Evidence map›Paper›PMID 37935888›Full record

ReviewNature reviews. Cancer2023

Deubiquitinases in cancer.

Grant Dewson, Pieter J A Eichhorn, David Komander

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Cancer, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 227 papers.

0numbers the graph read from it
0cells of the map it votes in
227citing papers in PubMed
41.1field-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

227 citing papers in PubMed, 267 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. USP38 promotes breast cancer immune evasion and malignant progression by deubiquitinating and stabilizing PD-L1.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Deubiquitination of Vangl by USP6 and USP32 Regulates Planar Cell Polarity Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

167 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

3 authors at 2 institutions in 2 countries.

Grant DewsonUbiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia. Dewson@wehi.edu.au.ORCID 0000-0003-4251-8898
Pieter J A EichhornCurtin Medical School, Curtin University, Perth, Western Australia, Australia. Pieter.eichhorn@curtin.edu.au.ORCID 0000-0001-5840-943X
David KomanderUbiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia. dk@wehi.edu.au.ORCID 0000-0002-8092-4320
The University of Melbourne · AUCurtin University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is an essential regulator of most, if not all, signalling pathways, and defects in cellular signalling are central to cancer initiation, progression and, eventually, metastasis. The attachment of ubiquitin signals by E3 ubiquitin ligases is directly opposed by the action of approximately 100 deubiquitinating enzymes (DUBs) in humans. Together, DUBs and E3 ligases coordinate ubiquitin signalling by providing selectivity for different substrates and/or ubiquitin signals. The balance between ubiquitination and deubiquitination is exquisitely controlled to ensure properly coordinated proteostasis and response to cellular stimuli and stressors. Not surprisingly, then, DUBs have been associated with all hallmarks of cancer. These relationships are often complex and multifaceted, highlighted by the implication of multiple DUBs in certain hallmarks and by the impact of individual DUBs on multiple cancer-associated pathways, sometimes with contrasting cancer-promoting and cancer-inhibiting activities, depending on context and tumour type. Although it is still understudied, the ever-growing knowledge of DUB function in cancer physiology will eventually identify DUBs that warrant specific inhibition or activation, both of which are now feasible. An integrated appreciation of the physiological consequences of DUB modulation in relevant cancer models will eventually lead to the identification of patient populations that will most likely benefit from DUB-targeted therapies.

Indexed as

NeoplasmsUbiquitinDeubiquitinating EnzymesHumansUbiquitinationUbiquitin-Protein LigasesDeubiquitinating EnzymesUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID37935888
OpenAlexW4388464266

What OpenQuestion holds

Textmetadata
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.