Evidence map›Paper›PMID 25590432›Full record

ArticlePloS one2015

The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages.

Mikael Altun, Thomas S Walter, Holger B Kramer, Patrick Herr, Alexander Iphöfer, Johan Boström, Yael David, Alia Komsany, Nicola Ternette, Ami Navon and 3 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The emerging role of Deubiquitinases (DUBs) in parasites: A foresight review.Frontiers in cellular and infection microbiology · 2022
    Review
  10. Molecular Mechanisms of DUBs Regulation in Signaling and Disease.International journal of molecular sciences · 2021
    Review
  11. Role of deubiquitinating enzymes in DNA double-strand break repair.Journal of Zhejiang University. Science. B · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. ISG15 in antiviral immunity and beyond.Nature reviews. Microbiology · 2018
    Review
  18. Revealing a Novel Otubain-Like Enzyme fromFrontiers in chemistry · 2017
    Article
  19. Article
  20. Review
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

13 authors at 6 institutions in 4 countries.

Mikael AltunTarget Discovery Institute, Nuffield Department of Medicine, Roosevelt Drive, University of Oxford, Oxford, OX3 7FZ, United Kingdom; Science for Life Laboratory, Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 21 Stockholm, Sweden.
Thomas S WalterDivision of Structural Biology, Nuffield Department of Medicine, Roosevelt Drive, University of Oxford, Oxford, OX3 7BN, United Kingdom.
Holger B KramerDepartment of Physiology, Anatomy and Genetics, South Parks Road, Oxford, OX1 3DQ, United Kingdom.
Patrick HerrScience for Life Laboratory, Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 21 Stockholm, Sweden.
Alexander IphöferHelmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.
Johan BoströmScience for Life Laboratory, Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 21 Stockholm, Sweden.
Yael DavidDepartment of Biological Regulation, The Weizmann Institute of Science, Rehovot 76100, Israel.
Alia KomsanyTarget Discovery Institute, Nuffield Department of Medicine, Roosevelt Drive, University of Oxford, Oxford, OX3 7FZ, United Kingdom.
Nicola TernetteTarget Discovery Institute, Nuffield Department of Medicine, Roosevelt Drive, University of Oxford, Oxford, OX3 7FZ, United Kingdom.
Ami NavonDepartment of Biological Regulation, The Weizmann Institute of Science, Rehovot 76100, Israel.
David I StuartDivision of Structural Biology, Nuffield Department of Medicine, Roosevelt Drive, University of Oxford, Oxford, OX3 7BN, United Kingdom.
Jingshan RenDivision of Structural Biology, Nuffield Department of Medicine, Roosevelt Drive, University of Oxford, Oxford, OX3 7BN, United Kingdom.
Benedikt M KesslerTarget Discovery Institute, Nuffield Department of Medicine, Roosevelt Drive, University of Oxford, Oxford, OX3 7FZ, United Kingdom.
University of Oxford · GBKarolinska Institutet · SEWeizmann Institute of Science · ILHelmholtz Centre for Infection Research · DEOxford Fertility · GBScience for Life Laboratory · SE

Funding

Medical Research Council G0501068Medical Research Council G1000099Medical Research Council G1100525Medical Research Council MR/N00065X/1Wellcome Trust 084655
6 · The paper itself

Abstract

Ovarian tumor domain containing proteases cleave ubiquitin (Ub) and ubiquitin-like polypeptides from proteins. Here we report the crystal structure of human otubain 2 (OTUB2) in complex with a ubiquitin-based covalent inhibitor, Ub-Br2. The ubiquitin binding mode is oriented differently to how viral otubains (vOTUs) bind ubiquitin/ISG15, and more similar to yeast and mammalian OTUs. In contrast to OTUB1 which has exclusive specificity towards Lys48 poly-ubiquitin chains, OTUB2 cleaves different poly-Ub linked chains. N-terminal tail swapping experiments between OTUB1 and OTUB2 revealed how the N-terminal structural motifs in OTUB1 contribute to modulating enzyme activity and Ub-chain selectivity, a trait not observed in OTUB2, supporting the notion that OTUB2 may affect a different spectrum of substrates in Ub-dependent pathways.

Indexed as

Crystallography, X-RayHumansModels, MolecularPolyubiquitinProtein BindingProtein Structure, TertiaryThiolester HydrolasesUbiquitinOTUB2 protein, humanPolyubiquitinThiolester HydrolasesUbiquitin

Identifiers

PMID25590432
PMCPMC4295869
OpenAlexW1974115460

What OpenQuestion holds

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LicenceCC BY
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.