Structural characterization of the Hepatitis C Virus NS3 protease from genotype 3a: The basis of the genotype 1b vs. 3a inhibitor potency shift
Author:
Funder
IRBM
Publisher
Elsevier BV
Subject
Virology
Reference47 articles.
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3. 15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanism;Bachovchin;Biochemistry,1986
4. The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism;Barbato;J. Mol. Biol.,1999
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1. Pan-NS3 protease inhibitors of hepatitis C virus based on an R3-elongated pyrazinone scaffold;European Journal of Medicinal Chemistry;2018-03
2. Associations between responses to interferon therapy and genetic variation in interleukin-28B and the core region of hepatitis C virus genotype 3a;J MED VIROL;2015
3. Bridging the past and the future of virology: Surface plasmon resonance as a powerful tool to investigate virus/host interactions;Critical Reviews in Microbiology;2013-09-23
4. Structural Modeling of HCV NS3/4A Serine Protease Drug-Resistance Mutations Using End-Point Continuum Solvation and Side-Chain Flexibility Calculations;Journal of Chemical Information and Modeling;2013-01-24
5. Hepacivirin;Handbook of Proteolytic Enzymes;2013
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