ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
A Molecular Recruitment Colocalization Platform for Visualizing Multi-Protein Interactions and Engineering Biomolecular Condensates in Living Cells.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Review
- A Molecular Recruitment Colocalization Platform for Visualizing Multi-Protein Interactions and Engineering Biomolecular Condensates in Living Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
Visualizing dynamic protein-protein interactions (PPIs) and phase-separated biomolecular condensates in live cells is crucial for understanding cellular processes. Here, a method is introduced for analyzing both PPIs and condensates, termed molecular recruitment colocalization (MRC), which localizes interacting partners and generates fluorescent signals at designated genomic loci. MRC enables the simultaneous visualization of multi-protein interactions and the preliminary estimation of binding affinities during PPIs. Through MRC, the study can quickly discover and validate new proteins or structural domains capable of forming condensates and can also integrate PPIs to study condensates. Furthermore, the versatility of MRC is demonstrated in phase-separated condensates research: programming phase separation sites to study the interactions and behaviors between different condensates, recruiting target proteins into programmable condensates, obtaining the properties of diverse engineered condensates, and probing the physical properties of condensates within live cells. Therefore, MRC can become a versatile platform for studying both PPIs and biomolecular condensates.
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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 Socratic graph.