ArticleNature communications2021
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 281 papers.
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Who cites it
281 citing papers in PubMed.
- Biomolecular coacervation-mediated materials: Phase states, phase transitions, and biomedical applications.Bioactive materials · 2027Review
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- TIME FOR COFFEE coordinates phase separation and chromatin regulation for salt tolerance.Science advances · 2026Article
- Active Field Theory Approach to Explain Size Control of Transcriptional Condensates.Macromolecular bioscience · 2026Article
- Holographic Fingerprinting Reveals Oligomer-Driven Phase Separation in Bovine Serum Albumin.Chemical & biomedical imaging · 2026Article
- Mapping high resolution, multidimensional phase diagrams of near-physiological protein condensates.Nature communications · 2026Article
- Pathway Controlled Phase Separation of Minimal Building Blocks Utilizing a Dissociative Chemical Transformation.Angewandte Chemie (International ed. in English) · 2026Article
- Phase separation in neurodegenerative disorders: a metabolic perspective on protein aggregation and therapeutic targeting.Translational neurodegeneration · 2026Review
- Sticker Valence Governs Chain Collapse and Liquid-Liquid Phase Separation in Peptide-Inspired Associative Polymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Multi-Site Aggregation of p53: Insights from Self- and Co-Aggregation of Multiple Aggregation-Prone Regions.ACS omega · 2026Article
- Structural Control of Dual Emission in Coumarin Fluorophores for Visualizing Protein Droplet Maturation.Angewandte Chemie (International ed. in English) · 2026Article
- A machine learning framework for predicting and modulating condition-dependent protein phase separation.Nature communications · 2026Article
- Annexin A11 and TDP-43: core players in neurodegeneration.Acta neuropathologica · 2026Review
- Recognition of multimolecular G-quadruplex regulates phase separation of cockayne syndrome B.Nucleic acids research · 2026Article
- Complex Effects of Salt on Small-Angle X-ray Scattering of BSA Originate from the Interplay of Ions and Hydration Water.The journal of physical chemistry letters · 2026Article
- Oppositely Charged Single Enzyme Nanogels Form Versatile Coacervates for Efficient Enzyme Cascade Catalysis.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- RNA G-quadruplexes function as a tunable switch of FUS phase separation.Nucleic acids research · 2026Article
- Article
- Physics-guided design of intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026Article
- K294E change in the rotavirus factory forming protein NSP2 stabilizes a rare C-terminal conformation.Journal of biomolecular structure & dynamics · 2026Article
221 more citing papers are in PubMed but not listed here.
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Authors and funding
19 authors.
Funding
Abstract
Liquid-liquid phase separation of proteins underpins the formation of membraneless compartments in living cells. Elucidating the molecular driving forces underlying protein phase transitions is therefore a key objective for understanding biological function and malfunction. Here we show that cellular proteins, which form condensates at low salt concentrations, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, can reenter a phase-separated regime at high salt concentrations. By bringing together experiments and simulations, we demonstrate that this reentrant phase transition in the high-salt regime is driven by hydrophobic and non-ionic interactions, and is mechanistically distinct from the low-salt regime, where condensates are additionally stabilized by electrostatic forces. Our work thus sheds light on the cooperation of hydrophobic and non-ionic interactions as general driving forces in the condensation process, with important implications for aberrant function, druggability, and material properties of biomolecular condensates.
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