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Article

Structure of the prion Ure2p in protein fibrils assembled in vitro.

The Journal of biological chemistry - 4 Nov 2005

Fay Nicolas, Redeker Virginie, Savistchenko Jimmy, Dubois Steven, Bousset Luc, Melki Ronald

Abstract excerpt

The Ure2 protein from the yeast Saccharomyces cerevisiae has prion properties. In vitro and at neutral pH, soluble Ure2p spontaneously forms long, straight, insoluble protein fibrils. Two models have been proposed to account for the assembly of Ure2p into protein fibrils. The "amyloid backbone" model postulates that a segment ranging from 40 to 70 amino acids in the flexible N-terminal domain from different Ure2p...

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Identifiers

PMID: 16131495
DOI: 10.1074/jbc.M506917200

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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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Structure of the prion Ure2p in protein fibrils assembled in vitro.PMID 16131495Read ↗

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