Evidence map›Paper›PMID 32556480›Full record

ReviewCurrent microbiology2020

The Function and Mechanism of Enterovirus 71 (EV71) 3C Protease.

Weihui Wen, Zixuan Qi, Jing Wang

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.7field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 39 citations in OpenAlex.

  1. In vitro enzymatic assays invalidate dihydromyricetin as a potential inhibitor against enterovirus A71 3C protease: beware of fluorescence quenching artifacts.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Advances in anti-EV-A71 drug development research.Journal of advanced research · 2024
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Regulation and functions of the NLRP3 inflammasome in RNA virus infection.Frontiers in cellular and infection microbiology · 2023
    Review
  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

3 authors at 1 institution in 1 country.

Weihui WenDepartment of Microbiology, School of Medicine, Nanchang University, Nanchang, Jiangxi, People's Republic of China.
Zixuan QiSchool of Medicine, Forth Clinical College, Nanchang University, Nanchang, Jiangxi, People's Republic of China.
Jing WangDepartment of Microbiology, School of Medicine, Nanchang University, Nanchang, Jiangxi, People's Republic of China. wangj8001@163.com.ORCID http://orcid.org/0000-0003-0817-5625
Nanchang University · CN

Funding

Health and Family Planning Project of Jiangxi Province 20155634National Natural Science Foundation of China 81660332Natural Science Foundation of Jiangxi Province 20151BAB205057
6 · The paper itself

Abstract

Enterovirus 71 (EV71) is the main pathogen of the hand, foot, and mouth disease. It was firstly isolated from sputum specimens of infants with central nervous system diseases in California in 1969, and has been repeatedly reported in various parts of the world, especially in the Asia-Pacific region. EV71 3C protein is a 183 amino acid cysteine protease that can cleave most structural and non-structural proteins of EV71. Based on the analysis and understanding of EV71 3C protease, it is helpful to study and treat diseases caused by EV71 virus infection. The EV71 3C protease promotes virus replication by cleaving EV71 synthesis or host proteins. Moreover, EV71 3C protease inhibits the innate immune system and causes apoptosis. At present, in order to deal with the damage caused by the EV71, it is urgent to develop antiviral drugs targeting 3C protease. This review will focus on the structure, function, and mechanism of EV71 3C protease.

Indexed as

EnterovirusEnterovirus A, Human3C Viral ProteasesCysteine EndopeptidasesHumansPeptide Hydrolases3C Viral ProteasesCysteine EndopeptidasesPeptide Hydrolases

Identifiers

PMID32556480
OpenAlexW3036235115

What OpenQuestion holds

Textmetadata
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.