HIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural Rearrangements-Reference-Cited by-同舟云学术

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

Published:2012-03-20 Issue:13 Volume:51 Page:2819-2828
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Agniswamy Johnson¹,Shen Chen-Hsiang¹,Aniana Annie²,Sayer Jane M.²,Louis John M.²,Weber Irene T.¹

Affiliation:

1. Department of Biology, Molecular Basis of Disease Program, Georgia State University, Atlanta, Georgia 30303, United States

2. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland 20892-0520, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi2018317

Reference51 articles.

1. Active human immunodeficiency virus protease is required for viral infectivity.

2. Development of Drug Resistance to HIV-1 Protease Inhibitors

3. Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection

4. Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors

5. Retracing the Evolutionary Pathways of Human Immunodeficiency Virus Type 1 Resistance to Protease Inhibitors: Virus Fitness in the Absence and in the Presence of Drug

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