Evidence map›Paper›PMID 37171085›Full record

ArticleBiochemical Society transactions2023

The function and regulation of ADP-ribosylation in the DNA damage response.

Lena Duma, Ivan Ahel

Abstract read
In one paragraph

Article in Biochemical Society transactions, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. 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

2 authors.

Lena DumaSir William Dunn School of Pathology, University of Oxford, Oxford, U.K.ORCID 0000-0003-4373-5106
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford, U.K.ORCID 0000-0002-9446-3756

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Cancer Research UK 22284Cancer Research UK BST00260.BV00.01Cancer Research UK C35050/A22284Wellcome Trust 210634Wellcome Trust 210634/Z/18/ZWellcome Trust 223107
6 · The paper itself

Abstract

ADP-ribosylation is a post-translational modification involved in DNA damage response (DDR). In higher organisms it is synthesised by PARP 1-3, DNA strand break sensors. Recent advances have identified serine residues as the most common targets for ADP-ribosylation during DDR. To ADP-ribosylate serine, PARPs require an accessory factor, HPF1 which completes the catalytic domain. Through ADP-ribosylation, PARPs recruit a variety of factors to the break site and control their activities. However, the timely removal of ADP-ribosylation is also key for genome stability and is mostly performed by two hydrolases: PARG and ARH3. Here, we describe the key writers, readers and erasers of ADP-ribosylation and their contribution to the mounting of the DDR. We also discuss the use of PARP inhibitors in cancer therapy and the ways to tackle PARPi treatment resistance.

Indexed as

ADP-RibosylationDNA DamageHydrolasesProtein Processing, Post-TranslationalSerineHydrolasesSerineADP-ribosylationDNA synthesis and repairPARP

Identifiers

PMID37171085
PMCPMC10317172

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.