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dc.contributor.authorCanduri, F.
dc.contributor.authorFadel, V
dc.contributor.authorBasso, L. A.
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorSantos, D. S.
dc.contributor.authorde Azevedo, W. F.
dc.date.accessioned2014-05-20T13:54:38Z
dc.date.available2014-05-20T13:54:38Z
dc.date.issued2005-02-18
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2004.12.052
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 327, n. 3, p. 646-649, 2005.
dc.identifier.issn0006-291X
dc.identifier.urihttp://hdl.handle.net/11449/19552
dc.description.abstractHuman purine nucleoside phosphorylase has been submitted to intensive structure-based design of inhibitors, most of them using low-resolution structures of human PNP. Recently, several structures of human PNP have been reported, which allowed redefinition of the active site and understanding of the structural basis for inhibition of PNP by acyclovir and immucillin-H. Based on previously solved human PNP structures, we proposed here a new catalytic mechanism for human PNP, which is supported by crystallographic studies and explains previously determined kinetic data. (C) 2004 Elsevier B.V. All rights reserved.en
dc.format.extent646-649
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.sourceWeb of Science
dc.subjectPNPpt
dc.subjectsynchrotron radiationpt
dc.subjectStructurept
dc.subjectdrug designpt
dc.titleNew catalytic mechanism for human purine nucleoside phosphorylaseen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionInstituto Butantan
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.description.affiliationUNESP, Dept Fis, Programa Posgraduacao Biofis Mol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationInst Butantan, Ctr Appl Toxinol, BR-05503900 São Paulo, Brazil
dc.description.affiliationUFRGS, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisas TB, BR-91501970 Porto Alegre, RS, Brazil
dc.description.affiliationUNESP, Inst Biosci, Dept Biol, Lab Struct Biol & Zoochem CEIS, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationPontif Univ Catolica Rio Grande Sul, Fac Farm, Inst Pesquisas Biomed, Porto Alegre, RS, Brazil
dc.description.affiliationUnespUNESP, Dept Fis, Programa Posgraduacao Biofis Mol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP, Inst Biosci, Dept Biol, Lab Struct Biol & Zoochem CEIS, BR-13506900 Rio Claro, SP, Brazil
dc.identifier.doi10.1016/j.bbrc.2004.12.052
dc.identifier.wosWOS:000226674800003
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Rio Claropt
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt
dc.identifier.lattes2835029061696580
unesp.author.lattes2835029061696580
unesp.author.orcid0000-0003-0903-2407[3]
unesp.author.orcid0000-0001-6368-8955[2]
unesp.author.orcid0000-0003-4971-463X[5]
unesp.author.orcid0000-0002-7363-8211[4]
dc.relation.ispartofjcr2.559
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