메뉴 건너뛰기




Volumn 76, Issue 1 I, 1999, Pages 207-218

A mutational analysis of the acetylcholine receptor channel transmitter binding site

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; CHOLINERGIC RECEPTOR; NEUROTRANSMITTER; POTASSIUM ION;

EID: 0032938313     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77190-0     Document Type: Article
Times cited : (40)

References (55)
  • 2
    • 0030032121 scopus 로고    scopus 로고
    • Inorganic, monovalent cations compete with agonists for the transmitter binding site of nicotinic acetylcholine receptors
    • Akk, G., and A. Auerbach. 1996. Inorganic, monovalent cations compete with agonists for the transmitter binding site of nicotinic acetylcholine receptors. Biophys. J. 70:2652-2658.
    • (1996) Biophys. J. , vol.70 , pp. 2652-2658
    • Akk, G.1    Auerbach, A.2
  • 3
    • 0029859799 scopus 로고    scopus 로고
    • Binding sites contribute unequally to the gating of mouse nicotinic αD200n acetylcholine receptors
    • Akk, G., S. Sine, and A. Auerbach. 1996. Binding sites contribute unequally to the gating of mouse nicotinic αD200N acetylcholine receptors. J. Physiol. (Lond.). 496:185-196.
    • (1996) J. Physiol. (Lond.). , vol.496 , pp. 185-196
    • Akk, G.1    Sine, S.2    Auerbach, A.3
  • 4
    • 0027410307 scopus 로고
    • A statistical analysis of acetylcholine receptor activation in Xenopus myocytes: Stepwise vs. concerted models of gating
    • Auerbach, A. 1993. A statistical analysis of acetylcholine receptor activation in Xenopus myocytes: stepwise vs. concerted models of gating. J. Physiol. (Lond.). 461:339-378.
    • (1993) J. Physiol. (Lond.). , vol.461 , pp. 339-378
    • Auerbach, A.1
  • 5
    • 0031870973 scopus 로고    scopus 로고
    • Desensitization of mouse nicotinic acetylcholine receptor channels: A two-gate mechanism
    • Auerbach, A., and G. Akk. 1998. Desensitization of mouse nicotinic acetylcholine receptor channels: a two-gate mechanism. J. Gen. Physiol. 112:181-197.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 181-197
    • Auerbach, A.1    Akk, G.2
  • 6
    • 0029934560 scopus 로고    scopus 로고
    • Different gating charge movements in doubly-, singly-, and unliganded acetylcholine receptors
    • Auerbach, A., W. Sigurdson, J. Chen, and G. Akk. 1996. Different gating charge movements in doubly-, singly-, and unliganded acetylcholine receptors. J. Physiol. (Lond.). 494:155-170.
    • (1996) J. Physiol. (Lond.). , vol.494 , pp. 155-170
    • Auerbach, A.1    Sigurdson, W.2    Chen, J.3    Akk, G.4
  • 8
    • 0019201173 scopus 로고
    • Structure of a complex between yeast hexokinase A and glucose
    • Bennett, W, S., Jr., and T. A. Steitz. 1980. Structure of a complex between yeast hexokinase A and glucose. J. Mol. Biol. 140:211-230.
    • (1980) J. Mol. Biol. , vol.140 , pp. 211-230
    • Bennett W.S., Jr.1    Steitz, T.A.2
  • 9
    • 0024725677 scopus 로고
    • Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor
    • Blount, P., and J. P. Merlie. 1989. Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor. Neuron. 3:349-357.
    • (1989) Neuron. , vol.3 , pp. 349-357
    • Blount, P.1    Merlie, J.P.2
  • 10
    • 0027095577 scopus 로고
    • Structure of the gammaless nicotinic acetylcholine receptor: Learning from omission
    • Charnet, P., C. Labarca, and H. A. Lester. 1992. Structure of the gammaless nicotinic acetylcholine receptor: learning from omission. Mol. Pharmacol. 41:708-717.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 708-717
    • Charnet, P.1    Labarca, C.2    Lester, H.A.3
  • 11
    • 0029153305 scopus 로고
    • Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: Mutations of α-subunit tyrosine 190 affect both binding and gating
    • Chen, J., Y. Zhang, G. Akk, S. Sine, and A. Auerbach. 1995. Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of α-subunit tyrosine 190 affect both binding and gating. Biophys. J. 69:849-859.
    • (1995) Biophys. J. , vol.69 , pp. 849-859
    • Chen, J.1    Zhang, Y.2    Akk, G.3    Sine, S.4    Auerbach, A.5
  • 12
    • 0025719155 scopus 로고
    • Agonist binding site of Torpedo electric tissue nicotinic acetylcholine receptor
    • Czajkowski, C., and A. Karlin. 1991. Agonist binding site of Torpedo electric tissue nicotinic acetylcholine receptor. J. Biol. Chem. 266: 22603-22612.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22603-22612
    • Czajkowski, C.1    Karlin, A.2
  • 13
    • 0027208097 scopus 로고
    • Negatively charged amino acid residues in the nicotinic receptor delta subunit that contribute to the binding of acetylcholine
    • Czajkowski, C., C. Kaufmann, and A. Karlin. 1993. Negatively charged amino acid residues in the nicotinic receptor delta subunit that contribute to the binding of acetylcholine. Proc. Natl. Acad. Sci. USA. 90: 6285-6289.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6285-6289
    • Czajkowski, C.1    Kaufmann, C.2    Karlin, A.3
  • 14
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetylcholine receptor a subunit labeled by a photoaffinity ligand for the acetylcholine binding site
    • Dennis, M., J. Giraudat, F. Kotzyba-Hibert, M. Goeldner, C. Hirth, J. Y. Chang, C. Lazure, M. Chretien, and J. P. Changeux. 1988. Amino acids of the Torpedo marmorata acetylcholine receptor a subunit labeled by a photoaffinity ligand for the acetylcholine binding site. Biochemistry. 27:2346-2357.
    • (1988) Biochemistry , vol.27 , pp. 2346-2357
    • Dennis, M.1    Giraudat, J.2    Kotzyba-Hibert, F.3    Goeldner, M.4    Hirth, C.5    Chang, J.Y.6    Lazure, C.7    Chretien, M.8    Changeux, J.P.9
  • 15
    • 0027522236 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: A prototype of ligand-gated ion channels
    • Devillers-Thiery, A., J. L. Galzi, J. L. Eisele, S. Bertrand, D. Bertrand, and J. P. Changeux. 1993. Functional architecture of the nicotinic acetylcholine receptor: a prototype of ligand-gated ion channels. J. Membr. Biol. 136:97-112.
    • (1993) J. Membr. Biol. , vol.136 , pp. 97-112
    • Devillers-Thiery, A.1    Galzi, J.L.2    Eisele, J.L.3    Bertrand, S.4    Bertrand, D.5    Changeux, J.P.6
  • 16
    • 0023868490 scopus 로고
    • Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: A mobile loop envelopes the transition state in an induced-fit mechanism
    • Fersht, A. R., J. W. Knill-Jones, H. Bedouelle, and G. Winter. 1988. Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism. Biochemistry. 27:1581-1587.
    • (1988) Biochemistry , vol.27 , pp. 1581-1587
    • Fersht, A.R.1    Knill-Jones, J.W.2    Bedouelle, H.3    Winter, G.4
  • 17
    • 0029123899 scopus 로고
    • The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating
    • Filatov, G. N., and M. M. White. 1995. The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating. Mol. Pharmacol. 48:379-384.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 379-384
    • Filatov, G.N.1    White, M.M.2
  • 18
    • 0025346780 scopus 로고
    • Identification of a novel amino acid a-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling
    • Galzi, J. L., F. Revah, D. Black, M. Goeldner, C. Hirth, and J. P. Changeux. 1990. Identification of a novel amino acid a-tyrosine 93 within the cholinergic ligands-binding sites of the 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
  • 19
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., A. Many, E. Neher, B. Sakmann, and F. J. Sigworth. 1981. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch. 391:85-100.
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Many, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 20
    • 0001823786 scopus 로고
    • Recombinant PCR
    • M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White, editors. Academic Press, San Diego, CA.
    • Higuchi, R. 1990. Recombinant PCR. In PCR Protocols. A Guide to Methods and Applications. M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White, editors. Academic Press, San Diego, CA. 177-183.
    • (1990) PCR Protocols. A Guide to Methods and Applications , pp. 177-183
    • Higuchi, R.1
  • 23
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin, A., and M. H. Akabas. 1995. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron. 15:1231-1244.
    • (1995) Neuron. , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 24
    • 77956904566 scopus 로고
    • The molecular basis for enzyme regulation
    • Paul D. Boyer, editor. Academic Press, New York
    • Koshland, D. E., Jr. 1970. The molecular basis for enzyme regulation. In The Enzymes. Paul D. Boyer, editor. Academic Press, New York.
    • (1970) The Enzymes
    • Koshland D.E., Jr.1
  • 25
    • 0029163027 scopus 로고
    • Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors
    • Labarca, C., M. W. Nowak, H. Zhang, L. Tang, P. Deshpande, and H. A. Lester. 1995. Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors. Nature. 376: 514-516.
    • (1995) Nature , vol.376 , pp. 514-516
    • Labarca, C.1    Nowak, M.W.2    Zhang, H.3    Tang, L.4    Deshpande, P.5    Lester, H.A.6
  • 26
    • 0031709523 scopus 로고    scopus 로고
    • Intrinsic protein fields: Basic non-covalent interactions and relationship to protein-induced stark effects
    • Laberge, M. 1998. Intrinsic protein fields: basic non-covalent interactions and relationship to protein-induced Stark effects. Biochim. Biophys. Acta. 1386:305-330.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 305-330
    • Laberge, M.1
  • 28
    • 0029929234 scopus 로고    scopus 로고
    • The contributions of aspartyl residues in the acetylcholine receptor gamma and delta subunits to the binding of agonists and competitive antagonists
    • Martin, M., C. Czajkowski, and A. Karlin. 1996. The contributions of aspartyl residues in the acetylcholine receptor gamma and delta subunits to the binding of agonists and competitive antagonists. J. Biol. Chem. 271:13497-13503.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13497-13503
    • Martin, M.1    Czajkowski, C.2    Karlin, A.3
  • 29
    • 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
  • 31
    • 0026758178 scopus 로고
    • Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor
    • O'Leary, M. E., and M. M. White. 1992. Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor. J. Biol. Chem. 267:8360-8365.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8360-8365
    • O'Leary, M.E.1    White, M.M.2
  • 32
    • 0025308169 scopus 로고
    • d-Tubocurarine binding sites are located at α-γ and α-δ subunit interfaces of the nicotinic acetylcholine receptor
    • Pedersen, S. E., and J. B. Cohen. 1990. d-Tubocurarine binding sites are located at α-γ and α-δ subunit interfaces of the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. USA. 87:2785-2789.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2785-2789
    • Pedersen, S.E.1    Cohen, J.B.2
  • 33
    • 0028839740 scopus 로고
    • Reexamination of induced fit as a determinant of substrate specificity in enzymatic reactions
    • Post, C. B., and W. J. Ray, Jr. 1995. Reexamination of induced fit as a determinant of substrate specificity in enzymatic reactions. Biochemistry. 34:15881-15885.
    • (1995) Biochemistry , vol.34 , pp. 15881-15885
    • Post, C.B.1    Ray W.J., Jr.2
  • 34
    • 0029958548 scopus 로고    scopus 로고
    • Molecular dissection of subunit interfaces in the acetylcholine receptor. Identification of residues that determine agonist selectivity
    • Prince, R. J., and S. M. Sine. 1996. Molecular dissection of subunit interfaces in the acetylcholine receptor. Identification of residues that determine agonist selectivity. J. Biol. Chem. 271:25770-25777.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25770-25777
    • Prince, R.J.1    Sine, S.M.2
  • 35
    • 0030061670 scopus 로고    scopus 로고
    • Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events
    • Qin, F., A. Auerbach, and F. Sachs. 1996. Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events. Biophys. J. 70:264-280.
    • (1996) Biophys. J. , vol.70 , pp. 264-280
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 36
    • 0344867346 scopus 로고    scopus 로고
    • Idealization of single-channel currents using the segmental k-means method
    • Qin, F., A. Auerbach, and F. Sachs. 1996a. Idealization of single-channel currents using the segmental k-means method. Biophys. J. 70:A227.
    • (1996) Biophys. J. , vol.70
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 38
    • 0030828982 scopus 로고    scopus 로고
    • Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase
    • Radic, Z., P. D. Kirchhoff, D. M. Quinn, J. A. McCammon, and P. Taylor. 1997. Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. J. Biol. Chem. 272:23265-23277.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23265-23277
    • Radic, Z.1    Kirchhoff, P.D.2    Quinn, D.M.3    McCammon, J.A.4    Taylor, P.5
  • 39
    • 0344102958 scopus 로고
    • Automated analysis of single-channel records
    • B. Sakmann and E. Neher, editors. Plenum Press, New York
    • Sachs, F. 1983. Automated analysis of single-channel records. In Single-Channel Recording. B. Sakmann and E. Neher, editors. Plenum Press, New York. 265-286.
    • (1983) Single-channel Recording , pp. 265-286
    • Sachs, F.1
  • 40
    • 0019215162 scopus 로고
    • Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist
    • Sakmann, B., J. Patlak, and E. Neher. 1980. Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist Nature. 286:71-73.
    • (1980) Nature , vol.286 , pp. 71-73
    • Sakmann, B.1    Patlak, J.2    Neher, E.3
  • 41
    • 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. USA. 90:9436-9440.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9436-9440
    • Sine, S.M.1
  • 42
    • 0026045588 scopus 로고
    • Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor
    • Sine, S. M., and T. Claudio. 1991. Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor. J. Biol. Chem. 266:19369-19377.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19369-19377
    • Sine, S.M.1    Claudio, T.2
  • 43
    • 0029087136 scopus 로고
    • Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenie syndrome by enhancing agonist binding activity
    • Sine, S. M., K. Ohno, C. Bouzat, A. Auerbach, M. Milone, J. N. Pruitt, and A. G. Engel. 1995. Mutation of the acetylcholine receptor α subunit causes a slow-channel myasthenie syndrome by enhancing agonist binding activity. Neuron. 15:229-239.
    • (1995) Neuron. , vol.15 , pp. 229-239
    • Sine, S.M.1    Ohno, K.2    Bouzat, C.3    Auerbach, A.4    Milone, M.5    Pruitt, J.N.6    Engel, A.G.7
  • 44
    • 0028292368 scopus 로고
    • Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists
    • Sine, S. M., P. Quiram, F. Papanikolaou, H. J. Kreienkamp, and P. Taylor. 1994. Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists. J. Biol. Chem. 269:8808-8816.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8808-8816
    • Sine, S.M.1    Quiram, P.2    Papanikolaou, F.3    Kreienkamp, H.J.4    Taylor, P.5
  • 45
    • 0019182078 scopus 로고
    • The relationship between agonist occupation and the permeability response of the cholinergic receptor revealed by bound cobra alpha-toxin
    • Sine, S. M., and P. Taylor. 1980. The relationship between agonist occupation and the permeability response of the cholinergic receptor revealed by bound cobra alpha-toxin. J. Biol. Chem. 255:10144-10156.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10144-10156
    • Sine, S.M.1    Taylor, P.2
  • 46
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototype acetylcholine-binding protein
    • Sussman, J. L., M. Harel, F. Frolow, C. Oefner, A. Goldman, L. Toker, and I. Silman. 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.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 47
    • 0026004411 scopus 로고
    • Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor
    • Tomaselli, G. F., J. T. McLaughlin, M. E. Jurman, E. Hawrot, and G. Yellen. 1991. Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor. Biophys. J. 60:721-727.
    • (1991) Biophys. J. , vol.60 , pp. 721-727
    • Tomaselli, G.F.1    McLaughlin, J.T.2    Jurman, M.E.3    Hawrot, E.4    Yellen, G.5
  • 48
    • 0030957191 scopus 로고    scopus 로고
    • A model of the nicotinic receptor extracellular domain based on sequence identity and residue location
    • Tsigelny, I., N. Sugiyama, S. M. Sine, and P. Taylor. 1997. A model of the nicotinic receptor extracellular domain based on sequence identity and residue location. Biophys. J. 73:52-66.
    • (1997) Biophys. J. , vol.73 , pp. 52-66
    • Tsigelny, I.1    Sugiyama, N.2    Sine, S.M.3    Taylor, P.4
  • 49
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin, N. 1993. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229:1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 50
    • 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
  • 51
    • 0029984543 scopus 로고    scopus 로고
    • Projection structure of the nicotinic acetylcholine receptor: Distinct conformations of the alpha subunits
    • Unwin, N. 1996. Projection structure of the nicotinic acetylcholine receptor: distinct conformations of the alpha subunits. J. Mol. Biol. 257:586-596.
    • (1996) J. Mol. Biol. , vol.257 , pp. 586-596
    • Unwin, N.1
  • 52
    • 0028268955 scopus 로고
    • Transverse distance between the membrane and agonist binding sites on the Torpedo acetyl-choline receptor: A fluorescence study
    • Valenzuela, C. F., E. P. Weign, J. Yguerabide, and D. A. Johnson. 1994. Transverse distance between the membrane and agonist binding sites on the Torpedo acetyl-choline receptor: a fluorescence study. Biophys. J. 66:674-682.
    • (1994) Biophys. J. , vol.66 , pp. 674-682
    • Valenzuela, C.F.1    Weign, E.P.2    Yguerabide, J.3    Johnson, D.A.4
  • 53
    • 0030906795 scopus 로고    scopus 로고
    • Mutation in the M1 domain of the acetylcholine receptor alpha subunit decreases the rate of agonist dissociation
    • Wang, H. L., A. Auerbach, N. Bren, K. Ohno, A. G. Engel, and S. M. Sine. 1997. Mutation in the M1 domain of the acetylcholine receptor alpha subunit decreases the rate of agonist dissociation. J. Gen. Physiol. 109:757-766.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 757-766
    • Wang, H.L.1    Auerbach, A.2    Bren, N.3    Ohno, K.4    Engel, A.G.5    Sine, S.M.6
  • 54
    • 0029041254 scopus 로고
    • Activation of recombinant mouse acetylcholine receptors by acetylcholine, carbamylcholine and tetramethylammonium
    • Zhang, Y., J. Chen, and A. Auerbach. 1995. Activation of recombinant mouse acetylcholine receptors by acetylcholine, carbamylcholine and tetramethylammonium. J. Physiol. (Lond.). 486:189-206.
    • (1995) J. Physiol. (Lond.) , vol.486 , pp. 189-206
    • Zhang, Y.1    Chen, J.2    Auerbach, A.3
  • 55
    • 0032482925 scopus 로고    scopus 로고
    • Conformational gating as a mechanism for enzyme specificity
    • Zhou, H., S. Wlodek, and J. A. McCammon. 1998. Conformational gating as a mechanism for enzyme specificity. Proc. Natl. Acad. Sci. USA. 95:9280-9283.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9280-9283
    • Zhou, H.1    Wlodek, S.2    McCammon, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.