ReviewPrion
Yeast prions: evolution of the prion concept.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- From aggregate structure to disease trajectory: the role of the proteostasis network.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Intrinsically disordered regions in the yeast transcriptional regulator Ixr1 support prion-like behavior.Scientific reports · 2026Article
- Modelling human proteostasis and organelle homeostasis disorders in yeast and its application in drug discovery.FEMS yeast research · 2026Review
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
- Yeast red pigment, protein aggregates, and amyloidoses: a review.Cell and tissue research · 2022Review
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- Loss of Elongator- and KEOPS-Dependent tRNA Modifications Leads to Severe Growth Phenotypes and Protein Aggregation in Yeast.Biomolecules · 2020Article
- Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.BMB reports · 2017Article
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
- Ion-specific effects on prion nucleation and strain formation.The Journal of biological chemistry · 2013Article
- Potential roles for prions and protein-only inheritance in cancer.Cancer metastasis reviews · 2012Review
- Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast.PLoS genetics · 2012Article
- Newly identified prions in budding yeast, and their possible functions.Seminars in cell & developmental biology · 2011Review
- Btn3 is a negative regulator of Btn2-mediated endosomal protein trafficking and prion curing in yeast.Molecular biology of the cell · 2011Article
- Destabilization and recovery of a yeast prion after mild heat shock.Journal of molecular biology · 2011Article
- Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission.Molecular microbiology · 2010Article
- Prions, protein homeostasis, and phenotypic diversity.Trends in cell biology · 2010Article
- Stress and prions: lessons from the yeast model.FEBS letters · 2007Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Prions (infectious proteins) analogous to the scrapie agent have been identified in Saccharomyces cerevisiae and Podospora anserina based on their special genetic characteristics. Each is a protein acting as a gene, much like nucleic acids have been shown to act as enzymes. The [URE3], [PSI(+)], [PIN(+)] and [Het-s] prions are self-propagating amyloids of Ure2p, Sup35p, Rnq1p and the HET-s protein, respectively. The [beta] and [C] prions are enzymes whose precursor activation requires their own active form. [URE3] and [PSI(+)] are clearly diseases, while [Het-s] and [beta] carry out normal cell functions. Surprisingly, the prion domains of Ure2p and Sup35p can be randomized without loss of ability to become a prion. Thus amino acid content and not sequence determine these prions. Shuffleability also suggests amyloids with a parallel in-register beta-sheet structure.
Indexed as
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What OpenQuestion holds
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.