ArticleMethods in molecular biology (Clifton, N.J.)2025
Assessing the Effect of Chromatin-Binding Enzymes on Condensed Chromatin with Optical Tweezers.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Insights from single-molecule force spectroscopy into chromatin topology.Biophysical reviews · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of biomolecular condensates in vitro and in vivo has become an increasingly important subject of studies. One particular area of interest is the phase separation of chromatin in the nucleus. However, the interplay of condensed chromatin and chromatin-binding enzymes has barely been studied as of now. Here, we show an optical tweezer-based assay that uses controlled fusion of two condensates to probe the effect of enzymes, such as chromatin remodeling motor proteins, on the fluidity of condensates. The assay provides a powerful tool that enables the study of if and how chromatin-enzyme interactions alter biophysical properties in these dense chromatin condensates.
Indexed as
Identifiers
39704952What OpenQuestion holds
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.