Evidence map›Paper›PMID 36334706›Full record

ArticleVirologica Sinica2023

Ubiquitin-specific protease 24 promotes EV71 infection by restricting K63-linked polyubiquitination of TBK1.

Lichao Zang, Jin Gu, Xinyu Yang, Yukang Yuan, Hui Guo, Wei Zhou, Jinhong Ma, Yan Chen, Yumin Wu, Hui Zheng and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Virologica Sinica, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. 1-L Transcription of SARS-CoV-2 Spike Protein S1 Subunit.International journal of molecular sciences · 2024
    Article
  9. Article
  10. 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

11 authors at 2 institutions in 1 country.

Lichao ZangDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China.
Jin GuHubei Hospital of Integrated Chinese and Western Medicine, Wuhan, 430015, China.
Xinyu YangDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China.
Yukang YuanInternational Institute of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, 215123, China; Jiangsu Key Laboratory of Infection and Immunity, Soochow University, Suzhou, 215123, China.
Hui GuoDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China.
Wei ZhouDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China.
Jinhong MaDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China.
Yan ChenDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China.
Yumin WuDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China.
Hui ZhengInternational Institute of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, 215123, China; Jiangsu Key Laboratory of Infection and Immunity, Soochow University, Suzhou, 215123, China. Electronic address: huizheng@suda.edu.cn.
Weifeng ShiDepartment of Laboratory Medicine, The Third Affiliated Hospital of Soochow University, Changzhou, 213003, China. Electronic address: swf67113@163.com.
Soochow University · CNIntegrated Chinese Medicine (China) · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TANK-binding kinase 1 (TBK1) is an essential protein kinase for activation of interferon regulatory factor 3 (IRF3) and induction of the type I interferons (IFN-I). Although the biochemical regulation of TBK1 activation has been studied, little is known about how enterovirus 71 (EV71) employs the deubiquitinases (DUBs) to regulate TBK1 activation for viral immune evasion. Here, we found that EV71 infection upregulated the expression of ubiquitin-specific protease 24 (USP24). Further studies revealed that USP24 physically interacted with TBK1, and can reduce K63-linked polyubiquitination of TBK1. Knockdown of USP24 upregulated TBK1 K63-linked polyubiquitination, promoted the phosphorylation and nuclear translocation of IRF3, and in turn improved IFN-I production during EV71 infection. As a consequence, USP24 knockdown dramatically inhibited EV71 infection. This study revealed USP24 as a novel regulator of TBK1 activation, which promotes the understanding of immune evasion mechanisms of EV71 and could provide a potential strategy for treatment of EV71 infection.

Indexed as

Interferon Type ISignal TransductionImmunity, InnatePhosphorylationUbiquitinationUbiquitin-Specific ProteasesInterferon Type IUbiquitin-Specific ProteasesEnterovirus 71 (EV71)Innate immunityTANK-binding kinase 1 (TBK1)Type I interferons (IFN-I)Ubiquitin-specific protease 24 (USP24)

Identifiers

PMID36334706
PMCPMC10006192
OpenAlexW4308147680

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.