ArticleActa crystallographica. Section F, Structural biology communications2025
Nucleotide-bound crystal structures of the SARS-CoV-2 helicase NSP13.
Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Recent advances in functional studies of coronavirus NSP13 helicase and challenges in inhibitor development.Virulence · 2026Review
- Repurposing drug screen for the identification of helicase inhibitors from viruses of pandemic concern.SLAS discovery : advancing life sciences R & D · 2026Article
- 2-Phenylquinolines Exhibit Anti-Severe Acute Respiratory Syndrome Coronavirus-2 Activity Through the Nonstructural Protein 13 Helicase Inhibition.ChemMedChem · 2026Article
- Structural and Computational Insights into the Attenuated Innate Immune Recognition of the SARS-CoV-2 N15 Lineage, an Early-Pandemic Variant.Computational and structural biotechnology journal · 2026Article
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4 authors.
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Abstract
Nucleotide-bound crystal structures of SARS-CoV-2 NSP13 in ADP- and ATP-bound states were resolved to 1.8 and 1.9 Å, respectively. The ADP-bound model captures a state immediately following ATP hydrolysis, with both ADP and orthophosphate still present in the active site. Further comparative analysis revealed that crystal packing influences NSP13 by stabilizing the nucleotide-binding site, underscoring the importance of accounting for these effects in structure-based drug design targeting NSP13.
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