Evidence map›Paper›PMID 28252050›Full record

ArticleScientific reports2017

Site-specific ADP-ribosylation of histone H2B in response to DNA double strand breaks.

Alina Rakhimova, Seiji Ura, Duen-Wei Hsu, Hong-Yu Wang, Catherine J Pears, Nicholas D Lakin

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
0.9field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Review
  6. Review
  7. Article
  8. Role of mono-ADP-ribosylation histone modification (Review).Experimental and therapeutic medicine · 2021
    Review
  9. Article
  10. Article
  11. Frontiers in cell and developmental biology · 2021
    Review
  12. Review
  13. Article
  14. Article
  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

6 authors at 1 institution in 1 country.

Alina RakhimovaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Seiji UraDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Duen-Wei HsuDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Hong-Yu WangDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Catherine J PearsDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Nicholas D LakinDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
University of Oxford · GB

Funding

Cancer Research UK 12353Cancer Research UK C1521/A12353Medical Research Council MR/L000164/1Medical Research Council MR/P028284/1National Centre for the Replacement, Refinement and Reduction of Animals in Research NC/M000834/1
6 · The paper itself

Abstract

ADP-ribosyltransferases (ARTs) modify proteins with single units or polymers of ADP-ribose to regulate DNA repair. However, the substrates for these enzymes are ill-defined. For example, although histones are modified by ARTs, the sites on these proteins ADP-ribosylated following DNA damage and the ARTs that catalyse these events are unknown. This, in part, is due to the lack of a eukaryotic model that contains ARTs, in addition to histone genes that can be manipulated to assess ADP-ribosylation events in vivo. Here we exploit the model Dictyostelium to identify site-specific histone ADP-ribosylation events in vivo and define the ARTs that mediate these modifications. Dictyostelium histones are modified in response to DNA double strand breaks (DSBs) in vivo by the ARTs Adprt1a and Adprt2. Adprt1a is a mono-ART that modifies H2BE18 in vitro, although disruption of this site allows ADP-ribosylation at H2BE19. Although redundancy between H2BE18 and H2BE19 ADP-ribosylation is also apparent following DSBs in vivo, by generating a strain with mutations at E18/E19 in the h2b locus we demonstrate these are the principal sites modified by Adprt1a/Adprt2. This identifies DNA damage induced histone mono-ADP-ribosylation sites by specific ARTs in vivo, providing a unique platform to assess how histone ADP-ribosylation regulates DNA repair.

Indexed as

ADP-RibosylationDNA Breaks, Double-StrandedAdenosine Diphosphate RiboseADP Ribose TransferasesDictyosteliumDNA RepairHistonesPoly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesAdenosine Diphosphate RiboseADP Ribose TransferasesHistonesPoly Adenosine Diphosphate RibosePoly(ADP-ribose) Polymerases

Identifiers

PMID28252050
PMCPMC5333086
OpenAlexW2591689499

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.