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

Cleavage of amyloid precursor protein by an archaeal presenilin homologue PSH.

Proceedings of the National Academy of Sciences of the United States of America - 17 Mar 2015

Dang Shangyu, Wu Shenjie, Wang Jiawei, Li Hongbo, Huang Min, He Wei, Li Yue-Ming, Wong Catherine C L, Shi Yigong

Abstract excerpt

Aberrant cleavage of amyloid precursor protein (APP) by γ-secretase contributes to the development of Alzheimer's disease. More than 200 disease-derived mutations have been identified in presenilin (the catalytic subunit of γ-secretase), making modulation of γ-secretase activity a potentially att...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Amyloid beta-Protein Precursor
Share to Amyloid Precursor Protein Secretases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Archaea

Share to Molecular Sequence Data

Share to Presenilins

Share to Sequence Homology, Amino Acid

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 25733893
DOI: 10.1073/pnas.1502150112
PMCID: PMC4371958

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25733893-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cleavage of amyloid precursor protein by an archaeal presenilin homologue PSH.PMID 25733893Read ↗

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

Identification of a novel family of presenilin homologues.Semantic proximity Read ↗

Effects of transmembrane phenylalanine residues on γ-secretase-mediated Notch-1 proteolysisSemantic proximity Read ↗

Hydrophilic loop 1 of Presenilin-1 and the APP GxxxG transmembrane motif regulate γ-secretase function in generating Alzheimer-causing Aβ peptides.Semantic proximity Read ↗

Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.Semantic proximity Read ↗

Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase.Semantic proximity Read ↗

γ-Secretase modulators show selectivity for γ-secretase-mediated amyloid precursor protein intramembrane processing.Semantic proximity Read ↗

γ-Secretase structure and activity are modified by alterations in its membrane localization and ambient environment.Semantic proximity Read ↗

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

γ-Secretase-mediated endoproteolysis of neuregulin-1 and E-cadherinSemantic proximity Read ↗

Modulation of Gamma-Secretase for the Treatment of Alzheimer's DiseaseSemantic proximity Read ↗

APP, Notch, and presenilin: molecular pieces in the puzzle of Alzheimer's disease.Semantic proximity Read ↗

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