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The Coronavirus helicase in replication.
Grimes, Samantha L; Denison, Mark R.
Affiliation
  • Grimes SL; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
  • Denison MR; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA. Electronic address: mark.denison@vumc.org.
Virus Res ; 346: 199401, 2024 Aug.
Article in En | MEDLINE | ID: mdl-38796132
ABSTRACT
The coronavirus nonstructural protein (nsp) 13 encodes an RNA helicase (nsp13-HEL) with multiple enzymatic functions, including unwinding and nucleoside phosphatase (NTPase) activities. Attempts for enzymatic inactivation have defined the nsp13-HEL as a critical enzyme for viral replication and a high-priority target for antiviral development. Helicases have been shown to play numerous roles beyond their canonical ATPase and unwinding activities, though these functions are just beginning to be explored in coronavirus biology. Recent genetic and biochemical studies, as well as work in structurally-related helicases, have provided evidence that supports new hypotheses for the helicase's potential role in coronavirus replication. Here, we review several aspects of the coronavirus nsp13-HEL, including its reported and proposed functions in viral replication and highlight fundamental areas of research that may aid the development of helicase inhibitors.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Virus Replication / Viral Nonstructural Proteins / RNA Helicases Limits: Animals / Humans Language: En Journal: Virus Res Journal subject: VIROLOGIA Year: 2024 Document type: Article Affiliation country: Estados Unidos

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Virus Replication / Viral Nonstructural Proteins / RNA Helicases Limits: Animals / Humans Language: En Journal: Virus Res Journal subject: VIROLOGIA Year: 2024 Document type: Article Affiliation country: Estados Unidos