ArticleNature methods2025
Characterizing protein sequence determinants of nuclear condensates by high-throughput pooled imaging with CondenSeq.
Article in Nature methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins.Nature communications · 2026Article
- AI-discovered protein fragments as generalizable regulators of biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- Rethinking bioinformatics in liquid-liquid phase separation: data resources, predictive models, and an event-centric perspective.Briefings in bioinformatics · 2026Review
- Disordered protein LAT encodes relative levels of signaling pathways in T cell activation.Science (New York, N.Y.) · 2026Article
- From chromosomal protein disorder to chromatin phase separation.Epigenetics & chromatin · 2026Review
- How to spy on condensates.Nature methods · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Biomolecular condensates organize numerous subcellular processes and have been implicated in diseases, including neurodegeneration and cancer. Protein sequences intrinsically encode their propensity to form condensates, but specific sequence features that regulate this behavior have not been systematically explored at scale. Here, we develop CondenSeq, a high-throughput pooled imaging with in situ sequencing approach to measure propensities of thousands of protein sequences to form nuclear condensates. Leveraging the large scale of these experiments, we evaluated the impacts of dozens of sequence features across a wide range of sequence contexts, identifying several features with highly consistent, context-independent effects and others with less-consistent effects. We also identified multiple classes of condensates and discovered distinct sequence properties that drive their formation. Our results provide a systematic overview of the relationships between protein sequences and nuclear condensate formation and establish a general approach for further dissecting these relationships at scale.
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Registered trials
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