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-β42 Interacts Mainly with Insoluble Prion Protein in the Alzheimer Brain

11 Mar 2011

Abstract excerpt

The prion protein (PrP) is best known for its association with prion diseases. However, a controversial new role for PrP in Alzheimer disease (AD) has recently emerged. In vitro studies and mouse models of AD suggest that PrP may be involved in AD pathogenesis through a highly specific interaction with amyloid-β (Aβ42) oligomers. Immobilized recombinant human PrP (huPrP) also exhibited high affinity and...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Prion Diseases and Protein Misfolding
Share to Trace Elements in Health

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21393248
DOI: 10.1074/jbc.m110.199356

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Amyloid-β42 Interacts Mainly with Insoluble Prion Protein in the Alzheimer BrainPMID 21393248Read ↗

Antibody against Small Aggregated Peptide Specifically Recognizes Toxic Aβ-42 Oligomers in Alzheimer’s DiseaseSemantic proximity Read ↗

Prion Protein Interactome: Identifying Novel Targets in Slowly and Rapidly Progressive Forms of Alzheimer’s DiseaseSemantic proximity Read ↗

An Aβ42 variant that inhibits intra- and extracellular amyloid aggregation and enhances cell viability.Semantic proximity Read ↗

„APP family member dimeric complexes are formed predominantly in synaptic compartments“Semantic proximity Read ↗

Tau oligomers impair memory and synaptic plasticity through the cellular prion proteinSemantic proximity Read ↗

Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopySemantic proximity Read ↗

Prion-like seeding and nucleation of intracellular amyloid-βSemantic proximity Read ↗

Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease?Semantic proximity Read ↗

A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling.Semantic proximity Read ↗

Intraneuronal APP/A beta trafficking and plaque formation in beta-amyloid precursor protein and presenilin-1 transgenic mice.Semantic proximity Read ↗

Amyloid imaging in distinguishing atypical prion disease from Alzheimer disease.Semantic proximity Read ↗

A Specific Enzyme-Linked Immunosorbent Assay for Measuring β-Amyloid Protein Oligomers in Human Plasma and Brain Tissue of Patients With Alzheimer DiseaseSemantic proximity Read ↗

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