Evidence map›Paper›PMID 23487472›Full record

ArticleJournal of virology2013

Structures of the compact helical core domains of feline calicivirus and murine norovirus VPg proteins.

Eoin N Leen, K Y Rex Kwok, James R Birtley, Peter J Simpson, Chennareddy V Subba-Reddy, Yasmin Chaudhry, Stanislav V Sosnovtsev, Kim Y Green, Sean N Prater, Michael Tong and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.3field-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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
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  15. Review
  16. Review
  17. Non-canonical Translation in Plant RNA Viruses.Frontiers in plant science · 2017
    Review
  18. Antiviral targets of human noroviruses.Current opinion in virology · 2016
    Review
  19. Review
  20. Allosteric inhibitors of Coxsackie virus A24 RNA polymerase.Bioorganic & medicinal chemistry · 2016
    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

18 authors at 4 institutions in 2 countries.

Eoin N LeenDivision of Cell and Molecular Biology, Department of Life Sciences, Imperial College London, London, United Kingdom.
K Y Rex Kwok
James R Birtley
Peter J Simpson
Chennareddy V Subba-Reddy
Yasmin Chaudhry
Stanislav V Sosnovtsev
Kim Y Green
Sean N Prater
Michael Tong
Joanna C Young
Liliane M W Chung
Jan Marchant
Lisa O Roberts
C Cheng Kao
Stephen Matthews
Ian G Goodfellow
Stephen Curry
Imperial College London · GBIndiana University Bloomington · USNational Institutes of Health · USUniversity of Surrey · GB

Funding

Noroviruses and Epidemic GastroenteritisZIAAI000897 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI GREEN, KIM Y. · 2009 to 2025
$29.6M
Biotechnology and Biological Sciences Research Council BB/I012303/1Biotechnology and Biological Sciences Research Council BB/I01232X/1Biotechnology and Biological Sciences Research Council BB/J001708/1Medical Research Council MR/J006874/1Wellcome Trust 083248Wellcome Trust 097997Wellcome Trust WT097997MA
6 · The paper itself

Abstract

We report the solution structures of the VPg proteins from feline calicivirus (FCV) and murine norovirus (MNV), which have been determined by nuclear magnetic resonance spectroscopy. In both cases, the core of the protein adopts a compact helical structure flanked by flexible N and C termini. Remarkably, while the core of FCV VPg contains a well-defined three-helix bundle, the MNV VPg core has just the first two of these secondary structure elements. In both cases, the VPg cores are stabilized by networks of hydrophobic and salt bridge interactions. The Tyr residue in VPg that is nucleotidylated by the viral NS7 polymerase (Y24 in FCV, Y26 in MNV) occurs in a conserved position within the first helix of the core. Intriguingly, given its structure, VPg would appear to be unable to bind to the viral polymerase so as to place this Tyr in the active site without a major conformation change to VPg or the polymerase. However, mutations that destabilized the VPg core either had no effect on or reduced both the ability of the protein to be nucleotidylated and virus infectivity and did not reveal a clear structure-activity relationship. The precise role of the calicivirus VPg core in virus replication remains to be determined, but knowledge of its structure will facilitate future investigations.

Indexed as

AnimalsCalicivirus, FelineMagnetic Resonance SpectroscopyModels, MolecularNorovirusProtein ConformationViral ProteinsViral Proteins

Identifiers

PMID23487472
PMCPMC3648151
OpenAlexW2027079803

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.