Evidence map›Paper›PMID 28847821›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2017

The tale of a tail: histone H4 acetylation and the repair of DNA breaks.

Surbhi Dhar, Ozge Gursoy-Yuzugullu, Ramya Parasuram, Brendan D Price

Open access · bronzeAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
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

74 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Comprehensive analysis and validation of mBMC veterinary research · 2026
    Article
  3. Article
  4. Review
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  6. Review
  7. Review
  8. Article
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  13. Article
  14. Article
  15. Article
  16. Cryo-EM structures reveal the acetylation process of piccolo NuA4.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Review
  18. Article
  19. Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Surbhi DharDepartment of Radiation Oncology, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02132, USA.
Ozge Gursoy-YuzugulluDepartment of Radiation Oncology, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02132, USA.
Ramya ParasuramDepartment of Radiation Oncology, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02132, USA.
Brendan D PriceDepartment of Radiation Oncology, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02132, USA brendan_price@dfci.harvard.edu.ORCID http://orcid.org/0000-0001-7075-4906
Google (United States) · US

Funding

RADIATION MODULATION OF THE P53 GENER01CA064585 · NCI · DANA-FARBER CANCER INSTITUTE · PI PRICE, BRENDAN D · 1995 to 2016
$4.6M
Functional Analysis of the Tip60 ComplexR01CA093602 · NCI · DANA-FARBER CANCER INSTITUTE · PI PRICE, BRENDAN D · 2002 to 2018
$4.3M
Nucleosome Dynamics and the Repair of DNA DamageR01CA177884 · NCI · DANA-FARBER CANCER INST · PI PRICE, BRENDAN D · 2013 to 2017
$1.8M
NCI NIH HHS R01 CA064585NCI NIH HHS R01 CA093602NCI NIH HHS R01 CA177884
6 · The paper itself

Abstract

The ability of cells to detect and repair DNA double-strand breaks (DSBs) within the complex architecture of the genome requires co-ordination between the DNA repair machinery and chromatin remodelling complexes. This co-ordination is essential to process damaged chromatin and create open chromatin structures which are required for repair. Initially, there is a PARP-dependent recruitment of repressors, including HP1 and several H3K9 methyltransferases, and exchange of histone H2A.Z by the NuA4-Tip60 complex. This creates repressive chromatin at the DSB in which the tail of histone H4 is bound to the acidic patch on the nucleosome surface. These repressor complexes are then removed, allowing rapid acetylation of the H4 tail by Tip60. H4 acetylation blocks interaction between the H4 tail and the acidic patch on adjacent nucleosomes, decreasing inter-nucleosomal interactions and creating open chromatin. Further, the H4 tail is now free to recruit proteins such as 53BP1 to DSBs, a process modulated by H4 acetylation, and provides binding sites for bromodomain proteins, including ZMYND8 and BRD4, which are important for DSB repair. Here, we will discuss how the H4 tail functions as a dynamic hub that can be programmed through acetylation to alter chromatin packing and recruit repair proteins to the break site.This article is part of the themed issue 'Chromatin modifiers and remodellers in DNA repair and signalling'.

Indexed as

DNA Breaks, Double-StrandedDNA RepairAcetylationAnimalsChromatinHistonesHumansChromatinHistones53BP1chromatin remodellingdouble-strand break repairgenome stabilityH2A.ZH4 acetylation

Identifiers

PMID28847821
PMCPMC5577462
OpenAlexW2749774911

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.