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Article

Role of presenilin in gamma-secretase cleavage of amyloid precursor protein.

Experimental gerontology - 1 Jul 2000

Xia W

Abstract excerpt

Cerebral accumulation of the amyloid beta-protein (Abeta) is an early and invariant event in the pathogenesis of Alzheimer's disease (AD). Mutations in the presenilin (PS) 1 and 2 genes that increase production of the highly amyloidogenic Abeta(42) are the most common cause of familial AD. Deletion of PS1 in mice reduces Abeta generation, indicating that PS1 mediates the last step in the generation of Abeta from...

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Source

Identifiers

PMID: 10959033
DOI: 10.1016/s0531-5565(00)00111-x

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Role of presenilin in gamma-secretase cleavage of amyloid precursor protein.PMID 10959033Read ↗

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A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activity.Semantic proximity Read ↗

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis.Semantic proximity Read ↗

Presenilin 1 mutations activate gamma 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch.Semantic proximity Read ↗

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Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch.Semantic proximity Read ↗

Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.Semantic proximity Read ↗

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