Evidence map›Paper›PMID 31848352›Full record

ArticleNature communications2019

PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome.

Deepti Sharma, Louis De Falco, Sivaraman Padavattan, Chang Rao, Susana Geifman-Shochat, Chuan-Fa Liu, Curt A Davey

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.0field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  5. Journal of applied crystallography · 2026
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  16. Review
  17. Beyond the mono-nucleosome.Biochemical Society transactions · 2025
    Review
  18. Review
  19. 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

7 authors at 1 institution in 2 countries.

Deepti SharmaSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore.ORCID http://orcid.org/0000-0003-1760-2705
Louis De FalcoSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore.ORCID http://orcid.org/0000-0003-1874-1838
Sivaraman PadavattanSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore.
Chang RaoSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore.
Susana Geifman-ShochatSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore.
Chuan-Fa LiuSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore.ORCID http://orcid.org/0000-0001-7433-2081
Curt A DaveySchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Singapore. davey@ntu.edu.sg.ORCID http://orcid.org/0000-0003-2632-775X
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The poly(ADP-ribose) polymerase, PARP1, plays a key role in maintaining genomic integrity by detecting DNA damage and mediating repair. γH2A.X is the primary histone marker for DNA double-strand breaks and PARP1 localizes to H2A.X-enriched chromatin damage sites, but the basis for this association is not clear. We characterize the kinetics of PARP1 binding to a variety of nucleosomes harbouring DNA double-strand breaks, which reveal that PARP1 associates faster with (γ)H2A.X- versus H2A-nucleosomes, resulting in a higher affinity for the former, which is maximal for γH2A.X-nucleosome that is also the activator eliciting the greatest poly-ADP-ribosylation catalytic efficiency. The enhanced activities with γH2A.X-nucleosome coincide with increased accessibility of the DNA termini resulting from the H2A.X-Ser139 phosphorylation. Indeed, H2A- and (γ)H2A.X-nucleosomes have distinct stability characteristics, which are rationalized by mutational analysis and (γ)H2A.X-nucleosome core crystal structures. This suggests that the γH2A.X epigenetic marker directly facilitates DNA repair by stabilizing PARP1 association and promoting catalysis.

Indexed as

Basic Helix-Loop-Helix ProteinsBiocatalysisCrystallography, X-RayDNA Breaks, Double-StrandedDNA RepairEpigenesis, GeneticHistonesModels, MolecularNerve Tissue ProteinsNucleosomesPoly (ADP-Ribose) Polymerase-1Poly ADP RibosylationRecombinant ProteinsBasic Helix-Loop-Helix ProteinsH2AX protein, humanHistonesNerve Tissue ProteinsNPAS1 protein, humanNucleosomesPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Recombinant Proteins

Identifiers

PMID31848352
PMCPMC6917767
OpenAlexW2996208548

What OpenQuestion holds

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Registered trials

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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.