Evidence map›Paper›PMID 37390817›Full record

ArticleMolecular cell2023

Molecular basis for the reversible ADP-ribosylation of guanosine bases.

Marion Schuller, Roberto Raggiaschi, Petra Mikolcevic, Johannes G M Rack, Antonio Ariza, YuGeng Zhang, Raphael Ledermann, Christoph Tang, Andreja Mikoc, Ivan Ahel

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Transition-state analysis of the arginine-specific human ADP-ribosyltransferase 1.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025
    Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. 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

10 authors at 3 institutions in 2 countries.

Marion SchullerSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Roberto RaggiaschiSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Petra MikolcevicDivision of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Johannes G M RackSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Antonio ArizaSchool of Biosciences, University of Sheffield, Sheffield, UK.
YuGeng ZhangSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Raphael LedermannDepartment of Biology, University of Oxford, Oxford, UK.
Christoph TangSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Andreja MikocDivision of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford, UK. Electronic address: ivan.ahel@path.ox.ac.uk.
University of Oxford · GBRudjer Boskovic Institute · HRUniversity of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Biotechnology and Biological Sciences Research Council BB/W016613/1Cancer Research UK 22284Cancer Research UK C35050/A22284Wellcome TrustWellcome Trust 210634Wellcome Trust 223107
6 · The paper itself

Abstract

Modification of nucleic acids by ADP-ribosylation is catalyzed by various ADP-ribosyltransferases, including the DarT enzyme. The latter is part of the bacterial toxin-antitoxin (TA) system DarTG, which was shown to provide control of DNA replication and bacterial growth as well as protection against bacteriophages. Two subfamilies have been identified, DarTG1 and DarTG2, which are distinguished by their associated antitoxins. While DarTG2 catalyzes reversible ADP-ribosylation of thymidine bases employing a macrodomain as antitoxin, the DNA ADP-ribosylation activity of DarTG1 and the biochemical function of its antitoxin, a NADAR domain, are as yet unknown. Using structural and biochemical approaches, we show that DarT1-NADAR is a TA system for reversible ADP-ribosylation of guanosine bases. DarT1 evolved the ability to link ADP-ribose to the guanine amino group, which is specifically hydrolyzed by NADAR. We show that guanine de-ADP-ribosylation is also conserved among eukaryotic and non-DarT-associated NADAR members, indicating a wide distribution of reversible guanine modifications beyond DarTG systems.

Indexed as

AntitoxinsGuanosineAdenosine Diphosphate RiboseADP Ribose TransferasesADP-RibosylationEukaryotic CellsAdenosine Diphosphate RiboseADP Ribose TransferasesAntitoxinsGuanosineADP-ribosylationADP-ribosyltransferasesDNA damageDNA modificationsPARPtoxin-antitoxin system

Identifiers

PMID37390817
PMCPMC11543638
OpenAlexW4382728082

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.