Evidence map›Paper›PMID 25113906›Full record

ArticleVirology2014

The identification and characterization of nucleic acid chaperone activity of human enterovirus 71 nonstructural protein 3AB.

Fenfen Tang, Hongjie Xia, Peipei Wang, Jie Yang, Tianyong Zhao, Qi Zhang, Yuanyang Hu, Xi Zhou

Abstract read
In one paragraph

Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

14 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. The regulatory roles of STAT3 protein in the pathogenesis of viral infections.Frontiers in cellular and infection microbiology · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Microorganisms · 2021
    Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. 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

8 authors at 1 institution in 1 country.

Fenfen TangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China.
Hongjie XiaState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China.
Peipei WangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China.
Jie YangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China.
Tianyong ZhaoState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China.
Qi ZhangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China.
Yuanyang HuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China. Electronic address: yyhu@whu.edu.cn.
Xi ZhouState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072 China. Electronic address: zhouxi@whu.edu.cn.
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human enterovirus 71 (EV71) belongs to the genus Enterovirus in the family Picornaviridae and has been recognized as one of the most important pathogens that cause emerging infectious disease. Despite of the importance of EV71, the nonstructural protein 3AB from this virus is little understood for its function during EV71 replication. Here we expressed EV71 3AB protein as recombinant protein in a eukaryotic expression system and uncovered that this protein possesses a nucleic acid helix-destabilizing and strand annealing acceleration activity in a dose-dependent manner, indicating that EV71 3AB is a nucleic acid chaperone protein. Moreover, we characterized the RNA chaperone activity of EV71 3AB, and revealed that divalent metal ions, such as Mg(2+) and Zn(2+), were able to inhibit the RNA helix-destabilizing activity of 3AB to different extents. Moreover, we determined that 3B plus the last 7 amino acids at the C-terminal of 3A (termed 3B+7) possess the RNA chaperone activity, and five amino acids, i.e. Lys-80, Phe-82, Phe-85, Tyr-89, and Arg-103, are critical and probably the active sites of 3AB for its RNA chaperone activity. This report reveals that EV71 3AB displays an RNA chaperone activity, adds a new member to the growing list of virus-encoded RNA chaperones, and provides novel knowledge about the virology of EV71.

Indexed as

Amino Acid MotifsBase SequenceEnterovirus A, HumanEnterovirus InfectionsHumansMolecular ChaperonesMolecular Sequence DataNucleic Acid ConformationProtein BindingRNA, ViralViral Nonstructural ProteinsMolecular ChaperonesRNA, ViralViral Nonstructural ProteinsAntivirals strategiesEnterovirus 71ReplicationRNA chaperoneRNA duplex unwinding

Identifiers

PMID25113906
PMCPMC7112070
OpenAlexW2076530773

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.