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

Presenilin-1-mediated retention of APP derivatives in early biosynthetic compartments.

Traffic (Copenhagen, Denmark) - 1 Mar 2006

Réchards Marloes, Xia Weiming, Oorschot Viola, van Dijk Suzanne, Annaert Willem, Selkoe Dennis J, Klumperman Judith

Abstract excerpt

Processing of the amyloid precursor protein (APP) leads to the production of amyloid-beta (Abeta), the major component of extracellular plaques in the brains of Alzheimer's disease (AD) patients. Presenilin-1 (PS-1) plays a key role in the final step of Abeta formation, the gamma-secretase cleavage. Previously, we showed that PS-1 is retained in pre-Golgi compartments by incorporation into COPI-coated membranes...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid beta-Peptides
Share to Amyloid beta-Protein Precursor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Embryo, Mammalian

Share to Endoplasmic Reticulum

Share to Endosomes

Share to Golgi Apparatus

Share to Microscopy, Immunoelectron

Share to Presenilin-1

Source

Identifiers

PMID: 16497228
DOI: 10.1111/j.1600-0854.2006.00388.x

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

Presenilin-1-mediated retention of APP derivatives in early biosynthetic compartments.PMID 16497228Read ↗

Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.Semantic proximity Read ↗

Presenilin 1 regulates the processing of beta-amyloid precursor protein C-terminal fragments and the generation of amyloid beta-protein in endoplasmic reticulum and Golgi.Semantic proximity Read ↗

Alzheimer's presenilin 1 modulates sorting of APP and its carboxyl-terminal fragments in cerebral neurons in vivo.Semantic proximity Read ↗

Advances in the cell biology of the trafficking and processing of amyloid precursor protein: impact of familial Alzheimer's disease mutations.Semantic proximity Read ↗

PS1 Affects the Pathology of Alzheimer's Disease by Regulating BACE1 Distribution in the ER and BACE1 Maturation in the Golgi Apparatus.Semantic proximity Read ↗

Presenilin 1 Regulates Membrane Homeostatic Pathways that are Dysregulated in Alzheimer’s DiseaseSemantic proximity Read ↗

Presenilin-1 mutations associated with familial Alzheimer's disease do not disrupt protein transport from the endoplasmic reticulum to the Golgi apparatus.Semantic proximity Read ↗

Mutant presenilin 1 increases the levels of Alzheimer amyloid beta-peptide Abeta42 in late compartments of the constitutive secretory pathway.Semantic proximity Read ↗

Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch.Semantic proximity Read ↗

Spatial-Temporal Mapping Reveals the Golgi as the Major Processing Site for the Pathogenic Swedish APP Mutation: Familial APP Mutant Shifts the Major APP Processing Site.Semantic proximity Read ↗

Trafficking and proteolytic processing of APP.Semantic proximity Read ↗

Presenilin 1 is involved in the maturation of beta-site amyloid precursor protein-cleaving enzyme 1 (BACE1).Semantic proximity Read ↗

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