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

The presenilin proteins are components of multiple membrane-bound complexes that have different biological activities.

The Journal of biological chemistry - 23 Jul 2004

Gu Yongjun, Sanjo Nobuo, Chen Fusheng, Hasegawa Hiroshi, Petit Agnes, Ruan Xueying, Li Wenping, Shier Cortney, Kawarai Toshitaka, Schmitt-Ulms Gerold, Westaway David, St George-Hyslop Peter, Fraser Paul E

Abstract excerpt

Several lines of evidence have indicated that the presenilin proteins function within macromolecular complexes and are necessary for the regulated intramembranous proteolysis of certain type 1 transmembrane proteins, including the amyloid precursor protein, Notch, and p75. Data from multiple complementary experiments now suggest that there may be several distinct presenilin complexes. We show here that presenilin...

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 Aspartic Acid Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Detergents

Share to Endopeptidases

Share to Macromolecular Substances

Share to Neuroglia

Share to Peptide Hydrolases

Share to Presenilin-1

Source

Identifiers

PMID: 15123598
DOI: 10.1074/jbc.M401548200

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

The presenilin proteins are components of multiple membrane-bound complexes that have different biological activities.PMID 15123598Read ↗

Intramembrane proteolysis by gamma-secretase.Semantic proximity Read ↗

Different cofactor activities in gamma-secretase assembly: evidence for a nicastrin-Aph-1 subcomplex.Semantic proximity Read ↗

Presenilins mutated at Asp-257 or Asp-385 restore Pen-2 expression and Nicastrin glycosylation but remain catalytically inactive in the absence of wild type Presenilin.Semantic proximity Read ↗

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

Intramembrane proteolysis by presenilin and presenilin-like proteases.Semantic proximity Read ↗

The presenilins.Semantic proximity Read ↗

Presenilin-1 D257A and D385A mutants fail to cleave Notch in their endoproteolyzed forms, but only presenilin-1 D385A mutant can restore its gamma-secretase activity with the compensatory overexpression of normal C-terminal fragment.Semantic proximity Read ↗

Mutation analysis of the presenilin 1 N-terminal domain reveals a broad spectrum of gamma-secretase activity toward amyloid precursor protein and other substrates.Semantic proximity Read ↗

Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a component of the gamma-secretase complex.Semantic proximity Read ↗

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

Alzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Semantic proximity Read ↗

Polar transmembrane-based amino acids in presenilin 1 are involved in endoplasmic reticulum localization, Pen2 protein binding, and γ-secretase complex stabilization.Semantic proximity Read ↗

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