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Article

APP intracellular domain formation and unaltered signaling in the presence of familial Alzheimer's disease mutations.

Experimental cell research - 1 Jul 2003

Bergman Anna, Religa Dorota, Karlström Helena, Laudon Hanna, Winblad Bengt, Lannfelt Lars, Lundkvist Johan, Näslund Jan

Abstract excerpt

One of the cardinal neuropathological findings in brains from Alzheimer's disease (AD) patients is the occurrence of amyloid beta-peptide (Abeta) deposits. The gamma-secretase-mediated intramembrane proteolysis event generating Abeta also results in the release of the APP intracellular domain (AICD), which may mediate nuclear signaling. It was recently shown that AICD starts at a position distal to the site...

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Source

Identifiers

PMID: 12799176
DOI: 10.1016/s0014-4827(03)00117-4

Genes

APP

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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.

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APP intracellular domain formation and unaltered signaling in the presence of familial Alzheimer's disease mutations.PMID 12799176Read ↗

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alpha-secretase mediated conversion of the amyloid precursor protein derived membrane stub C99 to C83 limits Abeta generation.Semantic proximity Read ↗

High content analysis of gamma-secretase activity reveals variable dominance of presenilin mutations linked to familial Alzheimer's disease.Semantic proximity Read ↗

Cellular functions of the amyloid precursor protein from development to dementia.Semantic proximity Read ↗

Familial Alzheimer's disease mutations inhibit gamma-secretase-mediated liberation of beta-amyloid precursor protein carboxy-terminal fragment.Semantic proximity Read ↗

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