ReviewFEMS microbiology reviews2014
Physiological and environmental control of yeast prions.
Review in FEMS microbiology reviews, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 57 citations in OpenAlex.
- Yeast red pigment, protein aggregates, and amyloidoses: a review.Cell and tissue research · 2022Review
- Come together now: Dynamic body-formation of key regulators integrates environmental cues in plant development.Frontiers in plant science · 2022Article
- Do microbes have a memory? History-dependent behavior in the adaptation to variable environments.Frontiers in microbiology · 2022Review
- Review
- Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association.International journal of molecular sciences · 2020Article
- Risk of Alzheimer's Disease in Cancer Patients: Analysis of Mortality Data from the US SEER Population-Based Registries.Cancers · 2020Article
- Downshifting Yeast Dominance: Cell Physiology and Phospholipid Composition Are Altered With Establishment of the [Frontiers in microbiology · 2020Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- Role of the Cell Asymmetry Apparatus and Ribosome-Associated Chaperones in the Destabilization of aGenetics · 2019Article
- Asymmetric Inheritance of Cell Fate Determinants: Focus on RNA.Non-coding RNA · 2019Review
- RNA Sequencing Reveals Specific TranscriptomicSignatures Distinguishing Effects of the [Genes · 2019Article
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- The Pub1 and Upf1 Proteins Act in Concert to Protect Yeast from Toxicity of the [PSI⁺] Prion.International journal of molecular sciences · 2018Article
- Repetitive sequences in malaria parasite proteins.FEMS microbiology reviews · 2017Review
- Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission.Molecular and cellular biology · 2017Article
- Review
- Epigenetic inheritance, prions and evolution.Journal of genetics · 2017Review
- Prion-based memory of heat stress in yeast.Prion · 2017Article
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Prions are self-perpetuating protein isoforms that cause fatal and incurable neurodegenerative disease in mammals. Recent evidence indicates that a majority of human proteins involved in amyloid and neural inclusion disorders possess at least some prion properties. In lower eukaryotes, such as yeast, prions act as epigenetic elements, which increase phenotypic diversity by altering a range of cellular processes. While some yeast prions are clearly pathogenic, it is also postulated that prion formation could be beneficial in variable environmental conditions. Yeast and mammalian prions have similar molecular properties. Crucial cellular factors and conditions influencing prion formation and propagation were uncovered in the yeast models. Stress-related chaperones, protein quality control deposits, degradation pathways, and cytoskeletal networks control prion formation and propagation in yeast. Environmental stresses trigger prion formation and loss, supposedly acting via influencing intracellular concentrations of the prion-inducing proteins, and/or by localizing prionogenic proteins to the prion induction sites via heterologous ancillary helpers. Physiological and environmental modulation of yeast prions points to new opportunities for pharmacological intervention and/or prophylactic measures targeting general cellular systems rather than the properties of individual amyloids and prions.
Indexed as
Identifiers
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.