ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2022
Reversible Kinetic Trapping of FUS Biomolecular Condensates.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 55 citations in OpenAlex.
- Nonequilibrium phases of a biomolecular condensate facilitated by enzyme activity.Soft matter · 2026Article
- Decoupling phase separation and fibrillization preserves activity of biomolecular condensates.Nature communications · 2026Article
- Molecular origins of viscoelasticity in biomolecular condensates.The Journal of chemical physics · 2026Article
- A high-throughput, flow cytometry approach to measure phase behavior and exchange in biomolecular condensates.Nature communications · 2026Article
- Nanocluster intermediates orchestrate the phase transition of ATP condensates.Communications chemistry · 2025Article
- Biomolecular condensate viscoelasticity is dictated by the interplay between single-molecule shape memory and mesh reconfigurability.bioRxiv : the preprint server for biology · 2025Article
- In situ secondary structure imaging of protein phase separation and aggregation by hyperspectral stimulated Raman scattering microscopy.Nature communications · 2025Article
- Article
- Charged peptides enriched in aromatic residues decelerate condensate ageing driven by cross-β-sheet formation.Nature communications · 2025Article
- Uncovering protein conformational dynamics within two-component viral biomolecular condensates.Protein science : a publication of the Protein Society · 2025Article
- A disordered linker in the Polycomb protein Polyhomeotic tunes phase separation and oligomerization.Molecular cell · 2025Article
- Benchmarking residue-resolution protein coarse-grained models for simulations of biomolecular condensates.PLoS computational biology · 2025Article
- A solid beta-sheet structure is formed at the surface of FUS droplets during aging.Nature chemical biology · 2024Article
- Fundamental Aspects of Phase-Separated Biomolecular Condensates.Chemical reviews · 2024Review
- Liquid-Liquid Phase Separation of the Intrinsically Disordered Domain of the Fused in Sarcoma Protein Results in Substantial Slowing of Hydration Dynamics.The journal of physical chemistry letters · 2023Article
- The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils.Nature chemistry · 2023Article
- Location and Concentration of Aromatic-Rich Segments Dictates the Percolating Inter-Molecular Network and Viscoelastic Properties of Ageing Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Challenges in studying the liquid-to-solid phase transitions of proteins using computer simulations.Current opinion in chemical biology · 2023Review
- Fibril formation and ordering of disordered FUS LC driven by hydrophobic interactions.Nature chemistry · 2023Article
- Time-Dependent Material Properties of Aging Biomolecular Condensates from Different Viscoelasticity Measurements in Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
Formation of membrane-less organelles by self-assembly of disordered proteins can be triggered by external stimuli such as pH, salt, or temperature. These organelles, called biomolecular condensates, have traditionally been classified as liquids, gels, or solids with limited subclasses. Here, the authors show that a thermal trigger can lead to formation of at least two distinct liquid condensed phases of the fused in sarcoma low complexity (FUS LC) domain. Forming FUS LC condensates directly at low temperature leads to formation of metastable, kinetically trapped condensates that show arrested coalescence, escape from which to untrapped condensates can be achieved via thermal annealing. Using experimental and computational approaches, the authors find that molecular structure of interfacial FUS LC in kinetically trapped condensates is distinct (more β-sheet like) compared to untrapped FUS LC condensates. Moreover, molecular motion within kinetically trapped condensates is substantially slower compared to that in untrapped condensates thereby demonstrating two unique liquid FUS condensates. Controlling condensate thermodynamic state, stability, and structure with a simple thermal switch may contribute to pathological protein aggregate stability and provides a facile method to trigger condensate mixing for biotechnology applications.
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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.