Evidence map›Paper›PMID 30088474›Full record

ArticleeLife2018

Poly(ADP-ribose) polymerase 1 searches DNA via a 'monkey bar' mechanism.

Johannes Rudolph, Jyothi Mahadevan, Pamela Dyer, Karolin Luger

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.0field-weighted citation impact, top 10% 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

51 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026
    Article
  4. Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.Nature structural & molecular biology · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Histone ADP-ribosylation promotes resistance to PARP inhibitors by facilitating PARP1 release from DNA lesions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. PARP1 UFMylation ensures the stability of stalled replication forks.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. 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 2 institutions in 1 country.

Johannes RudolphDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, United States.ORCID http://orcid.org/0000-0003-0230-3323
Jyothi MahadevanDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, United States.
Pamela DyerDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, United States.ORCID http://orcid.org/0000-0002-0142-5073
Karolin LugerDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, United States.ORCID http://orcid.org/0000-0001-5136-5331
Howard Hughes Medical Institute · USUniversity of Colorado Boulder · US

Funding

Structure and Mechanism of Chromatin-Bound PARP1R01CA218255 · NCI · UNIVERSITY OF COLORADO · PI Karolin Luger · 2017 to 2026
$4.5M
Howard Hughes Medical InstituteUniversity of Colorado Cancer Center Pilot Funding Grant ST63501792University of Colorado Cancer Center Pilot Funding Grant ST63501792
6 · The paper itself

Abstract

Poly(ADP-ribose) polymerase 1 (PARP1) is both a first responder to DNA damage and a chromatin architectural protein. How PARP1 rapidly finds DNA damage sites in the context of a nucleus filled with undamaged DNA, to which it also binds, is an unresolved question. Here, we show that PARP1 association with DNA is diffusion-limited, and release of PARP1 from DNA is promoted by binding of an additional DNA molecule that facilitates a 'monkey bar' mechanism, also known as intersegment transfer. The WGR-domain of PARP1 is essential to this mechanism, and a point mutation (W589A) recapitulates the altered kinetics of the domain deletion. Demonstrating the physiological importance of the monkey bar mechanism for PARP1 function, the W589A mutant accumulates at sites of DNA damage more slowly following laser micro-irradiation than wild-type PARP1. Clinically relevant inhibitors of PARP1 did not alter the rate or mechanism of the release of PARP1 from DNA.

Indexed as

DNA RepairAnimalsCell LineDNADNA Mutational AnalysisHumansMicePoint MutationPoly (ADP-Ribose) Polymerase-1Protein BindingDNAPoly (ADP-Ribose) Polymerase-1biochemistrychemical biologyDNA damageDNA repairhumanPARP1protein DNA interactionstopped flow kinetics

Identifiers

PMID30088474
PMCPMC6135609
OpenAlexW2953105201

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.