Evidence map›Paper›PMID 27587838›Full record

ArticleJournal of cell science2016

The role of ADP-ribosylation in regulating DNA interstrand crosslink repair.

Alasdair R Gunn, Benito Banos-Pinero, Peggy Paschke, Luis Sanchez-Pulido, Antonio Ariza, Joseph Day, Mehera Emrich, David Leys, Chris P Ponting, Ivan Ahel and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Frontiers in cell and developmental biology · 2021
    Review
  7. Article
  8. Article
  9. Targeting Nuclear NADCancers · 2020
    Article
  10. Review
  11. Article
  12. Review
  13. 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

11 authors at 3 institutions in 1 country.

Alasdair R GunnDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Benito Banos-PineroDunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
Peggy PaschkeDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Luis Sanchez-PulidoMRC Human Genetics Unit, The MRC Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, Scotland, UK.
Antonio ArizaDunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK.
Joseph DayDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Mehera EmrichDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
David LeysManchester Institute of Biotechnology, University of Manchester, Princess Street 131, Manchester, M1 7DN, UK.
Chris P PontingMRC Human Genetics Unit, The MRC Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, Scotland, UK.
Ivan AhelDunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK ivan.ahel@path.ox.ac.uk nicholas.lakin@bioch.ox.ac.uk.ORCID 0000-0002-9446-3756
Nicholas D LakinDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK ivan.ahel@path.ox.ac.uk nicholas.lakin@bioch.ox.ac.uk.ORCID 0000-0003-4999-5814
University of Oxford · GBWestern General Hospital · GBUniversity of Manchester · GB

Funding

Cancer Research UK 12353Cancer Research UK C1521/A12353European Research Council 281739Medical Research Council MC_UU_12008/1Medical Research Council MC_UU_12021/1Medical Research Council MR/L000164/1National Centre for the Replacement, Refinement and Reduction of Animals in Research NC/K00137X/1Wellcome Trust 101794
6 · The paper itself

Abstract

ADP-ribosylation by ADP-ribosyltransferases (ARTs) has a well-established role in DNA strand break repair by promoting enrichment of repair factors at damage sites through ADP-ribose interaction domains. Here, we exploit the simple eukaryote Dictyostelium to uncover a role for ADP-ribosylation in regulating DNA interstrand crosslink repair and redundancy of this pathway with non-homologous end-joining (NHEJ). In silico searches were used to identify a protein that contains a permutated macrodomain (which we call aprataxin/APLF-and-PNKP-like protein; APL). Structural analysis reveals that this permutated macrodomain retains features associated with ADP-ribose interactions and that APL is capable of binding poly(ADP-ribose) through this macrodomain. APL is enriched in chromatin in response to cisplatin treatment, an agent that induces DNA interstrand crosslinks (ICLs). This is dependent on the macrodomain of APL and the ART Adprt2, indicating a role for ADP-ribosylation in the cellular response to cisplatin. Although adprt2

Indexed as

DNA RepairCell NucleusChromatinCisplatinCross-Linking ReagentsDictyosteliumDNADNA DamageDNA End-Joining RepairModels, MolecularPoly Adenosine Diphosphate RiboseProtein BindingProtein DomainsProtozoan ProteinsChromatinCisplatinCross-Linking ReagentsDNAPoly Adenosine Diphosphate RiboseProtozoan ProteinsADP-ribosyltransferasesDictyosteliumInterstrand crosslinkPARPs

Identifiers

PMID27587838
PMCPMC5087659
OpenAlexW2511096017

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.