Evidence map›Paper›PMID 21415856›Full record

ArticleEMBO reports2011

Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain.

Mark P A Luna-Vargas, Alex C Faesen, Willem J van Dijk, Michael Rape, Alexander Fish, Titia K Sixma

RetractedOpen access · bronzeAbstract readRetracted Publication
In one paragraph

Article in EMBO reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
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  18. Solution structure of the E3 ligase HOIL-1 Ubl domain.Protein science : a publication of the Protein Society · 2012
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Mark P A Luna-VargasDivision of Biochemistry and Center for Biomedical Genetics, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Alex C Faesen
Willem J van Dijk
Michael Rape
Alexander Fish
Titia K Sixma
The Netherlands Cancer Institute · NLUniversity of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

USP4 is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes that has a role in spliceosome regulation. Here, we show that the crystal structure of the minimal catalytic domain of USP4 has the conserved USP-like fold with its typical ubiquitin-binding site. A ubiquitin-like (Ubl) domain inserted into the catalytic domain has autoregulatory function. This Ubl domain can bind to the catalytic domain and compete with the ubiquitin substrate, partially inhibiting USP4 activity against different substrates. Interestingly, other USPs, such as USP39, could relieve this inhibition.

Indexed as

Binding SitesCatalytic DomainCrystallography, X-RayHumansProtein BindingProtein Structure, TertiaryUbiquitinUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUbiquitinUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUSP4 protein, human

Identifiers

PMID21415856
PMCPMC3077250
OpenAlexW2162935379

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.