968 resultados para BINDS


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Pós-graduação em Microbiologia - IBILCE

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Pós-graduação em Ciências Biológicas (Genética) - IBB

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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The production of a dictionary always generates controversy about decisions to be taken by the lexicographer. They are based – a priori – in previous theoretical and methodological choices. What we mean by dictionary? Why making certain choices rather than others? How to reconcile (if there is a reconciliation) the different approaches to describe the lexicon? The objective here is to contribute with theoretical and methodological reflections related to the Juruna Lexicography (Yudjá), as well as for lexicographical studies camp. This text addresses critical points of dictionaries production processes – if we may so call it – the history of the act of making a dictionary, so we can discuss choices to be taken to the entries of verbs in the Juruna-Portuguese bilingual dictionary assembly provided as a long term project result, in which some collaborators are working, including community’s indigenous. The work contains sections that will raise historical and linguistic discussions about the compilation of a dictionary and how this act binds to the applicability for the subjects that use this instrument firming / mobilizer of the lexicon visions. The focus here will be to discuss the verbs entries in the Juruna dictionary (stemming), taking lexicographical history as a contributor to certain choices of dictionaries production nowadays, whether for mother tongue, for foreign language, specialized lexicons, semantic groups, and systematizations for languages that are starting/beginning a first publication of dictionaries

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Kaposi´s sarcoma associated herpesvirus (KSHV) or human herpesvirus 8 (HHV-8) is a gammaherpesvirus essential for the development of all forms of Kaposi´s sarcoma (KS). The KSHV’s life cycle is basically divided into latent and lytic phases, which have distinct viral gene expression profiles. Some important oncogenic products of KSHV are expressed during the lytic phase, including the viral K1 protein. As an effect of interfer-ence with intracellular signaling, K1 expression increases proliferation and survival of KSHV-infected cells. Due to its high level of genetic variability compared to other re-gions of the viral genome, the K1-encoding ORF (ORF-K1) is commonly evaluated for KSHV genotyping. It remains unclear whether different viral genotypes have particular biological effects that might modify the KSHV oncogenicity. The present study aimed to contribute to the establishment of an experimental in vitro model for evaluation of the K1 protein from common KSHV genotypes. Recombinant expression vectors with the ORF-K1 from KSHV genotypes A, B and C were prepared by genetic cloning. The recombi-nant vectors pKSHVOK1 obtained by cloning were sequenced for structural validation. After that, HEK293 cell line was transfected with the recombinant vectors, and proteins were extracted for expression analysis by Western blot technique, for K1 functional vali-dation. Results showed that ORF-K1 vectors containing KSHV ORF-K1 from the A, B and C genotypes were produced and structurally validated by DNA sequencing. The K1 expression at the protein level was also confirmed by immunoblots using an antibody for FLAG detection, an epitope from the vector that binds to K1. Based on presented re-sults, it´s possible to conclude that the recombinant vectors will be able to be used in future studies of K1 protein biological properties from distinct KSHV genotypes

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The award-winning and controversial movie by Pedro Almodóvar “The skin I live” (2011) is an adaptation of Mygale’s novel (1984), the French writer Thierry Jonquet (1954-2009), translated into Portuguese in 2005 as Tarântula. It is a horror story, full of suspense, in which a renowned surgeon, Robert Ledgard, played by Antonio Banderas, switches, without any scruples, the sex of the young Vincent. What it shown to the viewer since the first images of the movie is, therefore, Vicente/Vera in her new and perfect female body. Flashbacks clarify during the movie the events that culminated in the opening scene that is presented to us, surprising us and, of course, shocking us. References to myths and symbols can be noticed in the movie. They bring with them, to be recognized by the viewer, issues related to the creation or metamorphosis, among others, as the Pygmalion and Galatea myth, which binds to artistic creation. Artistic metamorphosis operated equally by the filmmaker in his modern version of the doctor and the monster, for example, but, especially, in the rereading of the Jonquet’s novel. This study seeks to highlight some of the major myths and symbols inserted in Almódovar’s movie and what interpretations such insertions may ensue.

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Eukaryotic translation initiation factor 5A (eIF5A) is the only cellular protein that contains the polyamine-modified lysine, hypusine [Nε-(4-amino-2-hydroxybutyl)lysine]. Hypusine occurs only in eukaryotes and certain archaea, but not in eubacteria. It is formed post-translationally by two consecutive enzymatic reactions catalyzed by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). Hypusine modification is essential for the activity of eIF5A and for eukaryotic cell proliferation. eIF5A binds to the ribosome and stimulates translation in a hypusine-dependent manner, but its mode of action in translation is not well understood. Since quantities of highly pure hypusine-modified eIF5A is desired for structural studies as well as for determination of its binding sites on the ribosome, we have used a polycistronic vector, pST39, to express eIF5A alone, or to co-express human eIF5A-1 with DHS or with both DHS and DOHH in Escherichia coli cells, to engineer recombinant proteins, unmodified eIF5A, deoxyhypusine- or hypusine-modified eIF5A. We have accomplished production of three different forms of recombinant eIF5A in high quantity and purity. The recombinant hypusine-modified eIF5A was as active in methionyl-puromycin synthesis as the native, eIF5A (hypusine form) purified from mammalian tissue. The recombinant eIF5A proteins will be useful tools in future structure/function and the mechanism studies in translation.