메뉴 건너뛰기




Volumn 270, Issue 9, 2003, Pages 1969-1979

Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom

Author keywords

defensin; Myotoxin; NMR; Scorpion toxin; Structure

Indexed keywords

BETA DEFENSIN; CROTAMINE; SCORPION VENOM; SODIUM CHANNEL;

EID: 0038368094     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03563.x     Document Type: Article
Times cited : (84)

References (75)
  • 1
    • 0013613139 scopus 로고    scopus 로고
    • Neurotoxins
    • Adams, M.D. & Swanson, G. (1996) Neurotoxins. TINS 19, 2-36.
    • (1996) TINS , vol.19 , pp. 2-36
    • Adams, M.D.1    Swanson, G.2
  • 2
    • 0016467463 scopus 로고
    • The primary structure of crotamine
    • Laure, C.J. (1975) The primary structure of crotamine. Hoppe Seylers Z. Physiol. Chem. 356, 213-215.
    • (1975) Hoppe Seylers Z. Physiol. Chem. , vol.356 , pp. 213-215
    • Laure, C.J.1
  • 3
    • 0016571258 scopus 로고
    • Analytical studies on crotamine hydrochloride
    • Giglio, J.R. (1975) Analytical studies on crotamine hydrochloride. Anal. Biochem. 69, 207-221.
    • (1975) Anal. Biochem. , vol.69 , pp. 207-221
    • Giglio, J.R.1
  • 4
    • 49649159574 scopus 로고
    • A comparison of the neuromuscolar action of crotamine and the venom of Crotalus durissus terrificus var. crotaminicus 1. Neuromuscular preparations in situ
    • Cheymol, J., Gonçalves, J.M., Bourillet, F. & Roch-Arveiller, M. (1971) A comparison of the neuromuscolar action of crotamine and the venom of Crotalus durissus terrificus var. crotaminicus 1. Neuromuscular preparations in situ. Toxicon 9, 279-286.
    • (1971) Toxicon , vol.9 , pp. 279-286
    • Cheymol, J.1    Gonçalves, J.M.2    Bourillet, F.3    Roch-Arveiller, M.4
  • 5
    • 0015090706 scopus 로고
    • A comparison of the neuromuscolar action of crotamine and the venom of crotalus durissus terrificus var. crotaminicus 2. Isolated preparations
    • Cheymol, J., Gonçalves, J.M., Bourillet, F. & Roch-Arveiller, M. (1971) A comparison of the neuromuscolar action of crotamine and the venom of crotalus durissus terrificus var. crotaminicus 2. Isolated preparations. Toxicon 9, 287-289.
    • (1971) Toxicon , vol.9 , pp. 287-289
    • Cheymol, J.1    Gonçalves, J.M.2    Bourillet, F.3    Roch-Arveiller, M.4
  • 6
    • 0018184217 scopus 로고
    • Effect of crotamine, a toxin of south american rattlesnake venom, on the sodium channel of murine skeletal muscle
    • Chang, C.C. & Tseng, K.H. (1978) Effect of crotamine, a toxin of south american rattlesnake venom, on the sodium channel of murine skeletal muscle. Br. J. Pharmacol. 63, 551-559.
    • (1978) Br. J. Pharmacol. , vol.63 , pp. 551-559
    • Chang, C.C.1    Tseng, K.H.2
  • 7
    • 0020571357 scopus 로고
    • A study on the membrane depolarization of skeletal muscles caused by a scorpion toxin, sea anemone toxin II and crotamine and the interaction between toxins
    • Chang, C.C., Hong, S.J. & Su, M.J. (1983) A study on the membrane depolarization of skeletal muscles caused by a scorpion toxin, sea anemone toxin II and crotamine and the interaction between toxins. Br. J. Pharmacol. 79, 673-680.
    • (1983) Br. J. Pharmacol. , vol.79 , pp. 673-680
    • Chang, C.C.1    Hong, S.J.2    Su, M.J.3
  • 8
    • 0021065831 scopus 로고
    • Potentiation by crotamine of the depolarizing effects of batrachotoxin, protoveratrine A and grayanotoxin I on the rat diaphragm
    • Hong, S.J. & Chang, C.C. (1983) Potentiation by crotamine of the depolarizing effects of batrachotoxin, protoveratrine A and grayanotoxin I on the rat diaphragm. Toxicon 21, 503-514.
    • (1983) Toxicon , vol.21 , pp. 503-514
    • Hong, S.J.1    Chang, C.C.2
  • 9
    • 0027223891 scopus 로고
    • Toxins as tools in the study of sodium channel distribution in the muscle fibre membrane
    • Vital-Brazil, O. & Fontana, M. D. (1993) Toxins as tools in the study of sodium channel distribution in the muscle fibre membrane. Toxicon, 31, 1085-1098.
    • (1993) Toxicon , vol.31 , pp. 1085-1098
    • Vital-Brazil, O.1    Fontana, M.D.2
  • 10
    • 0024356166 scopus 로고
    • Use of geographutoxin II (μ-conotoxin) for the study of neuromuscular transmission in mouse
    • Hong, S.J. & Chang, C.C. (1989) Use of geographutoxin II (μ-conotoxin) for the study of neuromuscular transmission in mouse. Br. J. Pharmacol. 97, 934-940.
    • (1989) Br. J. Pharmacol. , vol.97 , pp. 934-940
    • Hong, S.J.1    Chang, C.C.2
  • 12
    • 0032400766 scopus 로고    scopus 로고
    • The analgesic activity of crotamine, a neurotoxin from Crotalus durissus terrificus (South American rattlesnake) venom: A biochemical and pharmacological study
    • Mancin, A.C., Soares, A.M., Andrião-escarso, S.H., Faça, V.M., Greene, L.J., Zuccolotto, S., Pela, I.R. & Giglio, J.R. (1998) The analgesic activity of crotamine, a neurotoxin from Crotalus durissus terrificus (South American rattlesnake) venom: a biochemical and pharmacological study. Toxicon 36, 1927-1937.
    • (1998) Toxicon , vol.36 , pp. 1927-1937
    • Mancin, A.C.1    Soares, A.M.2    Andrião-Escarso, S.H.3    Faça, V.M.4    Greene, L.J.5    Zuccolotto, S.6    Pela, I.R.7    Giglio, J.R.8
  • 13
    • 0018258789 scopus 로고
    • Chemical and functional homology of myotoxin a from prairie rattlesnake venom and crotamine from South American rattlesnake venom
    • Cameron, D.L. & Tu, A.T. (1978) Chemical and functional homology of myotoxin a from prairie rattlesnake venom and crotamine from South American rattlesnake venom. Biochem. Biophys. Acta 532, 147-154.
    • (1978) Biochem. Biophys. Acta , vol.532 , pp. 147-154
    • Cameron, D.L.1    Tu, A.T.2
  • 14
    • 0030294854 scopus 로고    scopus 로고
    • Similarities and differences in mechanisms of cardiotoxins, melittin and other myotoxins
    • Fletcher, J.E., Hubert, M., Wieland, S.J., Gong, Q. & Jiang, M. (1996) Similarities and differences in mechanisms of cardiotoxins, melittin and other myotoxins. Toxicon 34, 1301-1311.
    • (1996) Toxicon , vol.34 , pp. 1301-1311
    • Fletcher, J.E.1    Hubert, M.2    Wieland, S.J.3    Gong, Q.4    Jiang, M.5
  • 15
    • 0018383525 scopus 로고
    • Amino acid sequence and disulfide bond assignment of myotoxin a isolated from the venom of prairie rattlesnake Crotalus viridis viridis
    • Fox, J.W., Elzinga, M. & Tu, A.T. (1979) Amino acid sequence and disulfide bond assignment of myotoxin a isolated from the venom of prairie rattlesnake Crotalus viridis viridis. Biochemistry 18, 678-684.
    • (1979) Biochemistry , vol.18 , pp. 678-684
    • Fox, J.W.1    Elzinga, M.2    Tu, A.T.3
  • 16
    • 0018090042 scopus 로고
    • Some chemical properties of the venom of rattlesnake Crotalus viridis helleri
    • Maeda, N., Tamiya, N., Pattabhiraman, T.R. & Russel, F.E. (1978) Some chemical properties of the venom of rattlesnake Crotalus viridis helleri. Toxicon 16, 431-441.
    • (1978) Toxicon , vol.16 , pp. 431-441
    • Maeda, N.1    Tamiya, N.2    Pattabhiraman, T.R.3    Russel, F.E.4
  • 17
    • 0023579222 scopus 로고
    • Amino acid sequences of myotoxins from Crotalus viridis concolor venom
    • Bieber, A.L., McParland, R.H. & Becker, R.R. (1987) Amino acid sequences of myotoxins from Crotalus viridis concolor venom. Toxicon 25, 677-680.
    • (1987) Toxicon , vol.25 , pp. 677-680
    • Bieber, A.L.1    McParland, R.H.2    Becker, R.R.3
  • 18
    • 0026036038 scopus 로고
    • Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus)
    • Samejima, Y., Aoki, Y. & Mebs, D. (1991) Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Toxicon 29, 461-468.
    • (1991) Toxicon , vol.29 , pp. 461-468
    • Samejima, Y.1    Aoki, Y.2    Mebs, D.3
  • 19
    • 0030961693 scopus 로고    scopus 로고
    • Structural, biological and biochemical studies of myotoxin a and homologous myotoxins
    • Bieber, A.L. & Nedelkov, D. (1997) Structural, biological and biochemical studies of myotoxin a and homologous myotoxins. J. Toxicol. Toxin Rev. 16, 33-52.
    • (1997) J. Toxicol. Toxin Rev. , vol.16 , pp. 33-52
    • Bieber, A.L.1    Nedelkov, D.2
  • 20
    • 0021114895 scopus 로고
    • Application of phase-sensitive two-dimensional correlated spectroscopy (COSY) for measurement of proton-proton spin-spin coupling constants
    • Marion, D. & Wüthrich, K. (1983) Application of phase-sensitive two-dimensional correlated spectroscopy (COSY) for measurement of proton-proton spin-spin coupling constants. Biochem. Biophys. Res. Commun. 113, 967-974.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 21
    • 0000163823 scopus 로고
    • Mapping proton-proton coupling via double-quantum coherence
    • Mareci, T.H. & Freeman, R. (1983) Mapping proton-proton coupling via double-quantum coherence. J. Magn. Res. 51, 531-535.
    • (1983) J. Magn. Res. , vol.51 , pp. 531-535
    • Mareci, T.H.1    Freeman, R.2
  • 22
    • 33845378943 scopus 로고
    • 1H-NMR spectra via two-dimensional homonuclear Hartman-Hahn spectroscopy
    • 1H-NMR spectra via two-dimensional homonuclear Hartman-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 24
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 25
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 26
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D.J, Haberkorn, R.A. & Ruben, D.J. (1982) A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Res. 48, 286-292.
    • (1982) J. Magn. Res. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 28
    • 45249128810 scopus 로고
    • Measurement of vicinal couplings from cross peaks in COSY spectra
    • Kim, Y. & Prestegard, J.H. (1989) Measurement of vicinal couplings from cross peaks in COSY spectra. J. Magn. Reson. 84, 9-13.
    • (1989) J. Magn. Reson. , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegard, J.H.2
  • 29
    • 0026032405 scopus 로고
    • Accurate measurements of coupling constants from two-dimensional nuclear magnetic resonance spectra of proteins and determination of φ-angles
    • Ludvigsen, S., Andersen, K.V. & Poulsen, F.M. (1991) Accurate measurements of coupling constants from two-dimensional nuclear magnetic resonance spectra of proteins and determination of φ-angles. J. Mol. Biol. 217, 731-736.
    • (1991) J. Mol. Biol. , vol.217 , pp. 731-736
    • Ludvigsen, S.1    Andersen, K.V.2    Poulsen, F.M.3
  • 30
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Lett. 239, 129-136.
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 31
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmann, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 32
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 33
    • 0020556816 scopus 로고
    • Conformational properties of the neurotoxins and cytotoxins isolated from Elapid snake venoms
    • Dufton, M.J. & Hider, R.C. (1983) Conformational properties of the neurotoxins and cytotoxins isolated from Elapid snake venoms. CRC Crit. Rev. Biochem. 14, 113-171.
    • (1983) CRC Crit. Rev. Biochem. , vol.14 , pp. 113-171
    • Dufton, M.J.1    Hider, R.C.2
  • 35
    • 0028102759 scopus 로고
    • Contribution of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody, R.W. (1994) Contribution of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur. Biophys. J. 23, 253-262.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 253-262
    • Woody, R.W.1
  • 36
    • 0023855264 scopus 로고
    • An analysis of the 225-230 nm CD band of elapid toxins
    • Hider, R.C., Drake, A.F. & Tamiya, N. (1988) An analysis of the 225-230 nm CD band of elapid toxins. Biopolymers 27, 113-122.
    • (1988) Biopolymers , vol.27 , pp. 113-122
    • Hider, R.C.1    Drake, A.F.2    Tamiya, N.3
  • 39
    • 0018142843 scopus 로고
    • Crotamine conformation effect of pH and temperature
    • Hampe, O.G., Vozari-Hampe, M.M. & Gonçalves, J.M. (1978) Crotamine conformation effect of pH and temperature. Toxicon 16, 453-460.
    • (1978) Toxicon , vol.16 , pp. 453-460
    • Hampe, O.G.1    Vozari-Hampe, M.M.2    Gonçalves, J.M.3
  • 40
    • 0025079134 scopus 로고
    • Polyacrylamide gel electrophoretic studies on the self association of crotamine: Characterization and molecular dimension of n-mer species
    • Hampe, O.G., Junqueira, N.O. & Vozari-Hampe, M.M. (1990) Polyacrylamide gel electrophoretic studies on the self association of crotamine: characterization and molecular dimension of n-mer species. Electrophoresis 11, 475-478.
    • (1990) Electrophoresis , vol.11 , pp. 475-478
    • Hampe, O.G.1    Junqueira, N.O.2    Vozari-Hampe, M.M.3
  • 41
    • 0036360507 scopus 로고    scopus 로고
    • 2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains
    • 2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains. Eur. J. Biochem. 269, 3779-3788.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3779-3788
    • Wecker, K.1    Morellet, N.2    Bouaziz, S.3    Roques, B.P.4
  • 42
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C
    • Gagné, S.M., Tsuda, S., Li, M.X., Chandra, M., Smillie, L.B. & Sykes, B.D. (1994) Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 3, 1961-1974.
    • (1994) Protein Sci. , vol.3 , pp. 1961-1974
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Chandra, M.4    Smillie, L.B.5    Sykes, B.D.6
  • 43
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-satured skeletal muscle troponin C
    • Slupsky, C.M. & Sykes, B.D. (1995) NMR solution structure of calcium-satured skeletal muscle troponin C. Biochemistry 34, 15953-15964.
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 44
    • 0029076557 scopus 로고
    • Calcium-induced dimerization of troponin C: Mode of interaction and use of trifluoroethanol as a denaturant of quaternary structure
    • Slupsky, C.M., Cyril, M.K., Reinach, F.C., Smillie, L.B. & Sykes, B.D. (1995) Calcium-induced dimerization of troponin C: mode of interaction and use of trifluoroethanol as a denaturant of quaternary structure. Biochemistry 34, 7365-7375.
    • (1995) Biochemistry , vol.34 , pp. 7365-7375
    • Slupsky, C.M.1    Cyril, M.K.2    Reinach, F.C.3    Smillie, L.B.4    Sykes, B.D.5
  • 45
    • 0024942624 scopus 로고
    • A proton nuclear magnetic resonance study on the solution structure of crotamine
    • Endo, T., Oya, M., Ozawa, H., Kawano, Y., Giglio, J.R. & Miyazawa, T. (1989) A proton nuclear magnetic resonance study on the solution structure of crotamine. J. Prot. Chem. 8, 807-815.
    • (1989) J. Prot. Chem. , vol.8 , pp. 807-815
    • Endo, T.1    Oya, M.2    Ozawa, H.3    Kawano, Y.4    Giglio, J.R.5    Miyazawa, T.6
  • 46
    • 0029983698 scopus 로고    scopus 로고
    • Evidence for isomerization in myotoxin a from the prairie rattlesnake (Crotalus viridis viridis)
    • O'Keefe, M.P., Nedelkov, D., Bieber, A.L. & Nieman, R.A. (1996) Evidence for isomerization in myotoxin a from the prairie rattlesnake (Crotalus viridis viridis). Toxicon 34, 417-434.
    • (1996) Toxicon , vol.34 , pp. 417-434
    • O'Keefe, M.P.1    Nedelkov, D.2    Bieber, A.L.3    Nieman, R.A.4
  • 47
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. (1981) The anatomy and taxonomy of protein structure. Adv. Protein. Chem. 34, 167-339.
    • (1981) Adv. Protein. Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 49
    • 0026418431 scopus 로고
    • Refined structure of Charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems, F., Roumestand, C., Gilquin, B., Menez, A. & Toma, F. (1991) Refined structure of Charybdotoxin: common motifs in scorpion toxins and insect defensins. Science 254, 1521-1523.
    • (1991) Science , vol.254 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Menez, A.4    Toma, F.5
  • 51
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of human β-defensins lead to a better understanding of the potent bactericidal activity of HBD-3 against Staphilococcus
    • Schibli, D., Hunter, H.N., Aseyev, V., Starner, TD., Wiencek, J.M., McCray, P.B., Tack, B.F. & Vogel, H.J. (2002) The solution structures of human β-defensins lead to a better understanding of the potent bactericidal activity of HBD-3 against Staphilococcus. J. Biol. Chem. 277, 8279-8289.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8279-8289
    • Schibli, D.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray, P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 54
    • 0035914442 scopus 로고    scopus 로고
    • The structure of human β-defensin-1
    • Hoover, D.M., Chertov, O. & Lubkowski, J. (2001) The structure of human β-defensin-1. J. Biol. Chem. 276, 39021-39026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39021-39026
    • Hoover, D.M.1    Chertov, O.2    Lubkowski, J.3
  • 56
    • 0030009637 scopus 로고    scopus 로고
    • Scorpion toxins affecting sodium current inactivation bind to distinct homologous receptor sites on rat brain and insect sodium channels
    • Gordon, D., Martin-Eauclaire, M.F., Cestele, S., Kopeyan, C., Carlier, E., Khafifa, R., Pelhate, M. & Rochat, H. (1996) Scorpion toxins affecting sodium current inactivation bind to distinct homologous receptor sites on rat brain and insect sodium channels. J. Biol. Chem. 271, 8034-8045.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8034-8045
    • Gordon, D.1    Martin-Eauclaire, M.F.2    Cestele, S.3    Kopeyan, C.4    Carlier, E.5    Khafifa, R.6    Pelhate, M.7    Rochat, H.8
  • 57
    • 2642619415 scopus 로고    scopus 로고
    • Depolarization differentially affects allosteric modulation by neurotoxins of scorpion α-toxin binding on voltage-gated sodium channels
    • Cestele, S. & Gordon, D. (1998) Depolarization differentially affects allosteric modulation by neurotoxins of scorpion α-toxin binding on voltage-gated sodium channels. J. Neurochem. 70, 1217-1226.
    • (1998) J. Neurochem. , vol.70 , pp. 1217-1226
    • Cestele, S.1    Gordon, D.2
  • 58
    • 0001456758 scopus 로고    scopus 로고
    • Sodium channels as target for neurotoxins
    • Gutman, Y. & Lazarowici, P., eds, Harwood. Academic Publishers, The Netherlands
    • Gordon, D. (1997) Sodium channels as target for neurotoxins. In Toxins and Signal Transduction (Gutman, Y. & Lazarowici, P., eds), pp. 119-149, Harwood. Academic Publishers, The Netherlands.
    • (1997) Toxins and Signal Transduction , pp. 119-149
    • Gordon, D.1
  • 59
    • 0024094439 scopus 로고
    • Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion Androctonus australis Hector
    • Fontecilla-Camps, J.C., Habersetzer-Rochat, C. & Rochat, H. (1988) Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion Androctonus australis Hector. Proc. Natl Acad. Sci. USA 85, 7443-7447.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7443-7447
    • Fontecilla-Camps, J.C.1    Habersetzer-Rochat, C.2    Rochat, H.3
  • 60
    • 0028233375 scopus 로고
    • Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution
    • Housset, D., Habersetzer-Rochat, C., Astier, J.P. & Fontecilla-Camps, J.C. (1994) Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution. J. Mol. Biol. 238, 88-103.
    • (1994) J. Mol. Biol. , vol.238 , pp. 88-103
    • Housset, D.1    Habersetzer-Rochat, C.2    Astier, J.P.3    Fontecilla-Camps, J.C.4
  • 61
    • 0024669542 scopus 로고
    • Structure/activity relationships of scorpion alpha-toxins. Multiple residues contribute to the interaction with receptors
    • Kharrat, R., Darbon, H., Rochat, H. & Granier, C. (1989) Structure/activity relationships of scorpion alpha-toxins. Multiple residues contribute to the interaction with receptors. Eur. J. Biochem. 181, 381-390.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 381-390
    • Kharrat, R.1    Darbon, H.2    Rochat, H.3    Granier, C.4
  • 64
    • 0030598925 scopus 로고    scopus 로고
    • Crystal structure of an acidic neurotoxin from scorpion Buthus martensii Karsch at 1.85 Å resolution
    • Li, H., Wang, D., Zeng, Z., Jin, L. & Hu, R. (1996) Crystal structure of an acidic neurotoxin from scorpion Buthus martensii Karsch at 1.85 Å resolution. J. Mol. Biol. 261, 415-431.
    • (1996) J. Mol. Biol. , vol.261 , pp. 415-431
    • Li, H.1    Wang, D.2    Zeng, Z.3    Jin, L.4    Hu, R.5
  • 65
    • 0020805736 scopus 로고
    • α-scorpion neurotoxin derivates suitable as potential markers of sodium channes
    • Darbon, H., Jover, E., Couraud, F. & Rochat, H. (1983) α-scorpion neurotoxin derivates suitable as potential markers of sodium channes. Int. J. Pept. Prot. Res. 22, 179-186.
    • (1983) Int. J. Pept. Prot. Res. , vol.22 , pp. 179-186
    • Darbon, H.1    Jover, E.2    Couraud, F.3    Rochat, H.4
  • 66
    • 0030951334 scopus 로고    scopus 로고
    • Identification of structural elements of a scorpion α-neurotoxin important for receptor site recognition
    • Zilberberg, N., Froy, O., Loret, E., Cestele, S., Arad, D., Gordon, D. & Gurevitz, M. (1997) Identification of structural elements of a scorpion α-neurotoxin important for receptor site recognition. J. Biol. Chem. 272, 14810-14816.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14810-14816
    • Zilberberg, N.1    Froy, O.2    Loret, E.3    Cestele, S.4    Arad, D.5    Gordon, D.6    Gurevitz, M.7
  • 67
    • 0023008978 scopus 로고
    • Use of antibodies specific to defined regions of scorpion alpha-toxin to study its interaction with its site on the sodium channel
    • El Ayeb, M., Bahraoui, E.M., Granier, C. & Rochat, H. (1986) Use of antibodies specific to defined regions of scorpion alpha-toxin to study its interaction with its site on the sodium channel. Biochemistry 25, 6671-6678.
    • (1986) Biochemistry , vol.25 , pp. 6671-6678
    • El Ayeb, M.1    Bahraoui, E.M.2    Granier, C.3    Rochat, H.4
  • 68
    • 0031017788 scopus 로고    scopus 로고
    • Solution structures of a highly insecticidal recombinant scorpion α-toxin and a mutant with increased activity
    • Tugarinov, V., Kustanovich, I., Zilberberg, N., Gurevitz, M. & Anglister, J. (1997) Solution structures of a highly insecticidal recombinant scorpion α-toxin and a mutant with increased activity. Biochemistry 36, 2414-2424.
    • (1997) Biochemistry , vol.36 , pp. 2414-2424
    • Tugarinov, V.1    Kustanovich, I.2    Zilberberg, N.3    Gurevitz, M.4    Anglister, J.5
  • 73
  • 74
    • 0028825285 scopus 로고
    • Solution structure of bovine neutrophyl β-defensin-12: The peptide fold of the β-defensins is identical to that of the classical defensins
    • Zimmermann, G.R., Legault, P., Selsted, M.E. & Pardi, A. (1995) Solution structure of bovine neutrophyl β-defensin-12: the peptide fold of the β-defensins is identical to that of the classical defensins. Biochemistry 34, 13663-13671.
    • (1995) Biochemistry , vol.34 , pp. 13663-13671
    • Zimmermann, G.R.1    Legault, P.2    Selsted, M.E.3    Pardi, A.4
  • 75
    • 0027968068 scopus 로고
    • CLUS-TALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994) CLUS-TALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22, 4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.