메뉴 건너뛰기




Volumn 43, Issue 5, 2004, Pages 555-574

Tarantulas: Eight-legged pharmacists and combinatorial chemists

Author keywords

Inhibitory cystine knot; Ion channels; Peptide toxins; Tarantula; Theraphosid; Three dimensional structure; Venom

Indexed keywords

ION CHANNEL; SPIDER VENOM;

EID: 1942438962     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2004.02.007     Document Type: Article
Times cited : (183)

References (88)
  • 1
    • 0020313808 scopus 로고
    • Isolation and partial characterization of a toxin from the venom of the East African orthognath spider Pterinochilus spec
    • Bachmann M. Isolation and partial characterization of a toxin from the venom of the East African orthognath spider Pterinochilus spec. Toxicon. 20:1982;547-552.
    • (1982) Toxicon , vol.20 , pp. 547-552
    • Bachmann, M.1
  • 2
    • 0034595899 scopus 로고    scopus 로고
    • Purification, structure determination and synthesis of covalitoxin-II, a short insect-specific neurotoxic peptide from the venom of the Coremiocnemis validus (Singapore tarantula)
    • Balaji R.A., Sasaki T., Gopalakrishnakone P., Sato K., Kini R.M., Bay B.H. Purification, structure determination and synthesis of covalitoxin-II, a short insect-specific neurotoxic peptide from the venom of the Coremiocnemis validus (Singapore tarantula). FEBS Lett. 474:2000;208-212.
    • (2000) FEBS Lett. , vol.474 , pp. 208-212
    • Balaji, R.A.1    Sasaki, T.2    Gopalakrishnakone, P.3    Sato, K.4    Kini, R.M.5    Bay, B.H.6
  • 3
    • 0035804258 scopus 로고    scopus 로고
    • Tarantula peptide inhibits atrial fibrillation
    • Bode F., Sachs F., Franz M.R. Tarantula peptide inhibits atrial fibrillation. Nature. 409:2001;35-36.
    • (2001) Nature , vol.409 , pp. 35-36
    • Bode, F.1    Sachs, F.2    Franz, M.R.3
  • 4
    • 0000450032 scopus 로고
    • Spiders
    • W. Bücherl, Buckley E.E. New York: Academic Press
    • Bücherl W. Spiders. Bücherl W., Buckley E.E. Venomous Animals and their Venoms. vol. III:1971;197-277 Academic Press, New York.
    • (1971) Venomous Animals and Their Venoms , vol.3 , pp. 197-277
    • Bücherl, W.1
  • 6
    • 0016437336 scopus 로고
    • Adenosine triphosphate in tarantula spider venoms and its synergistic effect with the venom toxin
    • 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
  • 8
    • 0033833498 scopus 로고    scopus 로고
    • Isolation, synthesis and pharmacological characterization of δ-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae)
    • Corzo G., Escoubas P., Stankiewicz M., Pelhate M., Kristensen C.P., Nakajima T. Isolation, synthesis and pharmacological characterization of δ-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae). Eur. J. Biochem. 267:2000;5783-5795.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5783-5795
    • Corzo, G.1    Escoubas, P.2    Stankiewicz, M.3    Pelhate, M.4    Kristensen, C.P.5    Nakajima, T.6
  • 9
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik D.J., Daly N.L., Waine C. The cystine knot motif in toxins and implications for drug design. Toxicon. 39:2001;43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 10
    • 0031608326 scopus 로고    scopus 로고
    • The dangers of pet tarantulas: Experience of the Marseilles Poison Centre
    • De Haro L., Jouglard J. The dangers of pet tarantulas: experience of the Marseilles Poison Centre. J. Toxicol. Clin. Toxicol. 36:1998;51-53.
    • (1998) J. Toxicol. Clin. Toxicol. , vol.36 , pp. 51-53
    • De Haro, L.1    Jouglard, J.2
  • 11
    • 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
    • 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
  • 12
    • 0036009367 scopus 로고    scopus 로고
    • Determination of species-specific components in the venom of Parabuthus scorpions from southern Africa using matrix-assisted laser desorption time-of-flight mass spectrometry
    • Dyason K., Brandt W., Prendini L., Verdonck F., Tytgat J., du Plessis J., Muller G., van der Walt J. Determination of species-specific components in the venom of Parabuthus scorpions from southern Africa using matrix-assisted laser desorption time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 16:2002;768-773.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 768-773
    • Dyason, K.1    Brandt, W.2    Prendini, L.3    Verdonck, F.4    Tytgat, J.5    Du Plessis, J.6    Muller, G.7    Van Der Walt, J.8
  • 13
    • 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
    • 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
  • 14
    • 0000477401 scopus 로고    scopus 로고
    • Two novel peptide neurotoxins from the venom of the tarantula Lasiodora parahybana
    • Escoubas P., Célérier M.L., Romi-Lebrun R., Nakajima T. Two novel peptide neurotoxins from the venom of the tarantula Lasiodora parahybana. Toxicon. 35:1997;805-806.
    • (1997) Toxicon , vol.35 , pp. 805-806
    • Escoubas, P.1    Célérier, M.L.2    Romi-Lebrun, R.3    Nakajima, T.4
  • 15
    • 0031825289 scopus 로고    scopus 로고
    • Multidimensional peptide fingerprinting by high performance liquid chromatography, capillary zone electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for the identification of tarantula venom samples
    • Escoubas P., Whiteley B.J., Kristensen C.P., Célérier M., Corzo G., Nakajima T. Multidimensional peptide fingerprinting by high performance liquid chromatography, capillary zone electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for the identification of tarantula venom samples. Rapid Commun. Mass Spectrom. 12:1998;1075-1084.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 1075-1084
    • Escoubas, P.1    Whiteley, B.J.2    Kristensen, C.P.3    Célérier, M.4    Corzo, G.5    Nakajima, T.6
  • 16
    • 0032834458 scopus 로고    scopus 로고
    • A comparison of matrix-assisted laser desorption/ionization time-of-flight and liquid chromatography electrospray ionization mass spectrometry methods for the analysis of crude tarantula venoms in the Pterinochilus group
    • Escoubas P., Chamot-Rooke J., Stöcklin R., Whiteley B.J., Corzo G., Genet R., Nakajima T. A comparison of matrix-assisted laser desorption/ ionization time-of-flight and liquid chromatography electrospray ionization mass spectrometry methods for the analysis of crude tarantula venoms in the Pterinochilus group. Rapid Commun. Mass Spectrom. 13:1999;1861-1868.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 1861-1868
    • Escoubas, P.1    Chamot-Rooke, J.2    Stöcklin, R.3    Whiteley, B.J.4    Corzo, G.5    Genet, R.6    Nakajima, T.7
  • 18
    • 0033731951 scopus 로고    scopus 로고
    • Structure and pharmacology of spider venom neurotoxins
    • Escoubas P., Diochot S., Corzo G. Structure and pharmacology of spider venom neurotoxins. Biochimie. 82:2000;893-907.
    • (2000) Biochimie , vol.82 , pp. 893-907
    • Escoubas, P.1    Diochot, S.2    Corzo, G.3
  • 19
    • 0036008567 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and high-performance liquid chromatography study of quantitative and qualitative variation in tarantula spider venoms
    • Escoubas P., Corzo G., Whiteley B.J., Célérier M.L., Nakajima T. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and high-performance liquid chromatography study of quantitative and qualitative variation in tarantula spider venoms. Rapid Commun. Mass Spectrom. 16:2002;403-413.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 403-413
    • Escoubas, P.1    Corzo, G.2    Whiteley, B.J.3    Célérier, M.L.4    Nakajima, T.5
  • 20
    • 0036088553 scopus 로고    scopus 로고
    • Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies
    • Escoubas P., Diochot S., Célérier M.L., Nakajima T., Lazdunski M. Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies. Mol. Pharmacol. 62:2002;48-57.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 48-57
    • Escoubas, P.1    Diochot, S.2    Célérier, M.L.3    Nakajima, T.4    Lazdunski, M.5
  • 21
    • 0037634059 scopus 로고    scopus 로고
    • Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated channels
    • Escoubas P., Bernard C., Lambeau G., Lazdunski M., Darbon H. Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated channels. Protein Sci. 12:2003;1332-1343.
    • (2003) Protein Sci. , vol.12 , pp. 1332-1343
    • Escoubas, P.1    Bernard, C.2    Lambeau, G.3    Lazdunski, M.4    Darbon, H.5
  • 22
    • 0015457811 scopus 로고
    • Poisonous and venomous animals in East Africa
    • Freyvogel T. Poisonous and venomous animals in East Africa. Acta Trop. 29:1972;401-451.
    • (1972) Acta Trop. , vol.29 , pp. 401-451
    • Freyvogel, T.1
  • 23
    • 0037376716 scopus 로고    scopus 로고
    • Bites by spiders of the family Theraphosidae in humans and canines
    • Isbister G.K., Seymour J.E., Gray M.R., Raven R.J. Bites by spiders of the family Theraphosidae in humans and canines. Toxicon. 41:2003;519-524.
    • (2003) Toxicon , vol.41 , pp. 519-524
    • Isbister, G.K.1    Seymour, J.E.2    Gray, M.R.3    Raven, R.J.4
  • 26
    • 0028850614 scopus 로고
    • Comparative actions of synthetic omega-grammotoxin SIA and synthetic omega-Aga-IVA on neuronal calcium entry and evoked release of neurotransmitters in vitro and in vivo
    • Keith R.A., Mangano T.J., Lampe R.A., DeFeo P.A., Hyde M.J., Donzanti B.A. Comparative actions of synthetic omega-grammotoxin SIA and synthetic omega-Aga-IVA on neuronal calcium entry and evoked release of neurotransmitters in vitro and in vivo. Neuropharmacology. 34:1995;1515-1528.
    • (1995) Neuropharmacology , vol.34 , pp. 1515-1528
    • Keith, R.A.1    Mangano, T.J.2    Lampe, R.A.3    Defeo, P.A.4    Hyde, M.J.5    Donzanti, B.A.6
  • 27
    • 0036447597 scopus 로고    scopus 로고
    • Structure and function of insecticidal neurotoxins from Australian funnel-web spiders
    • King G.F., Tedford H.W., Maggio F. Structure and function of insecticidal neurotoxins from Australian funnel-web spiders. J. Toxicol. Toxin Rev. 21:2002;359-389.
    • (2002) J. Toxicol. Toxin Rev. , vol.21 , pp. 359-389
    • King, G.F.1    Tedford, H.W.2    Maggio, F.3
  • 28
    • 1942430449 scopus 로고    scopus 로고
    • Analgesic peptides from venom of Grammostola spatulata and use thereof. US Patent 5,877,026.
    • Lampe, R.A., 1999. Analgesic peptides from venom of Grammostola spatulata and use thereof. US Patent 5,877,026.
    • (1999)
    • Lampe, R.A.1
  • 29
    • 0027186445 scopus 로고
    • Isolation and pharmacological characterization of omega-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses
    • Lampe R.A., Defeo P.A., Davison M.D., Young J., Herman J.L., Spreen R.C., Horn M.B., Mangano T.J., Keith R.A. Isolation and pharmacological characterization of omega-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, R.A.9
  • 30
    • 1942526669 scopus 로고    scopus 로고
    • Antiarrhytmic peptide from venom of spider. Grammostola spatulata. US Patent 5,968,838.
    • Lampe, R.A., Sachs, F., 1999. Antiarrhytmic peptide from venom of spider. Grammostola spatulata. US Patent 5,968,838.
    • (1999)
    • Lampe, R.A.1    Sachs, F.2
  • 31
    • 0029010047 scopus 로고
    • A lectin-like peptide isolated from the venom of the Chinese bird spider Selenocosmia huwena
    • Liang S.P., Pan X. A lectin-like peptide isolated from the venom of the Chinese bird spider Selenocosmia huwena. Toxicon. 33:1995;875-882.
    • (1995) Toxicon , vol.33 , pp. 875-882
    • Liang, S.P.1    Pan, X.2
  • 32
    • 0027218162 scopus 로고
    • Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena
    • 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
  • 33
    • 0033838709 scopus 로고    scopus 로고
    • Identification of venom proteins of spider S. huwena on two-dimensional electrophoresis gel by N-terminal microsequencing and mass spectrometric peptide mapping
    • Liang S., Li X., Cao M., Xie J., Chen P., Huang R. Identification of venom proteins of spider S. huwena on two-dimensional electrophoresis gel by N-terminal microsequencing and mass spectrometric peptide mapping. J. Protein Chem. 19:2000;225-229.
    • (2000) J. Protein Chem. , vol.19 , pp. 225-229
    • Liang, S.1    Li, X.2    Cao, M.3    Xie, J.4    Chen, P.5    Huang, R.6
  • 36
    • 0038010666 scopus 로고    scopus 로고
    • Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana
    • Liu Z., Dai J., Chen Z., Hu W., Xiao Y., Liang S. Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin- sensitive sodium channels from the Chinese bird spider Selenocosmia hainana. Cell. Mol. Life Sci. 60:2003;972-978.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 972-978
    • Liu, Z.1    Dai, J.2    Chen, Z.3    Hu, W.4    Xiao, Y.5    Liang, S.6
  • 38
    • 0032863018 scopus 로고    scopus 로고
    • Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR
    • Lu S., Liang S., Gu X. Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR. J. Protein Chem. 18:1999;609-617.
    • (1999) J. Protein Chem. , vol.18 , pp. 609-617
    • Lu, S.1    Liang, S.2    Gu, X.3
  • 39
    • 0028065345 scopus 로고
    • Mygalomorph spider bites: A report on 91 cases in the state of Sao Paulo, Brazil
    • Lucas S.M., Da Silva P.I. Jr, Bertani R., Cardoso J.L. Mygalomorph spider bites: a report on 91 cases in the state of Sao Paulo, Brazil. Toxicon. 32:1994;1211-1215.
    • (1994) Toxicon , vol.32 , pp. 1211-1215
    • Lucas, S.M.1    Da Silva Jr., P.I.2    Bertani, R.3    Cardoso, J.L.4
  • 40
    • 0033570060 scopus 로고    scopus 로고
    • Isolation, amino acid sequence and functional assays of SGTx1. the first toxin purified from the venom of the spider Scodra griseipes
    • Marvin L., De E., Cosette P., Gagnon J., Molle G., Lange C. Isolation, amino acid sequence and functional assays of SGTx1. The first toxin purified from the venom of the spider Scodra griseipes. Eur. J. Biochem. 265:1999;572-579.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 572-579
    • Marvin, L.1    De, E.2    Cosette, P.3    Gagnon, J.4    Molle, G.5    Lange, C.6
  • 41
    • 0031467725 scopus 로고    scopus 로고
    • Voltage-dependent inhibition of N- and P-type calcium channels by the peptide toxin omega-grammotoxin-SIA
    • 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 omega-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
  • 42
    • 0036229869 scopus 로고    scopus 로고
    • Interactions among toxins that inhibit N- and P-type calcium channels
    • McDonough S.I., Boland L.M., Mintz I.M., Bean B.P. Interactions among toxins that inhibit N- and P-type calcium channels. J. Gen. Physiol. 119:2002;313-328.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 313-328
    • McDonough, S.I.1    Boland, L.M.2    Mintz, I.M.3    Bean, B.P.4
  • 45
    • 0036378336 scopus 로고    scopus 로고
    • Spiders of medical importance in the Asia-Pacific: Atracotoxin, latrotoxin and related spider neurotoxins
    • Nicholson G.M., Graudins A. Spiders of medical importance in the Asia-Pacific: atracotoxin, latrotoxin and related spider neurotoxins. Clin. Exp. Pharmacol. Physiol. 29:2002;785-794.
    • (2002) Clin. Exp. Pharmacol. Physiol. , vol.29 , pp. 785-794
    • Nicholson, G.M.1    Graudins, A.2
  • 46
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton R.S., Pallaghy P.K. The cystine knot structure of ion channel toxins and related polypeptides. Toxicon. 36:1998;1573-1583.
    • (1998) Toxicon , vol.36 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 49
    • 1942430450 scopus 로고
    • Tarantula venom components: Brachypelma smithii, Brachypelma emilia, Dugesiella hentzi and Aphonopelma seemanni
    • Odell G.V., Hudiburg S.A., Herrero M., Cabbiness S.G., Chan T.K., Aird S.D., Kaiser I. Tarantula venom components: Brachypelma smithii, Brachypelma emilia, Dugesiella hentzi and Aphonopelma seemanni. Toxicon. 27:1989;67.
    • (1989) Toxicon , vol.27 , pp. 67
    • Odell, G.V.1    Hudiburg, S.A.2    Herrero, M.3    Cabbiness, S.G.4    Chan, T.K.5    Aird, S.D.6    Kaiser, I.7
  • 50
    • 0035239229 scopus 로고    scopus 로고
    • Conotoxins, in retrospect
    • Olivera B.M., Cruz L.J. Conotoxins, in retrospect. Toxicon. 39:2001;7-14.
    • (2001) Toxicon , vol.39 , pp. 7-14
    • Olivera, B.M.1    Cruz, L.J.2
  • 51
    • 0028292145 scopus 로고
    • Calcium channel diversity and neurotransmitter release: The ω-conotoxins and ω-agatoxins
    • Olivera B.M., Miljanich G.P., Ramachandran J., Adams M.E. Calcium channel diversity and neurotransmitter release: the ω-conotoxins and ω-agatoxins. Annu. Rev. Biochem. 63:1994;823-867.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 823-867
    • Olivera, B.M.1    Miljanich, G.P.2    Ramachandran, J.3    Adams, M.E.4
  • 52
    • 0037072815 scopus 로고    scopus 로고
    • Solution structure of peptide toxins that block mechanosensitive ion channels
    • Oswald R.E., Suchyna T.M., McFeeters R., Gottlieb P., Sachs F. Solution structure of peptide toxins that block mechanosensitive ion channels. J. Biol. Chem. 277:2002;34443-34450.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34443-34450
    • Oswald, R.E.1    Suchyna, T.M.2    McFeeters, R.3    Gottlieb, P.4    Sachs, F.5
  • 53
    • 0142042688 scopus 로고    scopus 로고
    • 2+ channels in differentiated NG108-15 cells, a patch-clamp study
    • 2+ channels in differentiated NG108-15 cells, a patch-clamp study. Toxicon. 39:2001;491-498.
    • (2001) Toxicon , vol.39 , pp. 491-498
    • Peng, K.1    Chen, X.D.2    Liang, S.P.3
  • 54
    • 0037033085 scopus 로고    scopus 로고
    • Function and solution structure of Huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena
    • Peng K., Shu Q., Liu Z., Liang S. Function and solution structure of Huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena. J. Biol. Chem. 277:2002;47564-47571.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47564-47571
    • Peng, K.1    Shu, Q.2    Liu, Z.3    Liang, S.4
  • 55
    • 0016135244 scopus 로고
    • The venom of the East African spider Pterinochilus sp
    • Perret B.A. The venom of the East African spider Pterinochilus sp. Toxicon. 12:1974;303-310.
    • (1974) Toxicon , vol.12 , pp. 303-310
    • Perret, B.A.1
  • 56
    • 0034856719 scopus 로고    scopus 로고
    • Moving pieces in a proteomic puzzle: Mass fingerprinting of toxic fractions from the venom of Tityus serrulatus (Scorpiones, Buthidae)
    • Pimenta A.M., Stöcklin R., Favreau P., Bougis P.E., Martin-Eauclaire M.F. Moving pieces in a proteomic puzzle: mass fingerprinting of toxic fractions from the venom of Tityus serrulatus (Scorpiones, Buthidae). Rapid Commun. Mass Spectrom. 15:2001;1562-1572.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1562-1572
    • Pimenta, A.M.1    Stöcklin, R.2    Favreau, P.3    Bougis, P.E.4    Martin-Eauclaire, M.F.5
  • 59
    • 0028820767 scopus 로고
    • Complete and reversible block by omega-grammotoxin SIA of glutamatergic synaptic transmission between cultured rat hippocampal neurons
    • Piser T.M., Lampe R.A., Keith R.A., Thayer S.A. Complete and reversible block by omega-grammotoxin SIA of glutamatergic synaptic transmission between cultured rat hippocampal neurons. Neurosci. Lett. 201:1995;135-138.
    • (1995) Neurosci. Lett. , vol.201 , pp. 135-138
    • Piser, T.M.1    Lampe, R.A.2    Keith, R.A.3    Thayer, S.A.4
  • 60
    • 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
    • Qu Y., Liang S., Ding J., Liu X., Zhang R., Gu X. Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena: 2. Three-dimensional structure in solution. J. Protein Chem. 16:1997;565-574.
    • (1997) J. Protein Chem. , vol.16 , pp. 565-574
    • Qu, Y.1    Liang, S.2    Ding, J.3    Liu, X.4    Zhang, R.5    Gu, X.6
  • 61
    • 0034768977 scopus 로고    scopus 로고
    • Pharmacology and biochemistry of spider venoms
    • Rash L.D., Hodgson W.C. Pharmacology and biochemistry of spider venoms. Toxicon. 40:2002;225-254.
    • (2002) Toxicon , vol.40 , pp. 225-254
    • Rash, L.D.1    Hodgson, W.C.2
  • 62
    • 0003015096 scopus 로고
    • The spider infraorder Mygalomorphae (Araneae)
    • Raven R. The spider infraorder Mygalomorphae (Araneae). Bull. Am. Mus. Nat. Hist. 182:1985;1-180.
    • (1985) Bull. Am. Mus. Nat. Hist. , vol.182 , pp. 1-180
    • Raven, R.1
  • 64
    • 0024318644 scopus 로고
    • Tarantula (Eurypelma californicum) venom, a multicomponent system
    • 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
  • 65
    • 0024312745 scopus 로고
    • Biochemical analysis of tarantula venom (Eurypelma californicum)
    • 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
  • 66
  • 68
    • 0024360827 scopus 로고
    • Efficacy of bites from Asiatic and African tarantulas
    • Schmidt G. Efficacy of bites from Asiatic and African tarantulas. Trop. Med. Parasitol. 40:1989;114.
    • (1989) Trop. Med. Parasitol. , vol.40 , pp. 114
    • Schmidt, G.1
  • 69
    • 0036979653 scopus 로고    scopus 로고
    • Molecular simulation reveals structural determinants of the hanatoxin binding in Kv2.1 channels
    • Shiau Y.S., Lin T.B., Liou H.H., Huang P.T., Lou K.L., Shiau Y.Y. Molecular simulation reveals structural determinants of the hanatoxin binding in Kv2.1 channels. J. Mol. Model. (Online). 8:2002;253-257.
    • (2002) J. Mol. Model. (Online) , vol.8 , pp. 253-257
    • Shiau, Y.S.1    Lin, T.B.2    Liou, H.H.3    Huang, P.T.4    Lou, K.L.5    Shiau, Y.Y.6
  • 70
    • 0033040926 scopus 로고    scopus 로고
    • Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena
    • Shu Q., Liang S.P. Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena. J. Pept. Res. 53:1999;486-491.
    • (1999) J. Pept. Res. , vol.53 , pp. 486-491
    • Shu, Q.1    Liang, S.P.2
  • 71
    • 0035022764 scopus 로고    scopus 로고
    • Assignment of the disulfide bonds of huwentoxin-II by Edman degradation sequencing and stepwise thiol modification
    • Shu Q., Huang R., Liang S. Assignment of the disulfide bonds of huwentoxin-II by Edman degradation sequencing and stepwise thiol modification. Eur. J. Biochem. 268:2001;2301-2307.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2301-2307
    • Shu, Q.1    Huang, R.2    Liang, S.3
  • 72
    • 0036147845 scopus 로고    scopus 로고
    • The structure of spider toxin huwentoxin-II with unique disulfide linkage: Evidence for structural evolution
    • Shu Q., Lu S.Y., Gu X.C., Liang S.P. The structure of spider toxin huwentoxin-II with unique disulfide linkage: evidence for structural evolution. Protein Sci. 11:2002;245-252.
    • (2002) Protein Sci. , vol.11 , pp. 245-252
    • Shu, Q.1    Lu, S.Y.2    Gu, X.C.3    Liang, S.P.4
  • 74
    • 0000002594 scopus 로고
    • On-line LC-ES-MS: A new method for direct analysis of crude venom
    • Stöcklin R., Savoy L.-A. On-line LC-ES-MS: a new method for direct analysis of crude venom. Toxicon. 32:1994;408.
    • (1994) Toxicon , vol.32 , pp. 408
    • Stöcklin, R.1    Savoy, L.-A.2
  • 75
    • 0034103610 scopus 로고    scopus 로고
    • Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels
    • Suchyna T.M., Johnson J.H., Hamer K., Leykam J.F., Gage D.A., Clemo H.F., Baumgarten C.M., Sachs F. Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels. J. Gen. Physiol. 115:2000;583-598.
    • (2000) J. Gen. Physiol. , vol.115 , pp. 583-598
    • Suchyna, T.M.1    Johnson, J.H.2    Hamer, K.3    Leykam, J.F.4    Gage, D.A.5    Clemo, H.F.6    Baumgarten, C.M.7    Sachs, F.8
  • 76
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz K.J., MacKinnon R. An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron. 15:1995;941-949.
    • (1995) Neuron , vol.15 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 78
    • 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
  • 81
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilization of prey by a fish-hunting marine snail
    • Terlau H., Shon K.J., Grilley M., Stocker M., Stuhmer W., Olivera B.M. Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 381:1996;148-151.
    • (1996) Nature , vol.381 , pp. 148-151
    • Terlau, H.1    Shon, K.J.2    Grilley, M.3    Stocker, M.4    Stuhmer, W.5    Olivera, B.M.6
  • 82
    • 0036027992 scopus 로고    scopus 로고
    • Alpha-latrotoxin: From structure to some functions
    • Ushkaryov Y. Alpha-latrotoxin: from structure to some functions. Toxicon. 40:2002;1-5.
    • (2002) Toxicon , vol.40 , pp. 1-5
    • Ushkaryov, Y.1
  • 85
    • 0033767401 scopus 로고    scopus 로고
    • A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels
    • Winterfield J.R., Swartz K.J. A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels. J. Gen. Physiol. 116:2000;637-644.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 637-644
    • Winterfield, J.R.1    Swartz, K.J.2
  • 86
    • 0037408077 scopus 로고    scopus 로고
    • Purification and characterization of Hainantoxin-V, a tetrodotoxin-sensitive sodium channel inhibitor from the venom of the spider Selenocosmia hainana
    • Xiao Y.C., Liang S.P. Purification and characterization of Hainantoxin-V, a tetrodotoxin-sensitive sodium channel inhibitor from the venom of the spider Selenocosmia hainana. Toxicon. 41:2003;643-650.
    • (2003) Toxicon , vol.41 , pp. 643-650
    • Xiao, Y.C.1    Liang, S.P.2
  • 87
    • 0027769658 scopus 로고
    • Assignment of the three disulfide bridges of huwentoxin-I, a neurotoxin from the spider Selenocosmia huwena
    • Zhang D., Liang S. Assignment of the three disulfide bridges of huwentoxin-I, a neurotoxin from the spider Selenocosmia huwena. J. Protein Chem. 12:1993;735-740.
    • (1993) J. Protein Chem. , vol.12 , pp. 735-740
    • Zhang, D.1    Liang, S.2
  • 88
    • 0031015813 scopus 로고    scopus 로고
    • Blockade of neuromuscular transmission by huwentoxin-I, purified from the venom of the Chinese bird spider Selenocosmia huwena
    • 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.