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Article

Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates.

Journal of molecular biology - 11 Jan 2002

Galani Despina, Fersht Alan R, Perrett Sarah

Abstract excerpt

The Saccharomyces cerevisiae non-Mendelian factor [URE3] propagates by a prion-like mechanism, involving aggregation of the chromosomally encoded protein Ure2. The N-terminal prion domain (PrD) of Ure2 is required for prion activity in vivo and amyloid formation in vitro. However, the molecular mechanism of the prion-like activity remains obscure. Here we measure the kinetics of folding of Ure2 and two N-terminal...

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Identifiers

PMID: 11779240
DOI: 10.1006/jmbi.2001.5234

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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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Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates.PMID 11779240Read ↗

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