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

Mutant PrPSc conformers induced by a synthetic peptide and several prion strains.

Journal of virology - 1 Feb 2004

Tremblay Patrick, Ball Haydn L, Kaneko Kiyotoshi, Groth Darlene, Hegde Ramanujan S, Cohen Fred E, DeArmond Stephen J, Prusiner Stanley B, Safar Jiri G

Abstract excerpt

Gerstmann-Sträussler-Scheinker (GSS) disease is a dominantly inherited, human prion disease caused by a mutation in the prion protein (PrP) gene. One mutation causing GSS is P102L, denoted P101L in mouse PrP (MoPrP). In a line of transgenic mice denoted Tg2866, the P101L mutation in MoPrP produced neurodegeneration when expressed at high levels. MoPrP(Sc)(P101L) was detected both by the conformation-dependent...

Read the complete abstract on PubMed

Topics

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

Share to PrPSc Proteins
Share to Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gerstmann-Straussler-Scheinker Disease

Share to Peptides

Share to Prion Diseases

Share to Prions

Share to Protein Conformation

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 14747574
DOI: 10.1128/jvi.78.4.2088-2099.2004
PMCID: PMC369494

Genes

GSS

Variants

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

Mutant PrPSc conformers induced by a synthetic peptide and several prion strains.PMID 14747574Read ↗

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

Transmissibility of Gerstmann-Sträussler-Scheinker syndrome in rodent models: New insights into the molecular underpinnings of prion infectivity.Semantic proximity Read ↗

Genetic and infectious prion diseases.Semantic proximity Read ↗

Phenotypic heterogeneity in inherited prion disease (P102L) is associated with differential propagation of protease-resistant wild-type and mutant prion protein.Semantic proximity Read ↗

Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171.Semantic 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 ↗

A single amino acid alteration (101L) introduced into murine PrP dramatically alters incubation time of transmissible spongiform encephalopathy.Semantic proximity Read ↗

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

Prion strain-dependent differences in conversion of mutant prion proteins in cell culture.Semantic proximity Read ↗

Mouse prion protein polymorphism Phe-108/Val-189 affects the kinetics of fibril formation and the response to seeding: evidence for a two-step nucleation polymerization mechanism.Semantic proximity Read ↗

Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice.Semantic proximity Read ↗

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

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