메뉴 건너뛰기




Volumn 10, Issue 2, 1999, Pages 235-251

Peptide toxins in spider venoms;Les toxines peptidiques dans les venins d'araignees

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; POSTSYNAPTIC RECEPTOR; POTASSIUM CHANNEL; SODIUM CHANNEL; SPIDER VENOM;

EID: 0032715539     PISSN: 09244204     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0924-4204(99)80037-7     Document Type: Article
Times cited : (2)

References (129)
  • 1
    • 0024562287 scopus 로고
    • Two classes of channel-specific toxins from funnel web spider venom
    • [1] Adams M.E., Herold E.E., Venema V.J., Two classes of channel-specific toxins from funnel web spider venom, J. Comp. Physiol. A 164 (1989) 333-342.
    • (1989) J. Comp. Physiol. A , vol.164 , pp. 333-342
    • Adams, M.E.1    Herold, E.E.2    Venema, V.J.3
  • 2
    • 0025055598 scopus 로고
    • ω-agatoxins: Novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom
    • [2] Adams M.E., Bindokas V.P., Hasegawa L., Venema V.J., ω-agatoxins: novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom, J. Biol. Chem. 265 (1990) 861-867.
    • (1990) J. Biol. Chem. , vol.265 , pp. 861-867
    • Adams, M.E.1    Bindokas, V.P.2    Hasegawa, L.3    Venema, V.J.4
  • 3
    • 0027332134 scopus 로고
    • Structure and properties of ω-agatoxin IVB, a new antagonist of P-type calcium channels
    • [3] Adams M.E., Mintz I.M., Reily M.D., Thanabal V., Bean B.P., Structure and properties of ω-agatoxin IVB, a new antagonist of P-type calcium channels, Mol. Pharmacol. 44 (1993) 681-688.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 681-688
    • Adams, M.E.1    Mintz, I.M.2    Reily, M.D.3    Thanabal, V.4    Bean, B.P.5
  • 7
    • 0027534564 scopus 로고
    • Effects of a toxic fraction, PhTx2, from the spider Phoneutria nigriventer on the sodium current
    • [7] Araujo D.A., Cordeiro M.N., Diniz C.R., Beirao P.S., Effects of a toxic fraction, PhTx2, from the spider Phoneutria nigriventer on the sodium current, Naunyn Schmiedebergs Arch. Pharmacol. 347 (1993) 205-208.
    • (1993) Naunyn Schmiedebergs Arch. Pharmacol. , vol.347 , pp. 205-208
    • Araujo, D.A.1    Cordeiro, M.N.2    Diniz, C.R.3    Beirao, P.S.4
  • 8
    • 0030176104 scopus 로고    scopus 로고
    • Effects of whole venom and venom fractions from several Australian spiders, including Atrax (Hadronyche) species, when injected into insects
    • [8] Atkinson R.K., Vonarx E.J., Howden M.E.H., Effects of whole venom and venom fractions from several Australian spiders, including Atrax (Hadronyche) species, when injected into insects, Comp. Biochem. Physiol. 114C (1996) 113-117.
    • (1996) Comp. Biochem. Physiol. , vol.114 C , pp. 113-117
    • Atkinson, R.K.1    Vonarx, E.J.2    Howden, M.E.H.3
  • 9
    • 0030245671 scopus 로고    scopus 로고
    • Mode of action of an insecticidal peptide toxin from the venom of a weaving spider (Diguetia canities)
    • [9] Bloomquist J.R., Kinne L.P., Deutsch V., Simpson S.F., Mode of action of an insecticidal peptide toxin from the venom of a weaving spider (Diguetia canities), Toxicon 34 (1996) 1072-1075.
    • (1996) Toxicon , vol.34 , pp. 1072-1075
    • Bloomquist, J.R.1    Kinne, L.P.2    Deutsch, V.3    Simpson, S.F.4
  • 11
    • 0023976277 scopus 로고
    • Amino acid sequence of versutoxin, a lethal neurotoxin from the venom of the funnel-web spider Atrax versutus
    • [11] Brown M.R., Sheumack D.D., Tyler M.I., Howden M.E., Amino acid sequence of versutoxin, a lethal neurotoxin from the venom of the funnel-web spider Atrax versutus Biochem, J. 250 (1988) 401-405.
    • (1988) Biochem, J. , vol.250 , pp. 401-405
    • Brown, M.R.1    Sheumack, D.D.2    Tyler, M.I.3    Howden, M.E.4
  • 16
    • 0016437336 scopus 로고
    • Adenosine triphosphate in tarantula spider venoms and its synergistic effect with the venom toxin
    • [16] Chan T.K., Geren C.R., Howell D.E., Odell G.V., Adenosine triphosphate in tarantula spider venoms and its synergistic effect with the venom toxin, Toxicon 13 (1975) 61-66.
    • (1975) Toxicon , vol.13 , pp. 61-66
    • Chan, T.K.1    Geren, C.R.2    Howell, D.E.3    Odell, G.V.4
  • 17
    • 0027048334 scopus 로고
    • High affinity block of myocardial L-type calcium channels by the spider toxin ω-agatoxin IIIA: Advantages over 1,4-dihydropyridines
    • [17] Cohen C.J., Ertel E.A., Smith M.M., Venema V.J., Adams M.E., Leibowitz M.D., High affinity block of myocardial L-type calcium channels by the spider toxin ω-agatoxin IIIA: advantages over 1,4-dihydropyridines, Mol. Pharmacol. 42 (1992) 947-951.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 947-951
    • Cohen, C.J.1    Ertel, E.A.2    Smith, M.M.3    Venema, V.J.4    Adams, M.E.5    Leibowitz, M.D.6
  • 18
    • 0026705696 scopus 로고
    • The purification and amino acid sequences of four Tx2 neurotoxins from the venom of the Brazilian'armed'spider Phoneutria nigriventer (Keys)
    • [18] Cordeiro M.D.N., Diniz C.R., Valentim A.D.C., von Eickstedt V.R., Gilroy J., Richardson M., The purification and amino acid sequences of four Tx2 neurotoxins from the venom of the Brazilian'armed'spider Phoneutria nigriventer (Keys), FEBS Lett. 310 (1992) 153-156.
    • (1992) FEBS Lett. , vol.310 , pp. 153-156
    • Cordeiro, M.D.N.1    Diniz, C.R.2    Valentim, A.D.C.3    Von Eickstedt, V.R.4    Gilroy, J.5    Richardson, M.6
  • 19
    • 0027465984 scopus 로고
    • Purification and amino acid sequences of six Tx3 type neurotoxins from the venom of the Brazilian armed spider Phoneutria nigriventer (Keyserling, 1891)
    • [19] Cordeiro M.D.N., De Figueiredo S.G., Valentim A.D.C., Diniz C.R., von Eickstedt V.R., Gilroy J., Richardson M., Purification and amino acid sequences of six Tx3 type neurotoxins from the venom of the Brazilian armed spider Phoneutria nigriventer (Keyserling, 1891), Toxicon 31 (1993) 35-42.
    • (1993) Toxicon , vol.31 , pp. 35-42
    • Cordeiro, M.D.N.1    De Figueiredo, S.G.2    Valentim, A.D.C.3    Diniz, C.R.4    Von Eickstedt, V.R.5    Gilroy, J.6    Richardson, M.7
  • 23
    • 0025349850 scopus 로고
    • The purification and amino acid sequence of the lethal neurotoxin Tx1 from the venom of the brazilian armed spider Phoneutria nigriventer
    • [23] Diniz C.R., Cordeiro M.D.N., Junor L.R., Kelly P., Fischer S., Reimann F., Oliveira E.B., Richardson M., The purification and amino acid sequence of the lethal neurotoxin Tx1 from the venom of the Brazilian armed spider Phoneutria nigriventer, FEBS Lett. 263 (1990) 251-253.
    • (1990) FEBS Lett. , vol.263 , pp. 251-253
    • Diniz, C.R.1    Cordeiro, M.D.N.2    Junor, L.R.3    Kelly, P.4    Fischer, S.5    Reimann, F.6    Oliveira, E.B.7    Richardson, M.8
  • 24
    • 0027234680 scopus 로고
    • Sequence of the cDNA coding for the lethal neurotoxin Tx1 from the Brazilian armed spider Phoneutria nigriventer predicts the synthesis and processing of a preprotoxin
    • [24] Diniz M.R., Paine M.J., Diniz C.R., Theakston R.D., Crampton J.M., Sequence of the cDNA coding for the lethal neurotoxin Tx1 from the Brazilian armed spider Phoneutria nigriventer predicts the synthesis and processing of a preprotoxin, J. Biol. Chem. 268 (1993) 15340-15342.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15340-15342
    • Diniz, M.R.1    Paine, M.J.2    Diniz, C.R.3    Theakston, R.D.4    Crampton, J.M.5
  • 25
    • 0032549630 scopus 로고    scopus 로고
    • Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4
    • [25] Diochot S., Schweitz H., Beress L., Lazdunski M., Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4, J. Biol. Chem. 273 (1998) 6744-6759.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6744-6759
    • Diochot, S.1    Schweitz, H.2    Beress, L.3    Lazdunski, M.4
  • 26
    • 0032921154 scopus 로고    scopus 로고
    • Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis
    • [26] Diochot S., Drici M.D., Moinier D., Fink M., Lazdunski M., Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis, Br. J. Pharmacol. 126 (1999) 251-263.
    • (1999) Br. J. Pharmacol. , vol.126 , pp. 251-263
    • Diochot, S.1    Drici, M.D.2    Moinier, D.3    Fink, M.4    Lazdunski, M.5
  • 27
    • 0029656272 scopus 로고    scopus 로고
    • Multiple actions of arylalkylamine arthropod toxins on the N-methyl-D-aspartate receptor
    • [27] Donevan S.D., Rogawski M.A., Multiple actions of arylalkylamine arthropod toxins on the N-methyl-D-aspartate receptor, Neuroscience 70 (1996) 361-375.
    • (1996) Neuroscience , vol.70 , pp. 361-375
    • Donevan, S.D.1    Rogawski, M.A.2
  • 28
    • 0023185936 scopus 로고
    • Presence of proteins and glutamate as major constituents of the venom of the spider Araneus gemma
    • [28] Early S.L., Michaelis E.K., Presence of proteins and glutamate as major constituents of the venom of the spider Araneus gemma, Toxicon 25 (1987) 433-442.
    • (1987) Toxicon , vol.25 , pp. 433-442
    • Early, S.L.1    Michaelis, E.K.2
  • 29
    • 0028174186 scopus 로고
    • Type III ω-agatoxins: A family of probes for similar binding sites on L- and N-type calcium channels
    • [29] Ertel E.A., Warren V.A., Adams M.E., Griffin P.R., Cohen C.J., Smith M.M., Type III ω-agatoxins: a family of probes for similar binding sites on L- and N-type calcium channels, Biochemistry 33 (1994) 5098-6108.
    • (1994) Biochemistry , vol.33 , pp. 5098-6108
    • Ertel, E.A.1    Warren, V.A.2    Adams, M.E.3    Griffin, P.R.4    Cohen, C.J.5    Smith, M.M.6
  • 30
    • 0030725532 scopus 로고    scopus 로고
    • High-performance liquid chromatography matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry peptide fingerprinting of tarantula venoms in the genus Brachypelma: Chemotaxonomic and biochemical applications
    • [30] Escoubas P., Célérier M.L., Nakajima T., High-performance liquid chromatography matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry peptide fingerprinting of tarantula venoms in the genus Brachypelma: chemotaxonomic and biochemical applications, Rapid Commun. Mass Spectrom. 11 (1997) 1891-1899.
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 1891-1899
    • Escoubas, P.1    Célérier, M.L.2    Nakajima, T.3
  • 31
    • 0000477401 scopus 로고    scopus 로고
    • Two novel peptide toxins from the venom of the tarantula Lasiodora parahybana
    • [31] Escoubas P., Célérier M.L., Romi-Lebrun R., Nakajima T., Two novel peptide toxins from the venom of the tarantula Lasiodora parahybana, Toxicon 35 (1997) 805.
    • (1997) Toxicon , vol.35 , pp. 805
    • Escoubas, P.1    Célérier, M.L.2    Romi-Lebrun, R.3    Nakajima, T.4
  • 33
    • 0028920782 scopus 로고
    • Purification and amino acid sequence of the insecticidal neurotoxin Tx4(6-1) from the venom of the armed spider Phoneutria nigriventer (Keyserling, 1891)
    • [33] Figueiredo S.G., Garcia M.E., Valentim A.C., Cordeiro M.N., Diniz C.R., Richardson M., Purification and amino acid sequence of the insecticidal neurotoxin Tx4(6-1) from the venom of the armed spider Phoneutria nigriventer (Keyserling, 1891), Toxicon 33 (1995) 83-93.
    • (1995) Toxicon , vol.33 , pp. 83-93
    • Figueiredo, S.G.1    Garcia, M.E.2    Valentim, A.C.3    Cordeiro, M.N.4    Diniz, C.R.5    Richardson, M.6
  • 34
    • 0030727613 scopus 로고    scopus 로고
    • The structure of versutoxin (5-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel
    • [34] Fletcher J.I., Chapman B.E., Mackay J.P., Howden M.E., King G.F., The structure of versutoxin (5-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel, Structure 5 (1997) 1525-1535.
    • (1997) Structure , vol.5 , pp. 1525-1535
    • Fletcher, J.I.1    Chapman, B.E.2    Mackay, J.P.3    Howden, M.E.4    King, G.F.5
  • 36
    • 0028260288 scopus 로고
    • Identification of noradrenaline in venom from the funnel-web spider Hololena curta
    • [36] Frew R., Hamilton M.G., Lundy P.M., Identification of noradrenaline in venom from the funnel-web spider Hololena curta, Toxicon 32 (1994) 511-515.
    • (1994) Toxicon , vol.32 , pp. 511-515
    • Frew, R.1    Hamilton, M.G.2    Lundy, P.M.3
  • 37
    • 0024563048 scopus 로고
    • Isolation and structure analysis of components from venom of the spider Argiope lobata
    • [37] Grishin E.V., Volkova T.M., Arseniev A.S., Isolation and structure analysis of components from venom of the spider Argiope lobata, Toxicon 27 (1989) 541-549.
    • (1989) Toxicon , vol.27 , pp. 541-549
    • Grishin, E.V.1    Volkova, T.M.2    Arseniev, A.S.3
  • 38
    • 0031740473 scopus 로고    scopus 로고
    • Black widow spider toxins: The present and the future
    • [38] Grishin E.V., Black widow spider toxins: the present and the future, Toxicon 36 (1998) 1693-1701.
    • (1998) Toxicon , vol.36 , pp. 1693-1701
    • Grishin, E.V.1
  • 41
    • 0031814848 scopus 로고    scopus 로고
    • Structures of spider toxins: Hydroxyindole-3-acetylpolyamines and a new generalized structure of type-E compounds obtained from the venom of the Joro spider, Nephila clavata
    • [41] Hisada M., Fujita T., Naoki H., Itagaki Y., Irie H., Miyashita M., Nakajima T., Structures of spider toxins: hydroxyindole-3-acetylpolyamines and a new generalized structure of type-E compounds obtained from the venom of the Joro spider, Nephila clavata, Toxicon 36 (1998) 1115-1125.
    • (1998) Toxicon , vol.36 , pp. 1115-1125
    • Hisada, M.1    Fujita, T.2    Naoki, H.3    Itagaki, Y.4    Irie, H.5    Miyashita, M.6    Nakajima, T.7
  • 49
    • 0028181740 scopus 로고
    • Effects of the venom of the theridiid spider, Steatoda capensis Hann, on autonomie transmission in rat isolated atria and caudal artery
    • [49] Korszniak N.V., Story D.F., Effects of the venom of the theridiid spider, Steatoda capensis Hann, on autonomie transmission in rat isolated atria and caudal artery, Toxicon 32 (1994) 85-96.
    • (1994) Toxicon , vol.32 , pp. 85-96
    • Korszniak, N.V.1    Story, D.F.2
  • 50
    • 0029379657 scopus 로고
    • Characterization and cloning of insecticidal peptides from the primitive weaving spider Diguetia canities
    • [50] Krapcho K.J., Kral R.M., Vanwagenen B.C., Eppler K.G., Morgan T.K., Characterization and cloning of insecticidal peptides from the primitive weaving spider Diguetia canities, Insect Biochem. Mol. Biol. 25 (1995) 991-1000.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 991-1000
    • Krapcho, K.J.1    Kral, R.M.2    Vanwagenen, B.C.3    Eppler, K.G.4    Morgan, T.K.5
  • 52
    • 0028218809 scopus 로고
    • Purification of toxic peptides and the amino acid sequence of CSTX-1 from the multicomponent venom of Cupiennius salei (Araneae:Ctenidae)
    • [52] Kuhn-Nentwig L., Schaller J., Nentwig W., Purification of toxic peptides and the amino acid sequence of CSTX-1 from the multicomponent venom of Cupiennius salei (Araneae:Ctenidae), Toxicon 32 (1994) 287-302.
    • (1994) Toxicon , vol.32 , pp. 287-302
    • Kuhn-Nentwig, L.1    Schaller, J.2    Nentwig, W.3
  • 53
    • 0027186445 scopus 로고
    • Isolation and pharmacological characterization of ω-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses
    • [53] Lampe R.A., Defeo P.A., Davison M.D., Young J., Herman J.L., Spreen R.C., Horn M.B., Mangano T.J., Keith K.A., Isolation and pharmacological characterization of ω-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses, Mol. Pharmacol. 44 (1993) 451-460.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 451-460
    • Lampe, R.A.1    Defeo, P.A.2    Davison, M.D.3    Young, J.4    Herman, J.L.5    Spreen, R.C.6    Horn, M.B.7    Mangano, T.J.8    Keith, K.A.9
  • 54
    • 0032472437 scopus 로고    scopus 로고
    • 2+-independent insulin exocytosis induced by α-latrotoxin requires latrophilin, a G protein-coupled receptor
    • 2+-independent insulin exocytosis induced by α-latrotoxin requires latrophilin, a G protein-coupled receptor, Embo J. 17 (1998) 648-657.
    • (1998) Embo J. , vol.17 , pp. 648-657
    • Lang, J.1    Ushkaryov, Y.2    Grasso, A.3    Wollheim, C.B.4
  • 57
    • 0024848636 scopus 로고
    • Spider toxins selectively block calcium currents in Drosophila
    • [57] Leung H.-T., Branton W.D., Phillips H.S., Jan L., Byerly L., Spider toxins selectively block calcium currents in Drosophila, Neuron 3 (1989) 767-772.
    • (1989) Neuron , vol.3 , pp. 767-772
    • Leung, H.-T.1    Branton, W.D.2    Phillips, H.S.3    Jan, L.4    Byerly, L.5
  • 59
    • 0027218162 scopus 로고
    • Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena
    • [59] Liang S.P., Zhang D.Y., Pan X., Chen Q., Zhou P.A., Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena, Toxicon 31 (1993) 969-978.
    • (1993) Toxicon , vol.31 , pp. 969-978
    • Liang, S.P.1    Zhang, D.Y.2    Pan, X.3    Chen, Q.4    Zhou, P.A.5
  • 60
    • 0031761564 scopus 로고    scopus 로고
    • S-atracotoxins from Australian funnel-web spiders compete with scorpion alpha-toxin binding on both rat brain and insect sodium channels
    • [60] Little M.J., Wilson H., Zappia C., Cestele S., Tyler M.I., Martin-Eauclaire M.F., Gordon D., Nicholson G.M., S-atracotoxins from Australian funnel-web spiders compete with scorpion alpha-toxin binding on both rat brain and insect sodium channels, FEBS Lett. 439 (1998) 246-252.
    • (1998) FEBS Lett. , vol.439 , pp. 246-252
    • Little, M.J.1    Wilson, H.2    Zappia, C.3    Cestele, S.4    Tyler, M.I.5    Martin-Eauclaire, M.F.6    Gordon, D.7    Nicholson, G.M.8
  • 61
    • 0032529698 scopus 로고    scopus 로고
    • α-latrotoxin alters spontaneous and depolarization-evoked quantal release from rat adrenal chromaffin cells: Evidence for multiple modes of action
    • [61] Liu J., Misler S., α-Latrotoxin alters spontaneous and depolarization-evoked quantal release from rat adrenal chromaffin cells: evidence for multiple modes of action, J. Neurosci. 18 (1998) 6113-6125.
    • (1998) J. Neurosci. , vol.18 , pp. 6113-6125
    • Liu, J.1    Misler, S.2
  • 62
    • 0001492765 scopus 로고
    • Blocking and isolation of a calcium channel from neurons in mammals and cephalopods utilizing a toxin fraction (FTX) from funnel-web spider poison
    • [62] Llinas R., Sugimori M., Lin J.W., Cherksey B., Blocking and isolation of a calcium channel from neurons in mammals and cephalopods utilizing a toxin fraction (FTX) from funnel-web spider poison, Proc. Natl. Acad. Sci. USA 86 (1989) 1689-1693.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1689-1693
    • Llinas, R.1    Sugimori, M.2    Lin, J.W.3    Cherksey, B.4
  • 63
    • 0026537012 scopus 로고
    • 2+ channel in rat synaptosomes by venom of the spider Hololena curta
    • 2+ channel in rat synaptosomes by venom of the spider Hololena curta, Eur. J. Pharmacol. 225 (1992) 51-56.
    • (1992) Eur. J. Pharmacol. , vol.225 , pp. 51-56
    • Lundy, P.M.1    Hong, A.2    Frew, R.3
  • 64
    • 0027331516 scopus 로고
    • 2+ channel inhibitors in venom of the spider Plectreurys tristis
    • 2+ channel inhibitors in venom of the spider Plectreurys tristis, Toxicon 31 (1993) 1249-1256.
    • (1993) Toxicon , vol.31 , pp. 1249-1256
    • Lundy, P.M.1    Frew, R.2
  • 65
    • 0031896768 scopus 로고    scopus 로고
    • Structure and function of voltage-gated sodium channels
    • [65] Marban E., Yamagishi T., Tomaselli G.F., Structure and function of voltage-gated sodium channels, J. Physiol. (Lond) 508 (1998) 647-657.
    • (1998) J. Physiol. (Lond) , vol.508 , pp. 647-657
    • Marban, E.1    Yamagishi, T.2    Tomaselli, G.F.3
  • 66
    • 0027137647 scopus 로고
    • Neurotoxic acylpolyamines from spider venoms
    • [66] McCormick K.D., Meinwald J., Neurotoxic acylpolyamines from spider venoms, J. Chem. Ecol. 19 (1993) 2411-2451.
    • (1993) J. Chem. Ecol. , vol.19 , pp. 2411-2451
    • McCormick, K.D.1    Meinwald, J.2
  • 67
    • 0027432527 scopus 로고
    • Characterization and synthesis of a new calcium antagonist from the venom of a fishing spider
    • [67] McCormick L.D., Kobayashi K., Goldin S.M., Reddy N.L., Meinwald J., Characterization and synthesis of a new calcium antagonist from the venom of a fishing spider, Tetrahedron 49 (1993) 11155-11168.
    • (1993) Tetrahedron , vol.49 , pp. 11155-11168
    • McCormick, L.D.1    Kobayashi, K.2    Goldin, S.M.3    Reddy, N.L.4    Meinwald, J.5
  • 68
    • 0030978579 scopus 로고    scopus 로고
    • Alteration of P-type calcium channel gating by the spider toxin ω-Aga-IVA
    • [68] McDonough S.I., Mintz I.M., Bean B.P., Alteration of P-type calcium channel gating by the spider toxin ω-Aga-IVA, Biophys. J. 72 (1997) 2117-2128.
    • (1997) Biophys. J. , vol.72 , pp. 2117-2128
    • McDonough, S.I.1    Mintz, I.M.2    Bean, B.P.3
  • 69
    • 0031467725 scopus 로고    scopus 로고
    • Voltage-dependent inhibition of N- and P-type calcium channels by the peptide toxin ω-grammotoxin-SIA
    • [69] McDonough S.I., Lampe R.A., Keith R.A., Bean B.P., Voltage-dependent inhibition of N- and P-type calcium channels by the peptide toxin ω-grammotoxin-SIA, Mol. Pharmacol. 52 (1997) 1095-1104.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 1095-1104
    • McDonough, S.I.1    Lampe, R.A.2    Keith, R.A.3    Bean, B.P.4
  • 74
    • 0028575955 scopus 로고
    • Diversité moléculaire des canaux calciques : Du gène à la fonction
    • [74] Nargeot J., Charnet P., Diversité moléculaire des canaux calciques : du gène à la fonction, Médecine/sciences 10 (1994) 1293-1308.
    • (1994) Médecine/Sciences , vol.10 , pp. 1293-1308
    • Nargeot, J.1    Charnet, P.2
  • 77
    • 0028111357 scopus 로고
    • Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta
    • [77] Nicholson G.M., Willow M., Howden M.E., Narahashi T., Modification of sodium channel gating and kinetics by versutoxin from the Australian funnel-web spider Hadronyche versuta, Pflugers Arch. 428 (1994) 400-409.
    • (1994) Pflugers Arch. , vol.428 , pp. 400-409
    • Nicholson, G.M.1    Willow, M.2    Howden, M.E.3    Narahashi, T.4
  • 78
    • 0030292981 scopus 로고    scopus 로고
    • Selective alteration of sodium channel gating by Australian funnel-web spider toxins
    • [78] Nicholson G.M., Little M.J., Tyler M., Narahashi T., Selective alteration of sodium channel gating by Australian funnel-web spider toxins, Toxicon 34 (1996) 1443-1453.
    • (1996) Toxicon , vol.34 , pp. 1443-1453
    • Nicholson, G.M.1    Little, M.J.2    Tyler, M.3    Narahashi, T.4
  • 79
    • 0031978687 scopus 로고    scopus 로고
    • Characterisation of the effects of robustoxin, the lethal neurotoxin from the Sydney funnel-web spider Atrax robustus, on sodium channel activation and inactivation
    • [79] Nicholson G.M., Walsh R., Little M.J., Tyler M.I., Characterisation of the effects of robustoxin, the lethal neurotoxin from the Sydney funnel-web spider Atrax robustus, on sodium channel activation and inactivation, Pflugers Arch. 436 (1998) 117-126.
    • (1998) Pflugers Arch. , vol.436 , pp. 117-126
    • Nicholson, G.M.1    Walsh, R.2    Little, M.J.3    Tyler, M.I.4
  • 83
    • 0029986992 scopus 로고    scopus 로고
    • Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities
    • [83] Omecinsky D.O., Holub K.E., Adams M.E., Reily M.D., Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities, Biochemistry 35 (1996) 2836-2844.
    • (1996) Biochemistry , vol.35 , pp. 2836-2844
    • Omecinsky, D.O.1    Holub, K.E.2    Adams, M.E.3    Reily, M.D.4
  • 84
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • [84] Pallaghy P.K., Nielsen K.J., Craik D.J., Norton R.S., A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides, Protein Sci. 3 (1994) 1833-1839.
    • (1994) Protein Sci. , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 85
    • 0031451746 scopus 로고    scopus 로고
    • Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus
    • [85] Pallaghy P.K., Alewood D., Alewood P.F., Norton R.S., Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus, FEBS Lett. 419 (1997) 191-196.
    • (1997) FEBS Lett. , vol.419 , pp. 191-196
    • Pallaghy, P.K.1    Alewood, D.2    Alewood, P.F.3    Norton, R.S.4
  • 88
    • 0026807658 scopus 로고
    • ω-agatoxins differentially block calcium channels in locust, chick and rat synaptosomes
    • [88] Pocock J.M., Venema V.J., Adams M.E., ω-agatoxins differentially block calcium channels in locust, chick and rat synaptosomes, Neurochem. Int. 20 (1992) 263-70.
    • (1992) Neurochem. Int. , vol.20 , pp. 263-270
    • Pocock, J.M.1    Venema, V.J.2    Adams, M.E.3
  • 89
    • 0026486232 scopus 로고
    • Molecular biology of voltage-dependent potassium channels
    • [89] Pongs O., Molecular biology of voltage-dependent potassium channels, Physiol. Rev. 72 (1992) S69-88.
    • (1992) Physiol. Rev. , vol.72
    • Pongs, O.1
  • 90
    • 0028847391 scopus 로고
    • Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena.1. Sequence-specific H1-NMR assignments
    • [90] Qu Y.X., Liang S.P., Ding J.Z., Ma L.B., Zhang R.J., Gu X.C., Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena.1. Sequence-specific H1-NMR assignments, J. Prot. Chem. 14 (1995) 549-557.
    • (1995) J. Prot. Chem. , vol.14 , pp. 549-557
    • Qu, Y.X.1    Liang, S.P.2    Ding, J.Z.3    Ma, L.B.4    Zhang, R.J.5    Gu, X.C.6
  • 91
    • 0030791931 scopus 로고    scopus 로고
    • Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena.2. Three-dimensional structure in solution
    • [91] Qu Y.X., Liang S.P., Ding J.Z., Liu X.C., Zhang R.J., Gu X.C., Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena.2. Three-dimensional structure in solution, J. Prot. Chem. 16 (1997) 565-574.
    • (1997) J. Prot. Chem. , vol.16 , pp. 565-574
    • Qu, Y.X.1    Liang, S.P.2    Ding, J.Z.3    Liu, X.C.4    Zhang, R.J.5    Gu, X.C.6
  • 94
    • 0028365066 scopus 로고
    • Isolation and sequencing of insecticidal peptides from the primitive hunting spider, Plectreurys tristis (Simon)
    • [94] Quistad G.B., Skinner W.S., Isolation and sequencing of insecticidal peptides from the primitive hunting spider, Plectreurys tristis (Simon), J. Biol. Chem. 269 (1994) 11098-11101.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11098-11101
    • Quistad, G.B.1    Skinner, W.S.2
  • 96
    • 0028725229 scopus 로고
    • Structure-activity relationships for P-type calcium channel-selective ω-agatoxins
    • [96] Reily M.D., Holub K.E., Gray W.R., Norris T.M., Adams M.E., Structure-activity relationships for P-type calcium channel-selective ω-agatoxins, Struct. Biol. 1 (1994) 853-856.
    • (1994) Struct. Biol. , vol.1 , pp. 853-856
    • Reily, M.D.1    Holub, K.E.2    Gray, W.R.3    Norris, T.M.4    Adams, M.E.5
  • 97
    • 0026049291 scopus 로고
    • Isolation of neurotoxic peptides from the venom of the armed spider Phoneutria nigriventer
    • [97] Rezende Jr. L., Cordeiro M.N., Oliveira E.B., Diniz C.R., Isolation of neurotoxic peptides from the venom of the armed spider Phoneutria nigriventer, Toxicon 29 (1991) 1225-1233.
    • (1991) Toxicon , vol.29 , pp. 1225-1233
    • Rezende L., Jr.1    Cordeiro, M.N.2    Oliveira, E.B.3    Diniz, C.R.4
  • 98
    • 0030760007 scopus 로고    scopus 로고
    • Structure and function of cardiac sodium and potassium channels
    • [98] Roden D.M., George A.L. Jr., Structure and function of cardiac sodium and potassium channels, Am. J. Physiol. 273 (1997) H511-525.
    • (1997) Am. J. Physiol. , vol.273
    • Roden, D.M.1    George A.L., Jr.2
  • 99
    • 0002896228 scopus 로고
    • Families of potassium channel genes in mammals: Toward an understanding of the molecular basis of potassium channel diversity
    • [99] Rudy B., Kentros C., Vega-Saenz De Miera E., Families of potassium channel genes in mammals: toward an understanding of the molecular basis of potassium channel diversity, Mol. Cell. Neurosci. 2 (1991) 89-102.
    • (1991) Mol. Cell. Neurosci. , vol.2 , pp. 89-102
    • Rudy, B.1    Kentros, C.2    Vega-Saenz De Miera, E.3
  • 103
    • 0024312745 scopus 로고
    • Biochemical analysis of tarantula venom (Eurypelma californicum)
    • [103] Savel-Niemann A., Roth D., Biochemical analysis of tarantula venom (Eurypelma californicum), Naturwissenschaften 76 (1989) 212-213.
    • (1989) Naturwissenschaften , vol.76 , pp. 212-213
    • Savel-Niemann, A.1    Roth, D.2
  • 104
    • 0024318644 scopus 로고
    • Tarantula (Eurypelma californicum) venom, a multicomponent system
    • [104] Savel-Niemann A., Tarantula (Eurypelma californicum) venom, a multicomponent system, Biol. Chem. Hoppe-Seyler 370 (1989) 485-498.
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 485-498
    • Savel-Niemann, A.1
  • 105
    • 0015924150 scopus 로고
    • Purification and characterization of tarantula, Dugesiella hentzi (Girard) venom hyaluronidase
    • [105] Schanbacher F.L., Lee C.K., Wilson I.B., Howell D.E., Odell G.V., Purification and characterization of tarantula, Dugesiella hentzi (Girard) venom hyaluronidase, Comp. Biochem. Physiol. 44B (1973) 389-396.
    • (1973) Comp. Biochem. Physiol. , vol.44 B , pp. 389-396
    • Schanbacher, F.L.1    Lee, C.K.2    Wilson, I.B.3    Howell, D.E.4    Odell, G.V.5
  • 109
    • 0021987031 scopus 로고
    • Complete amino acid sequence of a new type of lethal neurotoxin from the venom of the funnel-web spider Atrax robustus
    • [109] Sheumack D.D., Claassens R., Whiteley N.M., Howden M.E., Complete amino acid sequence of a new type of lethal neurotoxin from the venom of the funnel-web spider Atrax robustus, FEBS Lett. 181 (1985) 154-156.
    • (1985) FEBS Lett. , vol.181 , pp. 154-156
    • Sheumack, D.D.1    Claassens, R.2    Whiteley, N.M.3    Howden, M.E.4
  • 111
    • 0024500164 scopus 로고
    • Purification and characterization of two classes of neurotoxins from the runnel web spider, Agelenopsis aperta
    • [111] Skinner W.S., Adams M.E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A., Purification and characterization of two classes of neurotoxins from the runnel web spider, Agelenopsis aperta, J. Biol. Chem. 264 (1989) 2150-2155.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2150-2155
    • Skinner, W.S.1    Adams, M.E.2    Quistad, G.B.3    Kataoka, H.4    Cesarin, B.J.5    Enderlin, F.E.6    Schooley, D.A.7
  • 112
    • 0025329966 scopus 로고
    • Chemical characterization of acylpolyamine toxins from venom of a trap-door spider and two tarantulas
    • [112] Skinner W.S., Dennis P.A., Lui A., Carney R.L., Quistad G.B., Chemical characterization of acylpolyamine toxins from venom of a trap-door spider and two tarantulas, Toxicon 28 (1990) 541-546.
    • (1990) Toxicon , vol.28 , pp. 541-546
    • Skinner, W.S.1    Dennis, P.A.2    Lui, A.3    Carney, R.L.4    Quistad, G.B.5
  • 113
    • 0026630034 scopus 로고
    • Identification of insecticidal peptides from venom of the trap-door spider, Aptostichus schlingeri (Ctenizidae)
    • [113] Skinner W.S., Dennis P.A., Li J.B., Quistad B., Identification of insecticidal peptides from venom of the trap-door spider, Aptostichus schlingeri (Ctenizidae). Toxicon 30 (1992) 1043-1050.
    • (1992) Toxicon , vol.30 , pp. 1043-1050
    • Skinner, W.S.1    Dennis, P.A.2    Li, J.B.3    Quistad, B.4
  • 114
    • 0018666758 scopus 로고
    • Comparison of phospholipase activity with direct and indirect lytic effects of animal venoms upon human red cells
    • [114] Sosa B.P., Alagon A.C., Possani L.D., Julia J.Z., Comparison of phospholipase activity with direct and indirect lytic effects of animal venoms upon human red cells, Comp. Biochem. Physiol. B 64 (1979) 231-234.
    • (1979) Comp. Biochem. Physiol. B , vol.64 , pp. 231-234
    • Sosa, B.P.1    Alagon, A.C.2    Possani, L.D.3    Julia, J.Z.4
  • 118
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • [118] Swartz K.J., MacKinnon R., An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula, Neuron 15 (1995) 941-9.
    • (1995) Neuron , vol.15 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 120
    • 0030952979 scopus 로고    scopus 로고
    • + channel through multiple binding sites
    • + channel through multiple binding sites, Neuron 18 (1997) 665-673.
    • (1997) Neuron , vol.18 , pp. 665-673
    • Swartz, K.J.1    MacKinnon, R.2
  • 122
    • 0024205469 scopus 로고
    • Isolation and chemical characterization of a series of new spider toxin (Nephilatoxins) in the venom of Joro spider, Nephila clavata
    • [122] Toki T., Yasuhara T., Aramaki Y., Osawa K., Miwa A., Kawai N., Nakajima T., Isolation and chemical characterization of a series of new spider toxin (Nephilatoxins) in the venom of Joro spider, Nephila clavata, Biomed. Res. 9 (1988) 421-428.
    • (1988) Biomed. Res. , vol.9 , pp. 421-428
    • Toki, T.1    Yasuhara, T.2    Aramaki, Y.3    Osawa, K.4    Miwa, A.5    Kawai, N.6    Nakajima, T.7
  • 125
    • 0026802393 scopus 로고
    • Antagonism of synaptosomal calcium channels by subtypes of ω-agatoxins
    • [125] Venema V.J., Swiderek K.M., Lee T.D., Hathaway G.M., Adams M.E., Antagonism of synaptosomal calcium channels by subtypes of ω-agatoxins, J. Biol. Chem. 267 (1992) 2610-2615.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2610-2615
    • Venema, V.J.1    Swiderek, K.M.2    Lee, T.D.3    Hathaway, G.M.4    Adams, M.E.5
  • 126
    • 0022930566 scopus 로고
    • Single-channel studies of TTX-sensitive and TTX-resistant sodium channels in developing rat muscle reveal different open channel properties
    • [126] Weiss R.E., Horn R., Single-channel studies of TTX-sensitive and TTX-resistant sodium channels in developing rat muscle reveal different open channel properties, Ann. N.-Y. Acad. Sci. 479 (1986) 152-161.
    • (1986) Ann. N.-Y. Acad. Sci. , vol.479 , pp. 152-161
    • Weiss, R.E.1    Horn, R.2
  • 127
    • 0000655480 scopus 로고
    • 5-Hydroxytryptamine content of some arthropod venoms and venom-containing parts
    • [127] Welsh J.H., Batty C.S., 5-hydroxytryptamine content of some arthropod venoms and venom-containing parts, Toxicon 1 (1963) 165-173.
    • (1963) Toxicon , vol.1 , pp. 165-173
    • Welsh, J.H.1    Batty, C.S.2
  • 129
    • 0031015813 scopus 로고    scopus 로고
    • Blockade of neuromuscular transmission by huwentoxin-I, purified from the venom of the Chinese bird spider Selenocosmia huwena
    • [129] Zhou P.A., Xie X.J., Li M., Yang D.M., Xie Z.P., Zong X., Liang S.P., Blockade of neuromuscular transmission by huwentoxin-I, purified from the venom of the Chinese bird spider Selenocosmia huwena, Toxicon 35 (1997) 39-45.
    • (1997) Toxicon , vol.35 , pp. 39-45
    • Zhou, P.A.1    Xie, X.J.2    Li, M.3    Yang, D.M.4    Xie, Z.P.5    Zong, X.6    Liang, S.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.