ArticleVirology2015
Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses.
Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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.
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Who cites it
9 citing papers in PubMed.
- Sequences and Structures of Viral Proteins Linked to the Genomes (VPg) of RNA Viruses.Viruses · 2025Review
- Article
- Mechanisms of instantaneous inactivation of SARS-CoV-2 by silicon nitride bioceramic.Materials today. Bio · 2021Article
- DGraph Clusters Flaviviruses and β-Coronaviruses According to Their Hosts, Disease Type, and Human Cell Receptors.Bioinformatics and biology insights · 2021Article
- D-graph clusters flaviviruses and β-coronaviruses according to their hosts, disease type and human cell receptors.bioRxiv : the preprint server for biology · 2020Article
- Repurposing approved drugs on the pathway to novel therapies.Medicinal research reviews · 2020Review
- Polyglutamine Repeats in Viruses.Molecular neurobiology · 2019Review
- Picornaviral polymerase structure, function, and fidelity modulation.Virus research · 2017Review
- Allosteric inhibitors of Coxsackie virus A24 RNA polymerase.Bioorganic & medicinal chemistry · 2016Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Enteroviruses (EV) uridylylate a peptide, VPg, as the first step in their replication. VPgpUpU, found free in infected cells, serves as the primer for RNA elongation. The abilities of four polymerases (3D(pol)), from EV-species A-C, to uridylylate VPgs that varied by up to 60% of their residues were compared. Each 3D(pol) was able to uridylylate all five VPgs using polyA RNA as template, while showing specificity for its own genome encoded peptide. All 3D(pol) uridylylated a consensus VPg representing the physical chemical properties of 31 different VPgs. Thus the residues required for uridylylation and the enzymatic mechanism must be similar in diverse EV. As VPg-binding sites differ in co-crystal structures, the reaction is probably done by a second 3D(pol) molecule. The conservation of polymerase residues whose mutation reduces uridylylation but not RNA elongation is compared.
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