Exploring drug-resistant mechanisms of I84V mutation in HIV-1 protease toward different inhibitors by thermodynamics integration and solvated interaction energy method-Reference-Cited by-同舟云学术

Exploring drug-resistant mechanisms of I84V mutation in HIV-1 protease toward different inhibitors by thermodynamics integration and solvated interaction energy method

Published:2018-08 Issue: Volume:706 Page:400-408
ISSN:0009-2614
Container-title:Chemical Physics Letters
language:en
Short-container-title:Chemical Physics Letters

Author:

Gao Ya^ORCID,Zhu Tong^ORCID,Chen Jianzhong

Funder

National Natural Science Foundation of China

Shanghai Municipal Education Commission

China Postdoctoral Science Foundation, Shandong province university science and technology project

Shanghai University

Shandong Jiaotong University

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference56 articles.

1. INHIBITORS OF HIV-1 PROTEASE: A Major Success of Structure-Assisted Drug Design

2. HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: Possible contributions to drug resistance and a potential new target site for drugs

3. Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function

4. Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1

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