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Article

Different misfolding mechanisms converge on common conformational changes: human prion protein pathogenic mutants Y218N and E196K.

Prion - 1 Jan 2000

Cheng Chin Jung, Daggett Valerie

Abstract excerpt

Prion diseases are caused by misfolding and aggregation of the prion protein (PrP). Pathogenic mutations such as Y218N and E196K are known to cause Gerstmann-Sträussler-Scheinker syndrome and Creutzfeldt-Jakob disease, respectively. Here we describe molecular dynamics simulations of these mutant proteins to better characterize the detailed conformational effects of these sequence substitutions. Our results...

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Identifiers

PMID: 24509603
DOI: 10.4161/pri.27807
PMCID: PMC7030917

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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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