ReviewFEBS letters2007
Stress and prions: lessons from the yeast model.
Review in FEBS letters, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed, 83 citations in OpenAlex.
- An interchangeable prion-like domain is required for Ty1 retrotransposition.bioRxiv : the preprint server for biology · 2023Article
- Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response.Diseases (Basel, Switzerland) · 2023Review
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Protein aggregation and the evolution of stress resistance in clinical yeast.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
- The role of disorder in RNA binding affinity and specificity.Open biology · 2020Article
- Yeast-Based Biosensors: Current Applications and New Developments.Biosensors · 2020Review
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.PloS one · 2020Article
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- Epigenetic inheritance, prions and evolution.Journal of genetics · 2017Review
- Prion-based memory of heat stress in yeast.Prion · 2017Article
- Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017Review
- Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress.Cell reports · 2017Article
- Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion.The Journal of biological chemistry · 2014Article
- Extracellular environment modulates the formation and propagation of particular amyloid structures.Molecular microbiology · 2014Article
- Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.Molecular microbiology · 2014Article
- A proteomic survey of widespread protein aggregation in yeast.Molecular bioSystems · 2014Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Yeast self-perpetuating amyloids (prions) provide a convenient model for studying the cellular control of highly ordered aggregates involved in mammalian protein assembly disorders. The very ability of an amyloid to propagate a prion state in yeast is determined by its interactions with the stress-inducible chaperone Hsp104. Prion formation and propagation are also influenced by other stress-related chaperones (Hsp70 and Hsp40), and by alterations of the protein trafficking and degradation networks. Some stress conditions induce prion formation or loss. It is proposed that prions arise as byproducts of the reversible assembly of highly ordered complexes, protecting certain proteins during unfavorable conditions.
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.