Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Cell signaling abnormalities may drive neurodegeneration in familial Alzheimer disease.

Neurochemical research - 1 Jan 2014

Robakis Nikolaos K

Abstract excerpt

Presenilins (PSs) are catalytic components of the γ-secretase complex that produces Aβ peptides. Substrates of γ-secretase are membrane-bound protein fragments deriving from the cleavage of extracellular sequence of cell surface proteins. APP-derived γ-secretase substrates are cleaved at gamma (γ) sites to produce Aβ while cleavage at the epsilon (ε) site produces AICD proposed to function in transcription. In...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alzheimer Disease
Share to Amyloid Precursor Protein Secretases
Share to APP gene

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Predisposition to Disease

Share to Mutation

Share to Presenilins

Share to Signal Transduction

Source

Open in PubMed Open full text

Identifiers

PMID: 23436150
DOI: 10.1007/s11064-013-1003-6
PMCID: PMC3718870

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cell signaling abnormalities may drive neurodegeneration in familial Alzheimer disease.PMID 23436150Read ↗

Allelic interference: a mechanism for trans-dominant transmission of loss of function in the neurodegeneration of familial Alzheimer's disease.Semantic proximity Read ↗

Evidence For and Against a Pathogenic Role of Reduced γ-Secretase Activity in Familial Alzheimer's Disease.Semantic proximity Read ↗

Presenilin, γ-Secretase, and the Search for Pathogenic Triggers of Alzheimer's Disease.Semantic proximity Read ↗

Qualitative changes in human γ-secretase underlie familial Alzheimer's disease.Semantic proximity Read ↗

Major carboxyl terminal fragments generated by γ-secretase processing of the Alzheimer amyloid precursor are 50 and 51 amino acids long.Semantic proximity Read ↗

γ-Secretase Modulators and APH1 Isoforms Modulate γ-Secretase Cleavage but Not Position of ε-Cleavage of the Amyloid Precursor Protein (APP).Semantic proximity Read ↗

Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's diseaseSemantic proximity Read ↗

Identification of the role of presenilins beyond Alzheimer's disease.Semantic proximity Read ↗

The mechanism of γ‐Secretase dysfunction in familial Alzheimer diseaseSemantic proximity Read ↗

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

Pathogenic Aβ generation in familial Alzheimer's disease: novel mechanistic insights and therapeutic implications.Semantic proximity Read ↗

gamma-secretases: from cell biology to therapeutic strategies.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.