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

Amyloid beta precursor protein and prion protein have a conserved interaction affecting cell adhesion and CNS development.

PloS one - 1 Jan 2012

Kaiser Darcy M, Acharya Moulinath, Leighton Patricia L A, Wang Hao, Daude Nathalie, Wohlgemuth Serene, Shi Beipei, Allison W Ted

Abstract excerpt

Genetic and biochemical mechanisms linking onset or progression of Alzheimer Disease and prion diseases have been lacking and/or controversial, and their etiologies are often considered independent. Here we document a novel, conserved and specific genetic interaction between the proteins that underlie these diseases, amyloid-β precursor protein and prion protein, APP and PRP, respectively. Knockdown of APP and/or...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid beta-Protein Precursor
Share to Cell Adhesion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Central Nervous System

Share to Gene Knockdown Techniques

Share to Immunoprecipitation

Share to Morpholinos

Share to Prions

Share to Zebrafish

Source

Open in PubMed Open full text

Identifiers

PMID: 23236467
DOI: 10.1371/journal.pone.0051305
PMCID: PMC3517466

Genes

APP
PRNP

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

Amyloid beta precursor protein and prion protein have a conserved interaction affecting cell adhesion and CNS development.PMID 23236467Read ↗

Prion gene paralogs are dispensable for early zebrafish development and have nonadditive roles in seizure susceptibility.Semantic proximity Read ↗

Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesion.Semantic proximity Read ↗

PrPs: Proteins with a purpose: Lessons from the zebrafish.Semantic proximity Read ↗

Amyloid-β precursor protein mutant zebrafish exhibit seizure susceptibility that depends on prion protein.Semantic proximity Read ↗

Genetic dissection of the amyloid precursor protein in developmental function and amyloid pathogenesis.Semantic proximity Read ↗

Targeted mutation of the gene encoding prion protein in zebrafish reveals a conserved role in neuron excitability.Semantic proximity Read ↗

Amyloid precursor protein-b facilitates cell adhesion during early development in zebrafishSemantic proximity Read ↗

Knockdown of amyloid precursor protein in zebrafish causes defects in motor axon outgrowth.Semantic proximity Read ↗

Amyloid precursor protein-b facilitates cell adhesion during early development in zebrafish.Semantic proximity Read ↗

An ancient conserved role for prion protein in learning and memorySemantic proximity Read ↗

Drosophila models of prionopathies: insight into prion protein function, transmission, and neurotoxicity.Semantic proximity Read ↗

Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members.Semantic proximity Read ↗

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