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Phospholipase A(2) - A structural review

dc.contributor.authorArni, R. K.
dc.contributor.authorWard, R. J.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:21:17Z
dc.date.available2014-05-20T15:21:17Z
dc.date.issued1996-08-01
dc.description.abstractPhospholipases A(2) (PLA(2)) are widely distributed in nature and are well characterized proteins with respect to their catalytic and pharmacological activities, A wealth of structural information has recently become available both from X-ray diffraction and NMR studies, and although a detailed model of the catalytic mechanism of PLA(2) has been proposed, the structural bases of other aspects of PLA(2) function, such as interfacial activation and venom PLA(2) pharmacological activities, are still under debate. An appreciation of the PLA(2) protein structure will yield new insights with regard to these activities, the salient structural features of the class I, II and III PLA(2) are discussed with respect to their functional roles. Copyright (C) 1996 Published by Elsevier B.V. Ltden
dc.description.affiliationUNESP,IBILCE,DEPT PHYS,CP 136,BR-15054000 S JOSE RIO PR,SP,BRAZIL
dc.description.affiliationUnespUNESP,IBILCE,DEPT PHYS,CP 136,BR-15054000 S JOSE RIO PR,SP,BRAZIL
dc.format.extent827-841
dc.identifierhttp://dx.doi.org/10.1016/0041-0101(96)00036-0
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 34, n. 8, p. 827-841, 1996.
dc.identifier.doi10.1016/0041-0101(96)00036-0
dc.identifier.issn0041-0101
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/32440
dc.identifier.wosWOS:A1996VH83600002
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titlePhospholipase A(2) - A structural reviewen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dspace.entity.typePublication
unesp.author.lattes9162508978945887[1]
unesp.author.orcid0000-0003-2460-1145[1]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt

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