Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding
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Title
Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 49, Pages 20986-20991
Publisher
Proceedings of the National Academy of Sciences
Online
2010-11-18
DOI
10.1073/pnas.1006370107
References
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- Structure–activity relationship study on a novel series of cyclopentane-containing macrocyclic inhibitors of the hepatitis C virus NS3/4A protease leading to the discovery of TMC435350
- (2008) Pierre Raboisson et al. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
- Naturally occurring dominant resistance mutations to hepatitis C virus protease and polymerase inhibitors in treatment-naïve patients
- (2008) Thomas Kuntzen et al. HEPATOLOGY
- Discovery and Structure−Activity Relationship of P1−P3Ketoamide Derived Macrocyclic Inhibitors of Hepatitis C Virus NS3 Protease
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- HIV-1 Protease Inhibitors from Inverse Design in the Substrate Envelope Exhibit Subnanomolar Binding to Drug-Resistant Variants
- (2008) Michael D. Altman et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
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