ReviewVirulence2026
Recent advances in functional studies of coronavirus NSP13 helicase and challenges in inhibitor development.
Review in Virulence, 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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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.
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11 authors.
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Abstract
Coronavirus helicase NSP13 is essential for viral replication and transcription and is a promising target for broad-spectrum anti-coronavirus drugs due to its high sequence conservation and structural homology. This review summarizes NSP13 sequence features, structural organization, and functional activities across the seven human-infecting coronaviruses. We outline key enzymatic properties, including duplex RNA/DNA unwinding and NTP hydrolysis, and describe how NSP13 cooperates with other nonstructural proteins to drive replication and transcription. Beyond canonical helicase roles, we discuss the genomic distribution of G-quadruplex (G4) elements in coronaviruses and potential functional connections between G4 structures and NSP13 in regulating the viral life cycle. Finally, we highlight recent progress in developing NSP13-targeting inhibitors and consider their potential utility against COVID-19 and other emerging coronaviruses, providing a rationale for broad-spectrum antiviral design.
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