ArticleCurrent genetics2020
A complete catalog of wild-type Sup35 prion variants and their protein-only propagation.
Article in Current genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Detection system- and strain-dependent diversity of de novo [PSI+] prion generation and phenotypes in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2025Article
- Total propagation of yeast prion conformers in ssz1∆ upf1∆ Hsp104Current genetics · 2025Article
- On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins.International journal of molecular sciences · 2025Article
- Mapping of Prion Structures in the Yeast Rnq1.International journal of molecular sciences · 2024Article
- The Mutability of Yeast Prions.Viruses · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Amyloid Fragmentation and Disaggregation in Yeast and Animals.Biomolecules · 2021Review
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2 authors.
Funding
Abstract
Twenty-three prion variants of the wild-type Sup35 protein are obtained, including 19 novel ones and 4 previously documented, namely, VH, VK, VL, and W8. Their uniqueness and non-composite nature are demonstrated. Specific infectivity is generated de novo for most variants by adding prion particles to solutions of a purified Sup35 N-terminal fragment, thereby supporting the protein-only composition. Sup35 prions isolated by other laboratories are identified within the collection and found to fall into a narrow set of five variant types that are readily inducible in vivo by Sup35 overexpression. The work establishes an unambiguous and extensive collection of prion variants, demonstrating that a protein, by itself, in the absence of genetic and conformational co-factors, could adopt a great number of structures. In light of recent high-resolution structures of other amyloids, we discuss how the diverse folding is achieved in spite of apparent contradiction to the classical paradigm that a protein's structure is uniquely determined by its sequence.
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