ArticleJournal of molecular biology2008
Single strand binding proteins increase the processivity of DNA unwinding by the hepatitis C virus helicase.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- Monitoring helicase-catalyzed unwinding of multiple duplexes simultaneously.Methods in enzymology · 2022Article
- Article
- Dynamics of DNA nicking and unwinding by the RepC-PcrA complex.Nucleic acids research · 2020Article
- Zika virus NS3 is a canonical RNA helicase stimulated by NS5 RNA polymerase.Nucleic acids research · 2019Article
- Processivity, Velocity, and Universal Characteristics of Nucleic Acid Unwinding by Helicases.Biophysical journal · 2019Article
- Helicase processivity and not the unwinding velocity exhibits universal increase with force.Biophysical journal · 2015Article
- Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction.Biochemistry · 2015Article
- Two steps forward, one step back: determining XPD helicase mechanism by single-molecule fluorescence and high-resolution optical tweezers.DNA repair · 2014Review
- Interaction of T4 UvsW helicase and single-stranded DNA binding protein gp32 through its carboxy-terminal acidic tail.Journal of molecular biology · 2013Article
- A new helicase assay based on graphene oxide for anti-viral drug development.Molecules and cells · 2013Review
- Systematic functional comparative analysis of four single-stranded DNA-binding proteins and their affection on viral RNA metabolism.PloS one · 2013Article
- Physical and functional interaction between yeast Pif1 helicase and Rim1 single-stranded DNA binding protein.Nucleic acids research · 2013Article
- Structure and Mechanisms of SF1 DNA Helicases.Advances in experimental medicine and biology · 2013Article
- Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target.The Journal of biological chemistry · 2010Review
- Inching over hurdles: how DNA helicases move on crowded lattices.Cell cycle (Georgetown, Tex.) · 2010Review
- Investigation of translocation, DNA unwinding, and protein displacement by NS3h, the helicase domain from the hepatitis C virus helicase.Biochemistry · 2010Article
- Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.Nucleic acids research · 2010Article
- NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations.The Journal of biological chemistry · 2009Article
- Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The nonstructural NS3 protein of the hepatitis C virus is a multifunctional enzyme with an N-terminal serine protease activity and a C-terminal helicase activity. The helicase is capable of unwinding both DNA and RNA duplexes; however, the overall processivity of the helicase is fairly low. We show here that single-strand binding (SSB) proteins enhance the unwinding processivity of both the NS3 helicase domain (NS3h) and the full-length protease-helicase NS3-4A. The detailed study of the effect of SSB on the DNA unwinding activity of NS3h indicates that the SSB stabilizes the helicase at the unwinding junction and prevents its dissociation. These results suggest a potential role for either cellular or virus-encoded SSB protein in improving the processivity of the NS3 in vivo.
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What OpenQuestion holds
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.