ArticleInternational journal of molecular sciences2021
Integration of Data from Liquid-Liquid Phase Separation Databases Highlights Concentration and Dosage Sensitivity of LLPS Drivers.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 51 citations in OpenAlex.
- Liquid-liquid phase separation and the formation of amyloid fibrils from DcpS scavenger enzymes.Scientific reports · 2026Article
- Rethinking bioinformatics in liquid-liquid phase separation: data resources, predictive models, and an event-centric perspective.Briefings in bioinformatics · 2026Review
- Molecular basis and cellular effects of Janus-class-driven cytoplasmic PYK2 coacervates.Communications biology · 2026Article
- Protein language model identifies disordered, conserved motifs implicated in phase separation.eLife · 2025Article
- Phase-separating fusion proteins drive cancer by upsetting transcription regulation.Genome biology · 2025Article
- Comprehensive protein datasets and benchmarking for liquid-liquid phase separation studies.Genome biology · 2025Article
- Liquid-Liquid Phase Separation Associated with Intrinsically Disordered Proteins: Experimental and Computational Tools.Current protein & peptide science · 2025Review
- VUS next in rare diseases? Deciphering genetic determinants of biomolecular condensation.Orphanet journal of rare diseases · 2024Review
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- MLOsMetaDB, a meta-database to centralize the information on liquid-liquid phase separation proteins and membraneless organelles.Protein science : a publication of the Protein Society · 2024Article
- Article
- Theoretical and Data-Driven Approaches for Biomolecular Condensates.Chemical reviews · 2023Review
- Evolutionary Study of Protein Short Tandem Repeats in Protein Families.Biomolecules · 2023Article
- Time-Dependent Material Properties of Aging Biomolecular Condensates from Different Viscoelasticity Measurements in Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- Comparison of Biomolecular Condensate Localization and Protein Phase Separation Predictors.Biomolecules · 2023Article
- Viral dew: Phase separation and the formation of viral replication compartments.PLoS pathogens · 2023Article
- Article
- Modeling Concentration-dependent Phase Separation Processes Involving Peptides and RNA via Residue-Based Coarse-Graining.Journal of chemical theory and computation · 2023Article
- Intrinsically disordered regions that drive phase separation form a robustly distinct protein class.The Journal of biological chemistry · 2023Article
- Biomolecular condensate phase diagrams with a combinatorial microdroplet platform.Nature communications · 2022Article
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
Liquid-liquid phase separation (LLPS) is a molecular process that leads to the formation of membraneless organelles, representing functionally specialized liquid-like cellular condensates formed by proteins and nucleic acids. Integrating the data on LLPS-associated proteins from dedicated databases revealed only modest agreement between them and yielded a high-confidence dataset of 89 human LLPS drivers. Analysis of the supporting evidence for our dataset uncovered a systematic and potentially concerning difference between protein concentrations used in a good fraction of the in vitro LLPS experiments, a key parameter that governs the phase behavior, and the proteomics-derived cellular abundance levels of the corresponding proteins. Closer scrutiny of the underlying experimental data enabled us to offer a sound rationale for this systematic difference, which draws on our current understanding of the cellular organization of the proteome and the LLPS process. In support of this rationale, we find that genes coding for our human LLPS drivers tend to be dosage-sensitive, suggesting that their cellular availability is tightly regulated to preserve their functional role in direct or indirect relation to condensate formation. Our analysis offers guideposts for increasing agreement between in vitro and in vivo studies, probing the roles of proteins in LLPS.
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