ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2021
Protein aggregation and the evolution of stress resistance in clinical yeast.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 9 citations in OpenAlex.
- Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness.MicrobiologyOpen · 2026Review
- Article
- Tissue-specific landscape of protein aggregation and quality control in an aging vertebrate.Developmental cell · 2024Article
- Identification of protein aggregates in the aging vertebrate brain with prion-like and phase-separation properties.Cell reports · 2024Article
- Beyond resistance: antifungal heteroresistance and antifungal tolerance in fungal pathogens.Current opinion in microbiology · 2024Review
- Insights and Perspectives on the Role of Proteostasis and Heat Shock Proteins in Fungal Infections.Microorganisms · 2023Review
- How does epigenetics influence the course of evolution?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein aggregation, particularly in its prion-like form, has long been thought to be detrimental. However, recent studies have identified multiple instances where protein aggregation is important for normal physiological functions. Combining mass spectrometry and cell biological approaches, we developed a strategy for the identification of protein aggregates in cell lysates. We used this approach to characterize prion-based traits in pathogenic strains of the yeast
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.