ArticleFrontiers in biophysics2024
Chaperone regulation of biomolecular condensates.
Article in Frontiers in biophysics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The Epichaperome Matrix Theory: A systems-level model of active molecular organization.Cell stress & chaperones · 2026Article
- Redox-Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Phase Separation Drives Pathological Aggregation in Neurodegenerative Diseases: A 15-Year Bibliometric Landscape (2009-2024).Annals of the New York Academy of Sciences · 2026Review
- Insights into the function and structure of the R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1) chaperone complex.Cell stress & chaperones · 2026Review
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Proximity proteomics reveals the molecular architecture of phytochrome B photobodies inbioRxiv : the preprint server for biology · 2025Article
- BR-bodies facilitate adaptive responses and survival during copper stress in Caulobacter crescentus.The Journal of biological chemistry · 2025Article
- Accurate prediction of thermoresponsive phase behavior of disordered proteins.Protein science : a publication of the Protein Society · 2025Article
- Drosophila Clu ribonucleoprotein particle dynamics rely on the availability of functional Clu and translating ribosomes.Journal of cell science · 2025Article
- Extracellular phase separation mediates storage and release of thyroglobulin in the thyroid follicular lumen.Communications biology · 2025Article
- BR-Bodies Facilitate Adaptive Responses and Survival During Copper Stress inbioRxiv : the preprint server for biology · 2025Article
- Accurate prediction of thermoresponsive phase behavior of disordered proteins.bioRxiv : the preprint server for biology · 2025Article
- Protein quality control machinery: regulators of condensate architecture and functionality.Trends in biochemical sciences · 2025Review
- The CCT chaperonin and actin modulate the ER and RNA-binding protein condensation during oogenesis and maintain translational repression of maternal mRNA and oocyte quality.Molecular biology of the cell · 2024Article
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2 authors.
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Abstract
Biomolecular condensation allows for the dynamic organization of molecules in time and space. Condensate formation is regulated through many mechanisms including the action of molecular chaperones. While molecular chaperones have long been viewed through the lens of their roles in protein folding, misfolding, and quality control, their ability to manipulate protein-protein interactions is increasingly recognized to play a major role in the precise control of condensate biology. In this review we highlight recent studies investigating the roles of canonical and non-canonical chaperones in regulating condensate formation, material state, and dispersal. We discuss the broadening of longstanding conceptions of chaperone functions to include condensate regulation, and the discovery of previously unappreciated chaperone activities in well-known proteins. We close by considering the biological activities being uncovered during the ongoing upheaval at the boundary between chaperone biology and biomolecular condensation.
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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.