ArticleJournal of virology2005
Norovirus proteinase-polymerase and polymerase are both active forms of RNA-dependent RNA polymerase.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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.
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.
Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- The MNV-1 protease-polymerase precursor cleaves a novel site in the NS1-2 protein.The Journal of general virology · 2026Article
- Genomic diversity and comparative phylogenomic analysis of genus Norovirus.Scientific reports · 2025Article
- Activity and cryo-EM structure of the polymerase domain of the human norovirus ProPol precursor.Journal of virology · 2024Article
- 2-thiouridine is a broad-spectrum antiviral nucleoside analogue against positive-strand RNA viruses.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Human Norovirus Proteins: Implications in the Replicative Cycle, Pathogenesis, and the Host Immune Response.Frontiers in immunology · 2020Review
- Polyprotein processing and intermolecular interactions within the viral replication complex spatially and temporally control norovirus protease activity.The Journal of biological chemistry · 2019Article
- GII.4 Norovirus Protease Shows pH-Sensitive Proteolysis with a Unique Arg-His Pairing in the Catalytic Site.Journal of virology · 2019Article
- Calicivirus RNA-Dependent RNA Polymerases: Evolution, Structure, Protein Dynamics, and Function.Frontiers in microbiology · 2019Review
- Structure and Function of Caliciviral RNA Polymerases.Viruses · 2017Review
- Structure(s), function(s), and inhibition of the RNA-dependent RNA polymerase of noroviruses.Virus research · 2017Review
- Human norovirus transmission and evolution in a changing world.Nature reviews. Microbiology · 2016Review
- Recent Advances in the Discovery of Norovirus Therapeutics.Journal of medicinal chemistry · 2015Review
- Biochemical Evaluation of the Inhibition Properties of Favipiravir and 2'-C-Methyl-Cytidine Triphosphates against Human and Mouse Norovirus RNA Polymerases.Antimicrobial agents and chemotherapy · 2015Article
- Article
- A Cell-based Fluorescence Resonance Energy Transfer (FRET) Sensor Reveals Inter- and Intragenogroup Variations in Norovirus Protease Activity and Polyprotein Cleavage.The Journal of biological chemistry · 2015Article
- Advances in norovirus biology.Cell host & microbe · 2014Review
- Treatment of norovirus infections: moving antivirals from the bench to the bedside.Antiviral research · 2014Review
- Optimal terminal sequences for continuous or serial isothermal amplification of dsRNA with norovirus RNA replicase.Biophysics (Nagoya-shi, Japan) · 2014Article
- Characterization of norovirus RNA replicase for in vitro amplification of RNA.BMC biotechnology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
In vitro mapping studies of the MD145 norovirus (Caliciviridae) ORF1 polyprotein identified two stable cleavage products containing the viral RNA-dependent RNA polymerase (RdRp) domains: ProPol (a precursor comprised of both the proteinase and polymerase) and Pol (the mature polymerase). The goal of this study was to identify the active form (or forms) of the norovirus polymerase. The recombinant ProPol (expressed as Pro(-)Pol with an inactivated proteinase domain to prevent autocleavage) and recombinant Pol were purified after synthesis in bacteria and shown to be active RdRp enzymes. In addition, the mutant His-E1189A-ProPol protein (with active proteinase but with the natural ProPol cleavage site blocked) was active as an RdRp, confirming that the norovirus ProPol precursor could possess two enzymatic activities simultaneously. The effects of several UTP analogs on the RdRp activity of the norovirus and feline calicivirus Pro(-)Pol enzymes were compared and found to be similar. Our data suggest that the norovirus ProPol is a bifunctional enzyme during virus replication. The availability of this recombinant ProPol enzyme might prove useful in the development of antiviral drugs for control of the noroviruses associated with acute gastroenteritis.
Indexed as
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What OpenQuestion holds
Registered trials
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.