ArticleCell2015
Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress.
Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 274 papers, 2 of them syntheses that pooled it.
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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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Who cites it
274 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- Shift of the insoluble content of the proteome in the aging mouse brain.Proceedings of the National Academy of Sciences of the United States of America · 2023Pooled it
- A comparative meta-analysis of membraneless organelle-associated proteins with age related proteome of C. elegans.Cell stress & chaperones · 2022Pooled it
- Multiscale Structural Remodeling of Oleosins by Thermal Processing: Mechanisms and Implications for Allergenicity Modulation in Oilseed Crops.Comprehensive reviews in food science and food safety · 2026Review
- Interplay between stress granule-like structures and nuclear RNA export in a heat shock-specific manner.Nucleic acids research · 2026Article
- Heat Stress Triggers Nuclear Invagination and Spatial Compartmentalization of Protein Metabolism.Cell proliferation · 2026Article
- Nuclear Stress Bodies and Mitochondrial Signal Transduction Regulate Thermotolerance in Cattle: Insights Into Molecular Mechanisms.Animal genetics · 2026Review
- Chaperone condensates buffer the heat shock response against pleiotropic inputs.bioRxiv : the preprint server for biology · 2026Article
- Small bites for big problems: stepwise aggregate degradation by autophagy.Biochemical Society transactions · 2026Review
- High-throughput screening approach identifies substrate-selective Hsp104 variants that counter amyloid seeding with diminished off-target effects.Molecular cell · 2026Article
- Article
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Anhydrobiosis as a Model of Aging and Longevity: The Role of Autophagy and Metabolism in Yeast Cells.Microbial ecology · 2026Review
- Nutrient and heat stress induce changes to the solubility of predicted prion-like proteins in Dictyostelium discoideum.BMC molecular and cell biology · 2026Article
- Theoretical limits for sensing through phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Liquid-Liquid Phase Separation in Major Hallmarks of Cancer.Cell proliferation · 2026Review
- A Biochemical Analysis of LINC00896 RNA in Cortex Neuronal Cells and Its Possible Connection to the Development of Autism.Journal of nucleic acids · 2026Article
- Chaperone dependency during biogenesis does not correlate with chaperone dependency during refolding.Molecular systems biology · 2026Article
- Molecular basis for thermoresponsive protein condensation in plants.bioRxiv : the preprint server for biology · 2025Article
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Transcriptome-wide mRNP condensation precedes stress granule formation and excludes new mRNAs.Molecular cell · 2025Article
214 more citing papers are in PubMed but not listed here.
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14 authors.
Funding
Abstract
Heat causes protein misfolding and aggregation and, in eukaryotic cells, triggers aggregation of proteins and RNA into stress granules. We have carried out extensive proteomic studies to quantify heat-triggered aggregation and subsequent disaggregation in budding yeast, identifying >170 endogenous proteins aggregating within minutes of heat shock in multiple subcellular compartments. We demonstrate that these aggregated proteins are not misfolded and destined for degradation. Stable-isotope labeling reveals that even severely aggregated endogenous proteins are disaggregated without degradation during recovery from shock, contrasting with the rapid degradation observed for many exogenous thermolabile proteins. Although aggregation likely inactivates many cellular proteins, in the case of a heterotrimeric aminoacyl-tRNA synthetase complex, the aggregated proteins remain active with unaltered fidelity. We propose that most heat-induced aggregation of mature proteins reflects the operation of an adaptive, autoregulatory process of functionally significant aggregate assembly and disassembly that aids cellular adaptation to thermal stress.
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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.