ArticleNucleic acids research2026
Combinatorial histone modifications direct ATP-dependent chromatin remodeling by NURF to promoter-proximal nucleosomes.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
The nucleosome remodeling factor (NURF) is a conserved imitation switch-containing ATP-dependent chromatin remodeling complex that slides nucleosomes to control transcription and genome organization. Recognition of histone modifications (HPTMs) by reader domains has been proposed to focus remodeler action at discrete genome targets, either by controlling recruitment or through local allosteric regulation of core enzymatic activities. To distinguish mechanisms by which HPTMs influence NURF, we defined the HPTM-binding specificity of NURF by screening novel combinations of histone-reader interactions. We observe the NURF-selective subunit (BPTF/NURF301) recognizes multiple H3 and H4 tail modifications via C-terminal PHD2 and bromodomains. Modified H3 recognition requires a new binding-pocket on PHD2 for H3K9AcS10p that cooperates with the known H3K4me3-binding hydrophobic cage to enable high-affinity binding to triply modified H3K4me3K9AcS10p. This combinatorial HPTM recognition discriminates and stabilizes NURF recruitment to +1 nucleosomes of active genes, maintaining nucleosome position to control transcription. Our data establish direct, causal links between HPTM recognition, remodeler recruitment, and consequent activity.
Indexed as
Identifiers
What 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.