Journal
COLD SPRING HARBOR PERSPECTIVES IN MEDICINE
Volume 2, Issue 1, Pages -Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/cshperspect.a006304
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Funding
- K.U. Leuven
- Flemisch government
- Fund for Scientific Research Flanders (FWO-V)
- Foundation for Alzheimer Research (SAO/FRMA)
- Belgian Federal Science Policy Office [IAPP6/43]
- Ministry of Education, Culture, Sports, Science, and Technology
- Core Research for Evolutional Science and Technology of Japan
- National Institutes of Health
- Alzheimer's Association
- American Health Assistance Foundation
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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 gamma-secretases, membrane-embedded aspartyl protease complexes responsible for generating the carboxyl terminus of theamyloid beta-protein (A beta) from the amyloid protein precursor (APP). The protease complex also cleaves a variety of other type I integralmembrane proteins, most notably the Notch receptor, signaling from which is involved in many cell differentiation events. Although gamma-secretase is a top target for developing disease-modifying AD therapeutics, interference with Notch signaling should be avoided. Compounds that alter A beta production by gamma-secretase without affecting Notch proteolysis and signaling have been identified and are currently at various stages in the drug development pipeline.
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