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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleSir2-related Protein 1 From Leishmania Amazonensis Is A Glycosylated Nad +-dependent Deacetylasept_BR
dc.contributor.authorFessel M.R.pt_BR
dc.contributor.authorLira C.B.pt_BR
dc.contributor.authorGiorgio S.pt_BR
dc.contributor.authorRamos C.H.I.pt_BR
dc.contributor.authorCano M.I.N.pt_BR
unicamp.authorFessel, M.R., Chemistry Institute, University of Campinas UNICAMP, Campinas SP 13083-970, Brazilpt_BR
unicamp.authorGiorgio, S., Instituto de Biologia, Unicamp, Campinas, São Paulo, Brazilpt_BR
unicamp.authorRamos, C.H.I., Chemistry Institute, University of Campinas UNICAMP, Campinas SP 13083-970, Brazilpt_BR
unicamp.author.externalLira, C.B., Departamento de Genética, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho-UNESP, Botucatu, SP 18618-000, Brazilpt
unicamp.author.externalCano, M.I.N., Departamento de Genética, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho-UNESP, Botucatu, SP 18618-000, Brazilpt
dc.description.abstractSirtuin proteins form a family of NAD +-dependent protein deacetylases that are considered potential drug targets against parasites. Here, we present the first characterization of a sirtuin orthologue from Leishmania amazonensis, an aetiological agent of American tegumentary leishmaniasis that has been the subject of many studies focused in the development of therapeutic approaches. The protein has high sequence identity with other Kinetoplastid Silent information regulator 2 Related Protein 1 (Sir2RP1) and was named LaSir2RP1. The gene exists as a single copy, encoding a monomeric protein (LaSir2RP1) of approximately 41 kDa that has NAD +-dependent deacetylase activity. LaSir2RP1 was immunodetected in total protein extracts, in cytoplasmic granules, and in the secreted material of both promastigotes and lesion-derived amastigotes. Analysis of both lectin-affinity purified promastigote and amastigote extracts revealed the presence of a major enriched protein of approximately 66 kDa that was recognized by an anti-LaSir2RP1 serum, suggesting that a parasite sirtuin could be glycosylated in vivo. © 2011 Cambridge University Press.en
dc.relation.ispartofParasitologypt_BR
dc.date.issued2011pt_BR
dc.identifier.citationParasitology. , v. 138, n. 10, p. 1245 - 1258, 2011.pt_BR
dc.language.isoenpt_BR
dc.description.volume138pt_BR
dc.description.issuenumber10pt_BR
dc.description.firstpage1245pt_BR
dc.description.lastpage1258pt_BR
dc.rightsfechadopt_BR
dc.sourceScopuspt_BR
dc.identifier.issn311820pt_BR
dc.identifier.doi10.1017/S0031182011001077pt_BR
dc.identifier.urlhttp://www.scopus.com/inward/record.url?eid=2-s2.0-80053067069&partnerID=40&md5=2fee211a88b6d614ef66c0eaa420dc2bpt_BR
dc.date.available2015-06-30T20:21:21Z
dc.date.available2015-11-26T14:48:27Z-
dc.date.accessioned2015-06-30T20:21:21Z
dc.date.accessioned2015-11-26T14:48:27Z-
dc.description.provenanceMade available in DSpace on 2015-06-30T20:21:21Z (GMT). No. of bitstreams: 1 2-s2.0-80053067069.pdf: 1133343 bytes, checksum: e823353271c5dd821e3a00310a8d1823 (MD5) Previous issue date: 2011en
dc.description.provenanceMade available in DSpace on 2015-11-26T14:48:27Z (GMT). No. of bitstreams: 1 2-s2.0-80053067069.pdf: 1133343 bytes, checksum: e823353271c5dd821e3a00310a8d1823 (MD5) Previous issue date: 2011en
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/107665
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/107665-
dc.identifier.idScopus2-s2.0-80053067069pt_BR
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