Title: Presenilins and γ-Secretase: Structure, Function, and Role in Alzheimer Disease
Authors: De Strooper, Bart
Iwatsubo, Takeshi
Wolfe, Michael S # ×
Issue Date: Jan-2012
Publisher: Cold Spring Harbor Laboratory Press
Series Title: Cold Spring Harbor Perspectives in Medicine vol:2 issue:1 pages:a006304-na
Article number: a006304
Abstract: Presenilins were first discovered as sites of missense mutations responsible for early-onset Alzheimer disease (AD). The encoded multipass membrane proteins were subsequently found to be the catalytic components of γ-secretases, membrane-embedded aspartyl protease complexes responsible for generating the carboxyl terminus of the amyloid β-protein (Aβ) from the amyloid protein precursor (APP). The protease complex also cleaves a variety of other type I integral membrane proteins, most notably the Notch receptor, signaling from which is involved in many cell differentiation events. Although γ-secretase is a top target for developing disease-modifying AD therapeutics, interference with Notch signaling should be avoided. Compounds that alter Aβ production by γ-secretase without affecting Notch proteolysis and signaling have been identified and are currently at various stages in the drug development pipeline.
ISSN: 2157-1422
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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