Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados BJMBR (3) Biol. Res. (1) Autor Berry,C. (1) DANILA,CRISTINA I (1) Delmar,M. (1) Ek-Vitorin,J.F. (1) Favoreto Jr.,S. (1) Ferreira,A.T. (1) HAMILTON,SUSAN L (1) Manque,P.M. (1) Rush,P. (1) Taffet,S.M. (1) Touyz,R.M. (1) Yahuaca,P. (1) Yoshida,N. (1) Mais... Palavra-chave Protein kinase (4) Angiotensin receptors (1) Calcium response (1) Cell invasion (1) Connexin (1) FK506-binding protein (1) Metacyclic trypomastigotes (1) Phospholipase (1) Phosphorylation (1) Phosphorylation site (1) Phosphotransferases (1) Reactive oxygen species (1) Ryanodine receptor (1) Second messengers (1) Ser-2809/Ser-2843 (1) Signal transduction (1) Trypanosoma cruzi (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Journal article (1) Ano 2004 (1) 2002 (1) 2000 (2) País Brazil (3) Chile (1) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Identification of a protein kinase activity that phosphorylates connexin43 in a pH-dependent manner BJMBR Yahuaca,P.; Ek-Vitorin,J.F.; Rush,P.; Delmar,M.; Taffet,S.M.. The carboxyl-terminal (CT) domain of connexin43 (Cx43) has been implicated in both hormonal and pH-dependent gating of the gap junction channel. An in vitro assay was utilized to determine whether the acidification of cell extracts results in the activation of a protein kinase that can phosphorylate the CT domain. A glutathione S-transferase (GST)-fusion protein was bound to Sephadex beads and used as a target for protein kinase phosphorylation. A protein extract produced from sheep heart was allowed to bind to the fusion protein-coated beads. The bound proteins were washed and then incubated with 32P-ATP. Phosphorylation was assessed after the proteins were resolved by SDS-PAGE. Incubation at pH 7.5 resulted in a minimal amount of phosphorylation while... Tipo: Info:eu-repo/semantics/article Palavras-chave: Connexin; Phosphorylation; Phosphotransferases; Protein kinase. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000400005 Phosphorylation of Ryanodine Receptors Biol. Res. DANILA,CRISTINA I; HAMILTON,SUSAN L. Both cardiac and skeletal muscle ryanodine receptors (RyRs) are parts of large complexes that include a number of kinases and phosphatases. These RyRs have several potential phosphorylation sites in their cytoplasmic domains, but the functional consequences of phosphorylation and the identity of the enzymes responsible have been subjects of considerable controversy. Hyperphosphorylation of Ser-2809 in RyR2 (cardiac isoform) and Ser-2843 in RyR1 (skeletal isoform) has been suggested to cause the dissociation of the FK506-binding protein (FKBP) from RyRs, producing "leaky channels," but some laboratories find no relationship between phosphorylation and FKBP binding. Also debated is the identity of the kinases that phosphorylate these serines: cAMP-dependent... Tipo: Journal article Palavras-chave: Ryanodine receptor; Phosphorylation site; Protein kinase; Ser-2809/Ser-2843; FK506-binding protein. Ano: 2004 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400005 Recent advances in angiotensin II signaling BJMBR Touyz,R.M.; Berry,C.. Angiotensin II (Ang II)* is a multifunctional hormone that influences the function of cardiovascular cells through a complex series of intracellular signaling events initiated by the interaction of Ang II with AT1 and AT2 receptors. AT1 receptor activation leads to cell growth, vascular contraction, inflammatory responses and salt and water retention, whereas AT2 receptors induce apoptosis, vasodilation and natriuresis. These effects are mediated via complex, interacting signaling pathways involving stimulation of PLC and Ca2+ mobilization; activation of PLD, PLA2, PKC, MAP kinases and NAD(P)H oxidase, and stimulation of gene transcription. In addition, Ang II activates many intracellular tyrosine kinases that play a role in growth signaling and... Tipo: Info:eu-repo/semantics/article Palavras-chave: Angiotensin receptors; Second messengers; Phospholipase; Protein kinase; Reactive oxygen species. Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000900001 Signal transduction induced in Trypanosoma cruzi metacyclic trypomastigotes during the invasion of mammalian cells BJMBR Yoshida,N.; Favoreto Jr.,S.; Ferreira,A.T.; Manque,P.M.. Penetration of Trypanosoma cruzi into mammalian cells depends on the activation of the parasite's protein tyrosine kinase and on the increase in cytosolic Ca2+ concentration. We used metacyclic trypomastigotes, the T. cruzi developmental forms that initiate infection in mammalian hosts, to investigate the association of these two events and to identify the various components of the parasite signal transduction pathway involved in host cell invasion. We have found that i) both the protein tyrosine kinase activation, as measured by phosphorylation of a 175-kDa protein (p175), and Ca2+ mobilization were induced in the metacyclic forms by the HeLa cell extract but not by the extract of T. cruzi-resistant K562 cells; ii) treatment of parasites with the tyrosine... Tipo: Info:eu-repo/semantics/article Palavras-chave: Trypanosoma cruzi; Signal transduction; Metacyclic trypomastigotes; Protein kinase; Calcium response; Cell invasion. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000300003 Registros recuperados: 4 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco