ArticleeLife2025
Decoding phase separation of prion-like domains through data-driven scaling laws.
Article in eLife, 2025. 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.
- Quenching the thirst internally: separating miRNA from target mRNA by condensation of AGO1.The Plant cell · 2026Article
- Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026Article
- Backbone rigidity encodes universal viscoelastic signatures in biomolecular condensates.Biophysical journal · 2026Article
- A Systematic Evaluation of Protein Phase Separation Predictors across Diverse Protein Landscapes.Computational and structural biotechnology journal · 2026Article
- Molecular basis for thermoresponsive protein condensation in plants.bioRxiv : the preprint server for biology · 2025Article
- Biomolecular condensate microstructure is invariant to sequence-encoded molecular and macroscopic properties.Soft matter · 2025Article
- Biomolecular condensate microstructure couples molecular and mesoscale properties.bioRxiv : the preprint server for biology · 2025Article
- Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025Review
- Characterizing protein sequence determinants of nuclear condensates by high-throughput pooled imaging with CondenSeq.Nature methods · 2025Article
- FINCHES: A Computational Framework for Predicting Intermolecular Interactions in Intrinsically Disordered Proteins.International journal of molecular sciences · 2025Review
- Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates.Chemical science · 2025Article
- Sequence-based prediction of intermolecular interactions driven by disordered regions.Science (New York, N.Y.) · 2025Article
- Converging frontiers in biomolecular condensate and synthetic cell research.npj biomedical innovations · 2025Review
- Prediction of phase-separation propensities of disordered proteins from sequence.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Chemically Informed Coarse-Graining of Electrostatic Forces in Charge-Rich Biomolecular Condensates.ACS central science · 2025Article
- Article
- Benchmarking residue-resolution protein coarse-grained models for simulations of biomolecular condensates.PLoS computational biology · 2025Article
- Increased preference for lysine over arginine in spike proteins of SARS-CoV-2 BA.2.86 variant and its daughter lineages.PloS one · 2025Article
- Modeling biomolecular condensates across scales: Atomistic, coarse-grained, and data-driven approaches.Advances in physics: X · 2025Article
- Amino acid-dependent phase equilibrium and material properties of tetrapeptide condensates.Cell reports. Physical science · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Proteins containing prion-like low complexity domains (PLDs) are common drivers of the formation of biomolecular condensates and are prone to misregulation due to amino acid mutations. Here, we exploit the accuracy of our residue-resolution coarse-grained model, Mpipi, to quantify the impact of amino acid mutations on the stability of 140 PLD mutants from six proteins (hnRNPA1, TDP43, FUS, EWSR1, RBM14, and TIA1). Our simulations reveal the existence of scaling laws that quantify the range of change in the critical solution temperature of PLDs as a function of the number and type of amino acid sequence mutations. These rules are consistent with the physicochemical properties of the mutations and extend across the entire family tested, suggesting that scaling laws can be used as tools to predict changes in the stability of PLD condensates. Our work offers a quantitative lens into how the emergent behavior of PLD solutions vary in response to physicochemical changes of single PLD molecules.
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