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dc.contributor.authorGeorgieva, Dessislava-
dc.contributor.authorOehler, Michaela-
dc.contributor.authorSeifert, Jana-
dc.contributor.authorvon Bergen, Martin-
dc.contributor.authorArni, Raghuvir K.-
dc.contributor.authorGenov, Nicolay-
dc.contributor.authorBetzel, Christian-
dc.date.accessioned2014-05-20T14:02:34Z-
dc.date.accessioned2016-10-25T17:09:11Z-
dc.date.available2014-05-20T14:02:34Z-
dc.date.available2016-10-25T17:09:11Z-
dc.date.issued2010-05-01-
dc.identifierhttp://dx.doi.org/10.1021/pr901042p-
dc.identifier.citationJournal of Proteome Research. Washington: Amer Chemical Soc, v. 9, n. 5, p. 2302-2316, 2010.-
dc.identifier.issn1535-3893-
dc.identifier.urihttp://hdl.handle.net/11449/22055-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/22055-
dc.description.abstractThe snake venomic of Crotalus durissus terrificus was analyzed by 2-D and 1-D electrophoresis and subsequent MS/MS and enzymatic assays. The venomic of the South American rattlesnake comprises toxins from seven protein families: phospholipases A(2), serine proteinases, ecto-5'-nucleotidases, metalloproteinases, nerve growth factors, phosphodiesterases, and glutaminyl cyclase. The venom toxin composition correlates with the clinical manifestation of the crotalinae snake bites and explains pathological effects of the venom such as neurotoxicity, systemic myonecrosis, hemostatic disorders, myoglobinuria, and acute renal failure. The vast majority of toxins are potentially involved in neurotoxicity, myotoxicity, and coagulopathy. The predominant venom components are neurotoxic phospholipases A2 and serine proteinases. The venom is a rich source of 5'-nucleotidases (7.8% of the identified toxins) inducing hemostatic disorders. Analysis of the venom protein composition provided a catalogue for secreted toxins. The venomic composition of Crotalus d. terrificus and venom gland transcriptome of the synonymous subspecies Crotalus d. collilineatus show differences in the occurrence of protein families and in the abundance of toxins. Some of the venom components identified by the proteomic analysis were not reported in the transcriptome of the Crotalus d. collilineatus venom gland. Enzymatic activities of the Crotalus d. terrificus venom were determined and correlated with the proteomic composition.en
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG)-
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipBulgarian National Foundation for Scientific Research-
dc.format.extent2302-2316-
dc.language.isoeng-
dc.publisherAmer Chemical Soc-
dc.sourceWeb of Science-
dc.subjectSnake venomicen
dc.subjectCrotalus durissus terrificusen
dc.subject2-D electrophoresisen
dc.subjectelectrospray mass spectrometryen
dc.titleSnake Venomic of Crotalus durissus terrificus-Correlation with Pharmacological Activitiesen
dc.typeoutro-
dc.contributor.institutionUniv Hamburg-
dc.contributor.institutionUFZ Helmholtz Ctr Environm Res-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionBulgarian Acad Sci-
dc.description.affiliationUniv Hamburg, Lab Struct Biol Infect & Inflammat, Inst Biochem & Mol Biol, DESY, D-22603 Hamburg, Germany-
dc.description.affiliationUFZ Helmholtz Ctr Environm Res, Dept Prote, D-04318 Leipzig, Germany-
dc.description.affiliationIBILCE UNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationBulgarian Acad Sci, Inst Organ Chem, BU-1113 Sofia, Bulgaria-
dc.description.affiliationUnespIBILCE UNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.sponsorshipIdDFG: BE 1443-18-1-
dc.description.sponsorshipIdFAPESP: 07/54865-1-
dc.description.sponsorshipIdBulgarian National Foundation for Scientific Research: TK-B-1610/06-
dc.identifier.doi10.1021/pr901042p-
dc.identifier.wosWOS:000277353200022-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Proteome Research-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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