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Volumn 111, Issue 6, 1998, Pages 717-739

State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor: Inferences from rates of reaction of thiosulfonates with substituted cysteines in the M2 segment of the α subunit

Author keywords

Conductance; Gate; Ion selectivity; Reaction kinetics; Sulfhydryl

Indexed keywords

ACETYLCHOLINE; CHOLINERGIC RECEPTOR; CYSTEINE; ION CHANNEL; SULFONIC ACID DERIVATIVE; THIOL DERIVATIVE;

EID: 0031781630     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.111.6.717     Document Type: Article
Times cited : (105)

References (63)
  • 1
    • 0028809730 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the alpha subunit
    • Akabas, M.H., and A. Karlin. 1995. Identification of acetylcholine receptor channel-lining residues in the M1 segment of the alpha subunit. Biochemistry. 34:12496-12500.
    • (1995) Biochemistry , vol.34 , pp. 12496-12500
    • Akabas, M.H.1    Karlin, A.2
  • 2
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit
    • Akabas, M.H., C. Kaufmann, P. Archdeacon, and A. Karlin. 1994a. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit. Neuron. 13:919-927.
    • (1994) Neuron. , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 3
    • 0028264188 scopus 로고
    • Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator
    • Akabas, M.H., C. Kaufmann, T.A. Cook, and P. Archdeacon. 1994b. Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator. J. Biol Chem. 269: 14865-14868.
    • (1994) J. Biol Chem. , vol.269 , pp. 14865-14868
    • Akabas, M.H.1    Kaufmann, C.2    Cook, T.A.3    Archdeacon, P.4
  • 4
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M.H., D.A. Stauffer, M. Xu, and A. Karlin. 1992. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science. 258:307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 5
    • 0015741359 scopus 로고
    • Voltage clamp analysis of acetylcholine produced end-plate current fluctuations at frog neuromuscular junction
    • Anderson, C.R., and C.F. Stevens. 1973. Voltage clamp analysis of acetylcholine produced end-plate current fluctuations at frog neuromuscular junction. J. Physiol. (Camb.). 235:655-691.
    • (1973) J. Physiol. (Camb.) , vol.235 , pp. 655-691
    • Anderson, C.R.1    Stevens, C.F.2
  • 6
    • 0029934560 scopus 로고    scopus 로고
    • Voltage dependence of mouse acetylcholine receptor gating: Different charge movements in di-, mono- and unliganded receptors
    • Auerbach, A., W. Sigurdson, J. Chen, and G. Akk. 1996. Voltage dependence of mouse acetylcholine receptor gating: different charge movements in di-, mono- and unliganded receptors. J. Physiol. (Camb.). 494:155-170.
    • (1996) J. Physiol. (Camb.) , vol.494 , pp. 155-170
    • Auerbach, A.1    Sigurdson, W.2    Chen, J.3    Akk, G.4
  • 7
    • 0002169801 scopus 로고
    • Novel alkyl alkanethiosulfonate sulfhydryl reagents. Modification of derivatives of L-cysteine
    • Bruice, T.W., and G.L. Kenyon. 1982. Novel alkyl alkanethiosulfonate sulfhydryl reagents. Modification of derivatives of L-cysteine. J. Prot. Chem. 1:47-58.
    • (1982) J. Prot. Chem. , vol.1 , pp. 47-58
    • Bruice, T.W.1    Kenyon, G.L.2
  • 8
    • 0025355129 scopus 로고
    • An open-channel blocker interacts with adjacent turns of alpha-helices in the nicotinic acetylcholine receptor
    • Charnet, P., C. Labarca, R.J. Leonard, N.J. Vogelaar, L. Czyzyk, A. Gouin, N. Davidson, and H.A. Lester. 1990. An open-channel blocker interacts with adjacent turns of alpha-helices in the nicotinic acetylcholine receptor. Neuron. 4:87-95.
    • (1990) Neuron. , vol.4 , pp. 87-95
    • Charnet, P.1    Labarca, C.2    Leonard, R.J.3    Vogelaar, N.J.4    Czyzyk, L.5    Gouin, A.6    Davidson, N.7    Lester, H.A.8
  • 9
    • 0030893916 scopus 로고    scopus 로고
    • Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel
    • Cheung, M., and M.H. Akabas. 1997. Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. J. Gen. Physiol. 109:289-299.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 289-299
    • Cheung, M.1    Akabas, M.H.2
  • 10
    • 0026522550 scopus 로고
    • + permeability ratios of nicotinic acetylcholine receptors are reduced by mutations near the intracellular end of the M2 region
    • + permeability ratios of nicotinic acetylcholine receptors are reduced by mutations near the intracellular end of the M2 region. J. Gen. Physiol. 99:545-572.
    • (1992) J. Gen. Physiol. , vol.99 , pp. 545-572
    • Cohen, B.N.1    Labarca, C.2    Czyzyk, L.3    Davidson, N.4    Lester, H.A.5
  • 11
    • 0024511429 scopus 로고
    • Open channel structure and ion binding sites of the nicotinic acetylcholine receptor channel
    • Dani, J.A. 1989. Open channel structure and ion binding sites of the nicotinic acetylcholine receptor channel. J. Neurosci. 9:884-892.
    • (1989) J. Neurosci. , vol.9 , pp. 884-892
    • Dani, J.A.1
  • 12
    • 0023237915 scopus 로고
    • Monovalent and divalent cation permeation in acetylcholine receptor channels. Ion transport related to structure
    • Dani, J.A., and G. Eisenman. 1987. Monovalent and divalent cation permeation in acetylcholine receptor channels. Ion transport related to structure. J. Gen. Physiol. 89:959-983.
    • (1987) J. Gen. Physiol. , vol.89 , pp. 959-983
    • Dani, J.A.1    Eisenman, G.2
  • 13
    • 0025013784 scopus 로고
    • Diffusion and kinetic approaches to describe permeation in ionic channels
    • Dani, J.A., and D.G. Levitt. 1990. Diffusion and kinetic approaches to describe permeation in ionic channels. J. Theor. Biol. 146:289-301.
    • (1990) J. Theor. Biol. , vol.146 , pp. 289-301
    • Dani, J.A.1    Levitt, D.G.2
  • 14
    • 0025291849 scopus 로고
    • 3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor
    • 3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor. J. Biol. Chem. 265:11017-11029.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11017-11029
    • DiPaola, M.1    Kao, P.N.2    Karlin, A.3
  • 15
    • 0029876860 scopus 로고    scopus 로고
    • Computing the field in proteins and channels. J
    • Eisenberg, R. 1996. Computing the field in proteins and channels. J. Membr. Biol. 150:1-25.
    • (1996) Membr. Biol. , vol.150 , pp. 1-25
    • Eisenberg, R.1
  • 16
    • 0001223044 scopus 로고
    • Organic disulfides and related substances. VIII. Preparation and oxidation of some unsymmetrical dialkyl and alkyl pyridinium disulfides
    • Field, L., H. Harle, T.C. Owen, and A. Ferretti. 1964. Organic disulfides and related substances. VIII. Preparation and oxidation of some unsymmetrical dialkyl and alkyl pyridinium disulfides. J. Org. Chem. 29:1632-1635.
    • (1964) J. Org. Chem. , vol.29 , pp. 1632-1635
    • Field, L.1    Harle, H.2    Owen, T.C.3    Ferretti, A.4
  • 17
    • 0006374075 scopus 로고
    • Organic disulfides and related substances. IV. Thiolsulfonates and disulfides containing 2-aminoethyl moieties
    • Field, L., T.C. Owen, R.R. Crenshaw, and A.W. Bryan. 1961. Organic disulfides and related substances. IV. Thiolsulfonates and disulfides containing 2-aminoethyl moieties. J. Am. Chem. Soc. 83: 4414-4417.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 4414-4417
    • Field, L.1    Owen, T.C.2    Crenshaw, R.R.3    Bryan, A.W.4
  • 18
    • 0021530285 scopus 로고
    • Some unexpected consequences of a simple physical mechanism for voltage-dependent gating in biological membranes
    • Finkelstein, A., and C.S. Peskin. 1984. Some unexpected consequences of a simple physical mechanism for voltage-dependent gating in biological membranes. Biophys. J. 46:549-558.
    • (1984) Biophys. J. , vol.46 , pp. 549-558
    • Finkelstein, A.1    Peskin, C.S.2
  • 19
    • 0029046913 scopus 로고
    • Neuronal nicotinic receptors: Molecular organizations and regulations
    • Galzi, J.L., and J.P. Changeux. 1995. Neuronal nicotinic receptors: molecular organizations and regulations. Neuropharmacology. 34: 563-582.
    • (1995) Neuropharmacology , vol.34 , pp. 563-582
    • Galzi, J.L.1    Changeux, J.P.2
  • 20
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • Galzi, J.L., A. Devillers-Thiery, N. Hussy, S. Bertrand, J.P. Changeux, and D. Bertrand. 1992. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature. 359:500-505.
    • (1992) Nature , vol.359 , pp. 500-505
    • Galzi, J.L.1    Devillers-Thiery, A.2    Hussy, N.3    Bertrand, S.4    Changeux, J.P.5    Bertrand, D.6
  • 21
    • 0000123750 scopus 로고
    • Monte-Carlo simulation of the effects of charges on water and ions in a tapered pore
    • Green, M.E., and J. Lu. 1995. Monte-Carlo simulation of the effects of charges on water and ions in a tapered pore. J. Colloid Interface Sci. 171:117-126.
    • (1995) J. Colloid Interface Sci. , vol.171 , pp. 117-126
    • Green, M.E.1    Lu, J.2
  • 22
    • 0026026676 scopus 로고
    • Surface charges and ion channel function
    • Green, W.N., and O.S. Andersen. 1991. Surface charges and ion channel function. Annu. Rev. Physiol. 53:341-359.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 341-359
    • Green, W.N.1    Andersen, O.S.2
  • 23
    • 0021041862 scopus 로고
    • Rapid kinetics of agonist-binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata
    • Heidmann, T., J. Bernhardt, E. Neumann, and J.P. Changeux. 1983. Rapid kinetics of agonist-binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata. Biochemistry. 22:5452-5459.
    • (1983) Biochemistry , vol.22 , pp. 5452-5459
    • Heidmann, T.1    Bernhardt, J.2    Neumann, E.3    Changeux, J.P.4
  • 24
    • 0027458778 scopus 로고
    • Determination of the chemical mechanism of neurotransmitter receptor-mediated reaction by rapid chemical kinetic techniques
    • Hess, G. 1993. Determination of the chemical mechanism of neurotransmitter receptor-mediated reaction by rapid chemical kinetic techniques. Biochemistry. 32:989-1000.
    • (1993) Biochemistry , vol.32 , pp. 989-1000
    • Hess, G.1
  • 26
    • 0029860763 scopus 로고    scopus 로고
    • On the use of thiol-modifying agents to determine channel topology
    • Holmgren, M., Y. Liu, Y. Xu, and G. Yellen. 1996. On the use of thiol-modifying agents to determine channel topology. Neuropharmacology. 35:797-804.
    • (1996) Neuropharmacology , vol.35 , pp. 797-804
    • Holmgren, M.1    Liu, Y.2    Xu, Y.3    Yellen, G.4
  • 27
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 28
    • 0022458822 scopus 로고
    • The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits
    • Hucho, F., W. Oberthur, and F. Lottspeich. 1986. The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits. FEBS Lett. 205:137-142.
    • (1986) FEBS Lett. , vol.205 , pp. 137-142
    • Hucho, F.1    Oberthur, W.2    Lottspeich, F.3
  • 30
    • 0025745108 scopus 로고
    • A ring of uncharged polar amino acids as a component of channel constriction in the nicotinic acetylcholine receptor
    • Imoto, K., T. Konno, J. Nakai, F. Wang, M. Mishina, and S. Numa. 1991. A ring of uncharged polar amino acids as a component of channel constriction in the nicotinic acetylcholine receptor. FEBS Lett. 289:193-200.
    • (1991) FEBS Lett. , vol.289 , pp. 193-200
    • Imoto, K.1    Konno, T.2    Nakai, J.3    Wang, F.4    Mishina, M.5    Numa, S.6
  • 31
    • 0001736094 scopus 로고
    • Perfection of a synaptic receptor: Kinetics and energetics of the acetylcholine receptor
    • Jackson, M.B. 1989. Perfection of a synaptic receptor: kinetics and energetics of the acetylcholine receptor. Proc. Natl. Acad. Sci. USA. 86:2199-2203.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2199-2203
    • Jackson, M.B.1
  • 32
    • 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
  • 33
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine-accessibility method
    • P.M. Conn, editor. Academic Press Inc., San Diego, CA
    • Karlin, A., and M.H. Akabas. 1998. Substituted-cysteine-accessibility method. In Methods in Enzymology. Vol. 293. P.M. Conn, editor. Academic Press Inc., San Diego, CA. 123-136.
    • (1998) Methods in Enzymology , vol.293 , pp. 123-136
    • Karlin, A.1    Akabas, M.H.2
  • 34
    • 84965075853 scopus 로고
    • A study of 'desensitization' produced by acetylcholine at the motor end-plate
    • Katz, B., and S. Thesleff. 1957. A study of 'desensitization' produced by acetylcholine at the motor end-plate. J. Physiol. (Camb.). 138:63-80.
    • (1957) J. Physiol. (Camb.) , vol.138 , pp. 63-80
    • Katz, B.1    Thesleff, S.2
  • 36
    • 0030220889 scopus 로고    scopus 로고
    • Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines
    • Kuner, T., L.P. Wollmuth, A. Karlin, P.H. Seeburg, and B. Sakmann. 1996. Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines. Neuron. 17:343-352.
    • (1996) Neuron. , vol.17 , pp. 343-352
    • Kuner, T.1    Wollmuth, L.P.2    Karlin, A.3    Seeburg, P.H.4    Sakmann, B.5
  • 37
    • 0028941130 scopus 로고
    • + channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis
    • + channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis. Biophys. J. 68:900-905.
    • (1995) Biophys. J. , vol.68 , pp. 900-905
    • Kurz, L.L.1    Zuhlke, R.D.2    Zhang, H.J.3    Joho, R.H.4
  • 39
    • 0028960949 scopus 로고
    • Silver as a probe of pore-forming residues in a potassium channel
    • Lu, Q., and G. Miller. 1995. Silver as a probe of pore-forming residues in a potassium channel. Science. 268:304-307.
    • (1995) Science , vol.268 , pp. 304-307
    • Lu, Q.1    Miller, G.2
  • 40
    • 0017905087 scopus 로고
    • Local anaesthetics transiently block currents through single acetylcholine-receptor channels
    • Neher, E., and J.H. Steinbach. 1978. Local anaesthetics transiently block currents through single acetylcholine-receptor channels. J. Physiol. (Camb.). 277:153-176.
    • (1978) J. Physiol. (Camb.) , vol.277 , pp. 153-176
    • Neher, E.1    Steinbach, J.H.2
  • 41
    • 0019985295 scopus 로고
    • Conformations of Torpedo acetylcholine receptor associated with ion transport and desensitization
    • Neubig, R.R., N.D. Boyd, and J.B. Cohen. 1982. Conformations of Torpedo acetylcholine receptor associated with ion transport and desensitization. Biochemistry. 21:3460-3467.
    • (1982) Biochemistry , vol.21 , pp. 3460-3467
    • Neubig, R.R.1    Boyd, N.D.2    Cohen, J.B.3
  • 42
    • 0345163542 scopus 로고    scopus 로고
    • Binding site for QX-314, a quaternary lidocaine derivative, in the channel of the acetylcholine receptor
    • Pascual, J.M., and A. Karlin. 1997a. Binding site for QX-314, a quaternary lidocaine derivative, in the channel of the acetylcholine receptor. Biophys. J. 72:A151.
    • (1997) Biophys. J. , vol.72
    • Pascual, J.M.1    Karlin, A.2
  • 43
    • 13044297982 scopus 로고    scopus 로고
    • Electrostatic potential in the open and closed channel of the acetylcholine receptor
    • Pascual, J.M., and A. Karlin. 1997b. Electrostatic potential in the open and closed channel of the acetylcholine receptor. Soc. Neurosci. Abstr. 23:388.
    • (1997) Soc. Neurosci. Abstr. , vol.23 , pp. 388
    • Pascual, J.M.1    Karlin, A.2
  • 44
    • 0029070117 scopus 로고
    • + pore structure revealed by reporter cysteines at inner and outer surfaces
    • + pore structure revealed by reporter cysteines at inner and outer surfaces. Neuron. 14:1055-1063.
    • (1995) Neuron. , vol.14 , pp. 1055-1063
    • Pascual, J.M.1    Shieh, C.C.2    Kirsch, G.E.3    Brown, A.M.4
  • 45
    • 0026672984 scopus 로고
    • Structure of the noncompetitive antagonist-binding site of the Torpedo nicotinic acetylcholine receptor. [3H]meproadifen mustard reacts selectively with alpha-subunit Glu-262
    • Pedersen, S.E., S.D. Sharp, W.S. Liu, and J.B. Cohen. 1992. Structure of the noncompetitive antagonist-binding site of the Torpedo nicotinic acetylcholine receptor. [3H]meproadifen mustard reacts selectively with alpha-subunit Glu-262. J. Biol. Chem. 267:10489-10499.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10489-10499
    • Pedersen, S.E.1    Sharp, S.D.2    Liu, W.S.3    Cohen, J.B.4
  • 46
    • 0025195179 scopus 로고
    • The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: Implications for the alpha-helical organization of regions MII and for the structure of the ion channel
    • Revah, F., J.L. Galzi, J. Giraudat, P.Y. Haumont, F. Lederer, and J.P. Changeux. 1990. The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: implications for the alpha-helical organization of regions MII and for the structure of the ion channel. Proc. Natl. Acad. Sci. USA. 87:4675-4679.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4675-4679
    • Revah, F.1    Galzi, J.L.2    Giraudat, J.3    Haumont, P.Y.4    Lederer, F.5    Changeux, J.P.6
  • 47
    • 0027265211 scopus 로고
    • An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase
    • Ripoll, D.R., C.H. Faerman, P.H. Axelsen, I. Silman, and J.L. Sussman. 1993. An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. Proc. Natl. Acad. Sci. USA. 90:5128-5132.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5128-5132
    • Ripoll, D.R.1    Faerman, C.H.2    Axelsen, P.H.3    Silman, I.4    Sussman, J.L.5
  • 48
    • 0023055733 scopus 로고
    • Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate
    • Roberts, D.D., S.D. Lewis, D.P. Ballou, S.T. Olson, and J.A. Shafer. 1986. Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate. Biochemistry. 25:5595-5601.
    • (1986) Biochemistry , vol.25 , pp. 5595-5601
    • Roberts, D.D.1    Lewis, S.D.2    Ballou, D.P.3    Olson, S.T.4    Shafer, J.A.5
  • 49
    • 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
  • 50
    • 0022920987 scopus 로고
    • Slow permeation of organic cations in acetylcholine receptor channels
    • Sanchez, J.A., J.A. Dani, D. Siemen, and B. Hille. 1986. Slow permeation of organic cations in acetylcholine receptor channels. J. Gen. Physiol. 87:985-1001.
    • (1986) J. Gen. Physiol. , vol.87 , pp. 985-1001
    • Sanchez, J.A.1    Dani, J.A.2    Siemen, D.3    Hille, B.4
  • 51
    • 0028222912 scopus 로고
    • Voltage clamping of Xenopus laevis oocytes utilizing agarose-cushion electrodes
    • Schreibmayer, W., H.A. Lester, and N. Dascal. 1994. Voltage clamping of Xenopus laevis oocytes utilizing agarose-cushion electrodes. Pflügers Arch. 426:453-458.
    • (1994) Pflügers Arch. , vol.426 , pp. 453-458
    • Schreibmayer, W.1    Lester, H.A.2    Dascal, N.3
  • 52
    • 0028355745 scopus 로고
    • Electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates
    • Stauffer, D.A., and A. Karlin. 1994. Electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates. Biochemistry. 33:6840-6849.
    • (1994) Biochemistry , vol.33 , pp. 6840-6849
    • Stauffer, D.A.1    Karlin, A.2
  • 53
    • 0030057048 scopus 로고    scopus 로고
    • Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating
    • Sun, Z.P., M.H. Akabas, E.H. Goulding, A. Karlin, and S.A. Siegelbaum. 1996. Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating. Neuron. 16:141-149.
    • (1996) Neuron. , vol.16 , pp. 141-149
    • Sun, Z.P.1    Akabas, M.H.2    Goulding, E.H.3    Karlin, A.4    Siegelbaum, S.A.5
  • 54
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 A resolution
    • Unwin, N. 1993. Nicotinic acetylcholine receptor at 9 A resolution. J. Mol. Biol. 229:1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 55
    • 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
  • 56
    • 0026082583 scopus 로고
    • Location of a threonine residue in the alpha-subunit M2 transmembrane segment that determines the ion flow through the acetylcholine receptor channel
    • Villarroel, A., S. Herlitze, M. Koenen, and B. Sakmann. 1991. Location of a threonine residue in the alpha-subunit M2 transmembrane segment that determines the ion flow through the acetylcholine receptor channel. Proc. R. Soc. Lond. B Biol. Sci. 243:69-74.
    • (1991) Proc. R. Soc. Lond. B Biol. Sci. , vol.243 , pp. 69-74
    • Villarroel, A.1    Herlitze, S.2    Koenen, M.3    Sakmann, B.4
  • 57
    • 0032102496 scopus 로고    scopus 로고
    • The location of the gate in the acetylcholine channel
    • In press
    • Wilson, G.G., and A. Karlin. 1998. The location of the gate in the acetylcholine channel. Neuron. In press.
    • (1998) Neuron.
    • Wilson, G.G.1    Karlin, A.2
  • 58
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • Woodhull, A.M. 1973. Ionic blockage of sodium channels in nerve. J. Gen. Physiol. 61:687-708.
    • (1973) J. Gen. Physiol. , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 59
    • 0029865892 scopus 로고    scopus 로고
    • Identification of channel-lining residues in the M2 membrane-spanning segment of the GABA(A) receptor alphal subunit
    • Xu, M., and M.H. Akabas. 1996. Identification of channel-lining residues in the M2 membrane-spanning segment of the GABA(A) receptor alphal subunit. J. Physiol. 107:195-205.
    • (1996) J. Physiol. , vol.107 , pp. 195-205
    • Xu, M.1    Akabas, M.H.2
  • 60
    • 0028970548 scopus 로고
    • Interaction of picrotoxin with GABA(A) receptor channel-lining residues probed in cysteine mutants
    • Xu, M., D.F. Covey, and M.H. Akabas. 1995. Interaction of picrotoxin with GABA(A) receptor channel-lining residues probed in cysteine mutants. Biophys. J. 69:1858-1867.
    • (1995) Biophys. J. , vol.69 , pp. 1858-1867
    • Xu, M.1    Covey, D.F.2    Akabas, M.H.3
  • 61
    • 0030731887 scopus 로고    scopus 로고
    • Probing the outer vestibule of a sodium channel voltage sensor
    • Yang, N., A.L. George, and R. Horn. 1997. Probing the outer vestibule of a sodium channel voltage sensor. Biophys. J. 73:2260-2268.
    • (1997) Biophys. J. , vol.73 , pp. 2260-2268
    • Yang, N.1    George, A.L.2    Horn, R.3
  • 62
    • 0031456382 scopus 로고    scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the beta subunit
    • Zhang, H., and A. Karlin. 1997. Identification of acetylcholine receptor channel-lining residues in the M1 segment of the beta subunit. Biochemistry. 36:15856-15864.
    • (1997) Biochemistry , vol.36 , pp. 15856-15864
    • Zhang, H.1    Karlin, A.2
  • 63
    • 0032474432 scopus 로고    scopus 로고
    • Contribution of the beta subunit M2 segment to the ion-conducting pathway of the acetylcholine receptor
    • In press
    • Zhang, H., and A. Karlin. 1998. Contribution of the beta subunit M2 segment to the ion-conducting pathway of the acetylcholine receptor. Biochemistry. In press.
    • (1998) Biochemistry
    • Zhang, H.1    Karlin, A.2


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