The TryPIKinome of five human pathogenic trypanosomatids: Trypanosoma brucei, Trypanosoma cruzi, Leishmania major, Leishmania braziliensis and Leishmania infantum - New tools for designing specific inhibitors

dc.contributor.authorBahia, Diana [UNIFESP]
dc.contributor.authorOliveira, Luciana Marcia
dc.contributor.authorLima, Fabio Mitsuo [UNIFESP]
dc.contributor.authorOliveira, Priscila [UNIFESP]
dc.contributor.authorSilveira, Jose Franco da [UNIFESP]
dc.contributor.authorMortara, Renato Arruda [UNIFESP]
dc.contributor.authorRuiz, Jeronimo Conceicao
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionFiocruz MS
dc.date.accessioned2016-01-24T13:59:00Z
dc.date.available2016-01-24T13:59:00Z
dc.date.issued2009-12-18
dc.description.abstractPhosphatidylinositol (PI) kinases are at the heart of one of the major pathways of intracellular signal transduction. Herein, we present the first report on a survey made by similarity searches against the five human pathogenic trypanosomatids Trypanosoma brucei, Trypanosoma cruzi, Leishmania major, Leishmania braziliensis and Leishmania infantum genomes available to date for phosphatidylinositol- and related-kinases (TryPIKs). in addition to generating a panel called the TryPIKinome, we propose a model of signaling pathways for these TryPIKs. the involvement of TryPIKs in fundamental pathways, such as intracellular signal transduction and host invasion processes, makes the study of TryPIKs an important area for further inquiry. New subtype-specific inhibitors are expected to work on individual members of the PIK family and, therefore, can presumably neutralize trypanosomatid invasion processes. (C) 2009 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, São Paulo, Brazil
dc.description.affiliationFiocruz MS, Ctr Pesquisas Rene Rachou, BR-30190002 Belo Horizonte, MG, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIDFAPESP: JP3 07/50551-2
dc.format.extent963-970
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2009.10.086
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 390, n. 3, p. 963-970, 2009.
dc.identifier.doi10.1016/j.bbrc.2009.10.086
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/32022
dc.identifier.wosWOS:000272516700112
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsAcesso restrito
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectPhosphatidylinositol kinasesen
dc.subjectPhosphatidylinositol-related kinasesen
dc.subjectTrypanosomatidsen
dc.subjectInhibitorsen
dc.titleThe TryPIKinome of five human pathogenic trypanosomatids: Trypanosoma brucei, Trypanosoma cruzi, Leishmania major, Leishmania braziliensis and Leishmania infantum - New tools for designing specific inhibitorsen
dc.typeArtigo
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