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

Prion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.

The Journal of biological chemistry - 28 Aug 2015

Kraus Allison, Anson Kelsie J, Raymond Lynne D, Martens Craig, Groveman Bradley R, Dorward David W, Caughey Byron

Abstract excerpt

Human prion diseases can have acquired, sporadic, or genetic origins, each of which results in the conversion of prion protein (PrP) to transmissible, pathological forms. The genetic prion disease Gerstmann-Straussler-Scheinker syndrome can arise from point mutations of prolines 102 or 105. However, the structural effects of these two prolines, and mutations thereof, on PrP misfolding are not well understood....

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Endopeptidase K

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Prions

Share to Proline

Share to Protein Denaturation

Share to PrPSc Proteins

Share to Scrapie

Share to Spectroscopy, Fourier Transform Infrared

Source

Open in PubMed Open full text

Identifiers

PMID: 26175152
DOI: 10.1074/jbc.M115.665844
PMCID: PMC4571877

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Prion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.PMID 26175152Read ↗

PrP P102L and Nearby Lysine Mutations Promote Spontaneous In Vitro Formation of Transmissible Prions.Semantic proximity Read ↗

Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.Semantic proximity Read ↗

Allelic origin of protease-sensitive and protease-resistant prion protein isoforms in Gerstmann-Sträussler-Scheinker disease with the P102L mutation.Semantic proximity Read ↗

A novel PRNP-P105S mutation associated with atypical prion disease and a rare PrPSc conformation.Semantic proximity Read ↗

A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.Semantic proximity Read ↗

Identifying key components of the PrPC-PrPSc replicative interface.Semantic proximity Read ↗

Prion propagation is dependent on key amino acids in Charge cluster 2 within the prion proteinSemantic proximity Read ↗

Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.Semantic proximity Read ↗

Increasing prion propensity by hydrophobic insertion.Semantic proximity Read ↗

A novel Gerstmann-Sträussler-Scheinker disease mutation defines a precursor for amyloidogenic 8 kDa PrP fragments and reveals N-terminal structural changes shared by other GSS alleles.Semantic proximity Read ↗

Role of N-terminal familial mutations in prion protein fibrillization and prion amyloid propagation in vitro.Semantic proximity Read ↗

Characterization of a Novel Prion Protein Mutation of Serine to Proline at Residue 245 Linked to VPSPr-like PK-Resistant PrPScSemantic proximity Read ↗

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