ArticleNature communications2022
Intracellular phase separation of globular proteins facilitated by short cationic peptides.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Hydration free energy is an incomplete predictor of globular protein incorporation into condensates.Biophysical journal · 2026Article
- Reversible Nucleolar Complex Coacervation by Short Cationic Peptides.Journal of the American Chemical Society · 2026Article
- Protein lactylation in health and diseases: molecular mechanisms, biological significance, and clinical implications.Signal transduction and targeted therapy · 2026Review
- Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro.EMBO reports · 2026Article
- Enzymatically reconfigurable liquid crystalline coacervate microdroplets as protocell models.Nature communications · 2025Article
- POMPOMS: Crosslinked Biomolecular Condensates as a Versatile Platform for Multifunctional Protein Microparticles.Biomacromolecules · 2025Article
- Biomolecular condensates: molecular structure, biological functions, diseases, and therapeutic targets.Molecular biomedicine · 2025Review
- POMPOMS: Crosslinked biomolecular condensates as a versatile platform for multifunctional protein microparticles.bioRxiv : the preprint server for biology · 2025Article
- Cationic Amino Acid Identity and Net Charge Influence Condensate Properties inBiomacromolecules · 2025Article
- Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates.Chemical science · 2025Article
- Engineering Protein-Polyelectrolyte Interactions for Cellular Applications.Annual review of chemical and biomolecular engineering · 2025Review
- Glycosylation Weakens Skp1 Homodimerization inBiochemistry · 2025Article
- Recent advances in recombinant production of soluble proteins in E. coli.Microbial cell factories · 2025Review
- Article
- De novo designed YK peptides forming reversible amyloid for synthetic protein condensates in mammalian cells.Nature communications · 2024Article
- Fluorescent protein tags affect the condensation properties of a phase-separating viral protein.Molecular biology of the cell · 2024Article
- Selectivity of Complex Coacervation in Multi-Protein Mixtures.bioRxiv : the preprint server for biology · 2024Article
- Understanding the Impacts of Molecular and Macromolecular Crowding Agents on Protein-Polymer Complex Coacervates.Biomacromolecules · 2023Article
- Quantifying charge state heterogeneity for proteins with multiple ionizable residues.Biophysical journal · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Phase separation provides intracellular organization and underlies a variety of cellular processes. These biomolecular condensates exhibit distinct physical and material properties. Current strategies for engineering condensate formation include using intrinsically disordered domains and altering protein surface charge by chemical supercharging or site-specific mutagenesis. We propose adding to this toolbox designer peptide tags that provide several potential advantages for engineering protein phase separation in bacteria. Herein, we demonstrate the use of short cationic peptide tags for sequestration of proteins of interest into bacterial condensates and provide a foundational study for their development as tools for condensate engineering. Using a panel of GFP variants, we demonstrate how cationic tag and globular domain charge contribute to intracellular phase separation in E. coli and observe that the tag can affect condensate disassembly at a given net charge near the phase separation boundary. We showcase the broad applicability of these tags by appending them onto enzymes and demonstrating that the sequestered enzymes remain catalytically active.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.