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How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypes

2025-11-03

Abstract excerpt

<title>Abstract</title> <p> In the [ <italic>PSI</italic> <sup>+</sup> ] prion system, the yeast prion protein Sup35 can form structurally distinct amyloid fibrils that lead to distinct transmissible prion states, or strains. However, our understanding of how different Sup35 fibril structures arise and translate to phenotypic variations is limited. Here, using cryo-EM and single-monomer force spectroscopy wit...

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Literature Corpus work
158deb93-ce65-529c-add4-fd60c418b3c7
DOI
10.21203/rs.3.rs-7945345/v1
Open publication

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How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypesDOI 10.21203/rs.3.rs-7945345/v1
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