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Article

Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p.

Biochemistry - 4 May 2004

Bousset Luc, Redeker Virginie, Decottignies Paulette, Dubois Steven, Le Maréchal Pierre, Melki Ronald

Abstract excerpt

The protein Ure2 from the yeast Saccharomyces cerevisiae has prion properties. It assembles in vitro into long, straight, insoluble fibrils that are similar to amyloids in that they bind Congo Red and show green-yellow birefringence and have an increased resistance to proteolysis. We recently showed that Ure2p fibrils assembled under physiologically relevant conditions are devoid of a cross-beta-core. A model for...

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PMID: 15109261
DOI: 10.1021/bi049828e

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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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Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p.PMID 15109261Read ↗

Structure of the prion Ure2p in protein fibrils assembled in vitro.Semantic proximity Read ↗

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