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	Provedor de dados BJMBR (1) BJM (1) Genet. Mol. Biol. (1) Autor Carneiro,F.A. (1) Da Poian,A.T. (1) Ferreira Filho,Edivaldo X. (1) Firmino,Alexandre A.P. (1) Kumar,Rahul (1) Nejatizadeh,Azim (1) Pasha,Mohammad Qadar (1) Ricart,Carlos A.O. (1) Sousa,Marcelo V. (1) Stauffer,F. (1) Stobdanand,Tsering (1) Ulhoa,Cirano J. (1) Mais... Palavra-chave G protein (3) CAMP (1) Chitinase (1) Fusion proteins (1) GNB3 C825T polymorphism (1) Glycoprotein (1) Hypertension (1) Membrane fusion (1) N-acetylglucosaminidase (1) Plasma electrolytes (1) Rhabdovirus (1) Trichoderma (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Ano 2011 (1) 2005 (1) 2002 (1) País Brazil (3) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Association of GNB3 C825T polymorphism with plasma electrolyte balance and susceptibility to hypertension Genet. Mol. Biol. Nejatizadeh,Azim; Kumar,Rahul; Stobdanand,Tsering; Pasha,Mohammad Qadar. The role of G-protein activation in cardiovascular disorders is well-known. G-protein β3 subunit (GNB3) C825T polymorphism is associated with increased intracellular signal transduction. We investigated the role of the variant in plasma sodium and potassium concentrations and association with hypertension. 345 healthy controls and 455 patients with essential hypertension were enrolled. Plasma renin activity and aldosterone concentration were measured. The variant, typed by SNaPshot, was analyzed on an ABI Prism 3100 Genetic Analyzer and GeneScan. The TT genotype and T allele were over-represented in the patients (p < 0.001, p < 0.0001). Multiple-logistic regression disclosed that the risk of hypertension was significantly greater for TT (p <... Tipo: Info:eu-repo/semantics/article Palavras-chave: GNB3 C825T polymorphism; Hypertension; G protein; Plasma electrolytes. Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572011000400004 Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins? BJMBR Da Poian,A.T.; Carneiro,F.A.; Stauffer,F.. Enveloped viruses always gain entry into the cytoplasm by fusion of their lipid envelope with a cell membrane. Some enveloped viruses fuse directly with the host cell plasma membrane after virus binding to the cell receptor. Other enveloped viruses enter the cells by the endocytic pathway, and fusion depends on the acidification of the endosomal compartment. In both cases, virus-induced membrane fusion is triggered by conformational changes in viral envelope glycoproteins. Two different classes of viral fusion proteins have been described on the basis of their molecular architecture. Several structural data permitted the elucidation of the mechanisms of membrane fusion mediated by class I and class II fusion proteins. In this article, we review a number of... Tipo: Info:eu-repo/semantics/article Palavras-chave: Membrane fusion; Fusion proteins; Rhabdovirus; G protein; Glycoprotein. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000600002 Involvement of G proteins and cAMP in the production of chitinolytic enzymes by Trichoderma harzianum BJM Firmino,Alexandre A.P.; Ulhoa,Cirano J.; Sousa,Marcelo V.; Ferreira Filho,Edivaldo X.; Ricart,Carlos A.O.. The effect of G protein modulators and cyclic AMP (cAMP) on N-acetylglucosaminidase (NAGase) production was investigated during 84 h of growth of a Trichoderma harzianum strain in chitin-containing medium. Caffeine (5 mM), N6--2'-O-dibutyryladenosine 3'5'-cyclic monophosphate sodium salt (dBcAMP) (1 mM) and 3-isobutyl-1-methylxanthine (IBMX) (2 mM) decreased extracellular NAGase activity by 80%, 77% and 37%, respectively. AlCl3/KF (100 µM/10 mM and 200 µM/ 20 mM) decreased the activity by 85% and 95%, respectively. Cholera (10 µ/mL) and pertussis (20 µ/mL) toxins also affected NAGase activity, causing a decrease of approximately 75%. Upon all treatments, protein bands of approximately 73 kDa, 68 kDa and 45 kDa had their signals diminished whilst a 50 kDa... Tipo: Info:eu-repo/semantics/article Palavras-chave: Trichoderma; N-acetylglucosaminidase; Chitinase; CAMP; G protein. Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822002000200015 Registros recuperados: 3 Primeira ... 1 ... Última

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