Evidence map›Paper›PMID 37832523›Full record

ReviewCell2023

ADP-ribosylation from molecular mechanisms to therapeutic implications.

Marcin J Suskiewicz, Evgeniia Prokhorova, Johannes G M Rack, Ivan Ahel

Open access · hybridAbstract readReview
In one paragraph

Review in Cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
36.6field-weighted citation impact, top 1% 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

108 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
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  4. Review
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  11. 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
  12. NovelNeurology. Genetics · 2026
    Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Fully protected pyrophosphatesChemical science · 2026
    Article
  18. Article
  19. Article
  20. The Role of Stress Granules in Cardiovascular Diseases.Reviews in cardiovascular medicine · 2026
    Review

48 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 2 countries.

Marcin J SuskiewiczCentre de Biophysique Moléculaire, CNRS, Orléans, France.
Evgeniia ProkhorovaSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Johannes G M RackSir William Dunn School of Pathology, University of Oxford, Oxford, UK; MRC Centre of Medical Mycology, University of Exeter, Exeter, UK.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford, UK. Electronic address: ivan.ahel@path.ox.ac.uk.
University of Oxford · GBCentre National de la Recherche Scientifique · FRUniversity of Exeter · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Department of HealthMedical Research Council MR/N006364/2Medical Research Council MR/V033417/1Medical Research Council MR/X007472/1Wellcome Trust 210634Wellcome Trust 210634/Z/18/ZWellcome Trust 223107
6 · The paper itself

Abstract

ADP-ribosylation is a ubiquitous modification of biomolecules, including proteins and nucleic acids, that regulates various cellular functions in all kingdoms of life. The recent emergence of new technologies to study ADP-ribosylation has reshaped our understanding of the molecular mechanisms that govern the establishment, removal, and recognition of this modification, as well as its impact on cellular and organismal function. These advances have also revealed the intricate involvement of ADP-ribosylation in human physiology and pathology and the enormous potential that their manipulation holds for therapy. In this review, we present the state-of-the-art findings covering the work in structural biology, biochemistry, cell biology, and clinical aspects of ADP-ribosylation.

Indexed as

ADP-RibosylationADP Ribose TransferasesAnimalsDNAHumansPoly (ADP-Ribose) Polymerase-1Protein Processing, Post-TranslationalProteinsRNASignal TransductionADP Ribose TransferasesDNAPoly (ADP-Ribose) Polymerase-1ProteinsRNA

Identifiers

PMID37832523
PMCPMC10789625
OpenAlexW4387566852

What OpenQuestion holds

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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.