Three-dimensional structure of human γ-secretase.
Beijing, China. In Nature, Sep 2014
Aberrant cleavage of the amyloid precursor protein (APP) results in aggregation of amyloid-β, which accumulates in the brain and consequently causes Alzheimer's disease.
Complex regulation of γ-secretase: from obligatory to modulatory subunits.
New York City, United States. In Front Aging Neurosci, 2013
γ-Secretase is a four subunit, 19-pass transmembrane enzyme that cleaves amyloid precursor protein (APP), catalyzing the formation of amyloid beta (Aβ) peptides that form amyloid plaques, which contribute to Alzheimer's disease (AD) pathogenesis.
Structural origin of polymorphism of Alzheimer's amyloid β-fibrils.
Los Angeles, United States. In Biochem J, 2012
propose that the strength of inter-strand side-chain interactions determines the degree of beta-sheet twist, which then leads to the different association patterns between different cross beta-units and thus distinct fibril morphologies
Down's syndrome and Alzheimer's disease: towards secondary prevention.
More papers using
Trenton, United States. In Nat Rev Drug Discov, 2012
[review] Based on the apparent common pathogenic role of amyloid precursor protein in both Down's syndrome and Alzheimer's disease (AD), the idea that the dementia associated with Down's syndrome is in fact AD is supported on many levels.
Immune effects of cocoa procyanidin oligomers on peripheral blood mononuclear cells
In Genes and immunity, 2006
... For transcript stabilization studies, cells in X-VIVO were treated with APP (Apple PolyR, Littleton, CO, USA) at 54μg/mL, recombinant human TNFα (PeproTech, Rocky Hill, NJ, USA) at 50ng/mL, recombinant bovine TNFα (Thermo Scientific, Waltham, MA), PC1 (Phytolab, ...