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

Missense mutations associated with familial Alzheimer's disease in Sweden lead to the production of the amyloid peptide without internalization of its precursor.

Biochemical and biophysical research communications - 5 Jan 1996

Essalmani R, Macq A F, Mercken L, Octave J N

Abstract excerpt

Production of soluble amyloid peptide precursor (APP) and amyloid peptide (A beta) was measured in CHO cells transfected by the wild-type APP 695 cDNA sequence or by the same sequence carrying missense mutations associated with familial Alzheimer's disease in Sweden. Deletion of the C-terminal domain of the protein corresponding to residues 654 to 695 of APP 695 not only inhibited very significantly the...

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

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA Primers

Share to Gene Expression

Share to Molecular Sequence Data

Share to Mutation

Share to Polymerase Chain Reaction

Share to Restriction Mapping

Source

Identifiers

PMID: 8573182
DOI: 10.1006/bbrc.1996.0017

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Missense mutations associated with familial Alzheimer's disease in Sweden lead to the production of the amyloid peptide without internalization of its precursor.PMID 8573182Read ↗

The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway.Semantic proximity Read ↗

alpha-secretase mediated conversion of the amyloid precursor protein derived membrane stub C99 to C83 limits Abeta generation.Semantic proximity Read ↗

Intracellular accumulation of beta-amyloid in cells expressing the Swedish mutant amyloid precursor protein.Semantic proximity Read ↗

Increased generation of alternatively cleaved beta-amyloid peptides in cells expressing mutants of the amyloid precursor protein defective in endocytosis.Semantic proximity Read ↗

The Arctic mutation interferes with processing of the amyloid precursor protein.Semantic proximity Read ↗

Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor.Semantic proximity Read ↗

The E693Δ (Osaka) mutation in amyloid precursor protein potentiates cholesterol-mediated intracellular amyloid β toxicity via its impaired cholesterol efflux.Semantic proximity Read ↗

Increased beta-amyloid release and levels of amyloid precursor protein (APP) in fibroblast cell lines from family members with the Swedish Alzheimer's disease APP670/671 mutation.Semantic proximity Read ↗

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation.Semantic proximity Read ↗

Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the golgi apparatus.Semantic proximity Read ↗

Altered cleavage and secretion of a recombinant beta-APP bearing the Swedish familial Alzheimer's disease mutation.Semantic proximity Read ↗

Enhanced Release of Amyloid -Protein from Codon 670/671 Swedish Mutant -Amyloid Precursor Protein Occurs in Both Secretory and Endocytic PathwaysSemantic proximity Read ↗

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