Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein.

doi:10.1002/ana.22094

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

Community

Back to search

Article

Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein.

Annals of neurology - 1 Aug 2010

Zou Wen-Quan, Puoti Gianfranco, Xiao Xiangzhu, Yuan Jue, Qing Liuting, Cali Ignazio, Shimoji Miyuki, Langeveld Jan P M, Castellani Rudy, Notari Silvio, Crain Barbara, Schmidt Robert E, Geschwind Michael, Dearmond Stephen J, Cairns Nigel J, Dickson Dennis, Honig Lawrence, Torres Juan Maria, Mastrianni James, Capellari Sabina, Giaccone Giorgio, Belay Ermias D, Schonberger Lawrence B, Cohen Mark, Perry George, Kong Qingzhong, Parchi Piero, Tagliavini Fabrizio, Gambetti Pierluigi

Abstract excerpt

OBJECTIVE: The objective of the study is to report 2 new genotypic forms of protease-sensitive prionopathy (PSPr), a novel prion disease described in 2008, in 11 subjects all homozygous for valine at codon 129 of the prion protein (PrP) gene (129VV). The 2 new PSPr forms affect individuals who are either homozygous for methionine (129MM) or heterozygous for methionine/valine (129MV). METHODS: Fifteen affected...

Read the complete abstract on PubMed

Topics

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

Share to Aged, 80 and over

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Brain

Share to Dementia

Share to DNA Mutational Analysis

Share to Genetic Testing

Share to Peptide Hydrolases

Share to Prion Diseases

Share to Prions

Source

Open in PubMed Open full text

Identifiers

PMID: 20695009
DOI: 10.1002/ana.22094
PMCID: PMC3032610

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein.PMID 20695009Read ↗

Variably protease-sensitive prionopathy, a unique prion variant with inefficient transmission properties.Semantic proximity Read ↗

Variably protease-sensitive prionopathy: a novel disease of the prion protein.Semantic proximity Read ↗

Phenotypic Heterogeneity of Variably Protease-Sensitive Prionopathy: A Report of Three Cases Carrying Different Genotypes at PRNP Codon 129.Semantic proximity Read ↗

Search for a genetic cause of variably protease-sensitive prionopathySemantic proximity Read ↗

A novel form of human disease with a protease-sensitive prion protein and heterozygosity methionine/valine at codon 129: Case report.Semantic proximity Read ↗

Phenotypic variability of sporadic human prion disease and its molecular basis: past, present, and future.Semantic proximity Read ↗

Variably protease-sensitive prionopathy in a PRNP codon 129 heterozygous UK patient with co-existing tau, α synuclein and Aβ pathology.Semantic proximity Read ↗

A novel human disease with abnormal prion protein sensitive to protease.Semantic proximity Read ↗

The first case of protease-sensitive prionopathy (PSPr) in The Netherlands: a patient with an unusual GSS-like clinical phenotype.Semantic proximity Read ↗

Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease.Semantic proximity Read ↗

Type 1 protease resistant prion protein and valine homozygosity at codon 129 of PRNP identify a subtype of sporadic Creutzfeldt-Jakob disease.Semantic proximity Read ↗

Characterization of Variably Protease-Sensitive Prionopathy by Capillary ElectrophoresisSemantic proximity Read ↗

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