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	Provedor de dados Biol. Res. (4) Autor INESTROSA,NIBALDO C (4) CHACÓN,MARCELO A (1) GONZALEZ-BILLAUL,CHRISTIAN (1) OPAZO,CARLOS (1) RUIZ,FRANCISCA H (1) SANTOS,MANUEL J (1) TOLEDO,ENRIQUE M (1) VARELA-NALLAR,LORENA (1) Mais... Palavra-chave Alzheimer’s Disease (1) Amyloid fibrils (1) Aß peptide (1) Copper (1) Copper reduction (1) HSPG (1) Heparin (1) MRE (1) Oxidative damage (1) Prion protein (1) Prnp (1) Mais... Tipo do documento Journal article (4) Ano 2011 (1) 2006 (1) 2003 (1) 2000 (1) País Chile (4) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Contributions by researchers of "Ciencia de Frontera" of the Chilean Academy of Sciences Biol. Res. GONZALEZ-BILLAUL,CHRISTIAN; INESTROSA,NIBALDO C; SANTOS,MANUEL J. Tipo: Journal article Ano: 2011 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602011000100001 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 The functional links between prion protein and copper Biol. Res. VARELA-NALLAR,LORENA; TOLEDO,ENRIQUE M; CHACÓN,MARCELO A; INESTROSA,NIBALDO C. Prion diseases are fatal neurodegenerative disorders associated with the conversion of the cellular prion protein (PrPC) into a pathologic isoform. Although the physiological function of PrPC remains unknown, evidence relates PrPC to copper metabolism and oxidative stress as suggested by its copper-binding properties in the N-terminal octapeptide repeat region. This region also reduces copper ions in vitro, and this reduction ability is associated with the neuroprotection exerted by the octarepeat region against copper in vivo. In addition, the promoter region of the PrPC gene contains putative metal response elements suggesting it may be regulated by heavy metals. Here we address some of the evidence that support a physiological link between PrPC and... Tipo: Journal article Palavras-chave: Prion protein; Copper; Heparin; HSPG; Prnp; MRE. Ano: 2006 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000100005 EL APORTE DE LUCO A LA NEUROCIENCIA CHILENA Biol. Res. INESTROSA,NIBALDO C. Tipo: Journal article Ano: 2003 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000200003 Registros recuperados: 4 Primeira ... 1 ... Última

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