ReviewThe Journal of biological chemistry2019
Anti-prion systems in yeast.
Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 19 citations in OpenAlex.
- Modelling human proteostasis and organelle homeostasis disorders in yeast and its application in drug discovery.FEMS yeast research · 2026Review
- How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypes.Research square · 2025Article
- Osmotic stress induces formation of both liquid condensates and amyloids by a yeast prion domain.The Journal of biological chemistry · 2024Article
- Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.PLoS genetics · 2024Article
- Identifying Endogenous Cellular Proteins Destabilizing the Propagation of Swi1 Prion upon Overproduction.Viruses · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.International journal of molecular sciences · 2021Review
- Complex Networks of Prion-Like Proteins Reveal Cross Talk Between Stress and Memory Pathways in Plants.Frontiers in plant science · 2021Article
- 25 years of yeast prions.Prion · 2020Article
- Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.Molecular and cellular biology · 2020Article
- From Seeds to Fibrils and Back: Fragmentation as an Overlooked Step in the Propagation of Prions and Prion-Like Proteins.Biomolecules · 2020Review
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Review
- Celebrating the scientific legacy of Herbert Tabor.The Journal of biological chemistry · 2019Review
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 prions have become important models for the study of the basic mechanisms underlying human amyloid diseases. Yeast prions are pathogenic (unlike the [Het-s] prion of
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.