ArticleNature chemical biology2021
NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54 citing papers in PubMed, 102 citations in OpenAlex.
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- Condensates as Conformation Editors of Disordered Client Proteins.Journal of the American Chemical Society · 2026Article
- Versatile High-Sensitivity EPR Using Superconducting Spiral Microresonators.Small methods · 2026Article
- Isotopic and defect analysis of enriched molybdenum oxide using EPR spectroscopy and DFT simulation.Scientific reports · 2026Article
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- Liquid-Liquid Phase Separation in Cancer Drug Resistance: Mechanisms and Therapeutic Opportunities.Oncology research · 2026Review
- Multiplexed Analysis of Multicomponent Biomolecular Condensates without Any Tag.Journal of the American Chemical Society · 2025Article
- Quantifying the liquid-liquid transition in cold water/glycerol mixtures by intermolecular hyperfine relaxation-induced dipolar modulation enhancement (ih-RIDME).Physical chemistry chemical physics : PCCP · 2025Article
- Water-detected NMR allows dynamic observations of repeat-expansion RNA condensates.Nature chemistry · 2025Article
- Nucleotide-Specific RNA Conformations and Dynamics as Precursors to Ribonucleoprotein Condensates.Journal of the American Chemical Society · 2025Article
- Selective Ion Binding and Uptake Shape the Microenvironment of Biomolecular Condensates.Journal of the American Chemical Society · 2025Article
- Molecular mechanisms of biomolecular condensate formation in Drosophila melanogaster siRNA biogenesis.Nucleic acids research · 2025Article
- Investigating the Conformational Diversity of the TMR-3 Aptamer.Journal of the American Chemical Society · 2025Article
- LLPS REDIFINE allows the biophysical characterization of multicomponent condensates without tags or labels.Nature communications · 2025Article
- Aging-dependent evolving electrochemical potentials of biomolecular condensates regulate their physicochemical activities.Nature chemistry · 2025Article
- Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function.Trends in biochemical sciences · 2025Review
- RIDME Spectroscopy: New Topics Beyond the Determination of Electron Spin-Spin Distances.The journal of physical chemistry letters · 2025Review
- ih-RIDME: a pulse EPR experiment to probe the heterogeneous nuclear environment.Magnetic resonance (Gottingen, Germany) · 2025Article
- Conformations of a low-complexity protein in homogeneous and phase-separated frozen solutions.Biophysical journal · 2024Article
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Many RNA-binding proteins undergo liquid-liquid phase separation, which underlies the formation of membraneless organelles, such as stress granules and P-bodies. Studies of the molecular mechanism of phase separation in vitro are hampered by the coalescence and sedimentation of organelle-sized droplets interacting with glass surfaces. Here, we demonstrate that liquid droplets of fused in sarcoma (FUS)-a protein found in cytoplasmic aggregates of amyotrophic lateral sclerosis and frontotemporal dementia patients-can be stabilized in vitro using an agarose hydrogel that acts as a cytoskeleton mimic. This allows their spectroscopic characterization by liquid-phase NMR and electron paramagnetic resonance spectroscopy. Protein signals from both dispersed and condensed phases can be observed simultaneously, and their respective proportions can be quantified precisely. Furthermore, the agarose hydrogel acts as a cryoprotectant during shock-freezing, which facilitates pulsed electron paramagnetic resonance measurements at cryogenic temperatures. Surprisingly, double electron-electron resonance measurements revealed a compaction of FUS in the condensed phase.
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