메뉴 건너뛰기




Volumn 86, Issue 2, 2004, Pages 137-149

Snake postsynaptic neurotoxins: Gene structure, phylogeny and applications in research and therapy

Author keywords

Drug discovery; Evolutionary origin; Neurotoxins; Snake venom

Indexed keywords

ALPHA BUNGAROTOXIN; COBROTOXIN; COMPLEMENTARY DNA; NEUROTOXIN; SNAKE VENOM;

EID: 1542358054     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2003.11.012     Document Type: Article
Times cited : (41)

References (107)
  • 1
    • 1542332678 scopus 로고    scopus 로고
    • London: Natural History Museum of London
    • Stafford P. Snakes. 2000;5-6 Natural History Museum of London, London.
    • (2000) Snakes , pp. 5-6
    • Stafford, P.1
  • 2
    • 0002677718 scopus 로고
    • Phospholipases in snake venoms and their effects on nerve and muscle
    • Harvey A.L. New York: Pergamon Press
    • Harris J.B. Phospholipases in snake venoms and their effects on nerve and muscle. Harvey A.L. Snake Toxins. 1991;91-129 Pergamon Press, New York.
    • (1991) Snake Toxins , pp. 91-129
    • Harris, J.B.1
  • 3
    • 1542362460 scopus 로고
    • Separation and purification of toxins from snake venoms
    • Harvey A.L. New York: Pergamon Press
    • Hider R.C., Karlsson E., Namiranian S. Separation and purification of toxins from snake venoms. Harvey A.L. Snake Toxins. 1991;1-34 Pergamon Press, New York.
    • (1991) Snake Toxins , pp. 1-34
    • Hider, R.C.1    Karlsson, E.2    Namiranian, S.3
  • 5
    • 0025050799 scopus 로고
    • Neurotoxic snake envenoming
    • Minton S.A. Neurotoxic snake envenoming. Semin. Neurol. 10:1990;52-61.
    • (1990) Semin. Neurol. , vol.10 , pp. 52-61
    • Minton, S.A.1
  • 6
    • 0012326652 scopus 로고
    • New York: Facts on File Publications
    • Mattison C. Snakes of the World. 1986;160-179 Facts on File Publications, New York.
    • (1986) Snakes of the World , pp. 160-179
    • Mattison, C.1
  • 7
    • 0002329796 scopus 로고
    • The protein and non-protein constituents of snake venoms
    • W. Bucherl, E. Buckley, & V. Deulofeu. New York: Academic Press
    • Devi A. The protein and non-protein constituents of snake venoms. Bucherl W., Buckley E., Deulofeu V. Venomous Animals and Their Venoms. 1968;119-165 Academic Press, New York.
    • (1968) Venomous Animals and Their Venoms , pp. 119-165
    • Devi, A.1
  • 8
    • 0025636132 scopus 로고
    • Venomous bites by non-venomous snakes: An annotated bibliography of colubrid envenomation
    • Minton S.A. Venomous bites by non-venomous snakes: an annotated bibliography of colubrid envenomation. J. Wilderness Med. 1:1990;119-127.
    • (1990) J. Wilderness Med. , vol.1 , pp. 119-127
    • Minton, S.A.1
  • 9
    • 84981864799 scopus 로고
    • The amino acid sequence of neurotoxin from Naja nigricollis venom
    • Eaker D., Porath J. The amino acid sequence of neurotoxin from Naja nigricollis venom. Jpn J. Microbiol. 11:1967;353-355.
    • (1967) Jpn J. Microbiol. , vol.11 , pp. 353-355
    • Eaker, D.1    Porath, J.2
  • 10
    • 0002687075 scopus 로고
    • Structure-function relationship of postsynaptic neurotoxins from snake venoms
    • Harvey A.L. New York: Pergamon Press
    • Endo T., Tamiya N. Structure-function relationship of postsynaptic neurotoxins from snake venoms. Harvey A.L. Snake Toxins. 1991;165-222 Pergamon Press, New York.
    • (1991) Snake Toxins , pp. 165-222
    • Endo, T.1    Tamiya, N.2
  • 11
    • 0015538917 scopus 로고
    • Neurotoxins of animal venoms: Snakes
    • Tu A.T. Neurotoxins of animal venoms: snakes. Annu. Rev. Biochem. 42:1973;235-258.
    • (1973) Annu. Rev. Biochem. , vol.42 , pp. 235-258
    • Tu, A.T.1
  • 12
    • 0001607746 scopus 로고    scopus 로고
    • Snake toxins that interact with nicotinic acetylcholine receptors
    • Massaro E.J. Totowa, NJ: Humana Press
    • Servent D., Menez A. Snake toxins that interact with nicotinic acetylcholine receptors. Massaro E.J. Neurotoxicological Handbook. 1:2001;385-425 Humana Press, Totowa, NJ.
    • (2001) Neurotoxicological Handbook , vol.1 , pp. 385-425
    • Servent, D.1    Menez, A.2
  • 13
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67:1975;835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 14
    • 0023502533 scopus 로고
    • Current view on the structure-function relationship of postsynaptic neurotoxins from snake venoms
    • Endo T., Tamiya N. Current view on the structure-function relationship of postsynaptic neurotoxins from snake venoms. Pharmacol. Ther. 34:1987;403-451.
    • (1987) Pharmacol. Ther. , vol.34 , pp. 403-451
    • Endo, T.1    Tamiya, N.2
  • 15
    • 0000950985 scopus 로고
    • Structure-function relationship of postsynaptic neurotoxins from snake venoms
    • Harvey A.L. New York: Pergamon Press
    • Chiappinelli V.A. Structure-function relationship of postsynaptic neurotoxins from snake venoms. Harvey A.L. Snake Toxins. 1991;223-258 Pergamon Press, New York.
    • (1991) Snake Toxins , pp. 223-258
    • Chiappinelli, V.A.1
  • 16
    • 0028179132 scopus 로고
    • Site-directed mutagenesis of kappa-bungarotoxin: Implications for neuronal receptor specificity
    • Fiordalisi J.J., al-Rabiee R., Chiappinelli V.A., Grant G.A. Site-directed mutagenesis of kappa-bungarotoxin: implications for neuronal receptor specificity. Biochemistry. 33:1994;3872-3877.
    • (1994) Biochemistry , vol.33 , pp. 3872-3877
    • Fiordalisi, J.J.1    Al-Rabiee, R.2    Chiappinelli, V.A.3    Grant, G.A.4
  • 17
    • 0035844124 scopus 로고    scopus 로고
    • "weak toxin" from Naja kaouthia is a nontoxic antagonist of alpha 7 and muscle-type nicotinic acetylcholine receptors
    • Utkin Y.N., Kukhtina V.V., Kryukova E.V., Chiodini F., Bertrand D., Methfessel C., Tsetlin V.I. "Weak toxin" from Naja kaouthia is a nontoxic antagonist of alpha 7 and muscle-type nicotinic acetylcholine receptors. J. Biol. Chem. 276:2001;15810-15815.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15810-15815
    • Utkin, Y.N.1    Kukhtina, V.V.2    Kryukova, E.V.3    Chiodini, F.4    Bertrand, D.5    Methfessel, C.6    Tsetlin, V.I.7
  • 18
    • 0036042543 scopus 로고    scopus 로고
    • A synthetic weak neurotoxin binds with low affinity to Torpedo and chicken alpha7 nicotinic acetylcholine receptors
    • Poh S.L., Mourier G., Thai R., Armugam A., Molgo J., Servent D., Jeyaseelan K., Menez A. A synthetic weak neurotoxin binds with low affinity to Torpedo and chicken alpha7 nicotinic acetylcholine receptors. Eur. J. Biochem. 269:2002;4247-4256.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4247-4256
    • Poh, S.L.1    Mourier, G.2    Thai, R.3    Armugam, A.4    Molgo, J.5    Servent, D.6    Jeyaseelan, K.7    Menez, A.8
  • 20
    • 0022317995 scopus 로고
    • Erabutoxin b. Initial protein refinement and sequence analysis at 0.140 nm resolution
    • Bourne P.E., Sato A., Corfield P.W., Rosen L.S., Birken S., Low B.W. Erabutoxin b. Initial protein refinement and sequence analysis at 0.140 nm resolution. Eur. J. Biochem. 153:1985;521-527.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 521-527
    • Bourne, P.E.1    Sato, A.2    Corfield, P.W.3    Rosen, L.S.4    Birken, S.5    Low, B.W.6
  • 21
    • 0025788275 scopus 로고
    • The refined crystal structure of alpha-cobratoxin Naja naja siamensis at 2.4-Å resolution
    • Betzel C., Lange G., Pal G.P., Wilson K.S., Maelicke A., Saenger W. The refined crystal structure of alpha-cobratoxin Naja naja siamensis at 2. 4-Å resolution. J. Biol. Chem. 266:1991;21530-21536.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21530-21536
    • Betzel, C.1    Lange, G.2    Pal, G.P.3    Wilson, K.S.4    Maelicke, A.5    Saenger, W.6
  • 22
    • 0000045033 scopus 로고
    • α-Bungarotoxin structure revealed by a rapid method for averaging electro density of non-crystallographically translationally related molecules
    • Agard D.A., Stroud R.M. α-Bungarotoxin structure revealed by a rapid method for averaging electro density of non-crystallographically translationally related molecules. Acta Crystallogr. A. 38:1982;186-194.
    • (1982) Acta Crystallogr. a , vol.38 , pp. 186-194
    • Agard, D.A.1    Stroud, R.M.2
  • 23
    • 0028332247 scopus 로고
    • Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance
    • Hatanaka H., Oka M., Kohda D., Tate S., Suda A., Tamiya N., Inagaki F. Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance. J. Mol. Biol. 240:1994;155-166.
    • (1994) J. Mol. Biol. , vol.240 , pp. 155-166
    • Hatanaka, H.1    Oka, M.2    Kohda, D.3    Tate, S.4    Suda, A.5    Tamiya, N.6    Inagaki, F.7
  • 25
    • 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., Scheek R.M. Structural studies of alpha-bungarotoxin. 2. 1H NMR assignments via an improved relayed coherence transfer nuclear overhauser enhancement experiment. Biochemistry. 27:1988;2772-2775.
    • (1988) Biochemistry , vol.27 , pp. 2772-2775
    • Basus, V.J.1    Scheek, R.M.2
  • 27
    • 0027944677 scopus 로고
    • Crystal structure of kappa-bungarotoxin at 2.3-Å resolution
    • Dewan J.C., Grant G.A., Sacchettini J.C. Crystal structure of kappa-bungarotoxin at 2.3-Å resolution. Biochemistry. 33:1994;13147-13154.
    • (1994) Biochemistry , vol.33 , pp. 13147-13154
    • Dewan, J.C.1    Grant, G.A.2    Sacchettini, J.C.3
  • 28
    • 0030901614 scopus 로고    scopus 로고
    • Critical interactions at the dimer interface of kappa-bungarotoxin, a neuronal nicotinic acetylcholine receptor antagonist
    • Grant G.A., Al-Rabiee R., Xu X.L., Zhang Y. Critical interactions at the dimer interface of kappa-bungarotoxin, a neuronal nicotinic acetylcholine receptor antagonist. Biochemistry. 36:1997;3353-3358.
    • (1997) Biochemistry , vol.36 , pp. 3353-3358
    • Grant, G.A.1    Al-Rabiee, R.2    Xu, X.L.3    Zhang, Y.4
  • 29
    • 0019728871 scopus 로고
    • Restoration of 125I-alpha-bungarotoxin binding activity to the alpha subunit of Torpedo acetylcholine receptor isolated by gel electrophoresis in sodium dodecyl sulfate
    • Haggerty J.G., Froehner S.C. Restoration of 125I-alpha-bungarotoxin binding activity to the alpha subunit of Torpedo acetylcholine receptor isolated by gel electrophoresis in sodium dodecyl sulfate. J Biol. Chem. 256:1981;8294-8297.
    • (1981) J Biol. Chem. , vol.256 , pp. 8294-8297
    • Haggerty, J.G.1    Froehner, S.C.2
  • 31
    • 0034703102 scopus 로고    scopus 로고
    • Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal alpha 7-nicotinic acetylcholine receptor
    • Antil-Delbeke S., Gaillard C., Tamiya T., Corringer P.J., Changeux J.P., Servent D., Menez A. Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal alpha 7-nicotinic acetylcholine receptor. J. Biol. Chem. 275:2000;9594-9601.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9594-9601
    • Antil-Delbeke, S.1    Gaillard, C.2    Tamiya, T.3    Corringer, P.J.4    Changeux, J.P.5    Servent, D.6    Menez, A.7
  • 32
    • 0030766456 scopus 로고    scopus 로고
    • Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal alpha7 nicotinic receptor
    • Servent D., Winckler-Dietrich V., Hu H.Y., Kessler P., Drevet P., Bertrand D., Menez A. Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal alpha7 nicotinic receptor. J. Biol. Chem. 272:1997;24279-24786.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24279-24786
    • Servent, D.1    Winckler-Dietrich, V.2    Hu, H.Y.3    Kessler, P.4    Drevet, P.5    Bertrand, D.6    Menez, A.7
  • 33
    • 0001765604 scopus 로고
    • Chemistry of protein toxins in snake venoms
    • Lee C.Y. Berlin: Springer-Verlag
    • Karlsson E. Chemistry of protein toxins in snake venoms. Lee C.Y. Snake Venoms, Handbook of Experimental Pharmacology. 1979;159-212 Springer-Verlag, Berlin.
    • (1979) Snake Venoms, Handbook of Experimental Pharmacology , pp. 159-212
    • Karlsson, E.1
  • 34
    • 0015221781 scopus 로고
    • Characterization and chemical modifications of toxins isolated from the venoms of the sea snake, Laticauda semifasciata, from Philippines
    • Tu A.T., Hong B., Solie T.N. Characterization and chemical modifications of toxins isolated from the venoms of the sea snake, Laticauda semifasciata, from Philippines. Biochemistry. 10:1971;1295-1304.
    • (1971) Biochemistry , vol.10 , pp. 1295-1304
    • Tu, A.T.1    Hong, B.2    Solie, T.N.3
  • 35
    • 0015239187 scopus 로고
    • Isolation and characterization of the toxic component of Enhydrina schistosa (common sea snake) venom
    • Tu A.T., Toom P.M. Isolation and characterization of the toxic component of Enhydrina schistosa (common sea snake) venom. J. Biol. Chem. 246:1971;1012-1016.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1012-1016
    • Tu, A.T.1    Toom, P.M.2
  • 36
    • 0025064615 scopus 로고
    • The role of an invariant tryptophan residue in alpha-bungarotoxin and cobrotoxin. Investigation of active derivatives with the invariant tryptophan replaced by kynurenine
    • Chang C.C., Kawata Y., Sakiyama F., Hayashi K. The role of an invariant tryptophan residue in alpha-bungarotoxin and cobrotoxin. Investigation of active derivatives with the invariant tryptophan replaced by kynurenine. Eur. J. Biochem. 193:1990;567-572.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 567-572
    • Chang, C.C.1    Kawata, Y.2    Sakiyama, F.3    Hayashi, K.4
  • 37
    • 0017293920 scopus 로고
    • Preparation and activity of guanidinated or acetylated erabutoxins
    • Hori H., Tamiya N. Preparation and activity of guanidinated or acetylated erabutoxins. Biochem. J. 153:1976;217-222.
    • (1976) Biochem. J. , vol.153 , pp. 217-222
    • Hori, H.1    Tamiya, N.2
  • 38
    • 0020625407 scopus 로고
    • Role of indole and amino groups in the structure and function of Naja nigricollis toxin alpha
    • Faure G., Boulain J.C., Bouet F., Montenay-Garestier T., Fromageot P., Menez A. Role of indole and amino groups in the structure and function of Naja nigricollis toxin alpha. Biochemistry. 22:1983;2068-2076.
    • (1983) Biochemistry , vol.22 , pp. 2068-2076
    • Faure, G.1    Boulain, J.C.2    Bouet, F.3    Montenay-Garestier, T.4    Fromageot, P.5    Menez, A.6
  • 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., Tremeau O., Ducancel F., Drevet P., Zinn-Justin S., Pinkasfeld S., Boulain J.C., Menez 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. 268:1993;909-916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 909-916
    • Pillet, L.1    Tremeau, O.2    Ducancel, F.3    Drevet, P.4    Zinn-Justin, S.5    Pinkasfeld, S.6    Boulain, J.C.7    Menez, A.8
  • 40
    • 0033521033 scopus 로고    scopus 로고
    • Variability among the sites by which curaremimetic toxins bind to torpedo acetylcholine receptor, as revealed by identification of the functional residues of alpha-cobratoxin
    • Antil S., Servent D., Menez A. Variability among the sites by which curaremimetic toxins bind to torpedo acetylcholine receptor, as revealed by identification of the functional residues of alpha-cobratoxin. J. Biol. Chem. 274:1999;34851-34858.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34851-34858
    • Antil, S.1    Servent, D.2    Menez, A.3
  • 41
    • 1542362457 scopus 로고
    • Snake venom kappa-neurotoxins distinguish subtypes of neuronal nicotinic receptors
    • P. Gopalakrishakone, Tan C.K. Singapore: National University of Singapore Press
    • Chiappinelli V.A. Snake venom kappa-neurotoxins distinguish subtypes of neuronal nicotinic receptors. Gopalakrishakone P., Tan C.K. Recent Advances in Toxicology Research. 1992;103-120 National University of Singapore Press, Singapore.
    • (1992) Recent Advances in Toxicology Research , pp. 103-120
    • Chiappinelli, V.A.1
  • 42
    • 0021953776 scopus 로고
    • Kappa-bungarotoxin: Complete amino acid sequence of a neuronal nicotinic probe
    • Grant G.A., Chiappinelli V.A. Kappa-bungarotoxin: complete amino acid sequence of a neuronal nicotinic probe. Biochemistry. 24:1985;1532-1537.
    • (1985) Biochemistry , vol.24 , pp. 1532-1537
    • Grant, G.A.1    Chiappinelli, V.A.2
  • 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., 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. 31:1992;2962-2970.
    • (1992) Biochemistry , vol.31 , pp. 2962-2970
    • Sutcliffe, M.J.1    Dobson, C.M.2    Oswald, R.E.3
  • 44
    • 0024290419 scopus 로고
    • Amino acid sequence of kappa-flavitoxin: Establishment of a new family of snake venom neurotoxins
    • Grant G.A., Frazier M.W., Chiappinelli V.A. Amino acid sequence of kappa-flavitoxin: establishment of a new family of snake venom neurotoxins. Biochemistry. 27:1988;3794-3798.
    • (1988) Biochemistry , vol.27 , pp. 3794-3798
    • Grant, G.A.1    Frazier, M.W.2    Chiappinelli, V.A.3
  • 45
    • 0016705376 scopus 로고
    • Snake venom toxins. the primary structure of protein S4C11. a neurotoxin homologue from the venom of forest cobra (Naja melanoleuca)
    • Carlsson F.H. Snake venom toxins. The primary structure of protein S4C11. A neurotoxin homologue from the venom of forest cobra (Naja melanoleuca). Biochim. Biophys. Acta. 400:1975;310-321.
    • (1975) Biochim. Biophys. Acta , vol.400 , pp. 310-321
    • Carlsson, F.H.1
  • 48
    • 0035955692 scopus 로고    scopus 로고
    • Molecular cloning and expression of a functional snake venom vascular endothelium growth factor (VEGF) from the Bothrops insularis pit viper. a new member of the VEGF family of proteins
    • Junqueira de Azevedo I.L., Farsky S.H., Oliveira M.L., Ho P.L. Molecular cloning and expression of a functional snake venom vascular endothelium growth factor (VEGF) from the Bothrops insularis pit viper. A new member of the VEGF family of proteins. J. Biol. Chem. 276:2001;39836-39842.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39836-39842
    • Junqueira De Azevedo, I.L.1    Farsky, S.H.2    Oliveira, M.L.3    Ho, P.L.4
  • 49
    • 0034798169 scopus 로고    scopus 로고
    • Cloning of cDNAs encoding C-type lectins from Elapidae snakes Bungarus fasciatus and Bungarus multicinctus
    • Zha H.G., Lee W.H., Zhang Y. Cloning of cDNAs encoding C-type lectins from Elapidae snakes Bungarus fasciatus and Bungarus multicinctus. Toxicon. 39:2001;1887-1892.
    • (2001) Toxicon , vol.39 , pp. 1887-1892
    • Zha, H.G.1    Lee, W.H.2    Zhang, Y.3
  • 50
    • 0035543209 scopus 로고    scopus 로고
    • Cloning and functional expression of the mucrosobin protein, a beta-fibrinogenase of Trimeresurus mucrosquamatus (Taiwan Habu)
    • Guo Y.W., Chang T.Y., Lin K.T., Liu H.W., Shih K.C., Cheng S.H. Cloning and functional expression of the mucrosobin protein, a beta-fibrinogenase of Trimeresurus mucrosquamatus (Taiwan Habu). Protein Expr. Purif. 23:2001;483-490.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 483-490
    • Guo, Y.W.1    Chang, T.Y.2    Lin, K.T.3    Liu, H.W.4    Shih, K.C.5    Cheng, S.H.6
  • 54
    • 0033231385 scopus 로고    scopus 로고
    • Postsynaptic short-chain neurotoxins from Pseudonaja textilis. cDNA cloning, expression and protein characterization
    • Gong N., Armugam A., Jeyaseelan K. Postsynaptic short-chain neurotoxins from Pseudonaja textilis. cDNA cloning, expression and protein characterization. Eur. J. Biochem. 265:1999;982-989.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 982-989
    • Gong, N.1    Armugam, A.2    Jeyaseelan, K.3
  • 55
    • 0024822384 scopus 로고
    • Sequence analysis of a cDNA encoding a erabutoxin b from the sea-snake Laticauda semifasciata
    • Obara K., Fuse N., Tsuchiya T., Nonomura Y., Menez A., Tamiya T. Sequence analysis of a cDNA encoding a erabutoxin b from the sea-snake Laticauda semifasciata. Nucleic Acids Res. 17:1989;10490.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10490
    • Obara, K.1    Fuse, N.2    Tsuchiya, T.3    Nonomura, Y.4    Menez, A.5    Tamiya, T.6
  • 56
    • 0032889742 scopus 로고    scopus 로고
    • Complete nucleotide sequences of cDNAs encoding long chain alpha-neurotoxins from sea krait, Laticauda semifasciata
    • Tamiya T., Ohno S., Nishimura E., Fujimi T.J., Tsuchiya T. Complete nucleotide sequences of cDNAs encoding long chain alpha-neurotoxins from sea krait, Laticauda semifasciata. Toxicon. 37:1999;181-185.
    • (1999) Toxicon , vol.37 , pp. 181-185
    • Tamiya, T.1    Ohno, S.2    Nishimura, E.3    Fujimi, T.J.4    Tsuchiya, T.5
  • 57
    • 0025355079 scopus 로고
    • Nucleotide sequence and structure analysis of cDNAs encoding short-chain neurotoxins from venom glands of a sea snake (Aipysurus laevis)
    • Ducancel F., Guignery-Frelat G., Boulain J.C., Menez A. Nucleotide sequence and structure analysis of cDNAs encoding short-chain neurotoxins from venom glands of a sea snake (Aipysurus laevis). Toxicon. 28:1990;119-123.
    • (1990) Toxicon , vol.28 , pp. 119-123
    • Ducancel, F.1    Guignery-Frelat, G.2    Boulain, J.C.3    Menez, A.4
  • 58
    • 0025107412 scopus 로고
    • Structure of the snake short-chain neurotoxin, erabutoxin c, precursor gene
    • Fuse N., Tsuchiya T., Nonomura Y., Menez A., Tamiya T. Structure of the snake short-chain neurotoxin, erabutoxin c, precursor gene. Eur. J. Biochem. 193:1990;629-633.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 629-633
    • Fuse, N.1    Tsuchiya, T.2    Nonomura, Y.3    Menez, A.4    Tamiya, T.5
  • 59
    • 0017284145 scopus 로고
    • Isolation, properties, and amino acid sequences of three neurotoxins from the venom of a sea snake Aipysurus laevis
    • Maeda N., Tamiya N. Isolation, properties, and amino acid sequences of three neurotoxins from the venom of a sea snake Aipysurus laevis. Biochem. J. 153:1976;79-87.
    • (1976) Biochem. J. , vol.153 , pp. 79-87
    • Maeda, N.1    Tamiya, N.2
  • 60
    • 0032922732 scopus 로고    scopus 로고
    • Postsynaptic alpha-neurotoxin gene of splitting cobra, Naja naja sputatrix: Structure, organization and phylogenetic analysis
    • Afifiyan F., Armugam A., Tan C.H., Goplakrishnakone P., Jeyaseelan K. Postsynaptic alpha-neurotoxin gene of splitting cobra, Naja naja sputatrix: structure, organization and phylogenetic analysis. Genome Res. 9:1999;259-266.
    • (1999) Genome Res. , vol.9 , pp. 259-266
    • Afifiyan, F.1    Armugam, A.2    Tan, C.H.3    Goplakrishnakone, P.4    Jeyaseelan, K.5
  • 61
    • 0032402082 scopus 로고    scopus 로고
    • Four new postsynaptic neurotoxins from Naja naja sputatrix venom: CDNA cloning, protein expression, and phylogenetic analysis
    • Afifiyan F., Armugam A., Gopalakrishnakone P., Tan N.H., Tan C.H., Jeyaseelan K. Four new postsynaptic neurotoxins from Naja naja sputatrix venom: cDNA cloning, protein expression, and phylogenetic analysis. Toxicon. 36:1998;1871-1885.
    • (1998) Toxicon , vol.36 , pp. 1871-1885
    • Afifiyan, F.1    Armugam, A.2    Gopalakrishnakone, P.3    Tan, N.H.4    Tan, C.H.5    Jeyaseelan, K.6
  • 62
    • 0031590433 scopus 로고    scopus 로고
    • Genomic structures of cardiotoxin 4 and cobrotoxin from Naja naja atra (Taiwan cobra)
    • Chang L.S., Lin J., Chou Y.C., Hong E. Genomic structures of cardiotoxin 4 and cobrotoxin from Naja naja atra (Taiwan cobra). Biochem. Biophys. Res. Commun. 239:1997;756-762.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 756-762
    • Chang, L.S.1    Lin, J.2    Chou, Y.C.3    Hong, E.4
  • 63
    • 0033570288 scopus 로고    scopus 로고
    • Genetic organization of α-bungarotoxin from Bungarus multicinctus (Taiwan banded krait): Evidence showing that the production of α-bungarotoxin isotoxins is not derived from edited mRNAs
    • Chang L.S., Lin S.K., Huang H.B., Hsiao M. Genetic organization of α-bungarotoxin from Bungarus multicinctus (Taiwan banded krait): evidence showing that the production of α-bungarotoxin isotoxins is not derived from edited mRNAs. Nucleic Acids Res. 27:1999;3970-3975.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3970-3975
    • Chang, L.S.1    Lin, S.K.2    Huang, H.B.3    Hsiao, M.4
  • 64
    • 0036623407 scopus 로고    scopus 로고
    • Organization and phylogenetic analysis of kappa-bungarotoxin genes from Bungarus multicinctus (Taiwan banded krait)
    • Chang L.S., Chung C., Lin J., Hong E. Organization and phylogenetic analysis of kappa-bungarotoxin genes from Bungarus multicinctus (Taiwan banded krait). Genetica. 115:2002;213-221.
    • (2002) Genetica , vol.115 , pp. 213-221
    • Chang, L.S.1    Chung, C.2    Lin, J.3    Hong, E.4
  • 65
    • 0020596760 scopus 로고
    • Improvement of Malayan cobra (Naja naja sputatrix) antivenin
    • Tan N.H. Improvement of Malayan cobra (Naja naja sputatrix) antivenin. Toxicon. 21:1983;75-79.
    • (1983) Toxicon , vol.21 , pp. 75-79
    • Tan, N.H.1
  • 66
    • 0036685452 scopus 로고    scopus 로고
    • Alpha-neurotoxin gene expression in Naja sputatrix: Identification of a silencer element in the promoter region
    • Ma D., Armugam A., Jeyaseelan K. Alpha-neurotoxin gene expression in Naja sputatrix: identification of a silencer element in the promoter region. Arch. Biochem. Biophys. 404:2002;98-105.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 98-105
    • Ma, D.1    Armugam, A.2    Jeyaseelan, K.3
  • 67
    • 0034733563 scopus 로고    scopus 로고
    • Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity
    • Koipally J., Georgopoulos K. Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity. J. Biol. Chem. 275:2000;19594-19602.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19594-19602
    • Koipally, J.1    Georgopoulos, K.2
  • 68
    • 0032906386 scopus 로고    scopus 로고
    • In situ hybridization and immunohistochemical analysis of the expression of cardiotoxin and neurotoxin genes in Naja naja sputatrix
    • Lachumanan R., Armugam A., Durairaj P., Gopalakrishnakone P., Tan C.H., Jeyaseelan K. In situ hybridization and immunohistochemical analysis of the expression of cardiotoxin and neurotoxin genes in Naja naja sputatrix. J. Histochem. Cytochem. 47:1999;551-560.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 551-560
    • Lachumanan, R.1    Armugam, A.2    Durairaj, P.3    Gopalakrishnakone, P.4    Tan, C.H.5    Jeyaseelan, K.6
  • 69
    • 0032534713 scopus 로고    scopus 로고
    • Genetic characterization of the mRNAs encoding alpha-bungarotoxin: Isoforms and RNA editing in Bungarus multicinctus gland cells
    • Liu L.F., Chang C.C., Liau M.Y., Kuo K.W. Genetic characterization of the mRNAs encoding alpha-bungarotoxin: isoforms and RNA editing in Bungarus multicinctus gland cells. Nucleic Acids Res. 26:1998;5624-5629.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5624-5629
    • Liu, L.F.1    Chang, C.C.2    Liau, M.Y.3    Kuo, K.W.4
  • 70
    • 0242317451 scopus 로고    scopus 로고
    • Molecular evolution and diversification of snake toxin genes, revealed by analysis of intron sequences
    • Fujimi T.J., Nakajyo T., Nishimura E., Ogura E., Tsuchiya T., Tamiya T. Molecular evolution and diversification of snake toxin genes, revealed by analysis of intron sequences. Gene. 313:2003;111-118.
    • (2003) Gene , vol.313 , pp. 111-118
    • Fujimi, T.J.1    Nakajyo, T.2    Nishimura, E.3    Ogura, E.4    Tsuchiya, T.5    Tamiya, T.6
  • 71
    • 0001391305 scopus 로고
    • The evolution of toxins found in snake venoms
    • Lee C.Y. Berlin: Springer-Verlag
    • Strydom D.J. The evolution of toxins found in snake venoms. Lee C.Y. Snake Venom: Handbook of Experimental Pharmacology. 1979;258-275 Springer-Verlag, Berlin.
    • (1979) Snake Venom: Handbook of Experimental Pharmacology , pp. 258-275
    • Strydom, D.J.1
  • 72
    • 0021162771 scopus 로고
    • Classification of elapid snake neurotoxins and cytotoxins according to chain length: Evolutionary implications
    • Dufton M.J. Classification of elapid snake neurotoxins and cytotoxins according to chain length: evolutionary implications. J. Mol. Evol. 20:1984;128-134.
    • (1984) J. Mol. Evol. , vol.20 , pp. 128-134
    • Dufton, M.J.1
  • 73
    • 0021970405 scopus 로고
    • Non-divergence theory of evolution: Sequence comparison of some proteins from snakes and bacteria
    • Tamiya N., Yagi T. Non-divergence theory of evolution: sequence comparison of some proteins from snakes and bacteria. J. Biochem. (Tokyo). 98:1985;289-303.
    • (1985) J. Biochem. (Tokyo) , vol.98 , pp. 289-303
    • Tamiya, N.1    Yagi, T.2
  • 74
    • 0034685705 scopus 로고    scopus 로고
    • Molecular cloning, characterization and evolution of the gene encoding a new group of short-chain alpha-neurotoxins in an Australian elapid, Pseudonaja textilis
    • Gong N., Armugam A., Jeyaseelan K. Molecular cloning, characterization and evolution of the gene encoding a new group of short-chain alpha-neurotoxins in an Australian elapid, Pseudonaja textilis. FEBS Lett. 473:2000;303-310.
    • (2000) FEBS Lett. , vol.473 , pp. 303-310
    • Gong, N.1    Armugam, A.2    Jeyaseelan, K.3
  • 75
    • 0035884707 scopus 로고    scopus 로고
    • Cloning and characterization of the pseudonajatoxin b precursor
    • Gong N., Armugam A., Mirtschin P., Jeyaseelan K. Cloning and characterization of the pseudonajatoxin b precursor. Biochem. J. 358:2001;647-656.
    • (2001) Biochem. J. , vol.358 , pp. 647-656
    • Gong, N.1    Armugam, A.2    Mirtschin, P.3    Jeyaseelan, K.4
  • 76
    • 0033278654 scopus 로고    scopus 로고
    • How should species phylogenies be inferred from sequence data? How should species phylogenies be inferred from sequence data?
    • Slowinski J.B., Page R.D. How should species phylogenies be inferred from sequence data? How should species phylogenies be inferred from sequence data? Syst. Biol. 48:1999;814-825.
    • (1999) Syst. Biol. , vol.48 , pp. 814-825
    • Slowinski, J.B.1    Page, R.D.2
  • 78
    • 0023378002 scopus 로고
    • Pseudonajatoxin b: Unusual amino acid sequence of a lethal neurotoxin from the venom of the Australian common brown snake, Pseudonaja textiles
    • Tyler M.I., Spence I., Barnett D., Howden M.E. Pseudonajatoxin b: unusual amino acid sequence of a lethal neurotoxin from the venom of the Australian common brown snake, Pseudonaja textiles. Eur. J. Biochem. 166:1987;139-143.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 139-143
    • Tyler, M.I.1    Spence, I.2    Barnett, D.3    Howden, M.E.4
  • 79
    • 0035239228 scopus 로고    scopus 로고
    • Toxicity in animals. Trends in evolution?
    • Mebs D. Toxicity in animals. Trends in evolution? Toxicon. 39:2001;87-96.
    • (2001) Toxicon , vol.39 , pp. 87-96
    • Mebs, D.1
  • 81
    • 0033526450 scopus 로고    scopus 로고
    • Taking the bite out of snake venoms
    • Senior K. Taking the bite out of snake venoms. Lancet. 353:1999;1946.
    • (1999) Lancet , vol.353 , pp. 1946
    • Senior, K.1
  • 84
    • 0023755388 scopus 로고    scopus 로고
    • Antipeptide monoclonal antibodies inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor
    • Bracci L., Antoni G., Cusi M.G., Lozzi L., Niccolai N., Petreni S., Rustici M., Santucci A., Soldani P., Valensin P.E. Antipeptide monoclonal antibodies inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor. Mol. Immunol. 25:1998;881-888.
    • (1998) Mol. Immunol. , vol.25 , pp. 881-888
    • Bracci, L.1    Antoni, G.2    Cusi, M.G.3    Lozzi, L.4    Niccolai, N.5    Petreni, S.6    Rustici, M.7    Santucci, A.8    Soldani, P.9    Valensin, P.E.10
  • 85
    • 0020973920 scopus 로고
    • Cross-reactivity of anti-idiotypic antibodies as a tool to study nonimmunoglobulin proteins
    • Sege K. Cross-reactivity of anti-idiotypic antibodies as a tool to study nonimmunoglobulin proteins. Ann. N.Y. Acad. Sci. 418:1983;248-256.
    • (1983) Ann. N.Y. Acad. Sci. , vol.418 , pp. 248-256
    • Sege, K.1
  • 86
    • 0021678943 scopus 로고
    • Amino acid sequence similarity between rabies virus glycoprotein and snake venom curaremimetic neurotoxins
    • Lentz T.L., Wilson P.T., Hawrot E., Speicher D.W. Amino acid sequence similarity between rabies virus glycoprotein and snake venom curaremimetic neurotoxins. Science. 226:1984;847-848.
    • (1984) Science , vol.226 , pp. 847-848
    • Lentz, T.L.1    Wilson, P.T.2    Hawrot, E.3    Speicher, D.W.4
  • 87
    • 0025028790 scopus 로고
    • Sequence homology between HIV gp120, rabies virus glycoprotein, and snake venom neurotoxins. Is the nicotinic acetylcholine receptor an HIV receptor?
    • Neri P., Bracci L., Rustici M., Santucci A. Sequence homology between HIV gp120, rabies virus glycoprotein, and snake venom neurotoxins. Is the nicotinic acetylcholine receptor an HIV receptor? Arch. Virol. 114:1990;265-269.
    • (1990) Arch. Virol. , vol.114 , pp. 265-269
    • Neri, P.1    Bracci, L.2    Rustici, M.3    Santucci, A.4
  • 88
    • 0023834181 scopus 로고
    • The human medulloblastoma cell line TE671 expresses a muscle-like acetylcholine receptor. Cloning of the alpha-subunit cDNA
    • Schoepfer R., Luther M., Lindstrom J. The human medulloblastoma cell line TE671 expresses a muscle-like acetylcholine receptor. Cloning of the alpha-subunit cDNA. FEBS Lett. 226:1988;235-240.
    • (1988) FEBS Lett. , vol.226 , pp. 235-240
    • Schoepfer, R.1    Luther, M.2    Lindstrom, J.3
  • 89
    • 0024781884 scopus 로고
    • Snake venoms: Toolbox of the neurobiologist
    • Mebs D. Snake venoms: toolbox of the neurobiologist. Endeavour. 13:1989;157-161.
    • (1989) Endeavour , vol.13 , pp. 157-161
    • Mebs, D.1
  • 90
    • 0019443881 scopus 로고
    • The biology of myasthenia gravis
    • Drachman D.B. The biology of myasthenia gravis. Annu. Rev. Neurosci. 4:1981;195-225.
    • (1981) Annu. Rev. Neurosci. , vol.4 , pp. 195-225
    • Drachman, D.B.1
  • 91
    • 0037124025 scopus 로고    scopus 로고
    • Candoxin, a novel toxin from Bungarus candidus, is a reversible antagonist of muscle (alpha beta gamma delta) but a poorly reversible antagonist of neuronal alpha 7 nicotinic acetylcholine receptors
    • Nirthanan S., Charpantier E., Gopalakrishnakone P., Gwee M.C., Khoo H.E., Cheah L.S., Bertrand D., Kini R.M. Candoxin, a novel toxin from Bungarus candidus, is a reversible antagonist of muscle (alpha beta gamma delta) but a poorly reversible antagonist of neuronal alpha 7 nicotinic acetylcholine receptors. J. Biol. Chem. 277:2002;17811-17820.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17811-17820
    • Nirthanan, S.1    Charpantier, E.2    Gopalakrishnakone, P.3    Gwee, M.C.4    Khoo, H.E.5    Cheah, L.S.6    Bertrand, D.7    Kini, R.M.8
  • 92
    • 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., Lazarus R.A. Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins. Biochemistry. 31:1992;4766-4772.
    • (1992) Biochemistry , vol.31 , pp. 4766-4772
    • McDowell, R.S.1    Dennis, M.S.2    Louie, A.3    Shuster, M.4    Mulkerrin, M.G.5    Lazarus, R.A.6
  • 93
    • 0027214388 scopus 로고
    • Homologous kappa-neurotoxins exhibit residue-specific interactions with the alpha 3 subunit of the nicotinic acetylcholine receptor: A comparison of the structural requirements for kappa-bungarotoxin and kappa-flavitoxin binding
    • McLane K.E., Weaver W.R., Lei S., Chiappinelli V.A., Conti-Tronconi B.M. Homologous kappa-neurotoxins exhibit residue-specific interactions with the alpha 3 subunit of the nicotinic acetylcholine receptor: a comparison of the structural requirements for kappa-bungarotoxin and kappa-flavitoxin binding. Biochemistry. 32:1993;6988-6994.
    • (1993) Biochemistry , vol.32 , pp. 6988-6994
    • McLane, K.E.1    Weaver, W.R.2    Lei, S.3    Chiappinelli, V.A.4    Conti-Tronconi, B.M.5
  • 94
    • 0025968656 scopus 로고
    • Pharmacological and functional diversity of neuronal nicotinic acetylcholine receptors
    • Deneris E.S., Connolly J., Rogers S.W., Duvoisin R. Pharmacological and functional diversity of neuronal nicotinic acetylcholine receptors. Trends Pharmacol. Sci. 12:1991;34-40.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 34-40
    • Deneris, E.S.1    Connolly, J.2    Rogers, S.W.3    Duvoisin, R.4
  • 95
    • 0019175714 scopus 로고
    • Permeability control by cholinergic receptors in Torpedo postsynaptic membranes: Agonist dose-response relations measured at second and millisecond times
    • Neubig R.R., Cohen J.B. Permeability control by cholinergic receptors in Torpedo postsynaptic membranes: agonist dose-response relations measured at second and millisecond times. Biochemistry. 19:1980;2770-2779.
    • (1980) Biochemistry , vol.19 , pp. 2770-2779
    • Neubig, R.R.1    Cohen, J.B.2
  • 96
    • 0027518923 scopus 로고
    • Molecular cloning, functional properties, and distribution of rat brain alpha 7: A nicotinic cation channel highly permeable to calcium
    • Seguela P., Wadiche J., Dineley-Miller K., Dani J.A., Patrick J.W. Molecular cloning, functional properties, and distribution of rat brain alpha 7: a nicotinic cation channel highly permeable to calcium. J. Neurosci. 13:1993;596-604.
    • (1993) J. Neurosci. , vol.13 , pp. 596-604
    • Seguela, P.1    Wadiche, J.2    Dineley-Miller, K.3    Dani, J.A.4    Patrick, J.W.5
  • 97
    • 0018102059 scopus 로고
    • Nicotinic acetylcholine receptor of mammalian brain: Naja toxin binding to subcellular fractions of rat brain
    • Tindall R.S., Kent M., Baskin F., Rosenberg R.N. Nicotinic acetylcholine receptor of mammalian brain: naja toxin binding to subcellular fractions of rat brain. J. Neurochem. 30:1978;859-863.
    • (1978) J. Neurochem. , vol.30 , pp. 859-863
    • Tindall, R.S.1    Kent, M.2    Baskin, F.3    Rosenberg, R.N.4
  • 98
    • 0023863301 scopus 로고
    • Kappa-bungarotoxin: Binding of a neuronal nicotinic receptor antagonist to chick optic lobe and skeletal muscle
    • Wolf K.M., Ciarleglio A., Chiappinelli V.A. Kappa-bungarotoxin: binding of a neuronal nicotinic receptor antagonist to chick optic lobe and skeletal muscle. Brain Res. 439:1988;249-258.
    • (1988) Brain Res. , vol.439 , pp. 249-258
    • Wolf, K.M.1    Ciarleglio, A.2    Chiappinelli, V.A.3
  • 99
    • 0028178802 scopus 로고
    • Neuronal acetylcholine receptors that bind alpha-bungarotoxin with high affinity function as ligand-gated ion channels
    • Zhang Z.W., Vijayaraghavan S., Berg D.K. Neuronal acetylcholine receptors that bind alpha-bungarotoxin with high affinity function as ligand-gated ion channels. Neuron. 12:1994;167-177.
    • (1994) Neuron , vol.12 , pp. 167-177
    • Zhang, Z.W.1    Vijayaraghavan, S.2    Berg, D.K.3
  • 100
    • 0027382077 scopus 로고
    • Diversity of nicotinic acetylcholine receptors in rat hippocampal neurons. I. Pharmacological and functional evidence for distinct structural subtypes
    • Alkondon M., Albuquerque E.X. Diversity of nicotinic acetylcholine receptors in rat hippocampal neurons. I. Pharmacological and functional evidence for distinct structural subtypes. J. Pharmacol. Exp. Ther. 265:1993;1455-1473.
    • (1993) J. Pharmacol. Exp. Ther. , vol.265 , pp. 1455-1473
    • Alkondon, M.1    Albuquerque, E.X.2
  • 101
  • 102
  • 103
    • 0033136270 scopus 로고    scopus 로고
    • Lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS
    • Miwa J.M., Ibanez-Tallon I., Crabtree G.W., Sanchez R., Sali A., Role L.W., Heintz N. Lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS. Neuron. 23:1999;105-114.
    • (1999) Neuron , vol.23 , pp. 105-114
    • Miwa, J.M.1    Ibanez-Tallon, I.2    Crabtree, G.W.3    Sanchez, R.4    Sali, A.5    Role, L.W.6    Heintz, N.7
  • 104
    • 0037075542 scopus 로고    scopus 로고
    • Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1
    • Ibanez-Tallon I., Miwa J.M., Wang H.L., Adams N.C., Crabtree G.W., Sine S.M., Heintz N. Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1. Neuron. 33:2002;893-903.
    • (2002) Neuron , vol.33 , pp. 893-903
    • Ibanez-Tallon, I.1    Miwa, J.M.2    Wang, H.L.3    Adams, N.C.4    Crabtree, G.W.5    Sine, S.M.6    Heintz, N.7
  • 105
    • 18144437490 scopus 로고    scopus 로고
    • How do snake curaremimetic toxins discriminate between nicotinic acetylcholine receptor subtypes
    • Servent D., Mourier G., Antil S., Menez A. How do snake curaremimetic toxins discriminate between nicotinic acetylcholine receptor subtypes. Toxicol. Lett. 102-103:1998;199-203.
    • (1998) Toxicol. Lett. , vol.102-103 , pp. 199-203
    • Servent, D.1    Mourier, G.2    Antil, S.3    Menez, A.4
  • 106
  • 107
    • 0142138699 scopus 로고    scopus 로고
    • Structurally conserved alpha-neurotoxin genes encode functionally diversed proteins in the venom of Maja sputatrix
    • Jeyseelan K., Poh S.L., Mair R., Armugam A. Structurally conserved alpha-neurotoxin genes encode functionally diversed proteins in the venom of Maja sputatrix. FEBS Lett. 553:2003;333-341.
    • (2003) FEBS Lett. , vol.553 , pp. 333-341
    • Jeyseelan, K.1    Poh, S.L.2    Mair, R.3    Armugam, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.