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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleOverexpression And Characterization Of The C-terminal Domain Of Human Siva1, A Proapoptotic Factor And Cytoskeleton Binding Protein.pt_BR
dc.contributor.authorDantas, Larissa E Cpt_BR
dc.contributor.authorSaad, Sara T Opt_BR
dc.contributor.authorRamos, Carlos H Ipt_BR
dc.contributor.authorBénichou, Sergept_BR
unicamp.authorSara T O Saad, Hemocentro, Faculty of Medical Sciences at University of Campinas, Rua Carlos Chagas, 480pt_BR
unicamp.authorCampinas, São Paulo, Brasil. sara@unicamp.br.pt_BR
unicamp.author.externalLarissa E C Dantas,pt
unicamp.author.externalCidade Universitária Zeferino Vazpt
unicamp.author.external13083-878pt
unicamp.author.externalCarlos H I Ramos,pt
unicamp.author.externalSerge Bénichou,pt
dc.description.abstractSiva1 protein interacts with tumor protein p53 and with the member of the tumor necrosis factor receptor superfamily, stathmin, among others. These proteins are related to several pathways involved in cancer and are therefore strong candidate targets for drug design. This study aimed to characterize the biophysical properties of Siva 1 C- terminal domain to contribute to the discovery of new target directed drugs. Siva1 protein interacts with tumor protein p53 and with the member of the tumor necrosis factor receptor superfamily, stathmin, among others. These proteins are related to several pathways involved in cancer and are therefore strong candidate targets for drug design. This study aimed to characterize the biophysical properties of Siva 1 C- terminal domain to contribute to the discovery of new target directed drugs. The C-terminus Siva1 domain (residues 84-175) was fused to glutathione Stransferase (GST) and expressed in an E coli system and the recombinant GST-Siva C-terminus was purified by GSTTagged Protein affinity and gel filtration chromatography. We tested the biological activity of the purified Siva Cterminus domain in a Jurkat extract cell line and found that the protein interacted with natural binders. Biophysical and biochemical assays have demonstrated monodispersion of the protein in solution with a predominant unfolded and elongated shape. However, at high concentrations, the protein showed a tendency to form soluble aggregates. These results are expected to lead to further progress in the understanding of Siva1 properties and target-directed drug design.en
dc.relation.ispartofProtein And Peptide Letterspt_BR
dc.relation.ispartofabbreviationProtein Pept. Lett.pt_BR
dc.date.issued2016pt_BR
dc.identifier.citationProtein And Peptide Letters. v. 23, n. 1, p. 43-50, 2016.pt_BR
dc.language.isoengpt_BR
dc.description.volume23pt_BR
dc.description.firstpage43-50pt_BR
dc.rightsfechadopt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn1875-5305pt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/26497317pt_BR
dc.date.available2016-05-23T19:39:44Z-
dc.date.accessioned2016-05-23T19:39:44Z-
dc.description.provenanceMade available in DSpace on 2016-05-23T19:39:44Z (GMT). No. of bitstreams: 1 pmed_26497317.pdf: 477516 bytes, checksum: dd422d2deac5520390e9d0ea21cb4d7f (MD5) Previous issue date: 2016en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/235122-
dc.identifier.idPubmed26497317pt_BR
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