Evidence map›Paper›PMID 22388738›Full record

ArticleNature structural & molecular biology2012

A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71.

Xiangxi Wang, Wei Peng, Jingshan Ren, Zhongyu Hu, Jiwei Xu, Zhiyong Lou, Xumei Li, Weidong Yin, Xinliang Shen, Claudine Porta and 9 more

Open access · bronzeAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 267 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
267citing papers in PubMed, 1 pooled it
25.0field-weighted citation impact, top 1% 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

267 citing papers in PubMed, 1 synthesis or guideline pooled it, 393 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Particles of echovirus 18 open to release their genomes in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. An RNA-to-RNA pipeline for rapid antiviral antibody development.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
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  11. The low-density lipoprotein receptor LDLR mediates cellular entry of nonenveloped hepatitis A virus.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. Article
  13. Review
  14. SPNS1 is an essential cellular factor for EV-A71 by acting as a transporter of viral pocket factor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Journal of virology · 2025
    Review

207 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors at 7 institutions in 2 countries.

Xiangxi WangNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing, China.
Wei Peng
Jingshan Ren
Zhongyu Hu
Jiwei Xu
Zhiyong Lou
Xumei Li
Weidong Yin
Xinliang Shen
Claudine Porta
Thomas S Walter
Gwyndaf Evans
Danny Axford
Robin Owen
David J Rowlands
Junzhi Wang
David I Stuart
Elizabeth E Fry
Zihe Rao
Institute of Biophysics · CNDiamond Light Source · GBNational Institutes for Food and Drug Control · CNCentre for Human Genetics · GBUniversity of Oxford · GBInstitute of Structural and Molecular Biology · GBTsinghua University · CN

Funding

Medical Research Council G0200504Medical Research Council G0500365Medical Research Council G0600025Medical Research Council G1100525Medical Research Council G19/3Wellcome Trust 090532
6 · The paper itself

Abstract

Enterovirus 71 (EV71) is a major agent of hand, foot and mouth disease in children that can cause severe central nervous system disease and death. No vaccine or antiviral therapy is available. High-resolution structural analysis of the mature virus and natural empty particles shows that the mature virus is structurally similar to other enteroviruses. In contrast, the empty particles are markedly expanded and resemble elusive enterovirus-uncoating intermediates not previously characterized in atomic detail. Hydrophobic pockets in the EV71 capsid are collapsed in this expanded particle, providing a detailed explanation of the mechanism for receptor-binding triggered virus uncoating. These structures provide a model for enterovirus uncoating in which the VP1 GH loop acts as an adaptor-sensor for cellular receptor attachment, converting heterologous inputs to a generic uncoating mechanism, highlighting new opportunities for therapeutic intervention.

Indexed as

CapsidCapsid ProteinsCrystallography, X-RayEnterovirus A, HumanEnterovirus InfectionsHand, Foot and Mouth DiseaseHumansModels, MolecularVirionCapsid Proteins

Identifiers

PMID22388738
PMCPMC3378640
OpenAlexW2157586119

What OpenQuestion holds

Textmetadata
LicenceTDM
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.