Evidence map›Paper›PMID 40712289›Full record

ReviewDNA repair2025

Multiple functions of PARP1 in the repair of DNA double strand breaks.

Raquel Ortega, Benjamin G Bitler, Nausica Arnoult

Abstract readReview
In one paragraph

Review in DNA repair, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. PARP1-mediated 5' flap dynamics facilitate Okazaki fragment maturation.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
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.

Raquel OrtegaDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, CO 80309, USA; Division of Reproductive Sciences, Department of Obstetrics and Gynecology, University of Colorado Denver, Anschutz Medical Campus, Aurora, CO 80045, USA.
Benjamin G BitlerDivision of Reproductive Sciences, Department of Obstetrics and Gynecology, University of Colorado Denver, Anschutz Medical Campus, Aurora, CO 80045, USA.
Nausica ArnoultDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, CO 80309, USA. Electronic address: nausica.arnoult@colorado.edu.

Funding

Targeting Wnt signaling in therapy-resistant ovarian cancerR37CA261987 · NCI · UNIVERSITY OF COLORADO DENVER · PI Benjamin G Bitler · 2021 to 2026
$2.4M
Deciphering the role of heterochromatin in telomere function and maintenance mechanismsR35GM143108 · NIGMS · UNIVERSITY OF COLORADO · PI ARNOULT, NAUSICA C. · 2021 to 2025
$1.9M
Deciphering the function of the APE2 nuclease during repair by alternative end-joining and its role in HR-deficient cellsR01CA266100 · NCI · UNIVERSITY OF COLORADO · PI Nausica C. Arnoult · 2022 to 2026
$1.7M
NCI NIH HHS R01 CA266100NCI NIH HHS R37 CA261987NIGMS NIH HHS R35 GM143108
6 · The paper itself

Abstract

Poly(ADP-ribose) polymerase 1 (PARP1) is one of the most abundant nuclear proteins in human cells and plays critical roles in numerous cellular processes, including the response to DNA damage. PARP1 is activated by and rapidly localizes to both single- and double-strand breaks, where it catalyzes the addition of poly(ADP-ribose) chains onto itself and other chromatin- or repair-associated proteins. While the role of PARP in single-strand break repair is established, its functions at double-strand breaks (DSBs) are more complex, as it can promote or inhibit various steps in the multiple pathways that repair DSBs. In this review, we examine the DSB repair contributions of PARP1, as well as those of PARP2 and PARP3, which are also activated upon damage. We discuss their influence on chromatin regulation at break sites, their role in repair pathway selection, and finally, the regulation of repair mechanisms, including homologous recombination, non-homologous end-joining, and microhomology-mediated end-joining. Understanding these diverse and sometimes opposing roles is especially important in light of the clinical use of PARP inhibitors in cancers deficient in homologous recombination repair.

Indexed as

DNA Breaks, Double-StrandedDNA RepairPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesAnimalsChromatinDNADNA End-Joining RepairHumansChromatinDNAPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesDouble strand breakDSB repairHRMMEJNHEJPARPPARylation

Identifiers

PMID40712289
PMCPMC12494070

What OpenQuestion holds

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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.