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Article

Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency.

PLoS pathogens - 1 Aug 2017

Hannaoui Samia, Amidian Sara, Cheng Yo Ching, Duque Velásquez Camilo, Dorosh Lyudmyla, Law Sampson, Telling Glenn, Stepanova Maria, McKenzie Debbie, Wille Holger, Gilch Sabine

Abstract excerpt

Prion diseases are infectious neurodegenerative disorders of humans and animals caused by misfolded forms of the cellular prion protein PrPC. Prions cause disease by converting PrPC into aggregation-prone PrPSc. Chronic wasting disease (CWD) is the most contagious prion disease with substantial lateral transmission, affecting free-ranging and farmed cervids. Although the PrP primary structure is highly conserved...

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Identifiers

PMID: 28800624
DOI: 10.1371/journal.ppat.1006553
PMCID: PMC5568445

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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.

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