ReviewMicrobiology and molecular biology reviews : MMBR2015
Yeast prions: structure, biology, and prion-handling systems.
Review in Microbiology and molecular biology reviews : MMBR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 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.
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
89 citing papers in PubMed, 143 citations in OpenAlex.
- RcAlb-PepII Perturbs the Proteomic Profile ofMicroorganisms · 2026Article
- amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Modelling human proteostasis and organelle homeostasis disorders in yeast and its application in drug discovery.FEMS yeast research · 2026Review
- Detection system- and strain-dependent diversity of de novo [PSI+] prion generation and phenotypes in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2025Article
- Exogenous prion-like proteins and their potential to trigger cognitive dysfunction.Molecular systems biology · 2025Article
- Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025Review
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- [SNG2], a prion form of Cut4/Apc1, confers non-Mendelian inheritance of heterochromatin silencing defect in fission yeast.Nucleic acids research · 2024Article
- Understanding the molecular mechanisms of human diseases: the benefits of fission yeasts.Microbial cell (Graz, Austria) · 2024Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- MIL-CELL: a tool for multi-scale simulation of yeast replication and prion transmission.European biophysics journal : EBJ · 2023Article
- Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023Review
- Overexpression of Hsp104 by Causing Dissolution of the Prion Seeds Cures the Yeast [International journal of molecular sciences · 2023Article
- Prions are the greatest protein misfolding problem, and yeast has several solutions.PLoS pathogens · 2023Article
- A novel narnavirus is widespread in Saccharomyces cerevisiae and impacts multiple host phenotypes.G3 (Bethesda, Md.) · 2023Article
- Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response.Diseases (Basel, Switzerland) · 2023Review
- [PRIONPathogens (Basel, Switzerland) · 2022Article
- Anti-Prion Systems inViruses · 2022Review
- Review
29 more citing papers are in PubMed but not listed here.
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 3 institutions in 1 country.
Funding
Abstract
A prion is an infectious protein horizontally transmitting a disease or trait without a required nucleic acid. Yeast and fungal prions are nonchromosomal genes composed of protein, generally an altered form of a protein that catalyzes the same alteration of the protein. Yeast prions are thus transmitted both vertically (as genes composed of protein) and horizontally (as infectious proteins, or prions). Formation of amyloids (linear ordered β-sheet-rich protein aggregates with β-strands perpendicular to the long axis of the filament) underlies most yeast and fungal prions, and a single prion protein can have any of several distinct self-propagating amyloid forms with different biological properties (prion variants). Here we review the mechanism of faithful templating of protein conformation, the biological roles of these prions, and their interactions with cellular chaperones, the Btn2 and Cur1 aggregate-handling systems, and other cellular factors governing prion generation and propagation. Human amyloidoses include the PrP-based prion conditions and many other, more common amyloid-based diseases, several of which show prion-like features. Yeast prions increasingly are serving as models for the understanding and treatment of many mammalian amyloidoses. Patients with different clinical pictures of the same amyloidosis may be the equivalent of yeasts with different prion variants.
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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.