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

Aggregation of cellular prion protein is initiated by proximity-induced dimerization.

Journal of neurochemistry - 1 Aug 2007

Goggin Kevin, Bissonnette Cyntia, Grenier Catherine, Volkov Leonid, Roucou Xavier

Abstract excerpt

Prion diseases or transmissible spongiform encephalopathies (TSEs) are infectious and fatal neurodegenerative disorders in humans and animals. Pathological features of TSEs include the conversion of cellular prion protein (PrP(C)) into an altered disease-associated conformation generally designated PrP(Sc), abnormal deposition of PrP(Sc) aggregates, and spongiform degeneration of the brain. The molecular steps...

Read the complete abstract on PubMed

Topics

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

Share to Dimerization
Share to Endopeptidase K
Share to Glioma

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Microscopy, Electron, Transmission

Share to Neuroblastoma

Share to Prions

Share to Tacrolimus

Source

Open in PubMed Open full text

Identifiers

PMID: 17663754
DOI: 10.1111/j.1471-4159.2007.04611.x
PMCID: PMC2954962

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

Aggregation of cellular prion protein is initiated by proximity-induced dimerization.PMID 17663754Read ↗

Prions and Prion-like ProteinsSemantic proximity Read ↗

A Systems-Level Theoretical Framework for Prion Disease Resolution Through Coordinated Suppression, Clearance, Disaggregation, and Functional Protein ReplacementSemantic proximity Read ↗

In Vivo Generation of Neurotoxic Prion Protein: Role for Hsp70 in Accumulation of Misfolded IsoformsSemantic proximity Read ↗

Prion neurotoxicity: insights from prion protein mutants.Semantic proximity Read ↗

Prions.Semantic proximity Read ↗

Targeting prion-like protein spreading in neurodegenerative diseasesSemantic proximity Read ↗

Stress-protective signalling of prion protein is corrupted by scrapie prions.Semantic proximity Read ↗

Mutant prion protein-mediated aggregation of normal prion protein in the endoplasmic reticulum: implications for prion propagation and neurotoxicity.Semantic proximity Read ↗

Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion.Semantic proximity Read ↗

Ligands binding to the cellular prion protein induce its protective proteolytic release with therapeutic potential in neurodegenerative proteinopathiesSemantic proximity Read ↗

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

Neuroprotective and neurotoxic signaling by the prion protein.Semantic proximity Read ↗

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