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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/66932
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dc.contributor.authorFilgueira de Azevedo Jr., Walter-
dc.contributor.authorCanduri, Fernanda-
dc.contributor.authorFreitas da Silveira, Nelson José-
dc.date.accessioned2014-05-27T11:20:29Z-
dc.date.accessioned2016-10-25T18:17:52Z-
dc.date.available2014-05-27T11:20:29Z-
dc.date.available2016-10-25T18:17:52Z-
dc.date.issued2002-07-08-
dc.identifierhttp://dx.doi.org/10.1016/S0006-291X(02)00266-8-
dc.identifier.citationBiochemical and Biophysical Research Communications, v. 293, n. 1, p. 566-571, 2002.-
dc.identifier.issn0006-291X-
dc.identifier.urihttp://hdl.handle.net/11449/66932-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/66932-
dc.description.abstractFlavopiridol has been shown to potently inhibit CDK1 and 2 (cyclin-dependent kinases 1 and 2) and most recently it has been found that it also inhibits CDK9. The complex CDK9-cyclin T1 controls the elongation phase of transcription by RNA polymerase II. The present work describes a molecular model for the binary complex CDK9-flavopiridol. This structural model indicates that the inhibitor strongly binds to the ATP-binding pocket of CDK9 and the structural comparison of the complex CDK2-flavopiridol correlates the structural differences with differences in inhibition of these CDKs by flavopiridol. This structure opens the possibility of testing new inhibitor families, in addition to new substituents for the already known leading structures such as flavones and adenine derivatives. © 2002 Elsevier Science (USA). All rights reserved.en
dc.format.extent566-571-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectBioinformatics-
dc.subjectCDK-
dc.subjectDrug design-
dc.subjectFlavopiridol-
dc.subjectStructure-
dc.subject2,6 diamino 4 cyclohexylmethoxy 5 nitrosopyrimidine-
dc.subject6 n (3,3 dimethylallyl)adenine-
dc.subject6 o cyclohexylmethylguanine-
dc.subjectadenine derivative-
dc.subjectadenosine triphosphate-
dc.subjectcyclin dependent kinase-
dc.subjectcyclin dependent kinase 2-
dc.subjectcyclin dependent kinase 9-
dc.subjectcyclin T1-
dc.subjectdechloroflavopiridol-
dc.subjectenzyme inhibitor-
dc.subjectflavone derivative-
dc.subjectflavopiridol-
dc.subjecthymenialdisine-
dc.subjectindirubin-
dc.subjectolomoucine-
dc.subjectpkfo 49 38-
dc.subjectpurvalanol B-
dc.subjectroscovitine-
dc.subjectstaurosporine-
dc.subjectu 55-
dc.subjectunclassified drug-
dc.subjectcorrelation analysis-
dc.subjectdrug potency-
dc.subjectdrug protein binding-
dc.subjectdrug structure-
dc.subjectenzyme inhibition-
dc.subjectIC 50-
dc.subjectmolecular model-
dc.subjectpriority journal-
dc.subjectstructure activity relation-
dc.subjectstructure analysis-
dc.subjectAmino Acid Sequence-
dc.subjectCyclin-Dependent Kinase 9-
dc.subjectCyclin-Dependent Kinases-
dc.subjectEnzyme Inhibitors-
dc.subjectFlavonoids-
dc.subjectModels, Molecular-
dc.subjectMolecular Sequence Data-
dc.subjectPiperidines-
dc.subjectProtein Conformation-
dc.subjectSequence Alignment-
dc.subjectSequence Homology, Amino Acid-
dc.titleStructural basis for inhibition of cyclin-dependent kinase 9 by flavopiridolen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationDepartamento de Física IBILCE UNESP, Sao Jose do Rio Preto, SP 15054-000-
dc.description.affiliationUnespDepartamento de Física IBILCE UNESP, Sao Jose do Rio Preto, SP 15054-000-
dc.identifier.doi10.1016/S0006-291X(02)00266-8-
dc.identifier.wosWOS:000175514700086-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofBiochemical and Biophysical Research Communications-
dc.identifier.scopus2-s2.0-0036295220-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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