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

Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family.

Biochemistry - 24 Feb 1998

Grunberg J, Walter J, Loetscher H, Deuschle U, Jacobsen H, Haass C

Abstract excerpt

Mutations in the presenilin (PS) genes are linked to early onset familial Alzheimer's disease (FAD). PS-1 proteins are proteolytically processed by an unknown protease leading to the formation of two stable fragments of approximately 30 and approximately 20 kDa [Thinakaran, G., et al. (1996) Neur...

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 Base Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Line

Share to DNA Primers

Share to Membrane Proteins

Share to Mutation

Share to Polymerase Chain Reaction

Source

Identifiers

PMID: 9485372
DOI: 10.1021/bi972106l

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-9485372-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family.PMID 9485372Read ↗

Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease.Semantic proximity Read ↗

Endoproteolytic Processing and Stabilization of Wild-type and Mutant PresenilinSemantic proximity Read ↗

Processing of wild-type and mutant familial Alzheimer's disease-associated presenilin-1 in cultured neurons.Semantic proximity Read ↗

Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.Semantic proximity Read ↗

Staurosporine‐Induced Activation of Caspase‐3 Is Potentiated by Presenilin 1 Familial Alzheimer's Disease Mutations in Human Neuroglioma CellsSemantic proximity Read ↗

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis.Semantic proximity Read ↗

Recent insights on the pro-apoptotic phenotype elicited by presenilin 2 and its caspase and presenilinase-derived fragments.Semantic proximity Read ↗

[Molecular basics of Alzheimer's disease].Semantic proximity Read ↗

Alternative, non-secretase processing of Alzheimer's beta-amyloid precursor protein during apoptosis by caspase-6 and -8.Semantic proximity Read ↗

Two Novel Mutations in the First Transmembrane Domain of Presenilin1 Cause Young-Onset Alzheimer's Disease.Semantic proximity Read ↗

The role of caspases in Alzheimer’s disease; potential novel therapeutic opportunitiesSemantic proximity Read ↗

Presenilin-1 mutation activates the signaling pathway of caspase-4 in endoplasmic reticulum stress-induced apoptosis.Semantic proximity Read ↗

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