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Interactions between non-prion and prion domains of Rnq1 direct formation of amyloid vs liquid-like aggregates and create transmission barriers

2025-01-19

Abstract excerpt

Prions are self-propagating protein conformations usually existing as amyloid aggregates. [ PIN + ], a prion form of the Rnq1 protein occasionally found in wild and laboratory yeast strains, facilitates both the de novo formation and destabilization of other yeast prions, and affects aggregation and toxicity of human misfolding disease proteins expressed in yeast. Rnq1 contains a short N-terminus with no confir...

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Literature Corpus work
88f44769-42d2-5c14-acae-051375b755f6
DOI
10.1101/2025.01.14.633072
Open publication

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Interactions between non-prion and prion domains of Rnq1 direct formation of amyloid vs liquid-like aggregates and create transmission barriersDOI 10.1101/2025.01.14.633072
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