## Abstract For Abstract see ChemInform Abstract in Full Text.
Identity and function of γ-secretase
✍ Scribed by W. Taylor Kimberly; Michael S. Wolfe
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 184 KB
- Volume
- 74
- Category
- Article
- ISSN
- 0360-4012
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
γ‐Secretase catalyzes intramembrane proteolysis of various type I membrane proteins, including the amyloid‐β precursor protein and the Notch receptor. Despite its importance in the pathogenesis of Alzheimer's disease and to normal development, this protease has eluded identification until only very recently. Four membrane proteins are now known to be members of the protease complex: presenilin, nicastrin, aph‐1, and pen‐2. Recent findings suggest that these four proteins are sufficient to reconstitute the active γ‐secretase complex and that together they mediate the cell surface signaling of a variety of receptors via intramembrane proteolysis. © 2003 Wiley‐Liss, Inc.
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## Abstract The γ‐secretase complex has emerged as an unusual membrane‐bound aspartyl protease with the ability to cleave certain substrate proteins at peptide bonds believed to be buried within the hydrophobic environment of the lipid bilayer. This cleavage is responsible for a key biochemical ste
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