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

Analysis of alteration of p75NTR processing and signalling by PS2 mutation and gamma-secretase inhibition.

Neurobiology of disease - 1 Sept 2007

Ito Yoshio, Ishii Azusa, Passmore A Peter, McIlroy Stephen P

Abstract excerpt

The presenilins (PSs) were identified as causative genes in cases of early-onset familial Alzheimer's disease (AD) and current evidence indicates that PSs are part of the gamma-secretase complex responsible for proteolytic processing of type I membrane proteins. p75NTR, a common neurotrophin receptor, was shown to be subject to gamma-secretase processing. However, it is not clear if the p75NTR downstream signal...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid Precursor Protein Secretases
Share to Cell Line, Tumor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoblotting

Share to Mutation

Share to Presenilin-2

Share to Receptor, Nerve Growth Factor

Share to rhoA GTP-Binding Protein

Share to Signal Transduction

Source

Identifiers

PMID: 17582777
DOI: 10.1016/j.nbd.2007.05.002

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

Analysis of alteration of p75NTR processing and signalling by PS2 mutation and gamma-secretase inhibition.PMID 17582777Read ↗

Differential expression and modulation of presenilin-1 and presenilin-2 in neural cell linesSemantic proximity Read ↗

Familial Alzheimer's disease presenilin 1 mutation M146V increases gamma secretase cutting of p75NTR in vitro.Semantic proximity Read ↗

Endoproteolysis of presenilin in vitro: inhibition by gamma-secretase inhibitors.Semantic proximity Read ↗

gamma-cleavage-independent functions of presenilin, nicastrin, and Aph-1 regulate cell-junction organization and prevent tau toxicity in vivo.Semantic proximity Read ↗

Presenilins and the gamma-secretase: still a complex problem.Semantic proximity Read ↗

Mutational analysis of intrinsic regions of presenilin 2 that determine its endoproteolytic cleavage and pathological function.Semantic proximity Read ↗

Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms.Semantic proximity Read ↗

Pen-2 is essential for γ-secretase complex stability and trafficking but partially dispensable for endoproteolysis.Semantic proximity Read ↗

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

Divergent consequences of PSEN1 knockout and PSEN2 knockout in stem cell derived models of the brainSemantic proximity Read ↗

In silico phosphoproteomic analysis reveals divergent regulation of Presenilin 1 and Presenilin 2Semantic proximity Read ↗

Interactome analyses of mature γ-secretase complexes reveal distinct molecular environments of presenilin (PS) paralogs and preferential binding of signal peptide peptidase to PS2.Semantic proximity Read ↗

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