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

PrP P102L and Nearby Lysine Mutations Promote Spontaneous In Vitro Formation of Transmissible Prions.

Journal of virology - 1 Nov 2017

Kraus Allison, Raymond Gregory J, Race Brent, Campbell Katrina J, Hughson Andrew G, Anson Kelsie J, Raymond Lynne D, Caughey Byron

Abstract excerpt

Accumulation of fibrillar protein aggregates is a hallmark of many diseases. While numerous proteins form fibrils by prion-like seeded polymerization in vitro, only some are transmissible and pathogenic in vivo To probe the structural features that confer transmissibility to prion protein (PrP) fibrils, we have analyzed synthetic PrP amyloids with or without the human prion disease-associated P102L mutation. The...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Brain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cricetinae

Share to In Vitro Techniques

Share to Lysine

Share to Prion Diseases

Share to Prion Proteins

Share to Proline

Source

Open in PubMed Open full text

Identifiers

PMID: 28835493
DOI: 10.1128/JVI.01276-17
PMCID: PMC5640842

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

PrP P102L and Nearby Lysine Mutations Promote Spontaneous In Vitro Formation of Transmissible Prions.PMID 28835493Read ↗

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

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

PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions.Semantic proximity Read ↗

Emerging Principles of Conformation-Based Prion InheritanceSemantic proximity Read ↗

Conformation Determines the Seeding Potencies of Native and Recombinant Tau AggregatesSemantic proximity Read ↗

In Vivo Generation of Neurotoxic Prion Protein: Role for Hsp70 in Accumulation of Misfolded IsoformsSemantic proximity Read ↗

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

Prion-like aggregates: infectious agents in human disease.Semantic proximity Read ↗

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

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

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