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Article

Cryptic peptides of the kringle domains preferentially bind to disease-associated prion protein.

Journal of Alzheimer's disease : JAD - 1 Jan 2009

Hatcher Kristen, Zheng Jian, Chen Shu G

Abstract excerpt

Prion diseases are a group of fatal neurodegenerative disorders characterized by the accumulation of a misfolded form (PrP(Sc)) of the cellular prion protein (PrP(C)) in the brains of affected individuals. The conversion of PrP(C) to PrP(Sc) is thought to involve a change in protein conformation from a normal, primarily alpha-helical structure into a beta-sheet conformer. Few proteins have been identified that...

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Source

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Identifiers

PMID: 19221431
DOI: 10.3233/JAD-2009-0980
PMCID: PMC2741132

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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