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Article

Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.

The Journal of biological chemistry - 24 Apr 2009

Fei Li, Perrett Sarah

Abstract excerpt

Aggregation of the Ure2 protein is at the origin of the [URE3] prion trait in the yeast Saccharomyces cerevisiae. The N-terminal region of Ure2p is necessary and sufficient to induce the [URE3] phenotype in vivo and to polymerize into amyloid-like fibrils in vitro. However, as the N-terminal regi...

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Identifiers

PMID: 19258323
DOI: 10.1074/jbc.M809673200
PMCID: PMC2670118

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19258323-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.PMID 19258323Read ↗

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In vitro analysis of SpUre2p, a prion-related protein, exemplifies the relationship between amyloid and prion.Semantic proximity Read ↗

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