Evidence map›Paper›PMID 35941131›Full record

ArticleCell death & disease2022

OTUD1 deubiquitinase regulates NF-κB- and KEAP1-mediated inflammatory responses and reactive oxygen species-associated cell death pathways.

Daisuke Oikawa, Min Gi, Hidetaka Kosako, Kouhei Shimizu, Hirotaka Takahashi, Masayuki Shiota, Shuhei Hosomi, Keidai Komakura, Hideki Wanibuchi, Daisuke Tsuruta and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 1 pooled it
5.3field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 1 synthesis or guideline pooled it, 64 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Oxeiptosis - potential in cancer treatment?Expert reviews in molecular medicine · 2026
    Review
  6. Review
  7. Review
  8. Review
  9. OTU deubiquitinases in disease: roles and targeting.Trends in molecular medicine · 2026
    Review
  10. Review
  11. Article
  12. Article
  13. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

12 authors at 4 institutions in 1 country.

Daisuke OikawaDepartment of Medical Biochemistry, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.
Min GiDepartment of Environmental Risk Assessment, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.
Hidetaka KosakoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, Tokushima, Japan.
Kouhei ShimizuDepartment of Medical Biochemistry, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.ORCID 0000-0001-9523-4296
Hirotaka TakahashiDivision of Cell-Free Sciences, Proteo-Science Center (PROS), Ehime University, Matsuyama, Japan.
Masayuki ShiotaDepartment of Molecular Biology of Medicine, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.
Shuhei HosomiDepartment of Gastroenterology, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.
Keidai KomakuraDepartment of Medical Biochemistry, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.
Hideki WanibuchiDepartment of Molecular Pathology, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.
Daisuke TsurutaDepartment of Dermatology, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan.
Tatsuya SawasakiDivision of Cell-Free Sciences, Proteo-Science Center (PROS), Ehime University, Matsuyama, Japan.
Fuminori TokunagaDepartment of Medical Biochemistry, Graduate School of Medicine, Osaka Metropolitan University, Osaka, Japan. ftokunaga@omu.ac.jp.ORCID 0000-0003-3626-9119
Osaka Metropolitan University · JPCellFree Sciences (Japan) · JPOsaka City University · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deubiquitinating enzymes (DUBs) regulate numerous cellular functions by removing ubiquitin modifications. We examined the effects of 88 human DUBs on linear ubiquitin chain assembly complex (LUBAC)-induced NF-κB activation, and identified OTUD1 as a potent suppressor. OTUD1 regulates the canonical NF-κB pathway by hydrolyzing K63-linked ubiquitin chains from NF-κB signaling factors, including LUBAC. OTUD1 negatively regulates the canonical NF-κB activation, apoptosis, and necroptosis, whereas OTUD1 upregulates the interferon (IFN) antiviral pathway. Mass spectrometric analysis showed that OTUD1 binds KEAP1, and the N-terminal intrinsically disordered region of OTUD1, which contains an ETGE motif, is indispensable for the KEAP1-binding. Indeed, OTUD1 is involved in the KEAP1-mediated antioxidant response and reactive oxygen species (ROS)-induced cell death, oxeiptosis. In Otud1

Indexed as

NF-E2-Related Factor 2NF-kappa BAnimalsCell DeathDeubiquitinating EnzymesHumansKelch-Like ECH-Associated Protein 1MiceReactive Oxygen SpeciesUbiquitinUbiquitinationUbiquitin-Specific ProteasesDeubiquitinating EnzymesKEAP1 protein, humanKeap1 protein, mouseKelch-Like ECH-Associated Protein 1NF-E2-Related Factor 2NF-kappa BOTUD1 protein, humanReactive Oxygen SpeciesUbiquitinUbiquitin-Specific Proteases

Identifiers

PMID35941131
PMCPMC9360000
OpenAlexW4290721548

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.