ArticleEMBO reports2026
Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro.
Article in EMBO reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Development of Scanning Ion-Conductance Microscopy Based Tip-Enhanced Raman Spectroscopy in Liquid Environments.Nanotechnology · 2026Article
- Dual effect of α-synuclein disease variants on condensate formation.Nature communications · 2026Article
- Chain collapse, reduced dielectric, and water release drive protein phase separation.Biophysical journal · 2026Article
- Article
- Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.Nature communications · 2026Article
- Label-free biochemical imaging and time point analysis of neural organoids via deep learning-enhanced Raman microspectroscopy.Science advances · 2026Article
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- Bis-Tetrazine Fluorogenic (Silicon)-Rhodamine Dyes for Live-Cell Labeling.Journal of the American Chemical Society · 2026Article
- Conserved RNA helicase Vasa regulates ribonucleoprotein condensate dynamics and mRNA localization.iScience · 2026Article
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- Biomolecular condensation of cMLCK enables myosin motor phosphorylation in the heart.bioRxiv : the preprint server for biology · 2026Article
- Signal or noise? RNA-binding proteins and the challenges of binding site assignments.Nucleic acids research · 2026Review
- Biomolecular condensates provide a unique environment for redox-mediated protein crosslinking.bioRxiv : the preprint server for biology · 2026Article
- Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.bioRxiv : the preprint server for biology · 2026Article
- Meeting Review on India EMBO lecture course on RNA-protein complexes: from molecular assembly to physiological functions and disease.Biology open · 2026Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Fluorescent proteins and peptide tags are essential tools in cellular biology, but can alter the biochemical and physiological behavior of target proteins. Biomolecular condensates, which have emerged as key elements of cellular organization, are suggested to provide robustness to cells, yet they can also respond sensitively to small changes in environmental conditions including tags. Here, we investigate the effects of over twenty widely used tags on condensate formation in vitro, in cells, in various model organisms and by computational modelling. We find that tagging strongly influences condensation for some proteins, while others remain unaffected. Effects vary, with some tags enhancing and others decreasing condensation, with the outcome depending on the protein being tagged. Coarse-grained simulations suggest that the charge of the fluorescent protein tags is a critical factor modulating condensation behavior. Together, our results underscore the need to tag with caution and highlight the importance of careful experimental design and interpretation, especially in condensate studies, but also suggest that fluorescent protein tags could serve as a tool to modulate condensate properties.
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