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Article

Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions.

The Journal of biological chemistry - 27 Sept 2013

Saverioni Daniela, Notari Silvio, Capellari Sabina, Poggiolini Ilaria, Giese Armin, Kretzschmar Hans A, Parchi Piero

Abstract excerpt

Prion diseases are characterized by tissue accumulation of a misfolded, β-sheet-enriched isoform (scrapie prion protein (PrP(Sc))) of the cellular prion protein (PrP(C)). At variance with PrP(C), PrP(Sc) shows a partial resistance to protease digestion and forms highly aggregated and detergent-insoluble polymers, two properties that have been consistently used to distinguish the two proteins. In recent years,...

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Identifiers

PMID: 23897825
DOI: 10.1074/jbc.M113.477547
PMCID: PMC3784711

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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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