Evidence map›Paper›PMID 40000907›Full record

ArticleThe EMBO journal2025

Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose.

Daniel S Bejan, Rachel E Lacoursiere, Jonathan N Pruneda, Michael S Cohen

Abstract read
In one paragraph

Article in The EMBO journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. NADCell reports · 2026
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. ADPr gets a ubiquitin upgrade.Nature chemical biology · 2025
    Article
  18. The emergence of MARUbe - a hybrid ADP-ribose-ubiquitin modification.Nature reviews. Molecular cell biology · 2025
    Article
  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

4 authors.

Daniel S BejanDepartment of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, 97239, USA.ORCID http://orcid.org/0000-0002-5090-0299
Rachel E LacoursiereDepartment of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR, 97239, USA.ORCID http://orcid.org/0000-0002-3405-2170
Jonathan N PrunedaDepartment of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, 97239, USA. pruneda@ohsu.edu.ORCID http://orcid.org/0000-0002-0304-4418
Michael S CohenDepartment of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, 97239, USA. cohenmic@ohsu.edu.ORCID http://orcid.org/0000-0002-7636-4156

Funding

Decoding protein MARylation networks in astrocytes using chemical biology approachesR01NS088629 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI COHEN, MICHAEL S · 2014 to 2024
$4.2M
Exploiting bacterial effector proteins to study human ubiquitin signalingR35GM142486 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI Jonathan N Pruneda · 2021 to 2026
$2.6M
Chemical Biology-Based Tools to Uncover the Function of PARP16 in cancerF31CA284712 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI BEJAN, DANIEL · 2023 to 2024
$88k
HHS | NIH | National Cancer Institute (NCI) F31CA284712HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM142486HHS | NIH | National Institute of Neurological Disorders and Stroke (NINDS) 2R01NS088629NCI NIH HHS F31 CA284712NIGMS NIH HHS R35 GM142486NINDS NIH HHS R01 NS088629
6 · The paper itself

Abstract

The prevailing view on post-translational modifications (PTMs) is that a single amino acid is modified with a single PTM at any given time. However, recent work has demonstrated crosstalk between different PTMs, some occurring on the same residue. Such interplay is seen with ADP-ribosylation and ubiquitylation. For example, DELTEX E3 ligases were reported to ubiquitylate a hydroxyl group on free NAD

Indexed as

Adenosine Diphosphate RiboseEstersPoly(ADP-ribose) PolymerasesProtein Processing, Post-TranslationalUbiquitinADP-RibosylationHEK293 CellsHumansProto-Oncogene ProteinsUbiquitinationAdenosine Diphosphate RiboseEstersPARP10 protein, humanPoly(ADP-ribose) PolymerasesProto-Oncogene ProteinsUbiquitinADP-ribosylationInterferon ResponsePARPsPost-translational ModificationsUbiquitylation

Identifiers

PMID40000907
PMCPMC12000418

What OpenQuestion holds

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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.