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Article

Defining Key Residues of the Swi1 Prion Domain in Prion Formation and Maintenance.

Molecular and cellular biology - 23 Jun 2021

Goncharoff Dustin K, Cabral Raudel, Applebey Sarah V, Pagadala Manasa, Du Zhiqiang, Li Liming

Abstract excerpt

Prions are self-perpetuating, alternative protein conformations associated with neurological diseases and normal cellular functions. Saccharomyces cerevisiae contains many endogenous prions, providing a powerful system to study prionization. Previously, we demonstrated that Swi1, a component of the SWI/SNF chromatin-remodeling complex, can form the prion [SWI+]. A small region, Swi11-38, with a unique amino acid...

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Share to Chromatin Assembly and Disassembly
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 33941618
DOI: 10.1128/MCB.00044-21
PMCID: PMC8224238

Provenance

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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