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Volumn 17, Issue 2, 1998, Pages 239-260

Structure, function, and biophysical aspects of κ-neurotoxins

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA BUNGAROTOXIN; NEUROTOXIN; NICOTINIC RECEPTOR;

EID: 0031860263     PISSN: 07313837     EISSN: None     Source Type: Journal    
DOI: 10.3109/15569549809009251     Document Type: Review
Times cited : (4)

References (64)
  • 1
    • 0020508937 scopus 로고
    • Kappa-bungarotoxin: A probe for the neuronal nicotinic receptor in the avian ciliary ganglion
    • Chiappinelli, V. A., Kappa-bungarotoxin: a probe for the neuronal nicotinic receptor in the avian ciliary ganglion, Brain Res 277: 9, 1983.
    • (1983) Brain Res , vol.277 , pp. 9
    • Chiappinelli, V.A.1
  • 2
    • 0018393964 scopus 로고
    • Inhibition of neuronal acetylcholine sensitivity by alpha-toxins from Bungarus multicinctus venom
    • Ravdin, P. M., and Berg, D. K., Inhibition of neuronal acetylcholine sensitivity by alpha-toxins from Bungarus multicinctus venom., Proc. Nat. Acad. Sci. U.S.A. 76: 2072, 1979.
    • (1979) Proc. Nat. Acad. Sci. U.S.A. , vol.76 , pp. 2072
    • Ravdin, P.M.1    Berg, D.K.2
  • 3
    • 0021249412 scopus 로고
    • Characterization of a snake venom neurotoxin which blocks nicotinic transmission in the avian ciliary ganglion
    • Loring, R. H., Chiappinelli, V. A., Zigmond, R. E., and Cohen J. B., Characterization of a snake venom neurotoxin which blocks nicotinic transmission in the avian ciliary ganglion., Neuroscience 11(4): 989, 1984.
    • (1984) Neuroscience , vol.11 , Issue.4 , pp. 989
    • Loring, R.H.1    Chiappinelli, V.A.2    Zigmond, R.E.3    Cohen, J.B.4
  • 4
    • 0023459530 scopus 로고
    • Molecular studies of the neuronal nicotinic acetylcholine receptor family
    • Lindstrom, J., Schoepfer, R., and Whiting, P., Molecular studies of the neuronal nicotinic acetylcholine receptor family, Mol. Neurobiol. 1: 281, 1987.
    • (1987) Mol. Neurobiol. , vol.1 , pp. 281
    • Lindstrom, J.1    Schoepfer, R.2    Whiting, P.3
  • 5
    • 0018098589 scopus 로고
    • Alpha-Bungarotoxin blocks nicotinic transmission in the avian ciliary ganglion
    • Chiappinelli, V. A., and Zigmond, R. E., alpha-Bungarotoxin blocks nicotinic transmission in the avian ciliary ganglion., Proc Natl Acad Sci U S A 75(6): 2999, 1978.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , Issue.6 , pp. 2999
    • Chiappinelli, V.A.1    Zigmond, R.E.2
  • 6
    • 0019454527 scopus 로고
    • The effects of α- and β-neurotoxins from the venoms of various snakes on transmission in autonomie ganglia
    • Chiappinelli, V. A., Cohen, J. B., and Zigmond, R. E., The effects of α- and β-neurotoxins from the venoms of various snakes on transmission in autonomie ganglia., Brain Res. 211:107, 1981.
    • (1981) Brain Res. , vol.211 , pp. 107
    • Chiappinelli, V.A.1    Cohen, J.B.2    Zigmond, R.E.3
  • 7
    • 0021953776 scopus 로고
    • κ-Bungarotoxin: Complete amino acid sequence of a neuronal nicotinic receptor probe
    • Grant, G. A., and Chiappinelli, V. A., κ-Bungarotoxin: Complete amino acid sequence of a neuronal nicotinic receptor probe., Biochemistry 24:1532, 1985.
    • (1985) Biochemistry , vol.24 , pp. 1532
    • Grant, G.A.1    Chiappinelli, V.A.2
  • 8
    • 0021257583 scopus 로고
    • Nicotinic transmission in sympathetic ganglia: Blockade by the snake venom neurotoxin kappa-bungarotoxin
    • Chiappinelli, V. A., and Dryer, S. E., Nicotinic transmission in sympathetic ganglia: blockade by the snake venom neurotoxin kappa-bungarotoxin., Neurosci Lett 50(1-3): 239, 1984.
    • (1984) Neurosci Lett , vol.50 , Issue.1-3 , pp. 239
    • Chiappinelli, V.A.1    Dryer, S.E.2
  • 9
    • 0023863301 scopus 로고
    • Kappa-Bungarotoxin: Binding of a neuronal nicotinic receptor antagonist to chick optic lobe and skeletal muscle
    • Wolf, K. M., Ciarleglio, A., and Chiappinelli, V. A., kappa-Bungarotoxin: binding of a neuronal nicotinic receptor antagonist to chick optic lobe and skeletal muscle., Brain Res. 439: 249, 1988.
    • (1988) Brain Res. , vol.439 , pp. 249
    • Wolf, K.M.1    Ciarleglio, A.2    Chiappinelli, V.A.3
  • 11
    • 0000950985 scopus 로고
    • κ-neurotoxins and α-neurotoxins: Effects on neuronal nicotinic acetylcholine receptors
    • edited by A. L. Harvey, Pergammon Press, New York
    • Chiappinelli, V. A., κ-neurotoxins and α-neurotoxins: Effects on neuronal nicotinic acetylcholine receptors, in Snake Toxins, edited by A. L. Harvey, p. 223, Pergammon Press, New York, 1991.
    • (1991) Snake Toxins , pp. 223
    • Chiappinelli, V.A.1
  • 12
    • 0024284068 scopus 로고
    • Toxins from the venom of the green mamba Dendroaspis angusticeps that inhibit the binding of quinuclidinyl benzilate to muscarinic acetylcholine receptors
    • Adem, A., Asblom, A., Johansson, G., Mbugua, P.M., and Karlsson, E., Toxins from the venom of the green mamba Dendroaspis angusticeps that inhibit the binding of quinuclidinyl benzilate to muscarinic acetylcholine receptors., Biochim Biophys Acta 968: 340, 1988.
    • (1988) Biochim Biophys Acta , vol.968 , pp. 340
    • Adem, A.1    Asblom, A.2    Johansson, G.3    Mbugua, P.M.4    Karlsson, E.5
  • 13
    • 0026613082 scopus 로고
    • J.9-Å resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom
    • le Du, M.H., Marchot, P., Bougis, P.E., and Fontecilla-Camps, J.C., J.9-Å resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom., J.Biol. Chem. 267: 22122, 1992.
    • (1992) J.Biol. Chem. , vol.267 , pp. 22122
    • Le Du, M.H.1    Marchot, P.2    Bougis, P.E.3    Fontecilla-Camps, J.C.4
  • 14
    • 0026057992 scopus 로고
    • Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channel
    • de Weille, J.R., Schweitz, H., Maes, P., Tartar, A., and Lazdunski, M., Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channel., Proc. Natl. Acad. Sci. U. S. A. 88: 2437, 1991.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 2437
    • De Weille, J.R.1    Schweitz, H.2    Maes, P.3    Tartar, A.4    Lazdunski, M.5
  • 15
    • 0026650803 scopus 로고
    • Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins
    • McDowell, R.S., Dennis, M.S., Louie, A., Shuster, M., Mulkerrin, M.G., and Lazarus, R.A., Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins., Biochemistry 31:4766, 1992.
    • (1992) Biochemistry , vol.31 , pp. 4766
    • McDowell, R.S.1    Dennis, M.S.2    Louie, A.3    Shuster, M.4    Mulkerrin, M.G.5    Lazarus, R.A.6
  • 16
    • 0027219233 scopus 로고
    • Xenoxins, a family of peptides from dorsal gland secretion of Xenopus laevis related to snake venom cytotoxins and neurotoxins
    • Kolbe, H.V., Huber, A., Cordier, P., Rasmussen, U.B., Bouchon, B., Jaquinod, M., Vlasak, R., Delot, E.C., and Kreil, G., Xenoxins, a family of peptides from dorsal gland secretion of Xenopus laevis related to snake venom cytotoxins and neurotoxins., J. Biol. Chem. 268: 16458, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16458
    • Kolbe, H.V.1    Huber, A.2    Cordier, P.3    Rasmussen, U.B.4    Bouchon, B.5    Jaquinod, M.6    Vlasak, R.7    Delot, E.C.8    Kreil, G.9
  • 17
    • 0025181566 scopus 로고
    • 3 -bungarotoxin: Two new nueronal nicotinic receptor agonists isolated from the venom of Bungarus multicinctus
    • 3 -bungarotoxin: Two new nueronal nicotinic receptor agonists isolated from the venom of Bungarus multicinctus., Brain Research 509: 237, 1990.
    • (1990) Brain Research , vol.509 , pp. 237
    • Chiappinelli, V.A.1    Wolf, K.M.2    Grant, G.A.3    Shi-Jiu, C.4
  • 18
    • 0025266863 scopus 로고
    • cDNA deduced amino acid sequences of two novel kappa-neurotoxins from Bungarus multicinctus
    • Danse, J-M., and Garnier, J-M., cDNA deduced amino acid sequences of two novel kappa-neurotoxins from Bungarus multicinctus., Nucl. Acids Res. 18: 1050, 1990.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 1050
    • Danse, J.-M.1    Garnier, J.-M.2
  • 19
    • 0023137265 scopus 로고
    • Kappa-flavitoxin: Isolation of a new neuronal nicotinic receptor antagonist related to kappa-bungarotoxin
    • Chiappinelli, V. A., Wolf, K. M., DeBin, J. A., and Holt, I. L., Kappa-flavitoxin: isolation of a new neuronal nicotinic receptor antagonist related to kappa-bungarotoxin, Brain Research 402: 21, 1987.
    • (1987) Brain Research , vol.402 , pp. 21
    • Chiappinelli, V.A.1    Wolf, K.M.2    DeBin, J.A.3    Holt, I.L.4
  • 20
    • 0030026194 scopus 로고    scopus 로고
    • Facile production of native-like kappa-bungarotoxin in yeast: An enhanced system for the production of a neuronal nicotinic acetylcholine receptor probe
    • Fiordalisi, J. J., James, P. L., Zhang, Y., & Grant, G. A., Facile production of native-like kappa-bungarotoxin in yeast: an enhanced system for the production of a neuronal nicotinic acetylcholine receptor probe., Toxicon 34: 213, 1996.
    • (1996) Toxicon , vol.34 , pp. 213
    • Fiordalisi, J.J.1    James, P.L.2    Zhang, Y.3    Grant, G.A.4
  • 21
    • 7144239997 scopus 로고
    • Characterization of snake venom neurotoxin which blocks nicotinic transmission in autonomie ganglia
    • Loring, R. H., Chiappinelli, V. A., Zigmond, R. E., and Cohen J. B., Characterization of snake venom neurotoxin which blocks nicotinic transmission in autonomie ganglia., Soc. Neurosci. Abstr. 9: 1143, 1983.
    • (1983) Soc. Neurosci. Abstr. , vol.9 , pp. 1143
    • Loring, R.H.1    Chiappinelli, V.A.2    Zigmond, R.E.3    Cohen, J.B.4
  • 22
    • 0019795741 scopus 로고
    • Internalizatton of α-bungarotoxin on neurons induced by a neurotoxin that blocks neuronal acetrylcholine sensitivity
    • Ravdin, P. M., Nitkin, R. N., and Berg, D. K., Internalizatton of α-bungarotoxin on neurons induced by a neurotoxin that blocks neuronal acetrylcholine sensitivity. J. Neurosci. 1: 849, 1981.
    • (1981) J. Neurosci. , vol.1 , pp. 849
    • Ravdin, P.M.1    Nitkin, R.N.2    Berg, D.K.3
  • 23
    • 0018050372 scopus 로고
    • Time course of appearance of α-bungarotoxin binding sites during development of chick ciliary ganglion and iris
    • Chiappinelli, V. A., and Giocobini, E., Time course of appearance of α-bungarotoxin binding sites during development of chick ciliary ganglion and iris., Neurochem. Res. 3: 465, 1978.
    • (1978) Neurochem. Res. , vol.3 , pp. 465
    • Chiappinelli, V.A.1    Giocobini, E.2
  • 24
    • 0025605864 scopus 로고
    • A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BgTx
    • Couturier, S., Bertrand, D., Matter, J. M., Hernandez, M. C., Bertrand, S. , Miliar, N., Valera, S., Barkas, T., Ballivet, M., A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BgTx., Neuron 5: 847, 1990.
    • (1990) Neuron , vol.5 , pp. 847
    • Couturier, S.1    Bertrand, D.2    Matter, J.M.3    Hernandez, M.C.4    Bertrand, S.5    Miliar, N.6    Valera, S.7    Barkas, T.8    Ballivet, M.9
  • 25
    • 0023802813 scopus 로고
    • κ-Bungarotoxin blocks an α-bungarotoxin-sensitive nicotinic receptor in the insect central nervous system
    • Pinnock, R. D., Lummis S. C. R., Chiappinelli, V. A., and Sattelle, D. B., κ-Bungarotoxin blocks an α-bungarotoxin-sensitive nicotinic receptor in the insect central nervous system., Brain Res. 458: 45, 1988.
    • (1988) Brain Res. , vol.458 , pp. 45
    • Pinnock, R.D.1    Lummis, S.C.R.2    Chiappinelli, V.A.3    Sattelle, D.B.4
  • 26
    • 0030766456 scopus 로고    scopus 로고
    • Only Snake Curaremimetic Toxins with a Fifth Disulfide Bond Have High Affinity for the Neuronal α7 Nicotinic Receptor
    • Servent, D., Winckler-Dietrich, V., Hu, H-Y., Kessler, P., Drevet, P., Bertrand, D., and Menez, A., Only Snake Curaremimetic Toxins with a Fifth Disulfide Bond Have High Affinity for the Neuronal α7 Nicotinic Receptor. J. Biol. Chem. 272: 24279, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24279
    • Servent, D.1    Winckler-Dietrich, V.2    Hu, H.-Y.3    Kessler, P.4    Drevet, P.5    Bertrand, D.6    Menez, A.7
  • 27
    • 0022513746 scopus 로고    scopus 로고
    • Amino Acid sequence of Toxin F, a snake venom toxin that blocks neuronal nicotinic receptors
    • Loring, R. H., Andrews, D., Lane, W., and Zigmond, R. E., Amino Acid sequence of Toxin F, a snake venom toxin that blocks neuronal nicotinic receptors., Brain. Res. 385:30.
    • Brain. Res. , vol.385 , pp. 30
    • Loring, R.H.1    Andrews, D.2    Lane, W.3    Zigmond, R.E.4
  • 28
    • 0028171618 scopus 로고
    • Affinity of Native κ-Bungarotoxin and Site-Directed Mutants for the Muscle Nicotinic Acetylcholine Receptor
    • Fiordalisi, J. J., Al-Rabiee, R., Chiappineili, V. A., and Grant, G. A., Affinity of Native κ-Bungarotoxin and Site-Directed Mutants for the Muscle Nicotinic Acetylcholine Receptor., Biochemistry 33:12962, 1994.
    • (1994) Biochemistry , vol.33 , pp. 12962
    • Fiordalisi, J.J.1    Al-Rabiee, R.2    Chiappineili, V.A.3    Grant, G.A.4
  • 29
    • 0023447276 scopus 로고
    • Functional expression of two neuronal nicotinic acetylcholine receptors from cDNA clones identifies a gene family
    • Boulter, J., Connolly, J., Deneris, E., Goldman, D., Heinemann, S., and Patrick, J., Functional expression of two neuronal nicotinic acetylcholine receptors from cDNA clones identifies a gene family, Proc. Natl. Acad. Sci. USA 84:7763, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7763
    • Boulter, J.1    Connolly, J.2    Deneris, E.3    Goldman, D.4    Heinemann, S.5    Patrick, J.6
  • 30
    • 0025472462 scopus 로고    scopus 로고
    • Neurotoxins distinguish between different neuronal nicotinic acetylcholine receptor subunit combinations
    • Leutje, C. W., Wada, K., Rogers, S., Abramson, S. N., Tsuji, K., Heinemann, S., and Patrick, J., Neurotoxins distinguish between different neuronal nicotinic acetylcholine receptor subunit combinations., J. Neurochem. 55: 632.
    • J. Neurochem. , vol.55 , pp. 632
    • Leutje, C.W.1    Wada, K.2    Rogers, S.3    Abramson, S.N.4    Tsuji, K.5    Heinemann, S.6    Patrick, J.7
  • 31
    • 0024741286 scopus 로고
    • The functional diversity of the neuronal nicotinic acetylcholine receptors is increased by a novel subunit: β4
    • Duvoisin, R. M., Deneris, E. S., Patrick, J., and Heinemann, S., The functional diversity of the neuronal nicotinic acetylcholine receptors is increased by a novel subunit: β4., Neuron 3:487, 1989.
    • (1989) Neuron , vol.3 , pp. 487
    • Duvoisin, R.M.1    Deneris, E.S.2    Patrick, J.3    Heinemann, S.4
  • 32
    • 0027241760 scopus 로고
    • The amino terminal half of the nicotinic b-subunit extracellular domain regulates the kinetics of inhibition by neuronal bungarotoxin
    • Papke, R. L., Duvoisin, R. M., and Heinemann, S. F., The amino terminal half of the nicotinic b-subunit extracellular domain regulates the kinetics of inhibition by neuronal bungarotoxin., Proc. Roy. Soc. London B. Biol. Sci. 252:141, 1993.
    • (1993) Proc. Roy. Soc. London B. Biol. Sci. , vol.252 , pp. 141
    • Papke, R.L.1    Duvoisin, R.M.2    Heinemann, S.F.3
  • 33
    • 0028940759 scopus 로고
    • Neurons Can Maintain Multiple Classes of Nicotinic Acetylcholine Receptors Distinguished by Different Subunit Compositions
    • Conroy, W. G., and Berg, D. K., Neurons Can Maintain Multiple Classes of Nicotinic Acetylcholine Receptors Distinguished by Different Subunit Compositions., J. Biol. Chem. 270:4424, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4424
    • Conroy, W.G.1    Berg, D.K.2
  • 34
    • 0029998344 scopus 로고    scopus 로고
    • Assembly of Human Neuronal Nicotinic Receptor a5 Subunits with a3, b2, and b4 subunits
    • Wang, F., Gerzanich, V., Wells, G. B., Anand, R., Peng, X., Keyser, K., and Lindstrom, J., Assembly of Human Neuronal Nicotinic Receptor a5 Subunits with a3, b2, and b4 subunits., J. Biol. Chem. 271:17656, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17656
    • Wang, F.1    Gerzanich, V.2    Wells, G.B.3    Anand, R.4    Peng, X.5    Keyser, K.6    Lindstrom, J.7
  • 35
    • 0025316680 scopus 로고
    • Mapping of a cholinergic binding site by means of synthetic peptides, monoclonal antibodies, and α-bungarotoxin
    • Conti-Tronconi, B. M., Tang, F., Diethelm, B. M., Spencer, S. R., Reinhardt-Maelicke, S., and Maelicke, A, Mapping of a cholinergic binding site by means of synthetic peptides, monoclonal antibodies, and α-bungarotoxin., Biochemistry 29: 6221, 1990.
    • (1990) Biochemistry , vol.29 , pp. 6221
    • Conti-Tronconi, B.M.1    Tang, F.2    Diethelm, B.M.3    Spencer, S.R.4    Reinhardt-Maelicke, S.5    Maelicke, A.6
  • 36
    • 0025022320 scopus 로고
    • Localization of sequence segments forming a κ-bungarotoxin-binding site on the α3 neuronal nicotinic receptor
    • McLane, K. E., Tang, F., and Conti-Tronconi, B. M., Localization of sequence segments forming a κ-bungarotoxin-binding site on the α3 neuronal nicotinic receptor. J. Biol. Chem. 265:1537, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1537
    • McLane, K.E.1    Tang, F.2    Conti-Tronconi, B.M.3
  • 37
    • 0024290419 scopus 로고
    • Amino acid sequence of κ-flavitoxin: Establishment of a new family of snake venom neurotoxins
    • Grant, G. A., Frazier, M. W., and Chiappinelli, V. A., Amino acid sequence of κ-flavitoxin: Establishment of a new family of snake venom neurotoxins., Biochemistry 27:3794, 1988.
    • (1988) Biochemistry , vol.27 , pp. 3794
    • Grant, G.A.1    Frazier, M.W.2    Chiappinelli, V.A.3
  • 38
    • 0001765604 scopus 로고
    • Chemistry of Protein Toxins in Snake Venoms
    • edited by C.Y. Lee, Springer Verlag, Berlin
    • Karlsson, E., Chemistry of Protein Toxins in Snake Venoms.. In Snake Venoms: Handbook of Experimental Pharmacology, edited by C.Y. Lee, Vol. 52, p. 159, Springer Verlag, Berlin, 1979.
    • (1979) Snake Venoms: Handbook of Experimental Pharmacology , vol.52 , pp. 159
    • Karlsson, E.1
  • 39
    • 0027396750 scopus 로고
    • Genetic engineering of snake toxins: Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis
    • Pillet, L., Trémeau, O., Ducancel, F., Drevet, P., Zinn-Justin, S., Pinkasfeld, S., Boulain, J-C, and Ménez, A., Genetic engineering of snake toxins: Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis., J. Biol. Chem. 268:909, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 909
    • Pillet, L.1    Trémeau, O.2    Ducancel, F.3    Drevet, P.4    Zinn-Justin, S.5    Pinkasfeld, S.6    Boulain, J.-C.7    Ménez, A.8
  • 40
    • 0028934293 scopus 로고
    • Genetic engineering of snake toxins: The functional site of erabutoxin A, as delineated by site-directed mutagenesis, includes variant residues
    • Treméau, O., Lemaire, C., Drevet, P., Pinkasfeld, S., Ducancel, F., Boulain, J-C., and Menez, A., Genetic engineering of snake toxins: The functional site of erabutoxin A, as delineated by site-directed mutagenesis, includes variant residues., J. Biol. Chem. 270: 9362, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9362
    • Treméau, O.1    Lemaire, C.2    Drevet, P.3    Pinkasfeld, S.4    Ducancel, F.5    Boulain, J.-C.6    Menez, A.7
  • 42
    • 0025768399 scopus 로고
    • Solution structure of neuronal bunarotoxin determined by two-dimensional NMR spectroscopy: Sequence specific assignments, secondary structure, and dimer formation
    • Oswald, R. E., Sutcliffe, M. J., Bamberger, M., Loring, R. H., Braswell, E., and Dobson, C. M., Solution structure of neuronal bunarotoxin determined by two-dimensional NMR spectroscopy: Sequence specific assignments, secondary structure, and dimer formation., Biochemistry 30: 4901, 1991.
    • (1991) Biochemistry , vol.30 , pp. 4901
    • Oswald, R.E.1    Sutcliffe, M.J.2    Bamberger, M.3    Loring, R.H.4    Braswell, E.5    Dobson, C.M.6
  • 43
    • 0026538668 scopus 로고
    • Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy; Calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics
    • Sutcliffe, M. J., Dobson, C. M., and Oswald, R. E., Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy; Calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics., Biochemistry 31:2962, 1992.
    • (1992) Biochemistry , vol.31 , pp. 2962
    • Sutcliffe, M.J.1    Dobson, C.M.2    Oswald, R.E.3
  • 44
    • 0027944677 scopus 로고
    • The Crystal Structure of κ-Bungarotoxin to 2.3 Å Resolution
    • Dewan, J., Grant, G. A., and Sacchettini, J. C., The Crystal Structure of κ-Bungarotoxin to 2.3 Å Resolution., Biochemistry 33:13147, 1994.
    • (1994) Biochemistry , vol.33 , pp. 13147
    • Dewan, J.1    Grant, G.A.2    Sacchettini, J.C.3
  • 46
    • 0039996064 scopus 로고
    • Three-dimensional structure of the "long" neurotoxin from cobra venom
    • Walkinshaw, M. D., Saenger, W. & Maelicke, A., Three-dimensional structure of the "long" neurotoxin from cobra venom., Proc.Natl.Acad.Sci.USA 77:2400, 1980.
    • (1980) Proc.Natl.Acad.Sci.USA , vol.77 , pp. 2400
    • Walkinshaw, M.D.1    Saenger, W.2    Maelicke, A.3
  • 48
    • 0022943266 scopus 로고
    • The crystal structure of alpha-bungarotoxin at 2.5 A resolution: Relation to solution structure and binding to acetylcholine receptor
    • Love, R. A. & Stroud, R. M., The crystal structure of alpha-bungarotoxin at 2.5 A resolution: relation to solution structure and binding to acetylcholine receptor., Protein Engineering 1:37, 1986.
    • (1986) Protein Engineering , vol.1 , pp. 37
    • Love, R.A.1    Stroud, R.M.2
  • 49
    • 0023051107 scopus 로고
    • Erabutoxin b. Structure/function relationships following initial protein refinement at 0.140-nm resolution
    • Low, B. W. & Corfield, W. R., Erabutoxin b. Structure/function relationships following initial protein refinement at 0.140-nm resolution., Eur.J.Biochem. 161:579, 1986.
    • (1986) Eur.J.Biochem. , vol.161 , pp. 579
    • Low, B.W.1    Corfield, W.R.2
  • 50
    • 0024962029 scopus 로고
    • The crystal structure of erabutoxin a at 2.0-A resolution
    • Corfield, P. W. R., Lee, T. & Low, B. W., The crystal structure of erabutoxin a at 2.0-A resolution., J.Biol.Chem. 264:9239, 1989.
    • (1989) J.Biol.Chem. , vol.264 , pp. 9239
    • Corfield, P.W.R.1    Lee, T.2    Low, B.W.3
  • 51
    • 0025788275 scopus 로고
    • The refined crystal structure of alpha-cobratoxin from Naja naja siamensis at 2.4-A resolution
    • Betzel, C., Lange, G., Pal, G. P., Wilson, K. S., Maelicke, A. & Saenger, W., The refined crystal structure of alpha-cobratoxin from Naja naja siamensis at 2.4-A resolution, J.Biol.Chem., 266: 21530, 1991.
    • (1991) J.Biol.Chem. , vol.266 , pp. 21530
    • Betzel, C.1    Lange, G.2    Pal, G.P.3    Wilson, K.S.4    Maelicke, A.5    Saenger, W.6
  • 52
    • 0019774961 scopus 로고
    • Proton-nuclear-magnetic-resonance study on molecular conformations of long neurotoxins. alpha-Bungarotoxin from Bungarus multicinctus and Toxin B from Naja naja
    • Endo, T., Inagaki, F., Hayashi, K. & Miyazawa, T., Proton-nuclear-magnetic-resonance study on molecular conformations of long neurotoxins. alpha-Bungarotoxin from Bungarus multicinctus and Toxin B from Naja naja., Eur.J.Biochem. 120: 117, 1981.
    • (1981) Eur.J.Biochem. , vol.120 , pp. 117
    • Endo, T.1    Inagaki, F.2    Hayashi, K.3    Miyazawa, T.4
  • 53
    • 0019620233 scopus 로고
    • Structural differences between erabutoxins in aqueous solution and in crystalline states
    • Inagaki, F., Tamiya, N., Miyazawa, T. & Williams, R. J. P., Structural differences between erabutoxins in aqueous solution and in crystalline states., Eur J Biochem 118(3):621, 1981.
    • (1981) Eur J Biochem , vol.118 , Issue.3 , pp. 621
    • Inagaki, F.1    Tamiya, N.2    Miyazawa, T.3    Williams, R.J.P.4
  • 54
    • 0020490829 scopus 로고
    • Molecular conformation of alpha-cobratoxin as studied by nuclear magnetic resonance and circular dichroism
    • Hider, R. C., Drake, A. F., Inagaki, F., Williams, R. J. P., Endo, T. & Miyazawa, T., Molecular conformation of alpha-cobratoxin as studied by nuclear magnetic resonance and circular dichroism., J.Mol.Biol. 158:275, 1982.
    • (1982) J.Mol.Biol. , vol.158 , pp. 275
    • Hider, R.C.1    Drake, A.F.2    Inagaki, F.3    Williams, R.J.P.4    Endo, T.5    Miyazawa, T.6
  • 55
    • 0021809580 scopus 로고
    • Molecular conformation of alpha-bungarotoxin as studied by nuclear magnetic resonance and circular dichroism
    • Inagaki, F., Hider, R. C., Hodges, S. J. & Drake, A. F., Molecular conformation of alpha-bungarotoxin as studied by nuclear magnetic resonance and circular dichroism., Mol.Biol. 183: 575, 1985.
    • (1985) Mol.Biol. , vol.183 , pp. 575
    • Inagaki, F.1    Hider, R.C.2    Hodges, S.J.3    Drake, A.F.4
  • 56
    • 0024291668 scopus 로고
    • Structural studies of alpha-bungarotoxin. 1. Sequence-specific 1H NMR resonance assignments
    • Basus, V. J., Billeter, M., Love, R. A., Stroud, R. M. & Kuntz, I. D., Structural studies of alpha-bungarotoxin. 1. Sequence-specific 1H NMR resonance assignments., Biochemistry 27:2763, 1988.
    • (1988) Biochemistry , vol.27 , pp. 2763
    • Basus, V.J.1    Billeter, M.2    Love, R.A.3    Stroud, R.M.4    Kuntz, I.D.5
  • 57
    • 0024291645 scopus 로고
    • Structural studies of alpha-bungarotoxin. 2. 1H NMR assignments via an improved relayed coherence transfer nuclear overhauser enhancement experiment
    • Basus, V. J. & Scheck, R. M., Structural studies of alpha-bungarotoxin. 2. 1H NMR assignments via an improved relayed coherence transfer nuclear overhauser enhancement experiment., Biochemistry 27:2772, 1988.
    • (1988) Biochemistry , vol.27 , pp. 2772
    • Basus, V.J.1    Scheck, R.M.2
  • 58
    • 0025054214 scopus 로고
    • Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution
    • Yu, C., Lee, C., Chuang, L., Shei, Y. & Wang, C. Y., Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution, Eur.J.Biochem. 193: 789, 1990.
    • (1990) Eur.J.Biochem. , vol.193 , pp. 789
    • Yu, C.1    Lee, C.2    Chuang, L.3    Shei, Y.4    Wang, C.Y.5
  • 59
    • 0026472379 scopus 로고
    • Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: A proton NMR and molecular modeling study
    • Zinn-Justin, S., Roumestand, C., Gilquin, B., Bontems, F., Menez, A. & Toma, F., Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study. Biochemistry 31: 11335, 1992.
    • (1992) Biochemistry , vol.31 , pp. 11335
    • Zinn-Justin, S.1    Roumestand, C.2    Gilquin, B.3    Bontems, F.4    Menez, A.5    Toma, F.6
  • 60
    • 0029897591 scopus 로고    scopus 로고
    • Two novel α-neurotoxins from the Taipan snake, Oxyuranus scutellatus, exhibit reduced affinity for nicotinic acetylcholine receptors in brain and skeletal muscle
    • Zamudio, F., Wolf, K. M., Martin, B. M., Possani, L. D., and Chiappinelli, V. A. Two novel α-neurotoxins from the Taipan snake, Oxyuranus scutellatus, exhibit reduced affinity for nicotinic acetylcholine receptors in brain and skeletal muscle. Biochemistry 35: 7910, 1996.
    • (1996) Biochemistry , vol.35 , pp. 7910
    • Zamudio, F.1    Wolf, K.M.2    Martin, B.M.3    Possani, L.D.4    Chiappinelli, V.A.5
  • 61
    • 0028179132 scopus 로고
    • Site-directed mutagenesis of k-bungarotoxin: Implications for neuronal receptor specificity
    • Fiordalisi, J. J., Al-Rabiee, R., Chiappinelli, V. A. & Grant, G. A., Site-directed mutagenesis of k-bungarotoxin: Implications for neuronal receptor specificity, Biochemistry 33:3872, 1994.
    • (1994) Biochemistry , vol.33 , pp. 3872
    • Fiordalisi, J.J.1    Al-Rabiee, R.2    Chiappinelli, V.A.3    Grant, G.A.4
  • 62
    • 0030901614 scopus 로고    scopus 로고
    • Critical Interactions at the Dimer Interface of κ-Bungarotoxin
    • Grant, G. A., Al-Rabiee, R., Xu, X. L., and Zhang, Y., Critical Interactions at the Dimer Interface of κ-Bungarotoxin., Biochemistry, 36:3353, 1997.
    • (1997) Biochemistry , vol.36 , pp. 3353
    • Grant, G.A.1    Al-Rabiee, R.2    Xu, X.L.3    Zhang, Y.4
  • 63
    • 0024328738 scopus 로고
    • Distance between the agonist and noncompetitive inhibitor sites on the nicotinic acetylcholine receptor
    • Herz, J. M., Johnson, D. A., and Taylor, P., Distance between the agonist and noncompetitive inhibitor sites on the nicotinic acetylcholine receptor, J. Biol. Chem. 264:12439, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12439
    • Herz, J.M.1    Johnson, D.A.2    Taylor, P.3
  • 64
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 A resolution
    • Unwin, N., Nicotinic acetylcholine receptor at 9 A resolution., J. Mol. Biol. 229: 1101, 1993.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101
    • Unwin, N.1


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