Evidence map›Paper›PMID 35175282›Full record

ArticleThe Biochemical journal2022

Beyond protein modification: the rise of non-canonical ADP-ribosylation.

Marion Schuller, Ivan Ahel

Abstract read
In one paragraph

Article in The Biochemical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Poly-ADP-ribosylation dynamics, signaling, and analysis.Environmental and molecular mutagenesis · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation.The Journal of biological chemistry · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Fer and FerT: A New Regulatory Link between Sperm and Cancer Cells.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  19. Review
  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

2 authors.

Marion SchullerSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K.ORCID 0000-0002-1551-0359
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K.ORCID 0000-0002-9446-3756

Funding

Biotechnology and Biological Sciences Research Council BB/ R007195/1Cancer Research UK 22284Cancer Research UK C35050/ A22284Wellcome Trust 101794Wellcome Trust 210634Wellcome Trust 210634/Z/18/Z
6 · The paper itself

Abstract

ADP-ribosylation has primarily been known as post-translational modification of proteins. As signalling strategy conserved in all domains of life, it modulates substrate activity, localisation, stability or interactions, thereby regulating a variety of cellular processes and microbial pathogenicity. Yet over the last years, there is increasing evidence of non-canonical forms of ADP-ribosylation that are catalysed by certain members of the ADP-ribosyltransferase family and go beyond traditional protein ADP-ribosylation signalling. New macromolecular targets such as nucleic acids and new ADP-ribose derivatives have been established, notably extending the repertoire of ADP-ribosylation signalling. Based on the physiological relevance known so far, non-canonical ADP-ribosylation deserves its recognition next to the traditional protein ADP-ribosylation modification and which we therefore review in the following.

Indexed as

Adenosine DiphosphateADP Ribose TransferasesADP-RibosylationGuanosineN-Glycosyl HydrolasesPoly(ADP-ribose) PolymerasesRegulatory Sequences, Ribonucleic AcidSignal TransductionStructure-Activity RelationshipThymidineUbiquitinAdenosine DiphosphateADP Ribose TransferasesADP-ribosylarginine hydrolaseGuanosineN-Glycosyl HydrolasesPoly(ADP-ribose) PolymerasesRegulatory Sequences, Ribonucleic AcidThymidineUbiquitinADP-ribosylationnucleic acidsPARPprotein modification

Identifiers

PMID35175282
PMCPMC8883491

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.