Molecular Dynamic and Free Energy Studies of Primary Resistance Mutations in HIV-1 Protease−Ritonavir Complexes-Reference-Cited by-同舟云学术

Molecular Dynamic and Free Energy Studies of Primary Resistance Mutations in HIV-1 Protease−Ritonavir Complexes

Published:2006-08-24 Issue:5 Volume:46 Page:2085-2092
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Aruksakunwong Ornjira¹,Wolschann Peter¹,Hannongbua Supot¹,Sompornpisut Pornthep¹

Affiliation:

1. Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10400, Thailand, and Institute for Theoretical Chemistry, University of Vienna, Vienna 1090, Austria

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/ci060090c

Reference34 articles.

1. Proteolytic processing of polyproteins in the replication of RNA viruses

2. Human immunodeficiency virus type-1 protease inhibitors therapeutic successes and failures, suppression and resistance

3. Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease

4. ABT-538 is a potent inhibitor of human immunodeficiency virus protease and has high oral bioavailability in humans.

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