Evidence map›Paper›PMID 36675197›Full record

ReviewInternational journal of molecular sciences2023

Multiple Roles of TRIM21 in Virus Infection.

Xue Li, Lin Yang, Si Chen, Jiawei Zheng, Huimin Zhang, Linzhu Ren

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. TRIM21 is a molecular rheostat for influenza A virus replication.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. TRIM21enhances IL-17A signaling and drives autoimmune myocarditis by promoting TRAF3 lysosomaldegradation in cardiac fibroblasts.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Review
  8. Observational
  9. Article
  10. Article
  11. Review
  12. Article
  13. Hypertrophic Cardiomyopathy-Associated CRYABInternational journal of molecular sciences · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

6 authors at 1 institution in 1 country.

Xue LiCollege of Animal Sciences, Key Lab for Zoonoses Research, Ministry of Education, Jilin University, 5333 Xi'an Road, Changchun 130062, China.ORCID 0000-0003-2485-4812
Lin YangCollege of Animal Sciences, Key Lab for Zoonoses Research, Ministry of Education, Jilin University, 5333 Xi'an Road, Changchun 130062, China.
Si ChenCollege of Animal Sciences, Key Lab for Zoonoses Research, Ministry of Education, Jilin University, 5333 Xi'an Road, Changchun 130062, China.
Jiawei ZhengCollege of Animal Sciences, Key Lab for Zoonoses Research, Ministry of Education, Jilin University, 5333 Xi'an Road, Changchun 130062, China.
Huimin ZhangCollege of Animal Sciences, Key Lab for Zoonoses Research, Ministry of Education, Jilin University, 5333 Xi'an Road, Changchun 130062, China.
Linzhu RenCollege of Animal Sciences, Key Lab for Zoonoses Research, Ministry of Education, Jilin University, 5333 Xi'an Road, Changchun 130062, China.ORCID 0000-0002-1092-6435
Jilin University · CN

Funding

Changchun Science and Technology Bureau project 21ZGN18Jilin Province Science and Technology Development Projects 20200402043NCNational Natural Science Foundation of China 31772747
6 · The paper itself

Abstract

The tripartite motif protein 21 (TRIM21) belongs to the TRIM family, possessing an E3 ubiquitin ligase activity. Similar to other TRIMs, TRIM21 also contains three domains (named RBCC), including the Really Interesting New Gene (RING) domain, one or two B-Box domains (B-Box), and one PRY/SPRY domain. Notably, we found that the RING and B-Box domains are relatively more conservative than the PRY/SPRY domain, suggesting that TRIM21 of different species had similar functions. Recent results showed that TRIM21 participates in virus infection by directly interacting with viral proteins or modulating immune and inflammatory responses. TRIM21 also acts as a cytosol high-affinity antibody Fc receptor, binding to the antibody-virus complex and triggering an indirect antiviral antibody-dependent intracellular neutralization (ADIN). This paper focuses on the recent progress in the mechanism of TRIM21 during virus infection and the application prospects of TRIM21 on virus infection.

Indexed as

RibonucleoproteinsVirus DiseasesCytosolHumansProteinsSS-A AntigenTripartite Motif ProteinsUbiquitinationUbiquitin-Protein LigasesProteinsRibonucleoproteinsSS-A AntigenTripartite Motif ProteinsUbiquitin-Protein Ligasesinteractiontripartite motif protein 21 (TRIM21)viruses

Identifiers

PMID36675197
PMCPMC9867090
OpenAlexW4316664764

What OpenQuestion holds

Textmetadata
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.