ArticleThe EMBO journal2002
The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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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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Who cites it
110 citing papers in PubMed, 214 citations in OpenAlex.
- Co-Circulation of Divergent Strains Supports Vector-Mediated Transmission of Rodent Hepacivirus J (Viruses · 2026Article
- Structural basis for dual DNA and RNA specificity of the G-quadruplex-resolving DEAH-box helicase DHX36.Cell reports · 2025Article
- The nonstructural protein 13 of porcine deltacoronavirus coordinates ATP-driven duplex unwinding and ATP-independent strand annealing for nucleic acid remodeling.BMC veterinary research · 2025Article
- Thermodynamic and mechanistic analysis of the functional properties of dengue virus NS3 helicase.Biophysical reviews · 2023Review
- Allosteric activation of RhlB by RNase E induces partial duplex opening in substrate RNA.Frontiers in molecular biosciences · 2023Article
- Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Measuring the impact of cofactors on RNA helicase activities.Methods (San Diego, Calif.) · 2022Article
- Methods to assess helicase and translocation activities of human nuclear RNA exosome and RNA adaptor complexes.Methods in enzymology · 2022Article
- Compartmentalized replication organelle of flavivirus at the ER and the factors involved.Cellular and molecular life sciences : CMLS · 2021Review
- A positively charged surface patch on the pestivirus NS3 protease module plays an important role in modulating NS3 helicase activity and virus production.Archives of virology · 2021Article
- Duplex DNA engagement and RPA oppositely regulate the DNA-unwinding rate of CMG helicase.Nature communications · 2020Article
- A high ATP concentration enhances the cooperative translocation of the SARS coronavirus helicase nsP13 in the unwinding of duplex RNA.Scientific reports · 2020Article
- Zika virus NS3 is a canonical RNA helicase stimulated by NS5 RNA polymerase.Nucleic acids research · 2019Article
- Recombinant HCV NS3 and NS5B enzymes exhibit multiple posttranslational modifications for potential regulation.Virus genes · 2019Article
- N-Naphthoyl-substituted indole thio-barbituric acid analogs inhibit the helicase activity of the hepatitis C virus NS3.Bioorganic & medicinal chemistry letters · 2019Article
- Overview of HCV Life Cycle with a Special Focus on Current and Possible Future Antiviral Targets.Viruses · 2019Review
- NS3 from Hepatitis C Virus Strain JFH-1 Is an Unusually Robust Helicase That Is Primed To Bind and Unwind Viral RNA.Journal of virology · 2018Article
- The Human Replicative Helicase, the CMG Complex, as a Target for Anti-cancer Therapy.Frontiers in molecular biosciences · 2018Review
- Single-molecule imaging reveals the translocation and DNA looping dynamics of hepatitis C virus NS3 helicase.Protein science : a publication of the Protein Society · 2017Article
- A positive-strand RNA virus uses alternative protein-protein interactions within a viral protease/cofactor complex to switch between RNA replication and virion morphogenesis.PLoS pathogens · 2017Article
50 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 3 countries.
Funding
Abstract
The RNA helicase/protease NS3 plays a central role in the RNA replication of hepatitis C virus (HCV), a cytoplasmic RNA virus that represents a major worldwide health problem. NS3 is, therefore, an important drug target in the effort to combat HCV. Most work has focused on the protease, rather than the helicase, activities of the enzyme. In order to further characterize NS3 helicase activity, we evaluated individual stages of duplex unwinding by NS3 alone and in complex with cofactor NS4A. Despite a putative replicative role in RNA unwinding, we found that NS3 alone is a surprisingly poor helicase on RNA, but that RNA activity is promoted by cofactor NS4A. In contrast, NS3 alone is a highly processive helicase on DNA. Phylogenetic analysis suggests that this robust DNA helicase activity is not vestigial and may have specifically evolved in HCV. Given that HCV has no replicative DNA intermediate, these findings suggest that NS3 may have the capacity to affect host DNA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.