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

Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region.

Current biology : CB - 3 Apr 2001

Perera W S, Hooper N M

Abstract excerpt

The neurodegenerative spongiform encephalopathies, or prion diseases, are characterized by the conversion of the normal cellular form of the prion protein PrP(C) to a pathogenic form, PrP(Sc) [1]. There are four copies of an octarepeat PHGG(G/S)WGQ that specifically bind Cu(2+) ions within the N-terminal half of PrP(C) [2--4]. This has led to proposals that prion diseases may, in part, be due to abrogation of the...

Read the complete abstract on PubMed

Topics

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

Share to Copper
Share to Endocytosis
Share to Prion Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Prions

Share to PrPC Proteins

Share to PrPSc Proteins

Share to Rodentia

Source

Identifiers

PMID: 11413003
DOI: 10.1016/s0960-9822(01)00147-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region.PMID 11413003Read ↗

The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions.Semantic proximity Read ↗

Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice.Semantic proximity Read ↗

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

The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion.Semantic proximity Read ↗

Genetic mapping of activity determinants within cellular prion proteins: N-terminal modules in PrPC offset pro-apoptotic activity of the Doppel helix B/B' region.Semantic proximity Read ↗

The Octarepeat Region of the Prion Protein Is Conformationally Altered in PrPScSemantic proximity Read ↗

Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism.Semantic proximity Read ↗

Both N-Terminal and C-Terminal Histidine Residues of the Prion Protein Are Essential for Copper Coordination and Neuroprotective Self-Regulation.Semantic proximity Read ↗

Copper and Zinc Interactions with Cellular Prion Proteins Change Solubility of Full-Length Glycosylated Isoforms and Induce the Occurrence of Heterogeneous Phenotypes.Semantic proximity Read ↗

Prion protein reduces both oxidative and non-oxidative copper toxicity.Semantic proximity Read ↗

Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes.Semantic proximity Read ↗

Effects of the pathological Q212P mutation on human prion protein non-octarepeat copper-binding site.Semantic proximity Read ↗

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