Evidence map›Paper›PMID 31685935›Full record

ArticleScientific reports2019

Acetylation of the histone H3 tail domain regulates base excision repair on higher-order chromatin structures.

Deb Ranjan Banerjee, Charles E Deckard, Yu Zeng, Jonathan T Sczepanski

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Correlating histone acetylation with nucleosome core particle dynamics and function.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Generation of Recombinant Nucleosomes Containing Site-Specific DNA Damage.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. The impact of epigenetic information on genome evolution.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
    Review
  14. Histone tails as signaling antennas of chromatin.Current opinion in structural biology · 2021
    Review
  15. Review
  16. 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

4 authors at 3 institutions in 2 countries.

Deb Ranjan BanerjeeDepartment of Chemistry, National Institute of Technology, Durgapur, West Bengal, India.
Charles E DeckardDepartment of Chemistry, Texas A&M University, College Station, Texas, 77843, United States.
Yu ZengDepartment of Microbial Pathogenesis and Immunology, Texas A&M University, College Station, Texas, 77843, United States.
Jonathan T SczepanskiDepartment of Chemistry, Texas A&M University, College Station, Texas, 77843, United States. jon.sczepanski@chem.tamu.edu.ORCID http://orcid.org/0000-0002-9275-2597
Texas A&M University · USNational Institute of Technology Durgapur · INTexas A&M Health Science Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite recent evidence suggesting that histone lysine acetylation contributes to base excision repair (BER) in cells, their exact mechanistic role remains unclear. In order to examine the influence of histone acetylation on the initial steps of BER, we assembled nucleosome arrays consisting of homogeneously acetylated histone H3 (H3K18 and H3K27) and measured the repair of a site-specifically positioned 2'-deoxyuridine (dU) residue by uracil DNA glycosylase (UDG) and apurinic/apyrimidinic endonuclease 1 (APE1). We find that H3K18ac and H3K27ac differentially influence the combined activities of UDG/APE1 on compact chromatin, suggesting that acetylated lysine residues on the H3 tail domain play distinct roles in regulating the initial steps of BER. In addition, we show that the effects of H3 tail domain acetylation on UDG/APE1 activity are at the nucleosome level and do not influence higher-order chromatin folding. Overall, these results establish a novel regulatory role for histone H3 acetylation during the initiation of BER on chromatin.

Indexed as

DNA RepairProtein DomainsAcetylationChromatinDNA-(Apurinic or Apyrimidinic Site) LyaseHistonesHumansModels, MolecularMolecular ConformationNucleosomesStructure-Activity RelationshipUracil-DNA GlycosidaseAPEX1 protein, humanChromatinDNA-(Apurinic or Apyrimidinic Site) LyaseHistonesNucleosomesUracil-DNA Glycosidase

Identifiers

PMID31685935
PMCPMC6828659
OpenAlexW2988152034

What OpenQuestion holds

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LicenceCC BY
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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.