ArticleMethods in molecular biology (Clifton, N.J.)2010
A method to simultaneously monitor hepatitis C virus NS3 helicase and protease activities.
Article in Methods in molecular biology (Clifton, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Active DNA unwinding and transport by a membrane-adapted helicase nanopore.Nature communications · 2019Article
- Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells.The Journal of biological chemistry · 2017Article
- Simultaneously Targeting the NS3 Protease and Helicase Activities for More Effective Hepatitis C Virus Therapy.ACS chemical biology · 2015Article
- Discovery of the 2-phenyl-4,5,6,7-Tetrahydro-1H-indole as a novel anti-hepatitis C virus targeting scaffold.European journal of medicinal chemistry · 2015Article
- Ebselen inhibits hepatitis C virus NS3 helicase binding to nucleic acid and prevents viral replication.ACS chemical biology · 2014Article
- Identification and biochemical characterization of halisulfate 3 and suvanine as novel inhibitors of hepatitis C virus NS3 helicase from a marine sponge.Marine drugs · 2014Article
- Primuline derivatives that mimic RNA to stimulate hepatitis C virus NS3 helicase-catalyzed ATP hydrolysis.The Journal of biological chemistry · 2013Article
- Fluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation.Antiviral research · 2012Article
- Optimization of potent hepatitis C virus NS3 helicase inhibitors isolated from the yellow dyes thioflavine S and primuline.Journal of medicinal chemistry · 2012Article
- Identification and analysis of inhibitors targeting the hepatitis C virus NS3 helicase.Methods in enzymology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The hepatitis C virus NS3 protein contains an N-terminal serine protease and a C-terminal helicase that unwinds RNA or DNA duplexes. The HCV NS3 protein is the target for several antiviral drugs in clinical trials, which inhibit the protease function. A method is reported to simultaneously monitor the helicase and protease function of the NS3 protein in a single reaction using fluorescence spectroscopy and a single chain recombinant protein where NS3 is fused to its protease activator NS4A. The method monitors both activities together in real time and is amenable to high-throughput screening. This new procedure could be used to identify compounds that inhibit both the helicase and protease activity of NS3.
Indexed as
Identifiers
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.