ArticleThe Journal of biological chemistry2016
The N-terminal Region of Chromodomain Helicase DNA-binding Protein 4 (CHD4) Is Essential for Activity and Contains a High Mobility Group (HMG) Box-like-domain That Can Bind Poly(ADP-ribose).
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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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
37 citing papers in PubMed, 63 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
- Review
- Intrinsically Disordered Regions Define Unique Protein Interaction Networks in CHD Family Remodelers.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Article
- Review
- Case Report: Novel mutation in CHD4 triggers occult breast cancer with bone metastases.Frontiers in oncology · 2025Article
- How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024Review
- Microscale Thermophoresis Analysis of Chromatin Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Missense Mutation in Human CHD4 Causes Ventricular Noncompaction by Repressing ADAMTS1.Circulation research · 2023Article
- Characterization of the nuclear import of the human CHD4-NuRD complex.Journal of cell science · 2023Article
- The H2A.Z and NuRD associated protein HMG20A controls early head and heart developmental transcription programs.Nature communications · 2023Article
- The role of auxiliary domains in modulating CHD4 activity suggests mechanistic commonality between enzyme families.Nature communications · 2022Article
- Review
- Divergent regulatory roles of NuRD chromatin remodeling complex subunits GATAD2 and CHD4 in Caenorhabditis elegans.Genetics · 2022Article
- Unique protein interaction networks define the chromatin remodelling module of the NuRD complex.The FEBS journal · 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
- PARP1-modulated chromatin remodeling is a new target for cancer treatment.Medical oncology (Northwood, London, England) · 2021Review
- PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling.International journal of molecular sciences · 2021Review
- Role of Chromodomain-Helicase-DNA-Binding Protein 4 (CHD4) in Breast Cancer.Frontiers in oncology · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Chromodomain Helicase DNA-binding protein 4 (CHD4) is a chromatin-remodeling enzyme that has been reported to regulate DNA-damage responses through its N-terminal region in a poly(ADP-ribose) polymerase-dependent manner. We have identified and determined the structure of a stable domain (CHD4-N) in this N-terminal region. The-fold consists of a four-α-helix bundle with structural similarity to the high mobility group box, a domain that is well known as a DNA binding module. We show that the CHD4-N domain binds with higher affinity to poly(ADP-ribose) than to DNA. We also show that the N-terminal region of CHD4, although not CHD4-N alone, is essential for full nucleosome remodeling activity and is important for localizing CHD4 to sites of DNA damage. Overall, these data build on our understanding of how CHD4-NuRD acts to regulate gene expression and participates in the DNA-damage response.
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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.