Evidence map›Paper›PMID 19487668›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM.

James Z Chen, Ethan C Settembre, Scott T Aoki, Xing Zhang, A Richard Bellamy, Philip R Dormitzer, Stephen C Harrison, Nikolaus Grigorieff

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
–field-weighted citation impact
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

86 citing papers in PubMed.

  1. Article
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  9. Article
  10. Article
  11. Article
  12. Hidden Relationships betweenInternational journal of molecular sciences · 2022
    Review
  13. Viral Capsid and Polymerase in Reoviridae.Sub-cellular biochemistry · 2022
    Article
  14. Review
  15. Article
  16. Review
  17. Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020
    Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

James Z ChenRosenstiel Basic Medical Research Center, Brandeis University, Waltham, MA 02454, USA.
Ethan C Settembre
Scott T Aoki
Xing Zhang
A Richard Bellamy
Philip R Dormitzer
Stephen C Harrison
Nikolaus Grigorieff

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
STRUCTURE AND ASSEMBLY OF VIRUSES AND OF COATED VESICLESR01CA013202 · NCI · HARVARD UNIVERSITY · PI HARRISON, STEPHEN COPLAN · 1985 to 2024
$4.9M
Structure and Assembly of VirusesR37CA013202 · NCI · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2012
$3.7M
Rotavirus VP4: Structure and functionR01AI053174 · NIAID · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2007
$1.5M
Howard Hughes Medical InstituteNCI NIH HHS CA-13202NCI NIH HHS R01 CA013202NCI NIH HHS R37 CA013202NIAID NIH HHS AI-053174NIAID NIH HHS R01 AI053174NIGMS NIH HHS GM-62580NIGMS NIH HHS P01 GM062580
6 · The paper itself

Abstract

Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 A) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms" of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.

Indexed as

Antigens, ViralCalciumCapsid ProteinsCryoelectron MicroscopyCrystallography, X-RayModels, BiologicalModels, MolecularProtein MultimerizationProtein Structure, QuaternaryRotavirusViral Core ProteinsVirionAntigens, ViralCalciumCapsid ProteinsViral Core ProteinsVP1 protein, RotavirusVP2 protein, RotavirusVP3 protein, RotavirusVP7 protein, Rotavirus

Identifiers

PMID19487668
PMCPMC2689313

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.