Nsp5
Mostrando 25-36 de 87 artigos, teses e dissertações.
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25. Production, protein and oil content in soybean grain: heritabilities, correlations and selection of superior genotypes / Produção, conteúdo de proteína e óleo no grão da soja: herdabilidades, correlações e seleção de genótipos superiores
O desenvolvimento de procedimentos de melhoramento mais eficientes dependem de um melhor entendimento do padrão de herança e do tipo de ação gênica envolvidas no controle de características de interesse. Desta forma, no sentido de melhor entender o controle genético de características de interesse, em uma população de soja do programa de melhoramen
Publicado em: 2006
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26. The Genus Cyclospora (Apicomplexa: Eimeriidae), with a description of Cyclospora schneideri n.sp. in the snake Anilius scytale scytale (Aniliidae) from Amazonian Brazil: a review
A review is made of the recorded species of the coccidian genus Cyclospora and major events leading up to the discovery of C. cayetanensis, which is responsible for serious outbreaks of diarrhoea in man and is one of the aetiological agents of "traveller's diarrhoea". Humans appear to be the specific hosts, with the entire life-cycle in the intestine: to dat
Memórias do Instituto Oswaldo Cruz. Publicado em: 2005-04
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27. VariaÃÃo temporal da meiofauna e da nematofauna em uma Ãrea mediolitorÃnea da bacia do Pina (Pernambuco, Brasil)
The basin of Pina has been studied for many years in order to check the level of organic pollutants. Many rivers are discharged in this basin bringing a big amount of pollutants to it. This affects the quality of organisms fished by the poor population that lives in the neighborhood. Up to now thereâs only one studie on meiofauna, specifically on nematofaun
Publicado em: 2003
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28. The N- and C-Terminal Regions of Rotavirus NSP5 Are the Critical Determinants for the Formation of Viroplasm-Like Structures Independent of NSP2
Molecular events and the interdependence of the two rotavirus nonstructural proteins, NSP5 and NSP2, in producing viroplasm-like structures (VLS) were previously evaluated by using transient cellular coexpression of the genes for the two proteins, and VLS domains as well as the NSP2-binding region of NSP5 were mapped in the context of NSP2. Review of the pre
American Society for Microbiology.
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29. In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms.
NSP5 (NS26), the product of rotavirus gene 11, is a phosphoprotein whose role in the virus replication cycle is unknown. To gain further insight into its function, we obtained monoclonal antibodies against the baculovirus-expressed protein. By immunoprecipitation and immunoblotting experiments, we showed that (i) NSP5 appears in many different phosphorylated
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30. Analysis of Rotavirus Nonstructural Protein NSP5 Phosphorylation
The rotavirus nonstructural phosphoprotein NSP5 is encoded by a gene in RNA segment 11. Immunofluorescence analysis of fixed cells showed that NSP5 polypeptides remained confined to viroplasms even at a late stage when provirions migrated from these structures. When NSP5 was expressed in COS-7 cells in the absence of other viral proteins, it was uniformly di
American Society for Microbiology.
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31. RNA-Binding Activity of the Rotavirus Phosphoprotein NSP5 Includes Affinity for Double-Stranded RNA
Phosphoprotein NSP5 is a component of replication intermediates that catalyze the synthesis of the segmented double-stranded RNA (dsRNA) rotavirus genome. To study the role of the protein in viral replication, His-tagged NSP5 was expressed in bacteria and purified by affinity chromatography. In vitro phosphorylation assays showed that NSP5 alone contains min
American Society for Microbiology.
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32. Rotavirus NSP5: Mapping Phosphorylation Sites and Kinase Activation and Viroplasm Localization Domains
Rotavirus NSP5 is a nonstructural protein that localizes in cytoplasmic viroplasms of infected cells. NSP5 interacts with NSP2 and undergoes a complex posttranslational hyperphosphorylation, generating species with reduced polyacrylamide gel electrophoresis mobility. This process has been suggested to be due in part to autophosphorylation. We developed an in
American Society for Microbiology.
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33. Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
The rotavirus nonstructural protein NSP5, a product of the smallest genomic RNA segment, is a phosphoprotein containing O-linked N-acetylglucosamine. We investigated the phosphorylation of NSP5 in monkey MA104 cells infected with simian rotavirus SA11. Immunoprecipitated NSP5 was analyzed with respect to phosphorylation and protein kinase activity. After met
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34. Uncoupling substrate and activation functions of rotavirus NSP5: Phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation
Rotavirus NSP5 is a nonstructural protein that localizes in viroplasms of virus-infected cells. NSP5 interacts with NSP2 and undergoes a complex posttranslational hyperphosphorylation, generating species with reduced PAGE mobility. Here we show that NSP5 operates as an autoregulator of its own phosphorylation as a consequence of two distinct activities of th
National Academy of Sciences.
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35. Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine protease.
The C-terminal half of the replicase ORF1a polyprotein of the arterivirus equine arteritis virus is processed by a chymotrypsinlike serine protease (SP) (E. J. Snijder et al., J. Biol. Chem. 271:4864-4871, 1996) located in nonstructural protein 4 (nsp4). Three probable SP cleavage sites had previously been identified in the ORF1a protein. Their proteolysis e
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36. Rotavirus Nonstructural Protein NSP5 Interacts with Major Core Protein VP2
Rotavirus is a nonenveloped virus with a three-layered capsid. The inner layer, made of VP2, encloses the genomic RNA and two minor proteins, VP1 and VP3, with which it forms the viral core. Core assembly is coupled with RNA viral replication and takes place in definite cellular structures termed viroplasms. Replication and encapsidation mechanisms are still
American Society for Microbiology.