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

Major carboxyl terminal fragments generated by γ-secretase processing of the Alzheimer amyloid precursor are 50 and 51 amino acids long.

The American journal of geriatric psychiatry : official journal of the American Association for Geriatric Psychiatry - 1 May 2013

Pinnix Inga, Ghiso Jorge A, Pappolla Miguel A, Sambamurti Kumar

Abstract excerpt

OBJECTIVES: To understand the cleavage of the amyloid β protein (Aβ) precursor (APP) by γ-secretase and to determine its changes in a representative familial Alzheimer disease (FAD) mutation. METHODS: Transfected cells expressing wild-type and FAD mutant APP were analyzed for changes in the levels of the major secreted Aβ species and of the corresponding intracellular C-terminal APP fragments (APP intracellular...

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-Peptides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amyloid beta-Protein Precursor

Share to Amyloid Precursor Protein Secretases

Share to CHO Cells

Share to Cricetulus

Share to Peptide Fragments

Share to Presenilin-1

Source

Open in PubMed Open full text

Identifiers

PMID: 23570890
DOI: 10.1016/j.jagp.2013.02.009
PMCID: PMC3740189

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Major carboxyl terminal fragments generated by γ-secretase processing of the Alzheimer amyloid precursor are 50 and 51 amino acids long.PMID 23570890Read ↗

Familial Alzheimer's disease mutations in amyloid protein precursor alter proteolysis by γ-secretase to increase amyloid β-peptides of ≥45 residues.Semantic proximity Read ↗

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

Characterization of intermediate steps in amyloid beta (Aβ) production under near-native conditions.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 ↗

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

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

Presenilin-1 Familial Alzheimer Mutations Impair γ-Secretase Cleavage of APP Through Stabilized Enzyme-Substrate Complex Formation.Semantic proximity Read ↗

Familial Alzheimer's disease mutations inhibit gamma-secretase-mediated liberation of beta-amyloid precursor protein carboxy-terminal fragment.Semantic proximity Read ↗

Familial Alzheimer Mutations in Presenilin-1 Decrease APP Substrate Proteolysis by γ-Secretase via Stable Enzyme-Substrate Complex FormationSemantic proximity Read ↗

Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's diseaseSemantic proximity Read ↗

Genes and mechanisms involved in beta-amyloid generation and Alzheimer's disease.Semantic proximity Read ↗

Analysis of Non-Amyloidogenic Mutations in APP Supports Loss of Function Hypothesis of Alzheimer's Disease.Semantic proximity Read ↗

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