Computational and Crystallographic Analysis of Binding Structures of Inhibitory Compounds for HIV-1 RNase H Activity
Author:
Affiliation:
1. Graduate School of Pharmaceutical Sciences, Chiba University Inohana 1-8-1, Chuo-ku, Chiba 260-8675, Japan
2. Faculty of Pharmaceutical Sciences, Josai International University Gumyo 1, Togane-shi Chiba 283-8555, Japan
Funder
Adaptable and Seamless Technology Transfer Program through Target-Driven R and D
Japan Society for the Promotion of Science
Japan Science and Technology Agency
Publisher
American Chemical Society (ACS)
Subject
Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.2c00537
Reference41 articles.
1. Factors contributing to the inhibition of HIV reverse transcriptase by chain-terminating nucleotides in vitro and in vivo
2. Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase
3. Taking aim at a moving target: designing drugs to inhibit drug-resistant HIV-1 reverse transcriptases
4. Inhibitors of HIV-1 Reverse Transcriptase and Integrase: Classical and Emerging Therapeutical Approaches
5. Recent Progress in the Design of Small Molecule Inhibitors of HIV RNase H
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