ArticleGenetics2009
Prion variants and species barriers among Saccharomyces Ure2 proteins.
Article in Genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
46 citing papers in PubMed, 65 citations in OpenAlex.
- Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025Review
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- Review
- Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.Genetics · 2021Article
- Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.Molecular and cellular biology · 2020Article
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- The role of prion strain diversity in the development of successful therapeutic treatments.Progress in molecular biology and translational science · 2020Review
- Review
- Review
- [PSI+] prion propagation is controlled by inositol polyphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Hsp104 disaggregase at normal levels cures many [Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- Contributions of the Prion Protein Sequence, Strain, and Environment to the Species Barrier.The Journal of biological chemistry · 2016Article
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
- Article
- Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Amyloid diseases of yeast: prions are proteins acting as genes.Essays in biochemistry · 2014Article
- Amyloids and yeast prion biology.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
As hamster scrapie cannot infect mice, due to sequence differences in their PrP proteins, we find "species barriers" to transmission of the [URE3] prion in Saccharomyces cerevisiae among Ure2 proteins of S. cerevisiae, paradoxus, bayanus, cariocanus, and mikatae on the basis of differences among their Ure2p prion domain sequences. The rapid variation of the N-terminal Ure2p prion domains results in protection against the detrimental effects of infection by a prion, just as the PrP residue 129 Met/Val polymorphism may have arisen to protect humans from the effects of cannibalism. Just as spread of bovine spongiform encephalopathy prion variant is less impaired by species barriers than is sheep scrapie, we find that some [URE3] prion variants are infectious to another yeast species while other variants (with the identical amino acid sequence) are not. The species barrier is thus prion variant dependent as in mammals. [URE3] prion variant characteristics are maintained even on passage through the Ure2p of another species. Ure2p of Saccharomyces castelli has an N-terminal Q/N-rich "prion domain" but does not form prions (in S. cerevisiae) and is not infected with [URE3] from Ure2p of other Saccharomyces. This implies that conservation of its prion domain is not for the purpose of forming prions. Indeed the Ure2p prion domain has been shown to be important, though not essential, for the nitrogen catabolism regulatory role of the protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.