Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados Biol. Res. (1) BJMBR (1) Autor Heremans,K. (1) INESTROSA,NIBALDO C (1) OPAZO,CARLOS (1) RUIZ,FRANCISCA H (1) Palavra-chave Amyloid fibrils (2) Alzheimer’s Disease (1) Aß peptide (1) Copper reduction (1) High pressure (1) Oxidative damage (1) Protein dynamics (1) Stability diagram (1) Thermodynamics (1) Unfolding (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Journal article (1) Ano 2005 (1) 2000 (1) País Brazil (1) Chile (1) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state Biol. Res. OPAZO,CARLOS; RUIZ,FRANCISCA H; INESTROSA,NIBALDO C. Alzheimer’s disease (AD) is characterized by the deposition of amyloid b-peptide (Aß) and neuronal degeneration in brain regions involved in learning and memory. One of the leading etiologic hypotheses regarding AD is the involvement of free radical-mediated oxidative stress in neuronal degeneration. Recent evidence suggests that metals concentrated in amyloid deposits may contribute to the oxidative insults observed in AD-affected brains. We hypothesized that Aß peptide in the presence of copper enhances its neurotoxicity generating free radicals via copper reduction. In the present study, we have examined the effect of the aggregation state of amyloid-ß-peptide on copper reduction. In independent experiments we measured the copper-reducing ability of... Tipo: Journal article Palavras-chave: Aß peptide; Amyloid fibrils; Copper reduction; Oxidative damage; Alzheimer’s Disease. Ano: 2000 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602000000200012 Protein dynamics: hydration and cavities BJMBR Heremans,K.. The temperature-pressure behavior of proteins seems to be unique among the biological macromolecules. Thermodynamic as well as kinetic data show the typical elliptical stability diagram. This may be extended by assuming that the unfolded state gives rise to volume and enthalpy-driven liquid-liquid transitions. A molecular interpretation follows from the temperature and the pressure dependence of the hydration and cavities. We suggest that positron annihilation spectroscopy can provide additional quantitative evidence for the contributions of cavities to the dynamics of proteins. Only mature amyloid fibrils that form from unfolded proteins are very resistant to pressure treatment. Tipo: Info:eu-repo/semantics/article Palavras-chave: Stability diagram; Thermodynamics; High pressure; Unfolding; Amyloid fibrils; Protein dynamics. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800002 Registros recuperados: 2 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