Evidence map›Paper›PMID 22200497›Full record

ArticleVirology2012

Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay.

Kyeong-Ok Chang, Daisuke Takahashi, Om Prakash, Yunjeong Kim

Abstract read
In one paragraph

Article in Virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Journal of structural biology: X · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Current tools for norovirus drug discovery.Expert opinion on drug discovery · 2016
    Review
  15. Article
  16. Article
  17. Anti-norovirus therapeutics: a patent review (2010-2015).Expert opinion on therapeutic patents · 2016
    Review
  18. Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Kyeong-Ok ChangDepartment of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University, KS 66506, USA.
Daisuke Takahashi
Om Prakash
Yunjeong Kim
Kansas State University · US

Funding

TRANSEPITHELIAL ION TRANSPORT &ITS REGULATIONP20RR017686 · NCRR · KANSAS STATE UNIVERSITY · PI FONG, PEYING · 2002 to 2011
$21.8M
TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI FISCHER, CHRISTOPHER JAMES · 2002 to 2011
$20.1M
Development of Novel Therapeutic Agents for Norovirus InfectionU01AI081891 · NIAID · KANSAS STATE UNIVERSITY · PI CHANG, KYEONG-OK · 2009 to 2013
$4.9M
Purchase of a Cryo-Probe to Upgrade a 500 MHz NMR System for BioNMR ApplicationsS10RR025441 · NCRR · KANSAS STATE UNIVERSITY · PI PRAKASH, OM · 2009 to 2009
$316k
NCRR NIH HHS 1S10RR025441NCRR NIH HHS P20 RR017686NCRR NIH HHS P20 RR017708NCRR NIH HHS RR17686NCRR NIH HHS RR17708NCRR NIH HHS S10 RR025441NIAID NIH HHS U01 AI081891
6 · The paper itself

Abstract

Noroviruses are the major cause of food- or water-borne gastroenteritis outbreaks in humans. The norovirus protease that cleaves a large viral polyprotein to nonstructural proteins is essential for virus replication and an attractive target for antiviral drug development. Noroviruses show high genetic diversity with at least five genogroups, GI-GV, of which GI and GII are responsible for the majority of norovirus infections in humans. We cloned and expressed proteases of Norwalk virus (GI) and MD145 virus (GII) and characterized the enzymatic activities with fluorescence resonance energy transfer substrates. We demonstrated that the GI and GII proteases cleaved the substrates derived from the naturally occurring cleavage site in the open reading frame (ORF) 1 of G1 norovirus with similar efficiency, and that enzymatic activity of both proteases was inhibited by commercial protease inhibitors including chymostatin. The interaction of chymostatin to Norwalk virus protease was validated by nuclear magnetic resonance (NMR) spectroscopy.

Indexed as

Amino Acid SequenceDown-RegulationFluorescence Resonance Energy TransferGastroenteritisGenotypeHumansKineticsMolecular Sequence DataNorovirusNorwalk virusOligopeptidesPeptide HydrolasesProtease InhibitorsSequence AlignmentViral ProteinschymostatinOligopeptidesPeptide HydrolasesProtease InhibitorsViral Proteins

Identifiers

PMID22200497
PMCPMC3259199
OpenAlexW2076707317

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.