ArticleProtein science : a publication of the Protein Society1999
A novel recombinant single-chain hepatitis C virus NS3-NS4A protein with improved helicase activity.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 51 citations in OpenAlex.
- Simultaneously Targeting the NS3 Protease and Helicase Activities for More Effective Hepatitis C Virus Therapy.ACS chemical biology · 2015Article
- Nonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.Journal of virology · 2015Article
- Fluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation.Antiviral research · 2012Article
- Protease inhibitor-resistant hepatitis C virus mutants with reduced fitness from impaired production of infectious virus.Gastroenterology · 2011Article
- The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.The Journal of biological chemistry · 2010Article
- A method to simultaneously monitor hepatitis C virus NS3 helicase and protease activities.Methods in molecular biology (Clifton, N.J.) · 2010Article
- Fuel specificity of the hepatitis C virus NS3 helicase.Journal of molecular biology · 2009Article
- Single strand binding proteins increase the processivity of DNA unwinding by the hepatitis C virus helicase.Journal of molecular biology · 2008Article
- Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome.Genes & development · 2007Article
- The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target.Current issues in molecular biology · 2007Review
- Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase.Journal of virology · 2005Article
- The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently.The Journal of biological chemistry · 2004Article
- Hepatitis C virus NS3 ATPases/helicases from different genotypes exhibit variations in enzymatic properties.Journal of virology · 2003Article
- Establishment of a simple assay in vitro for hepatitis C virus NS3 serine protease based on recombinant substrate and single-chain protease.World journal of gastroenterology · 2002Article
- Comparative characterization of two DEAD-box RNA helicases in superfamily II: human translation-initiation factor 4A and hepatitis C virus non-structural protein 3 (NS3) helicase.The Biochemical journal · 2002Article
- The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding.The EMBO journal · 2002Article
- Virus-specific cofactor requirement and chimeric hepatitis C virus/GB virus B nonstructural protein 3.Journal of virology · 2000Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis C virus (HCV) nonstructural protein 3 (NS3) has been shown to possess protease and helicase activities and has also been demonstrated to spontaneously associate with nonstructural protein NS4A (NS4A) to form a stable complex. Previous attempts to produce the NS3/NS4A complex in recombinant baculovirus resulted in a protein complex that aggregated and precipitated in the absence of nonionic detergent and high salt. A single-chain form of the NS3/NS4A complex (His-NS4A21-32-GSGS-NS3-631) was constructed in which the NS4A core peptide is fused to the N-terminus of the NS3 protease domain as previously described (Taremi et al., 1998). This protein contains a histidine tagged NS4A peptide (a.a. 21-32) fused to the full-length NS3 (a.a. 3-631) through a flexible tetra amino acid linker. The recombinant protein was expressed to high levels in Escherichia coli, purified to homogeneity, and examined for NTPase, nucleic acid unwinding, and proteolytic activities. The single-chain recombinant NS3-NS4A protein possesses physiological properties equivalent to those of the NS3/NS4A complex except that this novel construct is stable, soluble and sixfold to sevenfold more active in unwinding duplex RNA. Comparison of the helicase activity of the single-chain recombinant NS3-NS4A with that of the full-length NS3 (without NS4A) and that of the helicase domain alone suggested that the presence of the protease domain and at least the NS4A core peptide are required for optimal unwinding activity.
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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.