ArticleNature communications2023
Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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87 citing papers in PubMed.
- Mechanistic Insights into the Formation of Complex Coacervates in Crowded Environments.Biomacromolecules · 2026Article
- Biomolecular condensates can function as inherent catalysts.Molecular cell · 2026Article
- Single Fluorogens and Orientation-Localization Microscopy for Quantifying Chemical and Biomolecular Dynamics at the Nanoscale.Accounts of chemical research · 2026Article
- Valency-Limited Molecular Dynamics Simulations of Stickers-and-Spacers Polymers Reveal a Tradeoff Between Condensation and Organization.bioRxiv : the preprint server for biology · 2026Article
- Opposing roles of serine and charge in IDR condensate miscibility.Nature chemical biology · 2026Article
- The role of the 2'-OH group in phase separation and percolation transitions of RNA.Nature communications · 2026Article
- AI-discovered protein fragments as generalizable regulators of biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- Mast cell extracellular granules are bioactive condensates assembled by heparin and polyamine.Nature chemical biology · 2026Article
- The Critical Role of the 2'-OH group in Phase Separation and Percolation Transitions of RNA.bioRxiv : the preprint server for biology · 2026Article
- Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026Article
- Short autoinhibitory sequences control phase separation of an essential bacterial transcription termination factor.The EMBO journal · 2026Article
- How intrinsically disordered regions shape the function of CREB-binding protein.Biochemical Society transactions · 2026Review
- Zα and Zβ domains of ADAR1 and ZBP1 bind G-quadruplexes with nanomolar affinities, establishing Zβ as a G-quadruplex-specific domain.Nucleic acids research · 2026Article
- Computational rheometry for modeling viscoelasticity and mechanical responses of biomolecular condensates.Biophysical journal · 2026Article
- Electrogenic protein condensates as intracellular electrochemical reactors.Nature materials · 2026Article
- AUXIN RESPONSE FACTOR thermostability.Nature communications · 2026Article
- Optically driven control of mechanochemistry and fusion dynamics of biomolecular condensates via thymine dimerization.Nature communications · 2026Article
- Measuring concentration and diffusivity within biomolecular condensates using calibration-free scanning fluorescence correlation spectroscopy.Chemical science · 2026Article
- Design and applications of synthetic biomolecular condensates.Nature nanotechnology · 2026Review
- Mast cell extracellular granules are bioactive condensates driven by heparin and polyamine.bioRxiv : the preprint server for biology · 2025Article
27 more citing papers are in PubMed but not listed here.
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Abstract
Prion-like low-complexity domains (PLCDs) are involved in the formation and regulation of distinct biomolecular condensates that form via phase separation coupled to percolation. Intracellular condensates often encompass numerous distinct proteins with PLCDs. Here, we combine simulations and experiments to study mixtures of PLCDs from two RNA-binding proteins, hnRNPA1 and FUS. Using simulations and experiments, we find that 1:1 mixtures of A1-LCD and FUS-LCD undergo phase separation more readily than either of the PLCDs on their own due to complementary electrostatic interactions. Tie line analysis reveals that stoichiometric ratios of different components and their sequence-encoded interactions contribute jointly to the driving forces for condensate formation. Simulations also show that the spatial organization of PLCDs within condensates is governed by relative strengths of homotypic versus heterotypic interactions. We uncover rules for how interaction strengths and sequence lengths modulate conformational preferences of molecules at interfaces of condensates formed by mixtures of proteins.
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