ArticleStructure (London, England : 1993)2012
Conformational changes in motif D of RdRPs as fidelity determinant.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed.
- Identification of fidelity-determined residues of Porcine reproductive and respiratory syndrome virus through structural alignment.Virulence · 2026Article
- Article
- Homology-Based Identification of a Mutation in the Coronavirus RNA-Dependent RNA Polymerase That Confers Resistance to Multiple Mutagens.Journal of virology · 2016Article
- Regulation of Flavivirus RNA synthesis and replication.Current opinion in virology · 2014Review
- The crystal structure of a cardiovirus RNA-dependent RNA polymerase reveals an unusual conformation of the polymerase active site.Journal of virology · 2014Article
- Repeated exposure to 5D9, an inhibitor of 3D polymerase, effectively limits the replication of foot-and-mouth disease virus in host cells.Antiviral research · 2013Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA-dependent RNA polymerases (RdRPs) are the central players in both transcription and viral genome replication. Using NMR spectroscopy, Yang and colleagues (in this issue of Structure) show that the conformational changes in the structural motif D of poliovirus RdRP correlate with the nature of the bound nucleotide (correct versus incorrect), with a conserved lysine within this motif playing a key role.
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Registered trials
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