ArticleNature chemical biology2012
Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function.
Article in Nature chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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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
52 citing papers in PubMed.
- Conformational Dynamics of Viral Protease Precursors in Maturation, Inhibition, and Drug-Resistance Development.Viruses · 2026Review
- Identification and optimization of first-in-class RNA helicase inhibitors of DDX1, LGP2, and MDA5.European journal of medicinal chemistry · 2026Article
- Review
- Structural Chemistry of Helicase Inhibition.Journal of medicinal chemistry · 2025Review
- Fragment-based drug discovery: A graphical review.Current research in pharmacology and drug discovery · 2025Review
- Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function.Nature communications · 2024Article
- VSpipe-GUI, an Interactive Graphical User Interface for Virtual Screening and Hit Selection.International journal of molecular sciences · 2024Article
- Using a Function-First "Scout Fragment"-Based Approach to Develop Allosteric Covalent Inhibitors of Conformationally Dynamic Helicase Mechanoenzymes.Journal of the American Chemical Society · 2024Article
- Characterization of a multipurpose NS3 surface patch coordinating HCV replicase assembly and virion morphogenesis.PLoS pathogens · 2022Article
- NS3 helicase inhibitory potential of the marine spongeRSC advances · 2022Article
- C-H functionalisation tolerant to polar groups could transform fragment-based drug discovery (FBDD).Chemical science · 2021Article
- Hepatitis C Viral Replication Complex.Viruses · 2021Review
- Targeting novel structural and functional features of coronavirus protease nsp5 (3CLThe Journal of general virology · 2021Review
- Article
- Fragment-based drug discovery: opportunities for organic synthesis.RSC medicinal chemistry · 2020Review
- Investigation of some benzoquinazoline and quinazoline derivatives as novel inhibitors of HCV-NS3/4A protease: biological, molecular docking and QSAR studies.RSC advances · 2020Article
- A Comprehensive Mapping of the Druggable Cavities within the SARS-CoV-2 Therapeutically Relevant Proteins by Combining Pocket and Docking Searches as Implemented in Pockets 2.0.International journal of molecular sciences · 2020Article
- Hepatitis C Virus Replication.Cold Spring Harbor perspectives in medicine · 2020Review
- Near-Neighbor Interactions in the NS3-4A Protease of HCV Impact Replicative Fitness of Drug-Resistant Viral Variants.Journal of molecular biology · 2019Article
- Co-evolution networks of HIV/HCV are modular with direct association to structure and function.PLoS computational biology · 2018Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Here we report a highly conserved new binding site located at the interface between the protease and helicase domains of the hepatitis C virus (HCV) NS3 protein. Using a chemical lead, identified by fragment screening and structure-guided design, we demonstrate that this site has a regulatory function on the protease activity via an allosteric mechanism. We propose that compounds binding at this allosteric site inhibit the function of the NS3 protein by stabilizing an inactive conformation and thus represent a new class of direct-acting antiviral agents.
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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.