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- W2034184423 abstract "Deposition of the amyloid-beta protein (Aβ) in the form of cerebral plaques is a defining pathological feature of Alzheimer's disease (AD), and all AD-causing genes identified to date affect Aβ production or deposition. For these reasons, the two proteases, β- and γ-secretases, that cut out Aβ from the amyloid-β precursor protein (APP) are considered important targets for the development of therapeutics for AD. AD-causing mutations in the presenilin genes alter γ-secretase activity, increasing production of the more deleterious 42-residue form of Aβ. Pharmacological profiling, site-directed mutagenesis, knockout studies, affinity labeling, and activity-dependent chromatography all strongly support the hypothesis that presenilin is an integral component of γ-secretase, a founding member of an emerging class of polytopic membrane proteases. γ-Secretase/presenilin also cleaves other proteins that are important for critical signaling events (the Notch family of receptors), raising concerns about mechanism-based toxicities that might arise as a consequence of inhibiting this protease. In light of these findings, the potential of γ-secretase vis-à-vis β-secretase as therapeutic targets for the prevention or treatment of AD will be discussed." @default.
- W2034184423 created "2016-06-24" @default.
- W2034184423 creator A5070207434 @default.
- W2034184423 date "2002-12-01" @default.
- W2034184423 modified "2023-10-17" @default.
- W2034184423 title "APP, Notch, and presenilin: molecular pieces in the puzzle of Alzheimer's disease" @default.
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- W2034184423 doi "https://doi.org/10.1016/s1567-5769(02)00179-0" @default.
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