ArticleNature chemistry2025
Homotypic RNA clustering accompanies a liquid-to-solid transition inside the core of multi-component biomolecular condensates.
Article in Nature chemistry, 2025. 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.
- Backbone Hydrogen Bonding as a Determinant of Condensate Material States.Journal of the American Chemical Society · 2026Article
- Biomolecular condensates as dynamic regulators of musculoskeletal homeostasis, disease, and therapeutic challenges.Bone research · 2026Review
- Dynamic Arrest and Tunable Gelation of Immunogenically Inert POEGMA Nanoparticles.ACS polymers Au · 2026Article
- The role of the 2'-OH group in phase separation and percolation transitions of RNA.Nature communications · 2026Article
- Visualization of G3BP1-RNA Condensate Nascent Assembly and Early Maturation by HS-AFM.International journal of molecular sciences · 2026Article
- Single-Molecule Dwell Times in Biomolecular Condensates.bioRxiv : the preprint server for 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
- Data-driven model reveals increased stability of CAG-expanded huntingtin RNA due to MID1 binding.PLoS computational biology · 2026Article
- Discrete 3' UTR sequence motifs regulate nanos RNA enrichment in Drosophila germ granules.Developmental biology · 2026Article
- Mapping RNA structure assembly and remodeling in biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- A tunable aqueous architecture modulates functional output in biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- Visualizing TERRA RNA G-quadruplex Unfolding in FUS Biomolecular Condensates.Journal of molecular biology · 2026Article
- Engineering Design of Artificial Phase-Separating Proteins.Biotechnology journal · 2026Review
- Computational rheometry for modeling viscoelasticity and mechanical responses of biomolecular condensates.Biophysical journal · 2026Article
- Nonequilibrium phases of a biomolecular condensate facilitated by enzyme activity.Soft matter · 2026Article
- TDP-43 pathology is linked to motor neuron loss and is independent of stress granulesbioRxiv : the preprint server for biology · 2026Article
- Condensate protein aggregation in ALS/FTD is regulated by GGGGCC-repeat RNA scaffolds.Nature structural & molecular biology · 2026Article
- Decoupling phase separation and fibrillization preserves activity of biomolecular condensates.Nature communications · 2026Article
- Recent advances in coacervate protocells from passive catalysts to chemically programmable systems.Communications chemistry · 2026Review
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Abstract
RNA-driven condensation plays a central role in organizing and regulating ribonucleoprotein granules within cells. Disruptions to this process-such as the aberrant aggregation of repeat-expanded RNA-are associated with numerous neurological disorders. Here we study the role of biomolecular condensates in irreversible RNA aggregation. We find that physiologically relevant and disease-associated repeat RNAs spontaneously undergo an age-dependent percolation transition inside multi-component condensates to form nanoscale clusters. Homotypic RNA clusters drive the emergence of multi-phasic condensate structures, with an RNA-rich solid core surrounded by an RNA-depleted fluid shell. The timescale of RNA clustering is determined by sequence, secondary structure and repeat length. Importantly, G3BP1, the core scaffold of stress granules, introduces heterotypic buffering to homotypic RNA-RNA interactions and prevents RNA clustering in an ATP-independent manner. Our work suggests that biomolecular condensates can act as sites for RNA aggregation and highlights the chaperone-like function of RNA-binding proteins against aberrant RNA phase transitions.
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