The Serine Protease Domain of Hepatitis C Viral NS3 Activates RNA Helicase Activity by Promoting the Binding of RNA Substrate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
1. Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease–helicase
2. The Nonstructural Protein 3 Protease/Helicase Requires an Intact Protease Domain to Unwind Duplex RNA Efficiently
3. A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase
4. Stimulation of Hepatitis C Virus (HCV) Nonstructural Protein 3 (NS3) Helicase Activity by the NS3 Protease Domain and by HCV RNA-Dependent RNA Polymerase
5. Hepatitis C Virus NS3 ATPases/Helicases from Different Genotypes Exhibit Variations in Enzymatic Properties
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3. Mechanical regulation of the helicase activity of Zika virus NS3;Biophysical Journal;2022-12
4. Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures;Journal of Biological Chemistry;2022-11
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