Free Energy-Based Virtual Screening and Optimization of RNase H Inhibitors of HIV-1 Reverse Transcriptase
Author:
Affiliation:
1. Department of Chemistry, Brooklyn College, City University of New York, Brooklyn, New York 11210, United States
Funder
U.S. Department of Health and Human Services
National Science Foundation
Publisher
American Chemical Society (ACS)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acsomega.6b00123
Reference72 articles.
1. Structure and Function of HIV-1 Reverse Transcriptase: Molecular Mechanisms of Polymerization and Inhibition
2. Mutations within the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Abolish Virus Infectivity
3. Identification of Alternative Binding Sites for Inhibitors of HIV-1 Ribonuclease H Through Comparative Analysis of Virtual Enrichment Studies
4. Structure of HIV-1 Reverse Transcriptase with the Inhibitor β-Thujaplicinol Bound at the RNase H Active Site
5. HIV-1 Reverse Transcriptase Structure with RNase H Inhibitor Dihydroxy Benzoyl Naphthyl Hydrazone Bound at a Novel Site
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