Structural and Thermodynamic Basis of Amprenavir/Darunavir and Atazanavir Resistance in HIV-1 Protease with Mutations at Residue 50-Reference-Cited by-同舟云学术

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Structural and Thermodynamic Basis of Amprenavir/Darunavir and Atazanavir Resistance in HIV-1 Protease with Mutations at Residue 50

Published:2013-01-30 Issue:8 Volume:87 Page:4176-4184
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:Journal of Virology

Author:

Mittal S.,Bandaranayake R. M.,King N. M.,Prabu-Jeyabalan M.,Nalam M. N. L.,Nalivaika E. A.,Kurt Yilmaz N.,Schiffer C. A.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference42 articles.

1. The HIV-1 protease as a therapeutic target for AIDS;Debouck;AIDS Res. Hum. Retroviruses,1992

2. In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors;Condra;Nature,1995

3. In vivo selection of HIV-1 variants with reduced susceptibility to the protease inhibitor L-735,524 and related compounds;Emini;Adv. Exp. Med. Biol.,1996

4. Drug-resistance patterns of saquinavir and other HIV proteinase inhibitors;Roberts;AIDS,1995

5. Predicting human immunodeficiency virus protease cleavage sites in proteins by a discriminant function method;Chou;Proteins,1996

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4. In silico evaluation of atazanavir as a potential HIV main protease inhibitor and its comparison with new designed analogs;Computers in Biology and Medicine;2022-06

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