ArticleProceedings of the National Academy of Sciences of the United States of America2012
Bivalent recognition of nucleosomes by the tandem PHD fingers of the CHD4 ATPase is required for CHD4-mediated repression.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 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.
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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
77 citing papers in PubMed, 118 citations in OpenAlex.
- Molecular Acrobats: How CHD Remodelers Shape the Genetic Playground to License Cell Identity.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Role of CHD4 in tumor progression, DNA damage response and treatment resistance (Review).Oncology reports · 2026Review
- Locus-specific proteomics identifies novel regulators of Epstein-Barr virus lytic reactivation.Journal of virology · 2026Article
- Myositis-specific autoantibodies recognising Mi2 also target the AIRE protein at a shared PHD zinc finger.Annals of the rheumatic diseases · 2026Article
- G34R cancer mutation alters the conformational ensemble and dynamics of the histone H3.3 tails.Nucleic acids research · 2026Article
- Review
- Anti-Mi2 autoantibodies target PHD fingers of SP140L and TIF1γ, while anti-TIF1γ autoantibodies primarily bind TIF1γ outside the PHD region.Rheumatology (Oxford, England) · 2025Article
- Anti-Mi2 autoantibodies target the PHD fingers of SP140L and TIF1γ, while anti-TIF1γ autoantibodies primarily recognize epitopes outside the PHD region of TIF1γ.medRxiv : the preprint server for health sciences · 2025Article
- Review
- Generation and characterization of a mouse model of conditional Chd4 knockout in the endometrial epithelium.PloS one · 2025Article
- How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024Review
- ISWI chromatin remodeling complexes recruit NSD2 and H3K36me2 in pericentromeric heterochromatin.The Journal of cell biology · 2024Article
- Chromodomain helicase DNA binding protein 4 in cell fate decisions.Hearing research · 2023Review
- Gene silencing dynamics are modulated by transiently active regulatory elements.Molecular cell · 2023Article
- DLX1 and the NuRD complex cooperate in enhancer decommissioning and transcriptional repression.Development (Cambridge, England) · 2022Article
- Chromodomain helicase DNA-binding 4 (CHD4) regulates early B cell identity and V(D)J recombination.Immunological reviews · 2022Review
- Sentinels of chromatin: chromodomain helicase DNA-binding proteins in development and disease.Genes & development · 2021Review
- Conformational Dynamics of Histone H3 Tails in Chromatin.The journal of physical chemistry letters · 2021Article
- Histone H3 N-terminal mimicry drives a novel network of methyl-effector interactions.The Biochemical journal · 2021Article
- Chromatin Remodeling in the Brain-aInternational journal of molecular sciences · 2021Review
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
CHD4 is a catalytic subunit of the NuRD (nucleosome remodeling and deacetylase) complex essential in transcriptional regulation, chromatin assembly and DNA damage repair. CHD4 contains tandem plant homeodomain (PHD) fingers connected by a short linker, the biological function of which remains unclear. Here we explore the combinatorial action of the CHD4 PHD1/2 fingers and detail the molecular basis for their association with chromatin. We found that PHD1/2 targets nucleosomes in a multivalent manner, concomitantly engaging two histone H3 tails. This robust synergistic interaction displaces HP1γ from pericentric sites, inducing changes in chromatin structure and leading to the dispersion of the heterochromatic mark H3K9me3. We demonstrate that recognition of the histone H3 tails by the PHD fingers is required for repressive activity of the CHD4/NuRD complex. Together, our data elucidate the molecular mechanism of multivalent association of the PHD fingers with chromatin and reveal their critical role in the regulation of CHD4 functions.
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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.