Multi-drug resistance profile of PR20 HIV-1 protease is attributed to distorted conformational and drug binding landscape: molecular dynamics insights-Reference-Cited by-同舟云学术

Multi-drug resistance profile of PR20 HIV-1 protease is attributed to distorted conformational and drug binding landscape: molecular dynamics insights

Published:2015-03-27 Issue:1 Volume:34 Page:135-151
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Chetty Sarentha,Bhakat Soumendranath,Martin Alberto J.M.,Soliman Mahmoud E.S.

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

http://www.tandfonline.com/doi/pdf/10.1080/10256018808623883

Reference47 articles.

1. HIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural Rearrangements

2. Extreme Multidrug Resistant HIV-1 Protease with 20 Mutations Is Resistant to Novel Protease Inhibitors with P1′-Pyrrolidinone or P2-Tris-tetrahydrofuran

3. Comparison of the Molecular Dynamics and Calculated Binding Free Energies for Nine FDA-Approved HIV-1 PR Drugs Against Subtype B and C-SA HIV PR

4. The Impact of Active Site Mutations of South African HIV PR on Drug Resistance: Insight from Molecular Dynamics Simulations, Binding Free Energy and Per-Residue Footprints

5. Integration of Genomic Information with Biological Networks Using Cytoscape

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