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dc.contributor.authordos Santos, Juliana I.-
dc.contributor.authorFernandes, Carlos A. H.-
dc.contributor.authorMagro, Angelo J.-
dc.contributor.authorFontes, Marcos R. M.-
dc.identifier.citationProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 16, n. 8, p. 887-893, 2009.-
dc.description.abstractPhospholipases A(2) homologues are found in the venom of Crotalinae snakes, being their main action related to myonecrosis induction. Although many studies on these toxins had already been performed, their mechanism of action remains unclear. Here, important aspects about these toxins are reviewed, including their correct biological assembly and how essential is the natural substitution D49K for their catalytic inactivity.en
dc.publisherBentham Science Publ Ltd-
dc.sourceWeb of Science-
dc.subjectPhospholipase A(2) homologuesen
dc.subjectsnake venomen
dc.subjectoligomeric conformationen
dc.subjectquaternary structureen
dc.subjectX-ray crystallographyen
dc.titleThe Intriguing Phospholipases A(2) Homologues: Relevant Structural Features on Myotoxicity and Catalytic Inactivityen
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUNESP, Inst Biociencias, Dept Fis & Biofis, BR-18618000 Botucatu, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Biociencias, Dept Fis & Biofis, BR-18618000 Botucatu, SP, Brazil-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofProtein and Peptide Letters-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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