Evidence map›Paper›PMID 34380612›Full record

ArticleScience advances2021

Single-molecule measurements reveal that PARP1 condenses DNA by loop stabilization.

Nicholas A W Bell, Philip J Haynes, Katharina Brunner, Taiana Maia de Oliveira, Maria M Flocco, Bart W Hoogenboom, Justin E Molloy

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.8field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 37 citations in OpenAlex.

  1. Current status of radionuclide therapy targeting PARP in cancer: challenges and prospects.European journal of nuclear medicine and molecular imaging · 2026
    Review
  2. Article
  3. Article
  4. PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Measuring bridging forces in protein-DNA condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. PARP1 modulates METTL3 promoter chromatin accessibility and associated LPAR5 RNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2023
    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

7 authors at 3 institutions in 4 countries.

Nicholas A W BellThe Francis Crick Institute, London NW1 1AT, UK. nicholas.bell@crick.ac.uk.ORCID 0000-0003-0074-7158
Philip J HaynesLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK.ORCID 0000-0001-6313-2359
Katharina BrunnerThe Francis Crick Institute, London NW1 1AT, UK.
Taiana Maia de OliveiraMechanistic and Structural Biology, Discovery Sciences, BioPharmaceuticals R&D, AstraZeneca, Cambridge, UK.
Maria M FloccoMechanistic and Structural Biology, Discovery Sciences, BioPharmaceuticals R&D, AstraZeneca, Cambridge, UK.ORCID 0000-0002-1584-1190
Bart W HoogenboomLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK.ORCID 0000-0002-8882-4324
Justin E MolloyThe Francis Crick Institute, London NW1 1AT, UK.ORCID 0000-0002-8307-2450
The Francis Crick Institute · GBAstraZeneca (Australia) · AULondon Centre for Nanotechnology · GB

Funding

Medical Research Council MC_U117570592Wellcome Trust FC001119
6 · The paper itself

Abstract

Poly(ADP-ribose) polymerase 1 (PARP1) is an abundant nuclear enzyme that plays important roles in DNA repair, chromatin organization and transcription regulation. Although binding and activation of PARP1 by DNA damage sites has been extensively studied, little is known about how PARP1 binds to long stretches of undamaged DNA and how it could shape chromatin architecture. Here, using single-molecule techniques, we show that PARP1 binds and condenses undamaged, kilobase-length DNA subject to sub-piconewton mechanical forces. Stepwise decondensation at high force and DNA braiding experiments show that the condensation activity is due to the stabilization of DNA loops by PARP1. PARP inhibitors do not affect the level of condensation of undamaged DNA but act to block condensation reversal for damaged DNA in the presence of NAD

Indexed as

DNA RepairPoly(ADP-ribose) Polymerase InhibitorsChromatinDNADNA DamageChromatinDNAPoly(ADP-ribose) Polymerase Inhibitors

Identifiers

PMID34380612
PMCPMC8357241
OpenAlexW3191745374

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.