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

Protease-sensitive conformers in broad spectrum of distinct PrPSc structures in sporadic Creutzfeldt-Jakob disease are indicator of progression rate.

PLoS pathogens - 1 Sept 2011

Kim Chae, Haldiman Tracy, Cohen Yvonne, Chen Wei, Blevins Janis, Sy Man-Sun, Cohen Mark, Safar Jiri G

Abstract excerpt

The origin, range, and structure of prions causing the most common human prion disease, sporadic Creutzfeldt-Jakob disease (sCJD), are largely unknown. To investigate the molecular mechanism responsible for the broad phenotypic variability of sCJD, we analyzed the conformational characteristics of protease-sensitive and protease-resistant fractions of the pathogenic prion protein (PrP(Sc)) using novel...

Read the complete abstract on PubMed

Topics

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

Share to Creutzfeldt-Jakob Syndrome
Share to Methionine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nonlinear Dynamics

Share to Peptide Hydrolases

Share to Prion Proteins

Share to Prions

Share to PrPSc Proteins

Share to Valine

Source

Open in PubMed Open full text

Identifiers

PMID: 21931554
DOI: 10.1371/journal.ppat.1002242
PMCID: PMC3169556

Genes

PRNP

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

Protease-sensitive conformers in broad spectrum of distinct PrPSc structures in sporadic Creutzfeldt-Jakob disease are indicator of progression rate.PMID 21931554Read ↗

Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions.Semantic proximity Read ↗

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

Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects.Semantic proximity Read ↗

Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes.Semantic proximity Read ↗

Two-dimensional mapping of three phenotype-associated isoforms of the prion protein 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 ↗

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

Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions.Semantic proximity Read ↗

Distinct glycoform ratios of protease resistant prion protein associated with PRNP point mutations.Semantic proximity Read ↗

Biochemical fingerprints of prion diseases: scrapie prion protein in human prion diseases that share prion genotype and type.Semantic proximity Read ↗

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

Molecular classification of sporadic Creutzfeldt-Jakob disease.Semantic proximity Read ↗

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