ArticleJournal of virology2001
Structure-based mutational analysis of the hepatitis C virus NS3 helicase.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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Who cites it
39 citing papers in PubMed, 69 citations in OpenAlex.
- Article
- Evaluation of Risk Determinants and Molecular Characterisation for Non-Primate Hepacivirus Infection in Turkish Horses.Pathogens (Basel, Switzerland) · 2025Article
- Sequential Phosphorylation of Hepatitis C Virus NS5A Protein Requires the ATP-Binding Domain of NS3 Helicase.Journal of virology · 2022Article
- Conserved motifs in the flavivirus NS3 RNA helicase enzyme.Wiley interdisciplinary reviews. RNA · 2022Review
- Structural basis for activation of Swi2/Snf2 ATPase RapA by RNA polymerase.Nucleic acids research · 2021Article
- Structure and function of DEAH-box helicase 32 and its role in cancer.Oncology letters · 2021Review
- An in silico approach to analyze HCV genotype-specific binding-site variation and its effect on drug-protein interaction.Scientific reports · 2020Article
- Motif V regulates energy transduction between the flavivirus NS3 ATPase and RNA-binding cleft.The Journal of biological chemistry · 2020Article
- Role of the Conserved DECH-Box Cysteine in Coupling Hepatitis C Virus Helicase-Catalyzed ATP Hydrolysis to RNA Unwinding.Biochemistry · 2018Article
- RecA-like domain 2 of DNA-dependent ATPase A domain, a SWI2/SNF2 protein, mediates conformational integrity and ATP hydrolysis.Bioscience reports · 2018Article
- Molecular mechanism of divalent-metal-induced activation of NS3 helicase and insights into Zika virus inhibitor design.Nucleic acids research · 2016Article
- Hepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteins.PLoS pathogens · 2015Article
- Analysis of the Enzymatic Activity of an NS3 Helicase Genotype 3a Variant Sequence Obtained from a Relapse Patient.PloS one · 2015Article
- Comparison of structural architecture of HCV NS3 genotype 1 versus Pakistani genotype 3a.BioMed research international · 2014Article
- Article
- Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV.Journal of molecular biology · 2011Article
- Intracytoplasmic stable expression of IgG1 antibody targeting NS3 helicase inhibits replication of highly efficient hepatitis C Virus 2a clone.Virology journal · 2010Article
- Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Bluetongue virus: dissection of the polymerase complex.The Journal of general virology · 2008Review
- NS3 helicase domains involved in infectious intracellular hepatitis C virus particle assembly.Journal of virology · 2008Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The carboxyl terminus of the hepatitis C virus (HCV) nonstructural protein 3 (NS3) possesses ATP-dependent RNA helicase activity. Based on the conserved sequence motifs and the crystal structures of the helicase domain, 17 mutants of the HCV NS3 helicase were generated. The ATP hydrolysis, RNA binding, and RNA unwinding activities of the mutant proteins were examined in vitro to determine the functional role of the mutated residues. The data revealed that Lys-210 in the Walker A motif and Asp-290, Glu-291, and His-293 in the Walker B motif were crucial to ATPase activity and that Thr-322 and Thr-324 in motif III and Arg-461 in motif VI significantly influenced ATPase activity. When the pairing between His-293 and Gln-460, referred to as gatekeepers, was replaced with the Asp-293/His-460 pair, which makes the NS3 helicase more like the DEAD helicase subgroup, ATPase activity was not restored. It thus indicated that the whole microenvironment surrounding the gatekeepers, rather than the residues per se, was important to the enzymatic activities. Arg-461 and Trp-501 are important residues for RNA binding, while Val-432 may only play a coadjutant role. The data demonstrated that RNA helicase activity was possibly abolished by the loss of ATPase activity or by reduced RNA binding activity. Nevertheless, a low threshold level of ATPase activity was found sufficient for helicase activity. Results in this study provide a valuable reference for efforts under way to develop anti-HCV therapeutic drugs targeting NS3.
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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.