ReviewCurrent issues in molecular biology2007
The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target.
Review in Current issues in molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
86 citing papers in PubMed, 133 citations in OpenAlex.
- Article
- Review
- Hepatitis C virus NS3 helicase contributes to (-) strand RNA synthesis.Nature communications · 2025Article
- From viruses to cancer: exploring the role of the hepatitis C virus NS3 protein in carcinogenesis.Infectious agents and cancer · 2024Review
- Advanced Theranostic Strategies for Viral Hepatitis Using Carbon Nanostructures.Micromachines · 2023Review
- Genetically Encoded Detection of Biosynthetic Protease Inhibitors.ACS synthetic biology · 2023Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Molecular docking analysis of fluoroquinolones and other natural and synthetic compounds with the HCV NS3 helicase.Bioinformation · 2022Article
- Epistatic interactions promote persistence of NS3-Q80K in HCV infection by compensating for protein folding instability.The Journal of biological chemistry · 2021Article
- Geminivirus Betasatellite-Encoded βC1 Protein Exhibits Novel ATP Hydrolysis Activity That Influences Its DNA-Binding Activity and Viral Pathogenesis.Journal of virology · 2021Article
- Antiviral Peptides Targeting the Helicase Activity of Enterovirus Nonstructural Protein 2C.Journal of virology · 2021Article
- The RNA helicase Dhx15 mediates Wnt-induced antimicrobial protein expression in Paneth cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- An in silico approach to analyze HCV genotype-specific binding-site variation and its effect on drug-protein interaction.Scientific reports · 2020Article
- The Structure, Function, and Mechanisms of Action of Enterovirus Non-structural Protein 2C.Frontiers in microbiology · 2020Review
- Molecular docking and simulation of Zika virus NS3 helicase.BMC chemistry · 2019Article
- Ebola virus VP35 has novel NTPase and helicase-like activities.Nucleic acids research · 2019Article
- Nucleotide triphosphatase and RNA chaperone activities of murine norovirus NS3.The Journal of general virology · 2018Article
- Role of the Conserved DECH-Box Cysteine in Coupling Hepatitis C Virus Helicase-Catalyzed ATP Hydrolysis to RNA Unwinding.Biochemistry · 2018Article
- Structural view of the helicase reveals that Zika virus uses a conserved mechanism for unwinding RNA.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Human Norovirus NS3 Has RNA Helicase and Chaperoning Activities.Journal of virology · 2018Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The C-terminal portion of hepatitis C virus (HCV) nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3' to 5' direction. Fueled byATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA and proteins bound to the nucleic acid. HCV helicase shares two domains common to other motor proteins, one of which appears to rotate upon ATP binding. Several models have been proposed to explain how this conformational change leads to protein movement and RNA unwinding, but no model presently explains all existing experimental data. Compounds recently reported to inhibit HCV helicase, which include numerous small molecules, RNA aptamers and antibodies, will be useful for elucidating the role of a helicase in positive-sense single-stranded RNA virus replication and might serve as templates for the design of novel antiviral drugs.
Indexed as
Identifiers
17263143PMC3571657W314374653What 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.