Evidence map›Paper›PMID 33087268›Full record

ReviewDNA repair2020

Fine-tuning of DNA base excision/strand break repair via acetylation.

Kishor K Bhakat, Shiladitya Sengupta, Sankar Mitra

Open access · greenAbstract readReview
In one paragraph

Review in DNA repair, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
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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

3 authors at 3 institutions in 1 country.

Kishor K BhakatDepartment of Genetics, Cell Biology and Anatomy, University of Nebraska Medical Center, Omaha, NE, 68198, USA. Electronic address: kishor.bhakat@unmc.edu.
Shiladitya SenguptaDepartment of Radiation Oncology, Houston Methodist Research Institute, Houston, TX, 77030, USA.
Sankar MitraHouston Methodist Cancer Center and Department of Radiation Oncology, Houston Methodist Research Institute, Houston, TX, 77030, USA; Weill Cornell Medical College, Cornell University, New York, NY, 10065, USA. Electronic address: smitra2@houstonmethodist.org.
Cornell University · USHouston Methodist · USUniversity of Nebraska Medical Center · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI WALTER J. CHAZIN · 2001 to 2026
$89.6M
Repair of Oxidative Genome Damage Associated with Gene ActivationR01GM105090 · NIGMS · METHODIST HOSPITAL RESEARCH INSTITUTE · PI MITRA, SANKAR · 2014 to 2017
$1.2M
Elucidating the role of acetylation of APE1 in tumor growth and chemoresistanceR03CA235214 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI BHAKAT, KISHOR K · 2019 to 2020
$161k
NCI NIH HHS P01 CA092584NCI NIH HHS R03 CA235214NIGMS NIH HHS R01 GM105090
6 · The paper itself

Abstract

In addition to the key roles of reversible acetylation of histones in chromatin in epigenetic regulation of gene expression, acetylation of nonhistone proteins by histone acetyltransferases (HATs) p300 and CBP is involved in DNA transactions, including repair of base damages and strand breaks. We characterized acetylation of human NEIL1 DNA glycosylase and AP-endonuclease 1 (APE1), which initiate repair of oxidized bases and single-strand breaks (SSBs), respectively. Acetylation induces localized conformation change because of neutralization of the positive charge of specific acetyl-acceptor Lys residues, which are often present in clusters. Acetylation in NEIL1, APE1, and possibly other base excision repair (BER)/SSB repair (SSBR) enzymes by HATs, prebound to chromatin, induces assembly of active repair complexes on the chromatin. In this review, we discuss the roles of acetylation of NEIL1 and APE1 in modulating their activities and complex formation with other proteins for fine-tuning BER in chromatin. Further, the implications of promoter/enhancer-bound acetylated BER protein complexes in the regulation of transcriptional activation, mediated by complex interplay of acetylation and demethylation of histones are discussed.

Indexed as

DNA RepairProtein Processing, Post-TranslationalAcetylationDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageDNA GlycosylasesHistone AcetyltransferasesHumansAPEX1 protein, humanDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA GlycosylasesHistone AcetyltransferasesNEIL1 protein, humanAcetylationAPE1Base excision repair (BER)BER complexesDNA base damageHistone acetyltransferases (HATs)NEIL1

Identifiers

PMID33087268
PMCPMC7586711
OpenAlexW3094520551

What OpenQuestion holds

Textmetadata
LicenceTDM
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.