ReviewInternational journal of molecular sciences2013
NS3 protease from hepatitis C virus: biophysical studies on an intrinsically disordered protein domain.
Review in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 23 citations in OpenAlex.
- Vitamin D and Metabolic Dysfunction-Associated Steatotic Liver Disease: Molecular Mechanisms and Clinical Implications-A Narrative Review.International journal of molecular sciences · 2026Review
- Antiviral potential of zinc ion: mechanisms and applications in viral infections.Frontiers in microbiology · 2026Review
- Lipid Accumulation and Insulin Resistance: Bridging Metabolic Dysfunction-Associated Fatty Liver Disease and Chronic Kidney Disease.International journal of molecular sciences · 2025Review
- Evaluation of the Potency of Repurposed Antiretrovirals in HBV Therapy: A Narrative Investigation of the Traditional Medicine Alternatives.International journal of molecular sciences · 2025Review
- Hemoadsorption Therapy for Critically Ill Patients with Acute Liver Dysfunction: A Meta-Analysis and Systematic Review.Biomedicines · 2023Review
- Allopurinol versus Febuxostat: A New Approach for the Management of Hepatic Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease.Biomedicines · 2023Article
- A Review of the Current State of Magnetic Force Microscopy to Unravel the Magnetic Properties of Nanomaterials Applied in Biological Systems and Future Directions for Quantum Technologies.Nanomaterials (Basel, Switzerland) · 2023Review
- Looking at the Molecular Target of NS5A Inhibitors throughout a Population Highly Affected with Hepatitis C Virus.Pathogens (Basel, Switzerland) · 2023Article
- Biological Role of Zinc in Liver Cirrhosis: An Updated Review.Biomedicines · 2023Review
- Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging.Biomolecules · 2022Review
- Protein Abundance of Drug Transporters in Human Hepatitis C Livers.International journal of molecular sciences · 2022Article
- Dissection of two drug-targeted regions of Hepatitis C virus subtype 4a infecting Egyptian patients.Virus genes · 2020Article
- Rescuing compound bioactivity in a secondary cell-based screening by using γ-cyclodextrin as a molecular carrier.International journal of nanomedicine · 2015Article
- pH-dependent conformational changes in the HCV NS3 protein modulate its ATPase and helicase activities.PloS one · 2014Article
- Post-translational modifications of hepatitis C viral proteins and their biological significance.World journal of gastroenterology · 2013Review
- Digested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013).Intrinsically disordered proteinsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nonstructural protein 3 (NS3) from the hepatitis C virus (HCV) is responsible for processing the non-structural region of the viral precursor polyprotein in infected hepatic cells. NS3 protease activity, located at the N-terminal domain, is a zinc-dependent serine protease. A zinc ion, required for the hydrolytic activity, has been considered as a structural metal ion essential for the structural integrity of the protein. In addition, NS3 interacts with another cofactor, NS4A, an accessory viral protein that induces a conformational change enhancing the hydrolytic activity. Biophysical studies on the isolated protease domain, whose behavior is similar to that of the full-length protein (e.g., catalytic activity, allosteric mechanism and susceptibility to inhibitors), suggest that a considerable global conformational change in the protein is coupled to zinc binding. Zinc binding to NS3 protease can be considered as a folding event, an extreme case of induced-fit binding. Therefore, NS3 protease is an intrinsically (partially) disordered protein with a complex conformational landscape due to its inherent plasticity and to the interaction with its different effectors. Here we summarize the results from a detailed biophysical characterization of this enzyme and present new experimental data.
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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.