Evidence map›Paper›PMID 35562987›Full record

ReviewInternational journal of molecular sciences2022

The Roles of Ubiquitination in Pathogenesis of Influenza Virus Infection.

Eun-Sook Park, Mehrangiz Dezhbord, Ah Ram Lee, Kyun-Hwan Kim

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 8% 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, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. TRIM21 is a molecular rheostat for influenza A virus replication.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Impaired K48-polyubiquitination downmodulates mouse norovirus propagation.Frontiers in cellular and infection microbiology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  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

4 authors at 2 institutions in 1 country.

Eun-Sook ParkInstitute of Biomedical Science and Technology, School of Medicine, Konkuk University, Seoul 05029, Korea.ORCID 0000-0002-6652-9404
Mehrangiz DezhbordDepartment of Precision Medicine, Sungkyunkwan University School of Medicine, Suwon 16419, Korea.ORCID 0000-0002-2852-2084
Ah Ram LeeDepartment of Precision Medicine, Sungkyunkwan University School of Medicine, Suwon 16419, Korea.ORCID 0000-0001-6075-3352
Kyun-Hwan KimDepartment of Precision Medicine, Sungkyunkwan University School of Medicine, Suwon 16419, Korea.ORCID 0000-0001-5266-072X
Sungkyunkwan University · KRKonkuk University · KR

Funding

National Research Foundation of Korea (NRF) (NRF-2019R1A2B5B01069635, 2022R1A2C2002809 (E.S.P) and NRF-2020R1A2C3010511, 2021M3A9I2080488, and 2021M3A9H3017086 (K.H.K)).
6 · The paper itself

Abstract

The ubiquitin system denotes a potent post-translational modification machinery that is capable of activation or deactivation of target proteins through reversible linkage of a single ubiquitin or ubiquitin chains. Ubiquitination regulates major cellular functions such as protein degradation, trafficking and signaling pathways, innate immune response, antiviral defense, and virus replication. The RNA sensor RIG-I ubiquitination is specifically induced by influenza A virus (IAV) to activate type I IFN production. Influenza virus modulates the activity of major antiviral proteins in the host cell to complete its full life cycle. Its structural and non-structural proteins, matrix proteins and the polymerase complex can regulate host immunity and antiviral response. The polymerase PB1-F2 of mutated 1918 IAV, adapts a novel IFN antagonist function by sending the DDX3 into proteasomal degradation. Ultimately the fate of virus is determined by the outcome of interplay between viral components and host antiviral proteins and ubiquitination has a central role in the encounter of virus and its host cell.

Indexed as

Influenza A virusInfluenza, HumanOrthomyxoviridae InfectionsUbiquitinationHumansImmunity, InnateUbiquitinVirus ReplicationUbiquitininfluenza a viruspathogenesispost-translational modificationubiquitination

Identifiers

PMID35562987
PMCPMC9105177
OpenAlexW4224254671

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.