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Presenilin structure, function and role in Alzheimer disease
journal contribution
posted on 2023-06-08, 09:11 authored by Paul E Fraser, Dun-Sheng Yang, Gang Yu, Lyne Lévesque, Masaki Nishimura, Shigeki Arawaka, Louise SerpellLouise Serpell, Ekaterina Rogaeva, Peter St George-HyslopNumerous missense mutations in the presenilins are associated with the autosomal dominant form of familial Alzheimer disease. Presenilin genes encode polytopic transmembrane proteins, which are processed by proteolytic cleavage and form high-molecular-weight complexes under physiological conditions. The presenilins have been suggested to be functionally involved in developmental morphogenesis, unfolded protein responses and processing of selected proteins including the ß-amyloid precursor protein. Although the underlying mechanism by which presenilin mutations lead to development of Alzheimer disease remains elusive, one consistent mutational effect is an overproduction of long-tailed amyloid ß-peptides. Furthermore, presenilins interact with ß-catenin to form presenilin complexes, and the physiological and mutational effects are also observed in the catenin signal transduction pathway.
History
Publication status
- Published
Journal
BBA - Molecular Basis of DiseaseISSN
0925-4439Publisher
ElsevierExternal DOI
Issue
1Volume
1502Department affiliated with
- Biochemistry Publications
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- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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