ArticleMolecular bioSystems2014
A proteomic survey of widespread protein aggregation in yeast.
Article in Molecular bioSystems, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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.
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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.
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Who cites it
31 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Imaging Techniques for the Study of Protein Condensates and Filaments and Their Applications.International journal of molecular sciences · 2026Review
- Nutrient and heat stress induce changes to the solubility of predicted prion-like proteins in Dictyostelium discoideum.BMC molecular and cell biology · 2026Article
- Enzyme Assemblies in Nucleotide Metabolism: Structure, Regulation, and Disease Implications.Advances in experimental medicine and biology · 2026Review
- Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins.Molecular biology of the cell · 2024Article
- Protein nonadditive expression and solubility contribute to heterosis inFrontiers in plant science · 2023Article
- Rewiring of the protein-protein-metabolite interactome during the diauxic shift in yeast.Cellular and molecular life sciences : CMLS · 2022Article
- The length scale of multivalent interactions is evolutionarily conserved in fungal and vertebrate phase-separating proteins.Genetics · 2022Article
- Cellular quiescence in budding yeast.Yeast (Chichester, England) · 2021Review
- ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.Nature communications · 2020Article
- Aggregation and disaggregation features of the human proteome.Molecular systems biology · 2020Article
- Freedom of assembly: metabolic enzymes come together.Molecular biology of the cell · 2020Article
- Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation.eLife · 2020Article
- Proteome-wide observation of the phenomenon of life on the edge of solubility.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
- A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network.Molecular biology of the cell · 2019Article
- Mechanism of Filamentation-Induced Allosteric Activation of the SgrAI Endonuclease.Structure (London, England : 1993) · 2019Article
- Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation.Cells · 2019Article
- Protein Phase Separation as a Stress Survival Strategy.Cold Spring Harbor perspectives in biology · 2019Review
- The fitness cost and benefit of phase-separated protein deposits.Molecular systems biology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Many normally cytosolic yeast proteins form insoluble intracellular bodies in response to nutrient depletion, suggesting the potential for widespread protein aggregation in stressed cells. Nearly 200 such bodies have been found in yeast by screening libraries of fluorescently tagged proteins. In order to more broadly characterize the formation of these bodies in response to stress, we employed a proteome-wide shotgun mass spectrometry assay in order to measure shifts in the intracellular solubilities of endogenous proteins following heat stress. As quantified by mass spectrometry, heat stress tended to shift the same proteins into insoluble form as did nutrient depletion; many of these proteins were also known to form foci in response to arsenic stress. Affinity purification of several foci-forming proteins showed enrichment for co-purifying chaperones, including Hsp90 chaperones. Tests of induction conditions and co-localization of metabolic enzymes participating in the same metabolic pathways suggested those foci did not correspond to multi-enzyme organizing centers. Thus, in yeast, the formation of stress bodies appears common across diverse, normally diffuse cytoplasmic proteins and is induced by multiple types of cell stress, including thermal, chemical, and nutrient stress.
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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.