ArticleNucleic acids research2004
Enhanced nucleic acid binding to ATP-bound hepatitis C virus NS3 helicase at low pH activates RNA unwinding.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- Hepatitis C virus NS3 helicase contributes to (-) strand RNA synthesis.Nature communications · 2025Article
- Conformational Changes and ATP Hydrolysis in Zika Helicase: The Molecular Basis of a Biomolecular Motor Unveiled by Multiscale Simulations.Journal of the American Chemical Society · 2023Article
- Role of the Conserved DECH-Box Cysteine in Coupling Hepatitis C Virus Helicase-Catalyzed ATP Hydrolysis to RNA Unwinding.Biochemistry · 2018Article
- X-ray structure of the pestivirus NS3 helicase and its conformation in solution.Journal of virology · 2015Article
- Benzothiazole and Pyrrolone Flavivirus Inhibitors Targeting the Viral Helicase.ACS infectious diseases · 2015Article
- Amodiaquine, an antimalarial drug, inhibits dengue virus type 2 replication and infectivity.Antiviral research · 2014Article
- Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activity.The Journal of biological chemistry · 2014Article
- pH-dependent conformational changes in the HCV NS3 protein modulate its ATPase and helicase activities.PloS one · 2014Article
- The interdomain interface in bifunctional enzyme protein 3/4A (NS3/4A) regulates protease and helicase activities.Protein science : a publication of the Protein Society · 2013Article
- Fluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation.Antiviral research · 2012Article
- Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA.Biochemistry · 2012Article
- Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target.The Journal of biological chemistry · 2010Review
- Mechanism and specificity of a symmetrical benzimidazolephenylcarboxamide helicase inhibitor.Biochemistry · 2010Article
- Fuel specificity of the hepatitis C virus NS3 helicase.Journal of molecular biology · 2009Article
- Helicase inhibitors as specifically targeted antiviral therapy for hepatitis C.Future virology · 2009Article
- Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase.The Journal of biological chemistry · 2008Article
- Effects of mutagenic and chain-terminating nucleotide analogs on enzymes isolated from hepatitis C virus strains of various genotypes.Antimicrobial agents and chemotherapy · 2008Article
- Role of divalent metal cations in ATP hydrolysis catalyzed by the hepatitis C virus NS3 helicase: magnesium provides a bridge for ATP to fuel unwinding.Journal of molecular biology · 2007Article
- The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target.Current issues in molecular biology · 2007Review
- Understanding helicases as a means of virus control.Current pharmaceutical design · 2006Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The molecular basis of the low-pH activation of the helicase encoded by the hepatitis C virus (HCV) was examined using either a full-length NS3 protein/NS4A cofactor complex or truncated NS3 proteins lacking the protease domain, which were isolated from three different viral genotypes. All proteins unwound RNA and DNA best at pH 6.5, which demonstrate that conserved NS3 helicase domain amino acids are responsible for low-pH enzyme activation. DNA unwinding was less sensitive to pH changes than RNA unwinding. Both the turnover rate of ATP hydrolysis and the K(m) of ATP were similar between pH 6 and 10, but the concentration of nucleic acid needed to stimulate ATP hydrolysis decreased almost 50-fold when the pH was lowered from 7.5 to 6.5. In direct-binding experiments, HCV helicase bound DNA weakly at high pH only in the presence of the non-hydrolyzable ATP analog, ADP(BeF3). These data suggest that a low-pH environment might be required for efficient HCV RNA translation or replication, and support a model in which an acidic residue rotates toward the RNA backbone upon ATP binding repelling nucleic acid from the binding cleft.
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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.