ArticleThe Journal of biological chemistry2026
SARS-CoV-2 Nsp13 helicase resolves G-quadruplexes and is inhibited by G4 ligands or an antiviral regulator: Implications for G4 anti-coronavirus therapies.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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8 authors.
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Abstract
The COVID-19 pandemic is often viewed as a once-in-a-century event. However, the rise of new variants and the potential for infections from related coronaviruses continues to be a significant concern. Vaccines were a successful deterrent to COVID-19, but anti-coronavirus drugs to treat individuals with COVID-19 or Long COVID are not robust. Efforts to identify novel coronaviruses and host targets for drug therapies are highly valued. We determined that the SARS-CoV-2 Nsp13 helicase resolves G-quadruplexes (G4) of various topologies in an ATP-stimulated manner. Additionally, the requirement for a 5'-single-stranded tail flanking DNA-G4 indicates its 5'- to 3'-translocation directionality. G4 ligands were tested for inhibition of Nsp13 G4 resolvase. PhenDC3 inhibited Nsp13 resolution of four-stranded parallel G4 (IC
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