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

Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans.

Proceedings of the National Academy of Sciences of the United States of America - 1 May 2007

Yin Shaoman, Pham Nancy, Yu Shuiliang, Li Chaoyang, Wong Poki, Chang Binggong, Kang Shin-Chung, Biasini Emiliano, Tien Po, Harris David A, Sy Man-Sun

Abstract excerpt

Mutation in the prion gene PRNP accounts for 10-15% of human prion diseases. However, little is known about the mechanisms by which mutant prion proteins (PrPs) cause disease. Here we investigated the effects of 10 different pathogenic mutations on the conformation and ligand-binding activity of recombinant human PrP (rPrP). We found that mutant rPrPs react more strongly with N terminus-specific antibodies,...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Epitopes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosaminoglycans

Share to Mice, Transgenic

Share to Mutation

Share to Prions

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 17456603
DOI: 10.1073/pnas.0610827104
PMCID: PMC1863438

Genes

PRNP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans.PMID 17456603Read ↗

Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack.Semantic proximity Read ↗

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

The protease-sensitive N-terminal polybasic region of prion protein modulates its conversion to the pathogenic prion conformer.Semantic proximity Read ↗

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

A novel seven-octapeptide repeat insertion in the prion protein gene (PRNP) in a Dutch pedigree with Gerstmann-Sträussler-Scheinker disease phenotype: comparison with similar cases from the literature.Semantic proximity Read ↗

[Molecular bases of prion diseases].Semantic proximity Read ↗

Aggregation of prion protein with insertion mutations is proportional to the number of inserts.Semantic proximity Read ↗

Autoantibodies against the prion protein in individuals with PRNP mutations.Semantic proximity Read ↗

Mutations and polymorphisms in the prion protein gene.Semantic proximity Read ↗

N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases.Semantic proximity Read ↗

Autoantibodies against the prion protein in individuals with <i>PRNP</i> mutationsSemantic proximity Read ↗

Conformational conversion of prion protein in prion diseases.Semantic proximity Read ↗

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