Evidence map›Paper›PMID 30733604›Full record

ReviewNature reviews. Molecular cell biology2019

Breaking the chains: deubiquitylating enzyme specificity begets function.

Michael J Clague, Sylvie Urbé, David Komander

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 525 papers.

0numbers the graph read from it
0cells of the map it votes in
525citing 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

525 citing papers in PubMed.

  1. Article
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  9. Review
  10. Review
  11. Deubiquitination of Vangl by USP6 and USP32 Regulates Planar Cell Polarity Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  12. Article
  13. Article
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  15. Article
  16. Article
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  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Michael J ClagueCellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, UK. clague@liv.ac.uk.ORCID http://orcid.org/0000-0003-3355-9479
Sylvie UrbéCellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, UK. urbe@liv.ac.uk.
David KomanderUbiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia. dk@wehi.edu.au.ORCID http://orcid.org/0000-0002-8092-4320

Funding

Medical Research Council MC_U105192732Medical Research Council MR/N00941X/1
6 · The paper itself

Abstract

The deubiquitylating enzymes (DUBs, also known as deubiquitylases or deubiquitinases) maintain the dynamic state of the cellular ubiquitome by releasing conjugated ubiquitin from proteins. In light of the many cellular functions of ubiquitin, DUBs occupy key roles in almost all aspects of cell behaviour. Many DUBs show selectivity for particular ubiquitin linkage types or positions within ubiquitin chains. Others show chain-type promiscuity but can select a distinct palette of protein substrates via specific protein-protein interactions established through binding modules outside of the catalytic domain. The ubiquitin chain cleavage mode or chain linkage specificity has been related directly to biological functions. Examples include regulation of protein degradation and ubiquitin recycling by the proteasome, DNA repair pathways and innate immune signalling. DUB cleavage specificity is also being harnessed for analysis of ubiquitin chain architecture that is assembled on specific proteins. The recent development of highly specific DUB inhibitors heralds their emergence as a new class of therapeutic targets for numerous diseases.

Indexed as

ProteolysisSignal TransductionUbiquitinationAnimalsDeubiquitinating EnzymesHumansProteasome Endopeptidase ComplexSubstrate SpecificityUbiquitinDeubiquitinating EnzymesProteasome Endopeptidase ComplexUbiquitin

Identifiers

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.