sörum, H. 1966. Structure of acetylcholine and other substrates of cholinergic systems. Nature 210: 907-909.
    • (1966) Nature , vol.210 , pp. 907-909
    • Canepa, F.G.1    Pauling, P.2    Sörum, H.3
  • 31
    • 0027057058 scopus 로고
    • The functional architecture of the nicotinic acetylcholine receptor explored by affinity labeling and site-directed mutagenesis
    • Changeux, J.-P., Galzi, J.-L., Devillers-Thiéry, A., and Bertrand, D. 1992. The functional architecture of the nicotinic acetylcholine receptor explored by affinity labeling and site-directed mutagenesis. Q. Rev. Biophys. 25: 395-432.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 395-432
    • Changeux, J.-P.1    Galzi, J.-L.2    Devillers-Thiéry, A.3    Bertrand, D.4
  • 32
    • 0029302994 scopus 로고
    • The acetylcholine receptor: A model for allosteric membrane proteins
    • Changeux, J.-P. 1995. The acetylcholine receptor: a model for allosteric membrane proteins Biochem. Soc. Trans. 23: 195-205.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 195-205
    • Changeux, J.-P.1
  • 33
    • 0026535476 scopus 로고
    • Substitution of Torpedo californica acetylcholine receptor α1-subunit residues with snake α1- and rat nerve α3-subunit residues in recombinant fusion proteins: Effect on α-bungarotoxin binding
    • Chaturvedi, V., Donnelly-Roberts, D. S., and Lentz, T. L. 1992. Substitution of Torpedo californica acetylcholine receptor α1-subunit residues with snake α1- and rat nerve α3-subunit residues in recombinant fusion proteins: effect on α-bungarotoxin binding. Biochemistry 31: 1370-1375.
    • (1992) Biochemistry , vol.31 , pp. 1370-1375
    • Chaturvedi, V.1    Donnelly-Roberts, D.S.2    Lentz, T.L.3
  • 34
    • 0027431495 scopus 로고
    • Effects of mutation of Torpedo californica acetylcholine receptor α1 subunit residues 184-200 on α-bungarotoxin binding in recombinant fusion protein
    • Chaturvedi, V., Donnelly-Roberts, D. L., and Lentz, T. L. 1993. Effects of mutation of Torpedo californica acetylcholine receptor α1 subunit residues 184-200 on α-bungarotoxin binding in recombinant fusion protein. Biochemistry 32: 9570-9576.
    • (1993) Biochemistry , vol.32 , pp. 9570-9576
    • Chaturvedi, V.1    Donnelly-Roberts, D.L.2    Lentz, T.L.3
  • 35
    • 0027461253 scopus 로고
    • Solution conformation of cobratoxin: A nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study
    • Chin, Y., Bhaskaran, R., Chuang, L.-C., and Yang, C.-C. 1993. Solution conformation of cobratoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry 32: 2131-2136.
    • (1993) Biochemistry , vol.32 , pp. 2131-2136
    • Chin, Y.1    Bhaskaran, R.2    Chuang, L.-C.3    Yang, C.-C.4
  • 36
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore, G. M. and Gronenbom, A. M. 1982. Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins. J. Magn. Reson. 48: 402-417.
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenbom, A.M.2
  • 37
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution: Three and four dimensional heteronuclear NMR spectroscopy
    • Clore, M. G. and Gronenborn, A. M. 1991. Structures of larger proteins in solution: three and four dimensional heteronuclear NMR spectroscopy. Science 252: 1390-1398.
    • (1991) Science , vol.252 , pp. 1390-1398
    • Clore, M.G.1    Gronenborn, A.M.2
  • 39
    • 0000942975 scopus 로고
    • The crystal and molecular structure of a potent neuromuscular blocking agent: D-tubocurarine dichloride pentahydrate
    • Codding, P. W. and James, M. N. G. 1973. The crystal and molecular structure of a potent neuromuscular blocking agent: d-tubocurarine dichloride pentahydrate. Acta Cryst. B 29:935-942.
    • (1973) Acta Cryst. B , vol.29 , pp. 935-942
    • Codding, P.W.1    James, M.N.G.2
  • 40
    • 0026344986 scopus 로고
    • Structure of the agonist-binding site of the nicotinic acetylcholine receptor
    • Cohen, J. B., Sharp, S. D., and Liu, W. S. 1991. Structure of the agonist-binding site of the nicotinic acetylcholine receptor, J. Biol. Chem. 266: 23354-23364.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23354-23364
    • Cohen, J.B.1    Sharp, S.D.2    Liu, W.S.3
  • 43
    • 0024962029 scopus 로고
    • The crystal structure of Erabutoxin a at 2.0 Å resolution
    • Corfield, P. W. R., Lee, T.-J., and Low, B. W. 1989. The crystal structure of Erabutoxin a at 2.0 Å resolution. J. Biol. Chem. 264: 9239-9242.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9239-9242
    • Corfield, P.W.R.1    Lee, T.-J.2    Low, B.W.3
  • 44
    • 0022409247 scopus 로고
    • Structure-activity relationships for the irreversible blockade of nicotinic receptor agonist sites by lophotoxin and congeneric diterpene lactones
    • Culver, P., Burch, M., Potenza, C., Wasserman, L., Fenical, W., and Taylor. P. 1985. Structure-activity relationships for the irreversible blockade of nicotinic receptor agonist sites by lophotoxin and congeneric diterpene lactones. Mol. Pharmacol. 28: 436-444.
    • (1985) Mol. Pharmacol. , vol.28 , pp. 436-444
    • Culver, P.1    Burch, M.2    Potenza, C.3    Wasserman, L.4    Fenical, W.5    Taylor, P.6
  • 46
    • 0028852622 scopus 로고
    • Structure of the nicotinic receptor acetylcholine-binding site
    • Czajkowski, C. and Karlin, A. 1995. Structure of the nicotinic receptor acetylcholine-binding site. J. Biol. Chem. 270: 3160-3164.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3160-3164
    • Czajkowski, C.1    Karlin, A.2
  • 47
    • 0027208097 scopus 로고
    • Negatively charged amino acids residues in the nicotinic receptor δ subunit that contribute to the binding of acetylcholine
    • Czajkowski, C., Kaufmann, C., and Karlin, A. 1993. Negatively charged amino acids residues in the nicotinic receptor δ subunit that contribute to the binding of acetylcholine. Proc. Natl. Acad. Sci. U.S.A. 90: 6285-6289.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6285-6289
    • Czajkowski, C.1    Kaufmann, C.2    Karlin, A.3
  • 48
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetylcholine receptor α subunit labeled by a photoaffinity ligand for the acetylcholine binding site
    • Dennis, M., Giraudat, J., Kotzyba-Hibert, F., Goeldner, M., Hirth, C., Chang, J.-Y., Lazure, C., Chretien, M., and Changeux, J.-P. 1988. Amino acids of the Torpedo marmorata acetylcholine receptor α subunit labeled by a photoaffinity ligand for the acetylcholine binding site. Biochemistry 27: 2346-2357.
    • (1988) Biochemistry , vol.27 , pp. 2346-2357
    • Dennis, M.1    Giraudat, J.2    Kotzyba-Hibert, F.3    Goeldner, M.4    Hirth, C.5    Chang, J.-Y.6    Lazure, C.7    Chretien, M.8    Changeux, J.-P.9
  • 50
    • 0025675821 scopus 로고
    • Acetylcholine binding by a synthetic receptor: Implications for biological recognition
    • Dougherty, D. A. and Stauffer, D. A. 1990. Acetylcholine binding by a synthetic receptor: implications for biological recognition. Science 250: 1558-1560.
    • (1990) Science , vol.250 , pp. 1558-1560
    • Dougherty, D.A.1    Stauffer, D.A.2
  • 51
    • 0030033588 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. A. 1996. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271: 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 56
    • 0027223874 scopus 로고
    • Selective enhancement of the interaction of curare with the nicotinic acetylcholine receptor
    • Filatov, G. N., Aylwin, M. L., and White, M. M. 1993. Selective enhancement of the interaction of curare with the nicotinic acetylcholine receptor. Mol. Pharmacol. 44: 237-241.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 237-241
    • Filatov, G.N.1    Aylwin, M.L.2    White, M.M.3
  • 59
    • 0026070147 scopus 로고
    • Acetylcholine interactions with tryptophan-184 of the α-subunit of the nicotinic acetylcholine receptor revealed by transferred nuclear Overhauser effect
    • Fraenkel, Y., Gershoni, J. M., and Navon, G. 1991a. Acetylcholine interactions with tryptophan-184 of the α-subunit of the nicotinic acetylcholine receptor revealed by transferred nuclear Overhauser effect. FEBS Lett. 291: 225-228.
    • (1991) FEBS Lett. , vol.291 , pp. 225-228
    • Fraenkel, Y.1    Gershoni, J.M.2    Navon, G.3
  • 60
    • 0026335516 scopus 로고
    • NMR studies of recombinant active site peptides of the nicotinic acetylcholine receptor
    • Fraenkel, Y., Ohana, B., Gershoni, J. M., and Navon, G. 1991b. NMR studies of recombinant active site peptides of the nicotinic acetylcholine receptor. J. Basic Clin. Physiol. Pharmacol. 2: 207-215.
    • (1991) J. Basic Clin. Physiol. Pharmacol. , vol.2 , pp. 207-215
    • Fraenkel, Y.1    Ohana, B.2    Gershoni, J.M.3    Navon, G.4
  • 61
    • 0028158083 scopus 로고
    • NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine
    • Fraenkel, Y., Gershoni, J. M., and Navon, G. 1994. NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine. Biochemistry 33: 644-650.
    • (1994) Biochemistry , vol.33 , pp. 644-650
    • Fraenkel, Y.1    Gershoni, J.M.2    Navon, G.3
  • 62
    • 0028130198 scopus 로고
    • Competitive antagonists bridge the α-γ subunit interface of the acetylcholine receptor through quaternary ammonium-aromatic interactions
    • Fu, D.-X. and Sine, S. M. 1994. Competitive antagonists bridge the α-γ subunit interface of the acetylcholine receptor through quaternary ammonium-aromatic interactions. J. Biol. Chem. 269: 26152-26157.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26152-26157
    • Fu, D.-X.1    Sine, S.M.2
  • 63
    • 0028125739 scopus 로고
    • Interaction of protein ligands with receptor fragments on the residues of curaremimetic toxins that recognize fragments 128-142 and 185-199 of the α-subunit of the nicotinic acetylcholine receptor
    • Fulachier, M.-H., Mourier, G., Cotton, J., Servent, D., and Ménez, A. 1994. Interaction of protein ligands with receptor fragments on the residues of curaremimetic toxins that recognize fragments 128-142 and 185-199 of the α-subunit of the nicotinic acetylcholine receptor. FEBS Lett. 338: 331-338.
    • (1994) FEBS Lett. , vol.338 , pp. 331-338
    • Fulachier, M.-H.1    Mourier, G.2    Cotton, J.3    Servent, D.4    Ménez, A.5
  • 64
    • 0025346780 scopus 로고
    • Identification of a novel amino acid-tyrosine 93 within the cholinergic ligands-binding sites of acetylcholine receptor by photoaffinity labeling
    • Galzi, J.-L., Revah, F., Black, D., Goeldner, M., Hirth, C., and Changeux, J.-P. 1990a. Identification of a novel amino acid-tyrosine 93 within the cholinergic ligands-binding sites of acetylcholine receptor by photoaffinity labeling. J. Biol. Chem. 265: 10430-10437.
    • (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
  • 65
    • 0025884565 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: From electric organ to brain
    • Galzi, J.-L., Revah, F., Bessis, A., and Changeux, J.-P. 1991a. Functional architecture of the nicotinic acetylcholine receptor: from electric organ to brain. Annu. Rev. Pharmacol. 31: 37-72.
    • (1991) Annu. Rev. Pharmacol. , vol.31 , pp. 37-72
    • Galzi, J.-L.1    Revah, F.2    Bessis, A.3    Changeux, J.-P.4
  • 66
    • 0025985732 scopus 로고
    • Functional significance of aromatic amino acids from three peptide loops of the α7 neuronal nicotinic receptor site investigated by site-directed mutagenesis
    • Galzi, J.-L., Bertrand, D., Devillers-Thiéry, A., Revah, F., Bertrand, S., and Changeux, J.-P. 1991b. Functional significance of aromatic amino acids from three peptide loops of the α7 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-Thiéry, A.3    Revah, F.4    Bertrand, S.5    Changeux, J.-P.6
  • 67
    • 0023498890 scopus 로고
    • Computer modeling of the neurotoxin binding site of acetylcholine receptor spanning residues 185 through 196
    • Gerduno-Juarez, R., Shibata, M., Zielinski, T. J., and Rein, R. 1987. Computer modeling of the neurotoxin binding site of acetylcholine receptor spanning residues 185 through 196. Acta Biochim. Biophys. Hung. 22: 391-402.
    • (1987) Acta Biochim. Biophys. Hung. , vol.22 , pp. 391-402
    • Gerduno-Juarez, R.1    Shibata, M.2    Zielinski, T.J.3    Rein, R.4
  • 68
    • 0020804196 scopus 로고
    • Binding of α-bungarotoxin to isolated α sub-unit of the acetylcholine receptor of Torpedo californica: Quantitative analysis with protein blots
    • Gershoni, J. M., Hawrot, E., and Lentz, T. L. 1983. Binding of α-bungarotoxin to isolated α sub-unit of the acetylcholine receptor of Torpedo californica: quantitative analysis with protein blots. Proc. Natl. Acad. Sci. U.S.A. 80: 4973-4977.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 4973-4977
    • Gershoni, J.M.1    Hawrot, E.2    Lentz, T.L.3
  • 69
    • 84988119557 scopus 로고
    • The application of ligand overlay of protein blots to the study of the nicotinic acetylcholine receptor
    • Gershoni, J. M. 1987a. The application of ligand overlay of protein blots to the study of the nicotinic acetylcholine receptor. Electrophoresis 8: 428-431. See also Gershoni, J. M. 1988. Protein blotting: a manual. Methods Biochem. Anal. 33: 1-58.
    • (1987) Electrophoresis , vol.8 , pp. 428-431
    • Gershoni, J.M.1
  • 70
    • 0023739598 scopus 로고
    • Protein blotting: A manual
    • Gershoni, J. M. 1987a. The application of ligand overlay of protein blots to the study of the nicotinic acetylcholine receptor. Electrophoresis 8: 428-431. See also Gershoni, J. M. 1988. Protein blotting: a manual. Methods Biochem. Anal. 33: 1-58.
    • (1988) Methods Biochem. Anal. , vol.33 , pp. 1-58
    • Gershoni, J.M.1
  • 71
    • 0023201921 scopus 로고
    • Expression of the α-bungarotoxin binding site of the nicotinic acetylcholine receptor by Escherichia coli transformants
    • Gershoni, J. M. 1987b. Expression of the α-bungarotoxin binding site of the nicotinic acetylcholine receptor by Escherichia coli transformants. Proc. Natl. Acad. Sci. U.S.A. 84: 4318-4321.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4318-4321
    • Gershoni, J.M.1
  • 72
    • 0019082804 scopus 로고
    • Specific photoaffinity labeling induced by energy transfer: Application to irreversible inhibition of acetylcholinesterase
    • Goeldner, M. P. and Hirth, C. G. 1980. Specific photoaffinity labeling induced by energy transfer: application to irreversible inhibition of acetylcholinesterase. Proc. Natl. Acad. Sci. U.S.A. 77: 6439-6442.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 6439-6442
    • Goeldner, M.P.1    Hirth, C.G.2
  • 73
    • 0024281207 scopus 로고
    • Nicotinic acetylcholine receptor: A structural model for α-subunit peptide 188-201, the putative binding site for cholinergic agents
    • Gotti, C., Frigerio, F., Bolognesi, M., Longhi, R., Racchetti, G., and Clementi, F. 1988. Nicotinic acetylcholine receptor: a structural model for α-subunit peptide 188-201, the putative binding site for cholinergic agents. FEBS Lett. 228: 118-122.
    • (1988) FEBS Lett. , vol.228 , pp. 118-122
    • Gotti, C.1    Frigerio, F.2    Bolognesi, M.3    Longhi, R.4    Racchetti, G.5    Clementi, F.6
  • 74
    • 0014941713 scopus 로고
    • The crystal structure of acetylcholine: A new conformation for acetylcholine
    • Herdklotz, J. K. and Sass, R. L. 1970. The crystal structure of acetylcholine: a new conformation for acetylcholine. Biochem. Biophys. Res. Commun. 40: 583-588.
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 583-588
    • Herdklotz, J.K.1    Sass, R.L.2
  • 75
    • 0027499870 scopus 로고
    • The ligand binding domain of the nicotinic acetylcholine receptor: Immunological analysis
    • Kachalsky, S. G., Aladjern, M., Barchan, D., and Fuchs, S. 1993. The ligand binding domain of the nicotinic acetylcholine receptor: immunological analysis. FEBS 318: 264-268.
    • (1993) FEBS , vol.318 , pp. 264-268
    • Kachalsky, S.G.1    Aladjern, M.2    Barchan, D.3    Fuchs, S.4
  • 76
    • 0028801048 scopus 로고
    • Two subsites in the binding domain of the acetylcholine receptor: An aromatic subsite and a proline subsite
    • Kachalsky, S. G., Jensen, B. S., Barchan, D., and Fuchs, S. 1995. Two subsites in the binding domain of the acetylcholine receptor: an aromatic subsite and a proline subsite. Proc. Natl. Acad. Sci. U.S.A. 92: 10801-10805.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10801-10805
    • Kachalsky, S.G.1    Jensen, B.S.2    Barchan, D.3    Fuchs, S.4
  • 77
    • 0021132711 scopus 로고
    • Identification of the a subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site
    • Kao, P. N. and Karlin, A. 1984. Identification of the a subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site. J. Biol. Chem. 259: 11662-11665.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11662-11665
    • Kao, P.N.1    Karlin, A.2
  • 78
    • 0022975251 scopus 로고
    • Acetylcholine receptor binding site contains a disulfide crosslink between adjacent half-cystinyl residues
    • Kao, P. N. and Karlin, A. 1986. Acetylcholine receptor binding site contains a disulfide crosslink between adjacent half-cystinyl residues. J. Biol. Chem. 261: 8085-8088.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8085-8088
    • Kao, P.N.1    Karlin, A.2
  • 79
    • 0001053688 scopus 로고
    • A theoretical study of distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra
    • Keepers, J. W. and James, T. L. 1984. A theoretical study of distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra. J. Magn. Reson. 57: 404-426.
    • (1984) J. Magn. Reson. , vol.57 , pp. 404-426
    • Keepers, J.W.1    James, T.L.2
  • 80
    • 0024291648 scopus 로고
    • Structural studies of α-bungarotoxin. 3. Corrections in the primary sequence and X-ray structure and characterization of an isotoxic α-bungarotoxin
    • Kosen, P. A., Finer-Moore, J., McCarthy, M. P., and Basus, V. 1988. Structural studies of α-bungarotoxin. 3. Corrections in the primary sequence and X-ray structure and characterization of an isotoxic α-bungarotoxin. Biochemistry 27: 2775-2781.
    • (1988) Biochemistry , vol.27 , pp. 2775-2781
    • Kosen, P.A.1    Finer-Moore, J.2    McCarthy, M.P.3    Basus, V.4
  • 81
    • 0022214795 scopus 로고
    • Synthetic and conformational studies on anatoxin-A: A potent acetylcholine agonist
    • Koskinen, A. M. P. and Rapoport, H. 1985. Synthetic and conformational studies on anatoxin-A: a potent acetylcholine agonist. J. Med. Chem. 28: 1301-1309.
    • (1985) J. Med. Chem. , vol.28 , pp. 1301-1309
    • Koskinen, A.M.P.1    Rapoport, H.2
  • 82
    • 0028346433 scopus 로고
    • Glycosylation sites selectivity interfere with α-toxin binding to the nicotinic acetylcholine receptor
    • Kreienkamp, H.-J., Sine, S. M., Maeda, R. K., and Taylor, P. 1994. Glycosylation sites selectivity interfere with α-toxin binding to the nicotinic acetylcholine receptor. J. Biol. Chem. 269: 8101-8114.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8101-8114
    • Kreienkamp, H.-J.1    Sine, S.M.2    Maeda, R.K.3    Taylor, P.4
  • 83
    • 0028914380 scopus 로고
    • Intersubunit contacts governing assembly of the mammalian nicotinic acetylcholine receptor
    • Kreienkamp, H.-J., Maeda, R. K., Sine, S. M., and Taylor, P. 1995. Intersubunit contacts governing assembly of the mammalian nicotinic acetylcholine receptor. Neuron 14: 635-644.
    • (1995) Neuron , vol.14 , pp. 635-644
    • Kreienkamp, H.-J.1    Maeda, R.K.2    Sine, S.M.3    Taylor, P.4
  • 84
    • 0343476296 scopus 로고
    • 1 for the investigation of binding of ligands
    • 1 for the investigation of binding of ligands. Bull. Magn. Reson. 6: 60-63.
    • (1983) Bull. Magn. Reson. , vol.6 , pp. 60-63
    • Kushnir, T.1    Navon, G.2
  • 85
    • 0008896605 scopus 로고
    • Dynamical NOE in multiple-spin systems undergoing chemical exchange
    • Landy, S. B. and Rao, B. D. N. 1989. Dynamical NOE in multiple-spin systems undergoing chemical exchange. J. Magn. Reson. 81: 371-377.
    • (1989) J. Magn. Reson. , vol.81 , pp. 371-377
    • Landy, S.B.1    Rao, B.D.N.2
  • 86
    • 0028219505 scopus 로고
    • Mutations in the M4-domain of Torpedo californica acetylcholine receptor dramatically alter ion channel function
    • Lee, Y.-H., Li, L., Lasalde, J., Rojas, L., McNamee, M., and Ortiz-Miranda, S. I. 1994. Mutations in the M4-domain of Torpedo californica acetylcholine receptor dramatically alter ion channel function. Biophys. J. 66: 646-653.
    • (1994) Biophys. J. , vol.66 , pp. 646-653
    • Lee, Y.-H.1    Li, L.2    Lasalde, J.3    Rojas, L.4    McNamee, M.5    Ortiz-Miranda, S.I.6
  • 87
    • 0027536977 scopus 로고
    • Allosteric modulations of the nicotinic acetylcholine receptor
    • Léna, C. and Changeux, J.-P. 1993. Allosteric modulations of the nicotinic acetylcholine receptor. TINS 16: 181-186.
    • (1993) TINS , vol.16 , pp. 181-186
    • Léna, C.1    Changeux, J.-P.2
  • 88
    • 0023757777 scopus 로고
    • Neurotoxin-binding site on the acetylcholine receptor
    • Lentz, T. A. and Wilson, P. T. 1988. Neurotoxin-binding site on the acetylcholine receptor. Int. Rev. Neurobiol. 29: 117-160.
    • (1988) Int. Rev. Neurobiol. , vol.29 , pp. 117-160
    • Lentz, T.A.1    Wilson, P.T.2
  • 89
    • 0000071182 scopus 로고
    • Theory and experimental results of transfer-NOE experiments. 1. The influence of the off rate versus cross-relaxation rates
    • Lippens, G. M., Cref, C., and Hallenga, K. 1992. Theory and experimental results of transfer-NOE experiments. 1. The influence of the off rate versus cross-relaxation rates. J. Magn. Reson. 99: 268-281.
    • (1992) J. Magn. Reson. , vol.99 , pp. 268-281
    • Lippens, G.M.1    Cref, C.2    Hallenga, K.3
  • 91
    • 0029287150 scopus 로고
    • Deriving accurate interproton distances from ROESY spectra with limited knowledge of scalar coupling constants via the CARNIVAL algorithm: An iterative complete relaxation matrix approach
    • Liu, H., Banville, D. L., Basus, V. J., and James, T. L. 1995. Deriving accurate interproton distances from ROESY spectra with limited knowledge of scalar coupling constants via the CARNIVAL algorithm: an iterative complete relaxation matrix approach. J. Magn. Reson. 107: 51-59.
    • (1995) J. Magn. Reson. , vol.107 , pp. 51-59
    • Liu, H.1    Banville, D.L.2    Basus, V.J.3    James, T.L.4
  • 92
    • 0002832937 scopus 로고
    • Relaxation-matrix analysis of the transferred nuclear Overhauser effect for finite exchange rates
    • London, R. E., Perlman, M., and Davis, D. G. 1992. Relaxation-matrix analysis of the transferred nuclear Overhauser effect for finite exchange rates. J. Magn. Reson. 97: 79-98.
    • (1992) J. Magn. Reson. , vol.97 , pp. 79-98
    • London, R.E.1    Perlman, M.2    Davis, D.G.3
  • 93
    • 0022943266 scopus 로고
    • The crystal structure of α-bungarotoxin at 2.5 Å resolution relation to solution structure and binding to acetylcholine receptor
    • Love, R. A. and Stroud, R. M. 1986. The crystal structure of α-bungarotoxin at 2.5 Å resolution relation to solution structure and binding to acetylcholine receptor. Protein Eng. 1: 37-46.
    • (1986) Protein Eng. , vol.1 , pp. 37-46
    • Love, R.A.1    Stroud, R.M.2
  • 94
    • 0023051107 scopus 로고
    • Erabutoxin b: Structure/function relationships following initial protein refinement at 0.140-nm resolution
    • Low, B. W. and Corfield, P. W. R. 1986. Erabutoxin b: structure/function relationships following initial protein refinement at 0.140-nm resolution. Eur. J. Biochem. 161: 579-587.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 579-587
    • Low, B.W.1    Corfield, P.W.R.2
  • 95
    • 0029114531 scopus 로고
    • Photolabeling reveals the proximity of the α-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor
    • Machold, J., Utkin, Y., Kirsch, D., Kaufmann, R., Tsetlin, V., and Hucho, F. 1995. Photolabeling reveals the proximity of the α-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. U.S.A. 92: 7282-7286.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7282-7286
    • Machold, J.1    Utkin, Y.2    Kirsch, D.3    Kaufmann, R.4    Tsetlin, V.5    Hucho, F.6
  • 97
    • 0027214388 scopus 로고
    • Homologous κ-neurotoxins exhibit residue-specific interactions with the α3 subunit of the nicotinic acetylcholine receptor: A comparison of the structural requirements for κ-Flavotoxin binding
    • McLane, K. E., Weaver, W. R., Lei, S., Chiappinelli, V. A., and Conti-Tronconi, B. M. 1993. Homologous κ-neurotoxins exhibit residue-specific interactions with the α3 subunit of the nicotinic acetylcholine receptor: a comparison of the structural requirements for κ-Flavotoxin binding. Biochemistry 32: 6988-6994.
    • (1993) Biochemistry , vol.32 , pp. 6988-6994
    • McLane, K.E.1    Weaver, W.R.2    Lei, S.3    Chiappinelli, V.A.4    Conti-Tronconi, B.M.5
  • 98
    • 0025866049 scopus 로고
    • Structural determinants of α-bungarotoxin binding to the sequence segment 181-200 of the muscle nicotinic acetylcholine receptor a subunit: Effects of cysteine/cysteine modification and species-specific amino acid substitutions
    • McLane, K. E., Wu, X., Diethelm, B., and Conti-Tronconi, B. M. 1991. Structural determinants of α-bungarotoxin binding to the sequence segment 181-200 of the muscle nicotinic acetylcholine receptor a subunit: effects of cysteine/cysteine modification and species-specific amino acid substitutions. Biochemistry 30: 4925-4934.
    • (1991) Biochemistry , vol.30 , pp. 4925-4934
    • McLane, K.E.1    Wu, X.2    Diethelm, B.3    Conti-Tronconi, B.M.4
  • 99
    • 0028175814 scopus 로고
    • An α-bungarotoxin-binding sequence on the Torpedo nicotinic acetylcholine receptor α-subunit: Conservative amino acid substitutions reveal side-chain specific interactions
    • McLane, K. E., Wu, X., and Conti-Tronconi, B. M. 1994. An α-bungarotoxin-binding sequence on the Torpedo nicotinic acetylcholine receptor α-subunit: conservative amino acid substitutions reveal side-chain specific interactions. Biochemistry 33: 2576-2585.
    • (1994) Biochemistry , vol.33 , pp. 2576-2585
    • McLane, K.E.1    Wu, X.2    Conti-Tronconi, B.M.3
  • 100
    • 0028361585 scopus 로고
    • Secondary structure of nicotinic acetylcholine receptor: Implications for structural models of a ligand-gated ion channel
    • Méthot, N., McCarthy, M. P., and Baenziger, J. E. 1994. Secondary structure of nicotinic acetylcholine receptor: implications for structural models of a ligand-gated ion channel. Biochemistry 33: 7709-7717.
    • (1994) Biochemistry , vol.33 , pp. 7709-7717
    • Méthot, N.1    McCarthy, M.P.2    Baenziger, J.E.3
  • 101
    • 0024297514 scopus 로고
    • Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements. Porcine pancreatic elastase and hexapeptide
    • Meyer, E. F., Clore, G. M., Gronenborn, A. M., and Hansen, H. A. S. 1988. Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements. Porcine pancreatic elastase and hexapeptide. Biochemistry 27: 725-730.
    • (1988) Biochemistry , vol.27 , pp. 725-730
    • Meyer, E.F.1    Clore, G.M.2    Gronenborn, A.M.3    Hansen, H.A.S.4
  • 102
    • 0025819979 scopus 로고
    • 3H]nicotine as an agonist photoaffinity label
    • 3H]nicotine as an agonist photoaffinity label. Biochemistry 30: 6987-6997.
    • (1991) Biochemistry , vol.30 , pp. 6987-6997
    • Middleton, R.E.1    Cohen, J.B.2
  • 103
    • 0025105211 scopus 로고
    • 1H nuclear magnetic resonance. Correlation between activities and membrane-bound conformations
    • 1H nuclear magnetic resonance. Correlation between activities and membrane-bound conformations. Biochemistry 29: 65-75.
    • (1990) Biochemistry , vol.29 , pp. 65-75
    • Milon, A.1    Miyazawa, T.2    Higashijima, T.3
  • 104
    • 0013532767 scopus 로고
    • Quantitative interpretation of a single NOESY spectrum
    • Mirau, P. A. 1988. Quantitative interpretation of a single NOESY spectrum. J. Magn. Reson. 80: 439-447.
    • (1988) J. Magn. Reson. , vol.80 , pp. 439-447
    • Mirau, P.A.1
  • 105
    • 0022467897 scopus 로고
    • Segment α182-198 of Torpedo californica acetylcholine receptor contains a second toxin-binding region and binds anti-receptor antibodies
    • Mulac-Jericeric, B. and Atassi, M. Z. 1986. Segment α182-198 of Torpedo californica acetylcholine receptor contains a second toxin-binding region and binds anti-receptor antibodies. FEBS Lett. 199: 68-74.
    • (1986) FEBS Lett. , vol.199 , pp. 68-74
    • Mulac-Jericeric, B.1    Atassi, M.Z.2
  • 106
    • 0027518128 scopus 로고
    • Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. I. Spatial disposition of cysteine residues in the γ subunit analyzed by fluorescence-quenching and energy-transfer measurements
    • Narayanaswami, V., Kim, J., and McNamee, M. G. 1993. Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. I. Spatial disposition of cysteine residues in the γ subunit analyzed by fluorescence-quenching and energy-transfer measurements. Biochemistry 32: 12413-12419.
    • (1993) Biochemistry , vol.32 , pp. 12413-12419
    • Narayanaswami, V.1    Kim, J.2    McNamee, M.G.3
  • 107
    • 0027441795 scopus 로고
    • Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. II. Membrane fluidity and ligand-mediated alteration in the accessibility of γ subunit cysteine residues to cholesterol
    • Narayanaswami, V. and McNamee, M. G. 1993. Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. II. Membrane fluidity and ligand-mediated alteration in the accessibility of γ subunit cysteine residues to cholesterol. Biochemistry 32: 12420-12427.
    • (1993) Biochemistry , vol.32 , pp. 12420-12427
    • Narayanaswami, V.1    McNamee, M.G.2
  • 108
    • 9544235958 scopus 로고
    • Studies of the binding of agonists to the acetylcholine receptor
    • (Jaroszewski, J. W., Schaumburg, K., and Kofod, H., Eds.) Copenhagen: Munksgaard
    • Navon, G., Yamane, T., and Jelinski, L. W. 1988. Studies of the binding of agonists to the acetylcholine receptor. In: NMR Spectroscopy in Drug Research, pp. 423-436. (Jaroszewski, J. W., Schaumburg, K., and Kofod, H., Eds.) Copenhagen: Munksgaard.
    • (1988) NMR Spectroscopy in Drug Research , pp. 423-436
    • Navon, G.1    Yamane, T.2    Jelinski, L.W.3
  • 110
    • 0345159134 scopus 로고
    • Antibodies to synthetic peptides as probes for the binding site on the α subunit of the acetylcholine receptor
    • Neumann, D., Gershoni, J. M., Fridkin, M., and Fuchs, S. 1985. Antibodies to synthetic peptides as probes for the binding site on the α subunit of the acetylcholine receptor. Proc. Natl. Acad. Sci. U.S.A. 82: 3490-3493.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 3490-3493
    • Neumann, D.1    Gershoni, J.M.2    Fridkin, M.3    Fuchs, S.4
  • 111
    • 0343203033 scopus 로고
    • Analysis of ligand binding to the synthetic dodecapeptide 185-196 of the acetylcholine receptor α subunit
    • Neumann, D., Barchan, D., Fridkin, M., and Fuchs, S. 1986a. Analysis of ligand binding to the synthetic dodecapeptide 185-196 of the acetylcholine receptor α subunit. Proc. Natl. Acad. Sci. U.S.A. 83: 9250-9253.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 9250-9253
    • Neumann, D.1    Barchan, D.2    Fridkin, M.3    Fuchs, S.4
  • 112
    • 0022499114 scopus 로고
    • Mapping of the α-bungarotoxin binding site within the α-sub-unit of the acetylcholine receptor
    • Neumann, D., Barchan, D., Safran, A., Gershoni, J. M., and Fuchs, S. 1986b. Mapping of the α-bungarotoxin binding site within the α-sub-unit of the acetylcholine receptor. Proc: Natl. Acad. Sci. U.S.A. 83: 3008-3011.
    • (1986) Proc: Natl. Acad. Sci. U.S.A. , vol.83 , pp. 3008-3011
    • Neumann, D.1    Barchan, D.2    Safran, A.3    Gershoni, J.M.4    Fuchs, S.5
  • 113
    • 0040615087 scopus 로고
    • Snake acetylcholine receptor: Cloning of the domain containing the four extracellular cysteins of the α subunit
    • Neumann, D., Barchan, D., Horowitz, M., Kochva, E., and Fuchs, S. 1989. Snake acetylcholine receptor: cloning of the domain containing the four extracellular cysteins of the α subunit. Proc. Natl. Acad. Sci. U.S.A. 86: 7255-7259.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7255-7259
    • Neumann, D.1    Barchan, D.2    Horowitz, M.3    Kochva, E.4    Fuchs, S.5
  • 114
    • 0025338124 scopus 로고
    • Thrombin-bound conformations of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects
    • Ni, F., Konishi, F. N., and Scheraga, H. A. 1990. Thrombin-bound conformations of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects. Biochemistry 29: 4479-4489.
    • (1990) Biochemistry , vol.29 , pp. 4479-4489
    • Ni, F.1    Konishi, F.N.2    Scheraga, H.A.3
  • 115
    • 0002624406 scopus 로고
    • Theory and experimental results of transfer NOE experiments. II. The influence of residual mobility and relaxation centers inside the protein on the size of transfer NOE's
    • Nirmala, N. R., Lippens, G. M., and Hallenga, K. 1992. Theory and experimental results of transfer NOE experiments. II. The influence of residual mobility and relaxation centers inside the protein on the size of transfer NOE's. J. Magn. Reson. 100: 25-42.
    • (1992) J. Magn. Reson. , vol.100 , pp. 25-42
    • Nirmala, N.R.1    Lippens, G.M.2    Hallenga, K.3
  • 116
    • 0019904425 scopus 로고
    • Primary structure of α-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence
    • Noda, M., Takahashi, H., Tanabe, H., Toyosato, M., Furutani, Y., Hirose, T., Asai, M., Inayama, S., Miyata, T., and Numa, S. 1982. Primary structure of α-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence. Nature 299: 793-797.
    • (1982) Nature , vol.299 , pp. 793-797
    • Noda, M.1    Takahashi, H.2    Tanabe, H.3    Toyosato, M.4    Furutani, Y.5    Hirose, T.6    Asai, M.7    Inayama, S.8    Miyata, T.9    Numa, S.10
  • 119
    • 0025316406 scopus 로고
    • Comparison of the toxin binding sites of the nicotinic acetylcholine receptor from Drosophila to human
    • Ohana, B. and Gershoni, J. M. 1990. Comparison of the toxin binding sites of the nicotinic acetylcholine receptor from Drosophila to human. Biochemistry 29: 6409-6415.
    • (1990) Biochemistry , vol.29 , pp. 6409-6415
    • Ohana, B.1    Gershoni, J.M.2
  • 120
    • 0025995917 scopus 로고
    • Molecular dissection of cholinergic binding sites: How do snakes escape the effect of their own toxin
    • Ohana, B., Fraenkel, Y., Navon, G., and Gershoni, J. M. 1991. Molecular dissection of cholinergic binding sites: how do snakes escape the effect of their own toxin. Biophys. Biochem. Res. Commun. 179: 648-654.
    • (1991) Biophys. Biochem. Res. Commun. , vol.179 , pp. 648-654
    • Ohana, B.1    Fraenkel, Y.2    Navon, G.3    Gershoni, J.M.4
  • 121
    • 0028316086 scopus 로고
    • Characterization of d-tubocurarine binding site of Torpedo acetylcholine receptor
    • O'Leary, M. E., Filatov, G. N., and White, M. M. 1994. Characterization of d-tubocurarine binding site of Torpedo acetylcholine receptor. Am. J. Physiol. 266: C648-C653.
    • (1994) Am. J. Physiol. , vol.266
    • O'Leary, M.E.1    Filatov, G.N.2    White, M.M.3
  • 122
    • 0022972430 scopus 로고
    • Location of ligand-binding sites on the nicotinic acetylcholine receptor α-subunit
    • Pedersen, S. E., Dreyer, E. B., and Cohen, J. B. 1986. Location of ligand-binding sites on the nicotinic acetylcholine receptor α-subunit. J. Biol. Chem. 261: 13735-13743.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13735-13743
    • Pedersen, S.E.1    Dreyer, E.B.2    Cohen, J.B.3
  • 123
    • 0024284235 scopus 로고
    • α-Toxin binding to acetylcholine receptor α179-191 peptides: Intrinsic fluorescence studies
    • Radding, W., Corfield, P. W. R., Levinson, L. S., Hashim, G. A., and Low, B. W. 1988. α-Toxin binding to acetylcholine receptor α179-191 peptides: intrinsic fluorescence studies. FEBS Lett. 231: 212-216.
    • (1988) FEBS Lett. , vol.231 , pp. 212-216
    • Radding, W.1    Corfield, P.W.R.2    Levinson, L.S.3    Hashim, G.A.4    Low, B.W.5
  • 124
    • 0001424428 scopus 로고
    • The crystal structure, absolute configuration and stereochemistry of (+)-tubocurarine dibromide methanol solvate: A potent neuromuscular blocking agent
    • Reynolds, C. C. and Palmer, R. A. 1976. The crystal structure, absolute configuration and stereochemistry of (+)-tubocurarine dibromide methanol solvate: a potent neuromuscular blocking agent. Acta Cryst. B 32: 1431-1439.
    • (1976) Acta Cryst. B , vol.32 , pp. 1431-1439
    • Reynolds, C.C.1    Palmer, R.A.2
  • 125
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini, J. M., Schultze-Gahmen, U., and Wilson, I. A. 1992. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 255: 959-965.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schultze-Gahmen, U.2    Wilson, I.A.3
  • 126
    • 0029278634 scopus 로고
    • Twist to open
    • Sansom, M. S. P. 1995. Twist to open. Curr. Biol. 5: 373-375.
    • (1995) Curr. Biol. , vol.5 , pp. 373-375
    • Sansom, M.S.P.1
  • 128
    • 0027989776 scopus 로고
    • Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents
    • Silman, I., Harel, M., Axelsen, P., Raves, M., and Sussman, J. L. 1994. Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents. Biochem. Soc. Trans. 22: 45-49.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 45-49
    • Silman, I.1    Harel, M.2    Axelsen, P.3    Raves, M.4    Sussman, J.L.5
  • 129
    • 0027482551 scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor: Identification of residues that determine curare selectivity
    • Sine, S. M. 1993. Molecular dissection of subunit interfaces in the acetylcholine receptor: identification of residues that determine curare selectivity. Proc. Natl. Acad. Sci. U.S.A. 90: 9436-9440.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9436-9440
    • Sine, S.M.1
  • 131
    • 0024324441 scopus 로고
    • Binding of semirigid nicotinic agonists to nicotinic and muscarinic receptors
    • Spivak, C. E., Waters, J. A., and Aronstam, R. S. 1989. Binding of semirigid nicotinic agonists to nicotinic and muscarinic receptors. J. Med. Chem. 36: 177-184.
    • (1989) J. Med. Chem. , vol.36 , pp. 177-184
    • Spivak, C.E.1    Waters, J.A.2    Aronstam, R.S.3
  • 132
    • 0028345212 scopus 로고
    • Lipid modulation of nicotinic acetylcholine receptor function: The role of membrane lipid composition and fluidity
    • Sunshine, C. and McNamee, M. G. 1994. Lipid modulation of nicotinic acetylcholine receptor function: the role of membrane lipid composition and fluidity. Biochim. Biophys. 1191: 59-64.
    • (1994) Biochim. Biophys. , vol.1191 , pp. 59-64
    • Sunshine, C.1    McNamee, M.G.2
  • 133
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototype acetylcholine-binding protein
    • Sussman, J., Harel, M., Frolow, F., Oefner, C. M., Goldman, A., Toker, L., and Silman, I. 1991. Atomic structure of acetylcholinesterase from Torpedo californica: a prototype acetylcholine-binding protein. Science 253: 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.1    Harel, M.2    Frolow, F.3    Oefner, C.M.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 134
    • 0022618899 scopus 로고
    • Molecular mechanisms of the potent and stereospecific nicotinic receptor agonist (+)-anatoxin-a
    • Swanson, K. L., Allen, C. N., Arostam, R. S., Rapoport, H., and Albuquerque, E. X. 1986. Molecular mechanisms of the potent and stereospecific nicotinic receptor agonist (+)-anatoxin-a. Mol. Pharmacol. 29: 250-257.
    • (1986) Mol. Pharmacol. , vol.29 , pp. 250-257
    • Swanson, K.L.1    Allen, C.N.2    Arostam, R.S.3    Rapoport, H.4    Albuquerque, E.X.5
  • 135
    • 0027215829 scopus 로고
    • The two-dimensional transferred nuclear Overhauser effect
    • Sykes, B. D. and Campbell, A. P. 1993. The two-dimensional transferred nuclear Overhauser effect Ann. Rev. Biophys. Biomed. Struct. 22: 99-122.
    • (1993) Ann. Rev. Biophys. Biomed. Struct. , vol.22 , pp. 99-122
    • Sykes, B.D.1    Campbell, A.P.2
  • 137
    • 0019879685 scopus 로고
    • Environment of ribothymidine in transfer ribonucleic acid studied by means of nuclear Overhauser effect
    • Tropp, J. and Redfield, A. G. 1981. Environment of ribothymidine in transfer ribonucleic acid studied by means of nuclear Overhauser effect. Biochemistry 20: 2133-2140.
    • (1981) Biochemistry , vol.20 , pp. 2133-2140
    • Tropp, J.1    Redfield, A.G.2
  • 138
    • 0027624926 scopus 로고
    • Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti-MIR antibody: A two-dimensional nuclear magnetic resonance and molecular dynamics approach
    • Tsikaris, V., Detsikas, E., Sakarellos-Daitsiotis, M., Sakarellos, C., Vatzaki, E., Tzaros, S. J., Marraud, M., and Cung, M. T. 1993. Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti-MIR antibody: a two-dimensional nuclear magnetic resonance and molecular dynamics approach. Biopolymers 33: 1123-1134.
    • (1993) Biopolymers , vol.33 , pp. 1123-1134
    • Tsikaris, V.1    Detsikas, E.2    Sakarellos-Daitsiotis, M.3    Sakarellos, C.4    Vatzaki, E.5    Tzaros, S.J.6    Marraud, M.7    Cung, M.T.8
  • 139
    • 0025666541 scopus 로고
    • Fine localization of the major α-bungarotoxin binding site to residues α189-195 of the Torpedo acetylcholine receptor
    • Tzartos, S. J. and Remoundos, M. S. 1990. Fine localization of the major α-bungarotoxin binding site to residues α189-195 of the Torpedo acetylcholine receptor. J. Biol. Chem. 265: 21462-21467.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21462-21467
    • Tzartos, S.J.1    Remoundos, M.S.2
  • 140
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor
    • Unwin, N. 1993. Nicotinic acetylcholine receptor. J. Mol. Biol. 229: 1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 141
    • 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
  • 142
    • 0028144775 scopus 로고
    • Relationship between the binding sites for an α-conotoxin and snake venom neurotoxins in the nicotinic acetylcholine receptor from Torpedo californica
    • Utkin, Y. N., Kobayashi, Y., Hucho, F., and Tsetlin, V. I. 1994. Relationship between the binding sites for an α-conotoxin and snake venom neurotoxins in the nicotinic acetylcholine receptor from Torpedo californica. Toxicon 32: 1153-1157.
    • (1994) Toxicon , vol.32 , pp. 1153-1157
    • Utkin, Y.N.1    Kobayashi, Y.2    Hucho, F.3    Tsetlin, V.I.4
  • 143
    • 0002785142 scopus 로고
    • Selective and non-selective proton spin-lattice relaxation studies of enzyme-substrate interactions
    • Valensin, G., Kushnir, T., and Navon, G. 1982. Selective and non-selective proton spin-lattice relaxation studies of enzyme-substrate interactions. J. Magn. Reson. 46: 23-29.
    • (1982) J. Magn. Reson. , vol.46 , pp. 23-29
    • Valensin, G.1    Kushnir, T.2    Navon, G.3
  • 144
    • 0028305085 scopus 로고
    • Antibody-induced conformational changes in the Torpedo nicotinic acetylcholine receptor: A fluorescence study
    • Valenzuela, C. F., Dowding, A. J., Arias, H. R., and Johnson, D. A. 1994. Antibody-induced conformational changes in the Torpedo nicotinic acetylcholine receptor: a fluorescence study. Biochemistry 33: 6586-6594.
    • (1994) Biochemistry , vol.33 , pp. 6586-6594
    • Valenzuela, C.F.1    Dowding, A.J.2    Arias, H.R.3    Johnson, D.A.4
  • 145
    • 0023915747 scopus 로고
    • Synthesis, pharmacology, and molecular modeling studies of semirigid, nicotinic agonists
    • Waters, J. A., Spivak, C. E., Hermsmeir, M., Yadav, J. S., Liang, R., and Gund, T. M. 1988. Synthesis, pharmacology, and molecular modeling studies of semirigid, nicotinic agonists. J. Med. Chem. 31: 545-554.
    • (1988) J. Med. Chem. , vol.31 , pp. 545-554
    • Waters, J.A.1    Spivak, C.E.2    Hermsmeir, M.3    Yadav, J.S.4    Liang, R.5    Gund, T.M.6
  • 147
    • 0025132889 scopus 로고
    • Anionic subsites of the acetylcholinesterase from Torpedo californica: Affinity labeling with the cationic reagent N,N-dimethyl-2-phenylaziridinium
    • Weise, C., Kreienkamp, H. J., Raba, R., Pedak, A., Aaviksaar, A., and Hucho, F. 1990. Anionic subsites of the acetylcholinesterase from Torpedo californica: affinity labeling with the cationic reagent N,N-dimethyl-2-phenylaziridinium. EMBO J. 9: 3885-3888.
    • (1990) EMBO J. , vol.9 , pp. 3885-3888
    • Weise, C.1    Kreienkamp, H.J.2    Raba, R.3    Pedak, A.4    Aaviksaar, A.5    Hucho, F.6
  • 148
    • 0024587230 scopus 로고
    • Protein structure determination in solution by nuclear magnetic resonance spectroscopy
    • Wuthrich, K. 1989. Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science 243: 45-50.
    • (1989) Science , vol.243 , pp. 45-50
    • Wuthrich, K.1
  • 149
    • 0025835156 scopus 로고
    • The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution
    • Wuthrich, K. 1991. The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution. Biochemistry 30: 6563-6574.
    • (1991) Biochemistry , vol.30 , pp. 6563-6574
    • Wuthrich, K.1
  • 150
    • 0001571821 scopus 로고
    • Protein indirect relaxation effects in exchange-transferred NOESY by a rate-matrix analysis
    • Zheng, J. and Post, C. B. 1993. Protein indirect relaxation effects in exchange-transferred NOESY by a rate-matrix analysis. J. Magn. Reson., Ser. B 101: 262-270.
    • (1993) J. Magn. Reson., Ser. B , vol.101 , pp. 262-270
    • Zheng, J.1    Post, C.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.