ArticleNature chemistry2023
Fibril formation and ordering of disordered FUS LC driven by hydrophobic interactions.
Article in Nature chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 50 citations in OpenAlex.
- Droplet growth, Ostwald's rule, and emergence of order in Fused in Sarcoma.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Molecular driving force of a small molecule-induced protein disorder-order transition.Communications chemistry · 2026Article
- Insights into de-mixing and morphology modulation in coacervate-membrane interactions from integrating experiments and simulations.Communications chemistry · 2025Article
- Association of Hemoglobin and Myoglobin into Supramolecular Complexes: Significance for Life and Practice.International journal of molecular sciences · 2025Review
- Molecular motor-driven reversible liquid-liquid phase separation of supramolecular assemblies.Nature communications · 2025Article
- Promoting organic nucleation of diclofenac: hydrophobic interfacial interactions drive self-assembly.Chemical science · 2025Article
- Regulating Enzyme Activity via Microaggregates Mediated by Phase Separation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Liquid-Liquid Phase Separation from the Viewpoint of Molecular Crowding Environment: A Raman Imaging Study.The journal of physical chemistry. B · 2025Review
- Expanding the molecular grammar of polar residues and arginine in FUS phase separation.Nature chemical biology · 2025Article
- Tunable metastability of condensates reconciles their dual roles in amyloid fibril formation.Molecular cell · 2025Article
- Water and Collagen: A Mystery Yet to Unfold.Biomacromolecules · 2025Review
- Unraveling the molecular grammar and the structural transitions underlying the fibrillation of a viral fibrillogenic domain.Protein science : a publication of the Protein Society · 2025Article
- The role of biomolecular condensates in protein aggregation.Nature reviews. Chemistry · 2024Review
- Structural adaptability and surface activity of peptides derived from tardigrade proteins.Protein science : a publication of the Protein Society · 2024Article
- The molecular basis for the increased stability of the FUS-LC fibril at the anionic membrane- and air-water interfaces.Chemical science · 2024Article
- From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain.The European physical journal. E, Soft matter · 2024Article
- Expanding the molecular grammar of polar residues and arginine in FUS prion-like domain phase separation and aggregation.bioRxiv : the preprint server for biology · 2024Article
- 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
- Single-molecule FRET unmasks structural subpopulations and crucial molecular events during FUS low-complexity domain phase separation.Nature communications · 2023Article
- Does the Sum-Frequency Generation Signal of Aromatic C-H Vibrations Reflect Molecular Orientation?The journal of physical chemistry. B · 2023Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Biomolecular condensates, protein-rich and dynamic membrane-less organelles, play critical roles in a range of subcellular processes, including membrane trafficking and transcriptional regulation. However, aberrant phase transitions of intrinsically disordered proteins in biomolecular condensates can lead to the formation of irreversible fibrils and aggregates that are linked to neurodegenerative diseases. Despite the implications, the interactions underlying such transitions remain obscure. Here we investigate the role of hydrophobic interactions by studying the low-complexity domain of the disordered 'fused in sarcoma' (FUS) protein at the air/water interface. Using surface-specific microscopic and spectroscopic techniques, we find that a hydrophobic interface drives fibril formation and molecular ordering of FUS, resulting in solid-like film formation. This phase transition occurs at 600-fold lower FUS concentration than required for the canonical FUS low-complexity liquid droplet formation in bulk. These observations highlight the importance of hydrophobic effects for protein phase separation and suggest that interfacial properties drive distinct protein phase-separated structures.
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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.