Evidence map›Paper›PMID 27235397›Full record

ArticleThe Journal of biological chemistry2016

CHD4 Is a Peripheral Component of the Nucleosome Remodeling and Deacetylase Complex.

Jason K K Low, Sarah R Webb, Ana P G Silva, Hinnerk Saathoff, Daniel P Ryan, Mario Torrado, Mattias Brofelth, Benjamin L Parker, Nicholas E Shepherd, Joel P Mackay

Abstract read
In one paragraph

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 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Human mutation · 2026
    Review
  7. Article
  8. Animals : an open access journal from MDPI · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Jason K K LowFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and.
Sarah R WebbFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and.
Ana P G SilvaFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and.
Hinnerk SaathoffFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and.
Daniel P Ryanthe Department of Genome Sciences, John Curtin School of Medical Research, Australian National University, Acton, Australian Capital Territory 2601, Australia.
Mario TorradoFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and.
Mattias BrofelthFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and.
Benjamin L ParkerFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and.
Nicholas E ShepherdFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and n.shepherd@imb.uq.edu.au.
Joel P MackayFrom the School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia and joel.mackay@sydney.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromatin remodeling enzymes act to dynamically regulate gene accessibility. In many cases, these enzymes function as large multicomponent complexes that in general comprise a central ATP-dependent Snf2 family helicase that is decorated with a variable number of regulatory subunits. The nucleosome remodeling and deacetylase (NuRD) complex, which is essential for normal development in higher organisms, is one such macromolecular machine. The NuRD complex comprises ∼10 subunits, including the histone deacetylases 1 and 2 (HDAC1 and HDAC2), and is defined by the presence of a CHD family remodeling enzyme, most commonly CHD4 (chromodomain helicase DNA-binding protein 4). The existing paradigm holds that CHD4 acts as the central hub upon which the complex is built. We show here that this paradigm does not, in fact, hold and that CHD4 is a peripheral component of the NuRD complex. A complex lacking CHD4 that has HDAC activity can exist as a stable species. The addition of recombinant CHD4 to this nucleosome deacetylase complex reconstitutes a NuRD complex with nucleosome remodeling activity. These data contribute to our understanding of the architecture of the NuRD complex.

Indexed as

AnimalsAutoantigensCell LineDNA HelicasesHistone Deacetylase 1Histone Deacetylase 2HumansMi-2 Nucleosome Remodeling and Deacetylase ComplexMiceNucleosomesAutoantigensCHD4 protein, humanDNA HelicasesHDAC1 protein, humanHdac1 protein, mouseHDAC2 protein, humanHdac2 protein, mouseHistone Deacetylase 1Histone Deacetylase 2Mi-2beta protein, mouseMi-2 Nucleosome Remodeling and Deacetylase ComplexNucleosomesCHD4chromatin remodelinggene regulationnucleosomenucleosome deacetylase complex (NuDe)nucleosome remodeling deacetylase (NuRD)structure-function

Identifiers

PMID27235397
PMCPMC4957066

What OpenQuestion holds

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Registered trials

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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.