Expression, purification, and circular dichroism analysis of human CDK9

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dc.contributor.authorLeopoldino, A. M.
dc.contributor.authorCanduri, F.
dc.contributor.authorCabral, H.
dc.contributor.authorJunqueira, M.
dc.contributor.authorMarqui, A, B. T. de
dc.contributor.authorApponi, L. H.
dc.contributor.authorda Fonseca, I. O.
dc.contributor.authorDomont, G. B.
dc.contributor.authorSantos, D. S.
dc.contributor.authorValentini, S.
dc.contributor.authorBonilla-Rodriguez, G. O.
dc.contributor.authorFossey, Marcelo Andrés [UNESP]
dc.contributor.authorAzevedo, W. F. de
dc.contributor.authorTajara, E. H.
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de Mato Grosso do Sul (UFMS)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.date.accessioned2014-05-20T13:24:36Z
dc.date.available2014-05-20T13:24:36Z
dc.date.issued2006-06-01
dc.description.abstractThe human cyclin-dependent kinase 9 (CDK9) protein was expressed in E coli BL21 using the pET23a vector at 30 degrees C. Several milligrams of protein were purified from soluble fraction using ionic exchange and ATP-affinity chromatography. The structural quality of recombinant CDK9 and the estimation of its secondary structure were obtained by circular dichroism. Structural models of CDK9 presented 26% of helices in agreement with the spectra by circular dichroism analysis. This is the first report on human CDK9 expression in Escherichia coli and structure analysis and provides the first step for the development of CDK9 inhibitors. (c) 2006 Elsevier B.V. All rights reserved.en
dc.description.affiliationFac Med Sao Jose do Rio Preto, Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUniv Fed Mato Grosso do Sul, Campo Grande, RS, Brazil
dc.description.affiliationUniv Estadual Paulista, São Paulo, Brazil
dc.description.affiliationUniv Fed Rio de Janeiro, Rede Proteom Rio, Rio de Janeiro, RJ, Brazil
dc.description.affiliationUNESP, Fac Ciências Farmaceut, Araraquara, SP, Brazil
dc.description.affiliationPUCRS, Ctr Pesquisas Biol Mol & Func, Porto Alegre, RS, Brazil
dc.description.affiliationPUCRS, Fac Biociencias, Porto Alegre, RS, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, São Paulo, Brazil
dc.description.affiliationUnespUNESP, Fac Ciências Farmaceut, Araraquara, SP, Brazil
dc.format.extent614-620
dc.identifierhttp://dx.doi.org/10.1016/j.pep.2006.02.012
dc.identifier.citationProtein Expression and Purification. San Diego: Academic Press Inc. Elsevier B.V., v. 47, n. 2, p. 614-620, 2006.
dc.identifier.doi10.1016/j.pep.2006.02.012
dc.identifier.issn1046-5928
dc.identifier.lattes4101562077663619
dc.identifier.urihttp://hdl.handle.net/11449/7685
dc.identifier.wosWOS:000238277000034
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofProtein Expression and Purification
dc.relation.ispartofjcr1.338
dc.relation.ispartofsjr0,648
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectCDK9pt
dc.subjectCâncerpt
dc.subjectAIDSpt
dc.subjectStructurept
dc.subjectdichroism analysispt
dc.subjectmolecular modelingpt
dc.subjectexpressionpt
dc.titleExpression, purification, and circular dichroism analysis of human CDK9en
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes4101562077663619
unesp.author.orcid0000-0002-2012-388X[12]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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