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Volumn 8, Issue 1, 2008, Pages

Unusual accelerated rate of deletions and insertions in toxin genes in the venom glands of the pygmy copperhead (Austrelaps labialis) from kangaroo island

Author keywords

[No Author keywords available]

Indexed keywords

LECTIN; METALLOPROTEINASE; NEUROTOXIN; PHOSPHOLIPASE A2; SERINE PROTEINASE INHIBITOR; SNAKE VENOM; ULINASTATIN;

EID: 41849121226     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-8-70     Document Type: Article
Times cited : (26)

References (67)
  • 2
    • 0018564639 scopus 로고
    • The lethality in mice of dangerous Australian and other snake venom
    • 10.1016/0041-0101(79)90245-9. 524395
    • The lethality in mice of dangerous Australian and other snake venom. AJ Broad SK Sutherland AR Coulter, Toxicon 1979 17 661 664 10.1016/0041-0101(79) 90245-9 524395
    • (1979) Toxicon , vol.17 , pp. 661-664
    • Broad, A.J.1    Sutherland, S.K.2    Coulter, A.R.3
  • 3
    • 72949148228 scopus 로고
    • Haemolysins in venoms of Australian snakes. Observations on the haemolysins of the venoms of some Australian snakes and the separation of phospholipase a from the venom of Pseudechis porphyriacus
    • 13723433
    • Haemolysins in venoms of Australian snakes. Observations on the haemolysins of the venoms of some Australian snakes and the separation of phospholipase A from the venom of Pseudechis porphyriacus. HM Doery JA Pearson, Biochem J 1961 78 820 827 13723433
    • (1961) Biochem J , vol.78 , pp. 820-827
    • Doery, H.M.1    Pearson, J.A.2
  • 4
    • 0030610957 scopus 로고    scopus 로고
    • Isolation and purification of superbins I and II from Austrelaps superbus (copperhead) snake venom and their anticoagulant and antiplatelet effects
    • 10.1016/S0041-0101(97)00014-7. 9278973
    • Isolation and purification of superbins I and II from Austrelaps superbus (copperhead) snake venom and their anticoagulant and antiplatelet effects. S Subburaju RM Kini, Toxicon 1997 35 1239 1250 10.1016/S0041-0101(97)00014-7 9278973
    • (1997) Toxicon , vol.35 , pp. 1239-1250
    • Subburaju, S.1    Kini, R.M.2
  • 5
    • 0034653921 scopus 로고    scopus 로고
    • Phospholipase A(2) with platelet aggregation inhibitor activity from Austrelaps superbus venom: Protein purification and cDNA cloning
    • 10.1006/abbi.1999.1672. 10700385
    • Phospholipase A(2) with platelet aggregation inhibitor activity from Austrelaps superbus venom: protein purification and cDNA cloning. SB Singh A Armugam RM Kini K Jeyaseelan, Arch Biochem Biophys 2000 375 289 303 10.1006/abbi.1999.1672 10700385
    • (2000) Arch Biochem Biophys , vol.375 , pp. 289-303
    • Singh, S.B.1    Armugam, A.2    Kini, R.M.3    Jeyaseelan, K.4
  • 6
    • 34249704527 scopus 로고    scopus 로고
    • Molecular isoforms of cobra venom factor-like proteins in the venom of Austrelaps superbus
    • 10.1016/j.toxicon.2007.02.016. 17412383
    • Molecular isoforms of cobra venom factor-like proteins in the venom of Austrelaps superbus. S Rehana RM Kini, Toxicon 2007 50 32 52 10.1016/j.toxicon.2007.02.016 17412383
    • (2007) Toxicon , vol.50 , pp. 32-52
    • Rehana, S.1    Kini, R.M.2
  • 7
    • 0023582757 scopus 로고
    • Ecological ramifications of prey size: Food habits and reproductive biology of Australian copperhead snakes (Austrelaps, Elapidae)
    • 10.2307/1564381
    • Ecological ramifications of prey size: food habits and reproductive biology of Australian copperhead snakes (Austrelaps, Elapidae). R Shine, Journal of Herpetology 1987 21 71 74 10.2307/1564381
    • (1987) Journal of Herpetology , vol.21 , pp. 71-74
    • Shine, R.1
  • 8
    • 41849114079 scopus 로고
    • Genus Austrelaps Worrell, the Copperheads
    • Melbourne: Oxford University Press
    • Genus Austrelaps Worrell, the Copperheads. SK Sutherland, Australian Animal Toxins Melbourne: Oxford University Press 1983 86 90
    • (1983) Australian Animal Toxins , pp. 86-90
    • Sutherland, S.K.1
  • 9
    • 33644606606 scopus 로고    scopus 로고
    • FastGroupII: A web-based bioinformatics platform for analyses of large 16S rDNA libraries
    • 16464253. 10.1186/1471-2105-7-57
    • FastGroupII: a web-based bioinformatics platform for analyses of large 16S rDNA libraries. Y Yu M Breitbart P McNairnie F Rohwer, BMC Bioinformatics 2006 7 57 16464253 10.1186/1471-2105-7-57
    • (2006) BMC Bioinformatics , vol.7 , pp. 57
    • Yu, Y.1    Breitbart, M.2    McNairnie, P.3    Rohwer, F.4
  • 10
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 7984417. 10.1093/nar/22.22.4673
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. JD Thompson DG Higgins TJ Gibson, Nucleic Acids Res 1994 22 4673 4680 7984417 10.1093/nar/22.22.4673
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 11
    • 1342288004 scopus 로고    scopus 로고
    • The Jalview Java alignment editor
    • 10.1093/bioinformatics/btg430. 14960472
    • The Jalview Java alignment editor. M Clamp J Cuff SM Searle GJ Barton, Bioinformatics 2004 20 426 427 10.1093/bioinformatics/btg430 14960472
    • (2004) Bioinformatics , vol.20 , pp. 426-427
    • Clamp, M.1    Cuff, J.2    Searle, S.M.3    Barton, G.J.4
  • 12
    • 23144433822 scopus 로고    scopus 로고
    • PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference
    • 15980534. 10.1093/nar/gki352
    • PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference. S Guindon F Lethiec P Duroux O Gascuel, Nucleic Acids Res 2005 33 W557 W559 15980534 10.1093/nar/gki352
    • (2005) Nucleic Acids Res , vol.33
    • Guindon, S.1    Lethiec, F.2    Duroux, P.3    Gascuel, O.4
  • 13
    • 0036381024 scopus 로고    scopus 로고
    • Molecular moulds with multiple missions: Functional sites in three-finger toxins
    • 10.1046/j.1440-1681.2002.03725.x. 12165048
    • Molecular moulds with multiple missions: functional sites in three-finger toxins. RM Kini, Clin Exp Pharmacol Physiol 2002 29 815 822 10.1046/j.1440-1681.2002.03725.x 12165048
    • (2002) Clin Exp Pharmacol Physiol , vol.29 , pp. 815-822
    • Kini, R.M.1
  • 14
    • 0343671345 scopus 로고    scopus 로고
    • Functional architectures of animal toxins: A clue to drug design?
    • 10.1016/S0041-0101(98)00148-2. 9792172
    • Functional architectures of animal toxins: a clue to drug design? A Menez, Toxicon 1998 36 1557 1572 10.1016/S0041-0101(98)00148-2 9792172
    • (1998) Toxicon , vol.36 , pp. 1557-1572
    • Menez, A.1
  • 15
    • 0033198876 scopus 로고    scopus 로고
    • Snake venom alpha-neurotoxins and other 'three-finger' proteins
    • 10.1046/j.1432-1327.1999.00623.x. 10491072
    • Snake venom alpha-neurotoxins and other 'three-finger' proteins. V Tsetlin, Eur J Biochem 1999 264 281 286 10.1046/j.1432-1327.1999.00623.x 10491072
    • (1999) Eur J Biochem , vol.264 , pp. 281-286
    • Tsetlin, V.1
  • 16
    • 35948930215 scopus 로고    scopus 로고
    • {beta}-Cardiotoxin: A new three-finger toxin from Ophiophagus hannah (king cobra) venom with beta-blocker activity
    • 17616557
    • {beta}-Cardiotoxin: a new three-finger toxin from Ophiophagus hannah (king cobra) venom with beta-blocker activity. N Rajagopalan YF Pung YZ Zhu PT Wong PP Kumar RM Kini, FASEB J 2007 17616557
    • (2007) FASEB J
    • Rajagopalan, N.1    Pung, Y.F.2    Zhu, Y.Z.3    Wong, P.T.4    Kumar, P.P.5    Kini, R.M.6
  • 17
    • 14644404946 scopus 로고    scopus 로고
    • Eggs-only diet: Its implications for the toxin profile changes and ecology of the marbled sea snake (Aipysurus eydouxii)
    • 10.1007/s00239-004-0138-0. 15696370
    • Eggs-only diet: its implications for the toxin profile changes and ecology of the marbled sea snake (Aipysurus eydouxii). M Li BG Fry RM Kini, J Mol Evol 2005 60 81 89 10.1007/s00239-004-0138-0 15696370
    • (2005) J Mol Evol , vol.60 , pp. 81-89
    • Li, M.1    Fry, B.G.2    Kini, R.M.3
  • 18
    • 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
    • 10.1074/jbc.274.49.34851. 10574958
    • Variability among the sites by which curaremimetic toxins bind to torpedo acetylcholine receptor, as revealed by identification of the functional residues of alpha-cobratoxin. S Antil D Servent A Menez, J Biol Chem 1999 274 34851 34858 10.1074/jbc.274.49.34851 10574958
    • (1999) J Biol Chem , vol.274 , pp. 34851-34858
    • Antil, S.1    Servent, D.2    Menez, A.3
  • 19
    • 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
    • 10.1074/jbc.M909746199. 10852927
    • Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal alpha 7-nicotinic acetylcholine receptor. S Antil-Delbeke C Gaillard T Tamiya PJ Corringer JP Changeux D Servent A Menez, J Biol Chem 2000 275 29594 29601 10.1074/jbc.M909746199 10852927
    • (2000) J Biol Chem , vol.275 , pp. 29594-29601
    • Antil-Delbeke, S.1    Gaillard, C.2    Tamiya, T.3    Corringer, P.J.4    Changeux, J.P.5    Servent, D.6    Menez, A.7
  • 20
    • 0020529179 scopus 로고
    • Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides
    • 6615431
    • Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides. N Tamiya N Maeda HG Cogger, Biochem J 1983 213 31 38 6615431
    • (1983) Biochem J , vol.213 , pp. 31-38
    • Tamiya, N.1    Maeda, N.2    Cogger, H.G.3
  • 21
    • 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
    • 8419369
    • 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. L Pillet O Tremeau F Ducancel P Drevet S Zinn-Justin S Pinkasfeld JC Boulain A Menez, J Biol Chem 1993 268 909 916 8419369
    • (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
  • 22
    • 0028934293 scopus 로고
    • Genetic engineering of snake toxins. the functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues
    • 10.1074/jbc.270.16.9362. 7721859
    • Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues. O Tremeau C Lemaire P Drevet S Pinkasfeld F Ducancel JC Boulain A Menez, J Biol Chem 1995 270 9362 9369 10.1074/jbc.270.16.9362 7721859
    • (1995) J Biol Chem , vol.270 , pp. 9362-9369
    • Tremeau, O.1    Lemaire, C.2    Drevet, P.3    Pinkasfeld, S.4    Ducancel, F.5    Boulain, J.C.6    Menez, A.7
  • 23
    • 33751028489 scopus 로고    scopus 로고
    • The phospholipase A2 superfamily and its group numbering system
    • 16973413
    • The phospholipase A2 superfamily and its group numbering system. RH Schaloske EA Dennis, Biochim Biophys Acta 2006 1761 1246 1259 16973413
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 1246-1259
    • Schaloske, R.H.1    Dennis, E.A.2
  • 24
    • 0002556781 scopus 로고    scopus 로고
    • Phospholipase A2 a Complex Multifunctional Protein Puzzle
    • Chichester, England: John Wiley & Sons Kini RM
    • Phospholipase A2 A Complex Multifunctional Protein Puzzle. RM Kini, Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism Chichester, England: John Wiley & Sons, Kini RM, 1997 1 28
    • (1997) Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism , pp. 1-28
    • Kini, R.M.1
  • 25
    • 0028782092 scopus 로고
    • Molecular evolution of serine protease and its inhibitor with special reference to domain evolution
    • 10.1098/rstb.1994.0080. 7800711
    • Molecular evolution of serine protease and its inhibitor with special reference to domain evolution. T Gojobori K Ikeo, Philos Trans R Soc Lond B Biol Sci 1994 344 411 415 10.1098/rstb.1994.0080 7800711
    • (1994) Philos Trans R Soc Lond B Biol Sci , vol.344 , pp. 411-415
    • Gojobori, T.1    Ikeo, K.2
  • 26
    • 0022961424 scopus 로고
    • Protein inhibitors of serine proteinases - mechanism and classification
    • 3541508
    • Protein inhibitors of serine proteinases - mechanism and classification. M Laskowski Jr, Adv Exp Med Biol 1986 199 1 17 3541508
    • (1986) Adv Exp Med Biol , vol.199 , pp. 1-17
    • Laskowski, M.1    Jr2
  • 27
    • 0025080866 scopus 로고
    • Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide from the venom of cobra (Naja naja naja)
    • 10.1016/0014-5793(90)81426-O. 2262001
    • Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide from the venom of cobra (Naja naja naja). J Shafqat ZH Zaidi H Jornvall, FEBS Lett 1990 275 6 8 10.1016/0014-5793(90)81426-O 2262001
    • (1990) FEBS Lett , vol.275 , pp. 6-8
    • Shafqat, J.1    Zaidi, Z.H.2    Jornvall, H.3
  • 28
    • 0034116824 scopus 로고    scopus 로고
    • Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model
    • 10.1097/00001721-200006000-00011. 10847427
    • Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model. PP Masci AN Whitaker LG Sparrow J de Jersey DJ Winzor DJ Watters MF Lavin PJ Gaffney, Blood Coagul Fibrinolysis 2000 11 385 393 10.1097/00001721-200006000-00011 10847427
    • (2000) Blood Coagul Fibrinolysis , vol.11 , pp. 385-393
    • Masci, P.P.1    Whitaker, A.N.2    Sparrow, L.G.3    De Jersey, J.4    Winzor, D.J.5    Watters, D.J.6    Lavin, M.F.7    Gaffney, P.J.8
  • 29
    • 0030959314 scopus 로고    scopus 로고
    • Identification and cloning of human placental bikunin, a novel serine protease inhibitor containing two Kunitz domains
    • 10.1074/jbc.272.18.12202. 9115294
    • Identification and cloning of human placental bikunin, a novel serine protease inhibitor containing two Kunitz domains. CW Marlor KA Delaria G Davis DK Muller JM Greve PP Tamburini, J Biol Chem 1997 272 12202 12208 10.1074/jbc.272.18.12202 9115294
    • (1997) J Biol Chem , vol.272 , pp. 12202-12208
    • Marlor, C.W.1    Delaria, K.A.2    Davis, G.3    Muller, D.K.4    Greve, J.M.5    Tamburini, P.P.6
  • 30
  • 31
    • 0027321118 scopus 로고
    • Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG) and the novel related CRISP-3 are expressed under androgen control in the mouse salivary gland
    • 10.1210/en.133.1.192. 8319566
    • Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG) and the novel related CRISP-3 are expressed under androgen control in the mouse salivary gland. B Haendler J Kratzschmar F Theuring WD Schleuning, Endocrinology 1993 133 192 198 10.1210/en.133.1.192 8319566
    • (1993) Endocrinology , vol.133 , pp. 192-198
    • Haendler, B.1    Kratzschmar, J.2    Theuring, F.3    Schleuning, W.D.4
  • 32
    • 0037376935 scopus 로고    scopus 로고
    • Wide distribution of cysteine-rich secretory proteins in snake venoms: Isolation and cloning of novel snake venom cysteine-rich secretory proteins
    • 10.1016/S0003-9861(03)00028-6. 12646276
    • Wide distribution of cysteine-rich secretory proteins in snake venoms: isolation and cloning of novel snake venom cysteine-rich secretory proteins. Y Yamazaki F Hyodo T Morita, Arch Biochem Biophys 2003 412 133 141 10.1016/S0003-9861(03)00028-6 12646276
    • (2003) Arch Biochem Biophys , vol.412 , pp. 133-141
    • Yamazaki, Y.1    Hyodo, F.2    Morita, T.3
  • 33
    • 12844277423 scopus 로고    scopus 로고
    • Cobra venom contains a pool of cysteine-rich secretory proteins
    • 10.1016/j.bbrc.2004.12.154. 15670767
    • Cobra venom contains a pool of cysteine-rich secretory proteins. AV Osipov MY Levashov VI Tsetlin YN Utkin, Biochem Biophys Res Commun 2005 328 177 182 10.1016/j.bbrc.2004.12.154 15670767
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 177-182
    • Osipov, A.V.1    Levashov, M.Y.2    Tsetlin, V.I.3    Utkin, Y.N.4
  • 34
    • 16644394108 scopus 로고    scopus 로고
    • Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms
    • 10.1107/S0907444904005670. 15159571
    • Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms. X Tu J Wang M Guo D Zheng M Teng L Niu Q Liu Q Huang Q Hao, Acta Crystallogr D Biol Crystallogr 2004 60 1108 1111 10.1107/S0907444904005670 15159571
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1108-1111
    • Tu, X.1    Wang, J.2    Guo, M.3    Zheng, D.4    Teng, M.5    Niu, L.6    Liu, Q.7    Huang, Q.8    Hao, Q.9
  • 35
    • 0037167616 scopus 로고    scopus 로고
    • Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels
    • 10.1021/bi026132h. 12234174
    • Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels. Y Yamazaki RL Brown T Morita, Biochemistry 2002 41 11331 11337 10.1021/bi026132h 12234174
    • (2002) Biochemistry , vol.41 , pp. 11331-11337
    • Yamazaki, Y.1    Brown, R.L.2    Morita, T.3
  • 36
    • 0033582176 scopus 로고    scopus 로고
    • Pseudechetoxin: A peptide blocker of cyclic nucleotide-gated ion channels
    • 9892706. 10.1073/pnas.96.2.754
    • Pseudechetoxin: a peptide blocker of cyclic nucleotide-gated ion channels. RL Brown TL Haley KA West JW Crabb, Proc Natl Acad Sci USA 1999 96 754 759 9892706 10.1073/pnas.96.2.754
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 754-759
    • Brown, R.L.1    Haley, T.L.2    West, K.A.3    Crabb, J.W.4
  • 37
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • 10708855
    • Snake venom proteases affecting hemostasis and thrombosis. T Matsui Y Fujimura K Titani, Biochim Biophys Acta 2000 1477 146 156 10708855
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 39
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • 10.1016/0014-5793(93)80312-I. 8405391
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. W Bode FX Gomis-Ruth W Stockler, FEBS Lett 1993 331 134 140 10.1016/0014-5793(93)80312-I 8405391
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 40
    • 0028337108 scopus 로고
    • CDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins
    • 10.1006/abbi.1994.1026. 8311451
    • cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins. LA Hite LG Jia JB Bjarnason JW Fox, Arch Biochem Biophys 1994 308 182 191 10.1006/abbi.1994.1026 8311451
    • (1994) Arch Biochem Biophys , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 41
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • 10.1016/0163-7258(94)90049-3. 7972338
    • Hemorrhagic metalloproteinases from snake venoms. JB Bjarnason JW Fox, Pharmacol Ther 1994 62 325 372 10.1016/0163-7258(94)90049-3 7972338
    • (1994) Pharmacol Ther , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 42
    • 0030175550 scopus 로고    scopus 로고
    • Insights into the mechanism of haemorrhage caused by snake venom metalloproteinases
    • 10.1016/0041-0101(96)00017-7. 8817809
    • Insights into the mechanism of haemorrhage caused by snake venom metalloproteinases. AS Kamiguti CR Hay RD Theakston M Zuzel, Toxicon 1996 34 627 642 10.1016/0041-0101(96)00017-7 8817809
    • (1996) Toxicon , vol.34 , pp. 627-642
    • Kamiguti, A.S.1    Hay, C.R.2    Theakston, R.D.3    Zuzel, M.4
  • 43
    • 0028848625 scopus 로고
    • Skeletal muscle necrosis and regeneration after injection of BaH1, a hemorrhagic metalloproteinase isolated from the venom of the snake Bothrops asper (Terciopelo)
    • 10.1006/exmp.1995.1004. 7556589
    • Skeletal muscle necrosis and regeneration after injection of BaH1, a hemorrhagic metalloproteinase isolated from the venom of the snake Bothrops asper (Terciopelo). JM Gutierrez M Romero J Nunez F Chaves G Borkow M Ovadia, Exp Mol Pathol 1995 62 28 41 10.1006/exmp.1995.1004 7556589
    • (1995) Exp Mol Pathol , vol.62 , pp. 28-41
    • Gutierrez, J.M.1    Romero, M.2    Nunez, J.3    Chaves, F.4    Borkow, G.5    Ovadia, M.6
  • 44
    • 19544369492 scopus 로고    scopus 로고
    • Platelets as targets of snake venom metalloproteinases
    • 10.1016/j.toxicon.2005.02.026. 15922773
    • Platelets as targets of snake venom metalloproteinases. AS Kamiguti, Toxicon 2005 45 1041 1049 10.1016/j.toxicon.2005.02.026 15922773
    • (2005) Toxicon , vol.45 , pp. 1041-1049
    • Kamiguti, A.S.1
  • 45
    • 0028924054 scopus 로고
    • Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)
    • 10.1016/0041-0101(94)00138-X. 7778126
    • Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo). JM Gutierrez M Romero C Diaz G Borkow M Ovadia, Toxicon 1995 33 19 29 10.1016/0041-0101(94)00138-X 7778126
    • (1995) Toxicon , vol.33 , pp. 19-29
    • Gutierrez, J.M.1    Romero, M.2    Diaz, C.3    Borkow, G.4    Ovadia, M.5
  • 46
    • 0029840014 scopus 로고    scopus 로고
    • Processing of pro-tumor necrosis factor-alpha by venom metalloproteinases: A hypothesis explaining local tissue damage following snake bite
    • 10.1002/eji.1830260905. 8814237
    • Processing of pro-tumor necrosis factor-alpha by venom metalloproteinases: a hypothesis explaining local tissue damage following snake bite. AM Moura-da-Silva GD Laing MJ Paine JM Dennison V Politi JM Crampton RD Theakston, Eur J Immunol 1996 26 2000 2005 10.1002/eji.1830260905 8814237
    • (1996) Eur J Immunol , vol.26 , pp. 2000-2005
    • Moura-Da-Silva, A.M.1    Laing, G.D.2    Paine, M.J.3    Dennison, J.M.4    Politi, V.5    Crampton, J.M.6    Theakston, R.D.7
  • 47
    • 0033178496 scopus 로고    scopus 로고
    • Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri
    • 10417338. 10.1042/0264-6021:3410733
    • Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri. Q Xu XF Wu QC Xia KY Wang, Biochem J 1999 341 Pt 3 733 737 10417338 10.1042/0264-6021:3410733
    • (1999) Biochem J , vol.341 , Issue.PART 3 , pp. 733-737
    • Xu, Q.1    Wu, X.F.2    Xia, Q.C.3    Wang, K.Y.4
  • 48
    • 19544368798 scopus 로고    scopus 로고
    • Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on haemostasis
    • 10.1016/j.toxicon.2005.02.022. 15876445
    • Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on haemostasis. Q Lu A Navdaev JM Clemetson KJ Clemetson, Toxicon 2005 45 1089 1098 10.1016/j.toxicon.2005.02.022 15876445
    • (2005) Toxicon , vol.45 , pp. 1089-1098
    • Lu, Q.1    Navdaev, A.2    Clemetson, J.M.3    Clemetson, K.J.4
  • 49
    • 0037144572 scopus 로고    scopus 로고
    • Ophioluxin, a convulxin-like C-type lectin from Ophiophagus hannah (King cobra) is a powerful platelet activator via glycoprotein VI
    • 10.1074/jbc.M204372200. 12130642
    • Ophioluxin, a convulxin-like C-type lectin from Ophiophagus hannah (King cobra) is a powerful platelet activator via glycoprotein VI. XY Du JM Clemetson A Navdaev EM Magnenat TN Wells KJ Clemetson, J Biol Chem 2002 277 35124 35132 10.1074/jbc.M204372200 12130642
    • (2002) J Biol Chem , vol.277 , pp. 35124-35132
    • Du, X.Y.1    Clemetson, J.M.2    Navdaev, A.3    Magnenat, E.M.4    Wells, T.N.5    Clemetson, K.J.6
  • 50
    • 0032904607 scopus 로고    scopus 로고
    • Primary structure and biological activity of snake venom lectin (APL) from Agkistrodon p. piscivorus (Eastern cottonmouth)
    • 10.1016/S0041-0101(98)00239-6. 10484740
    • Primary structure and biological activity of snake venom lectin (APL) from Agkistrodon p. piscivorus (Eastern cottonmouth). Y Komori T Nikai T Tohkai H Sugihara, Toxicon 1999 37 1053 1064 10.1016/S0041-0101(98)00239-6 10484740
    • (1999) Toxicon , vol.37 , pp. 1053-1064
    • Komori, Y.1    Nikai, T.2    Tohkai, T.3    Sugihara, H.4
  • 51
    • 34447649919 scopus 로고    scopus 로고
    • Cloning, expression and characterization of two C-type lectins from the venom gland of Bungarus multicinctus
    • 10.1016/j.toxicon.2007.04.019. 17561224
    • Cloning, expression and characterization of two C-type lectins from the venom gland of Bungarus multicinctus. LP Lin Q Lin YQ Wang, Toxicon 2007 50 411 419 10.1016/j.toxicon.2007.04.019 17561224
    • (2007) Toxicon , vol.50 , pp. 411-419
    • Lin, L.P.1    Lin, Q.2    Wang, Y.Q.3
  • 52
    • 0023014079 scopus 로고
    • Isolation and characterization of lactose-binding lectins from the venoms of the snakes Lachesis muta and Dendroaspis jamesonii
    • Isolation and characterization of lactose-binding lectins from the venoms of the snakes Lachesis muta and Dendroaspis jamesonii. ML Ogilvie ME Dockter L Wenz TK Gartner, J Biochem (Tokyo) 1986 100 1425 1431
    • (1986) J Biochem (Tokyo) , vol.100 , pp. 1425-1431
    • Ogilvie, M.L.1    Dockter, M.E.2    Wenz, L.3    Gartner, T.K.4
  • 53
    • 0034798169 scopus 로고    scopus 로고
    • Cloning of cDNAs encoding C-type lectins from Elapidae snakes Bungarus fasciatus and Bungarus multicinctus
    • 10.1016/S0041-0101(01)00172-6. 11600152
    • Cloning of cDNAs encoding C-type lectins from Elapidae snakes Bungarus fasciatus and Bungarus multicinctus. HG Zha WH Lee Y Zhang, Toxicon 2001 39 1887 1892 10.1016/S0041-0101(01)00172-6 11600152
    • (2001) Toxicon , vol.39 , pp. 1887-1892
    • Zha, H.G.1    Lee, W.H.2    Zhang, Y.3
  • 56
    • 2942614836 scopus 로고    scopus 로고
    • Polyadenylation of rRNA in Saccharomyces cerevisiae
    • 15173578. 10.1073/pnas.0402888101
    • Polyadenylation of rRNA in Saccharomyces cerevisiae. L Kuai F Fang JS Butler F Sherman, Proc Natl Acad Sci USA 2004 101 8581 8586 15173578 10.1073/pnas.0402888101
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8581-8586
    • Kuai, L.1    Fang, F.2    Butler, J.S.3    Sherman, F.4
  • 58
    • 33745116597 scopus 로고    scopus 로고
    • Polyadenylation of ribosomal RNA in human cells
    • 16738135. 10.1093/nar/gkl357
    • Polyadenylation of ribosomal RNA in human cells. S Slomovic D Laufer D Geiger G Schuster, Nucleic Acids Res 2006 34 2966 2975 16738135 10.1093/nar/gkl357
    • (2006) Nucleic Acids Res , vol.34 , pp. 2966-2975
    • Slomovic, S.1    Laufer, D.2    Geiger, D.3    Schuster, G.4
  • 59
    • 0042171600 scopus 로고    scopus 로고
    • Molecular evolution and phylogeny of elapid snake venom three-finger toxins
    • 10.1007/s00239-003-2461-2. 12962311
    • Molecular evolution and phylogeny of elapid snake venom three-finger toxins. BG Fry W Wuster RM Kini V Brusic A Khan D Venkataraman AP Rooney, J Mol Evol 2003 57 110 129 10.1007/s00239-003-2461-2 12962311
    • (2003) J Mol Evol , vol.57 , pp. 110-129
    • Fry, B.G.1    Wuster, W.2    Kini, R.M.3    Brusic, V.4    Khan, A.5    Venkataraman, D.6    Rooney, A.P.7
  • 61
    • 16344384549 scopus 로고    scopus 로고
    • Putting the brakes on snake venom evolution: The unique molecular evolutionary patterns of Aipysurus eydouxii (Marbled sea snake) phospholipase A2 toxins
    • 10.1093/molbev/msi077. 15635056
    • Putting the brakes on snake venom evolution: the unique molecular evolutionary patterns of Aipysurus eydouxii (Marbled sea snake) phospholipase A2 toxins. M Li BG Fry RM Kini, Mol Biol Evol 2005 22 934 941 10.1093/molbev/ msi077 15635056
    • (2005) Mol Biol Evol , vol.22 , pp. 934-941
    • Li, M.1    Fry, B.G.2    Kini, R.M.3
  • 62
    • 1042298845 scopus 로고    scopus 로고
    • Molecular evolution of myotoxic phospholipases A2 from snake venom
    • 10.1016/j.toxicon.2003.11.003. 15019486
    • Molecular evolution of myotoxic phospholipases A2 from snake venom. M Ohno T Chijiwa N Oda-Ueda T Ogawa S Hattori, Toxicon 2003 42 841 854 10.1016/j.toxicon.2003.11.003 15019486
    • (2003) Toxicon , vol.42 , pp. 841-854
    • Ohno, M.1    Chijiwa, T.2    Oda-Ueda, N.3    Ogawa, T.4    Hattori, S.5
  • 63
    • 0034655712 scopus 로고    scopus 로고
    • Regional evolution of venom-gland phospholipase A2 isoenzymes of Trimeresurus flavoviridis snakes in the southwestern islands of Japan
    • 10749679. 10.1042/0264-6021:3470491
    • Regional evolution of venom-gland phospholipase A2 isoenzymes of Trimeresurus flavoviridis snakes in the southwestern islands of Japan. T Chijiwa M Deshimaru I Nobuhisa M Nakai T Ogawa N Oda K Nakashima Y Fukumaki Y Shimohigashi S Hattori M Ohno, Biochem J 2000 347 491 499 10749679 10.1042/0264-6021:3470491
    • (2000) Biochem J , vol.347 , pp. 491-499
    • Chijiwa, T.1    Deshimaru, M.2    Nobuhisa, I.3    Nakai, M.4    Ogawa, T.5    Oda, N.6    Nakashima, K.7    Fukumaki, Y.8    Shimohigashi, Y.9    Hattori, S.10    Ohno, M.11
  • 64
    • 0039996064 scopus 로고
    • Three-dimensional structure of the "long" neurotoxin from cobra venom
    • 6930640. 10.1073/pnas.77.5.2400
    • Three-dimensional structure of the "long" neurotoxin from cobra venom. MD Walkinshaw W Saenger A Maelicke, Proc Natl Acad Sci USA 1980 77 2400 2404 6930640 10.1073/pnas.77.5.2400
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2400-2404
    • Walkinshaw, M.D.1    Saenger, W.2    Maelicke, A.3
  • 65
    • 0242317451 scopus 로고    scopus 로고
    • Molecular evolution and diversification of snake toxin genes, revealed by analysis of intron sequences
    • 10.1016/S0378-1119(03)00637-1. 12957382
    • Molecular evolution and diversification of snake toxin genes, revealed by analysis of intron sequences. TJ Fujimi T Nakajyo E Nishimura E Ogura T Tsuchiya T Tamiya, Gene 2003 313 111 118 10.1016/S0378-1119(03)00637-1 12957382
    • (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
  • 66
    • 28344453534 scopus 로고    scopus 로고
    • Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species
    • 10.1007/s00018-005-5384-9. 16261251
    • Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species. L St Pierre R Woods S Earl PP Masci MF Lavin, Cell Mol Life Sci 2005 62 2679 2693 10.1007/s00018-005-5384-9 16261251
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2679-2693
    • St Pierre, L.1    Woods, R.2    Earl, S.3    Masci, P.P.4    Lavin, M.F.5


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