Defective Hydrophobic Sliding Mechanism and Active Site Expansion in HIV-1 Protease Drug Resistant Variant Gly48Thr/Leu89Met: Mechanisms for the Loss of Saquinavir Binding Potency-Reference-Cited by-同舟云学术

Defective Hydrophobic Sliding Mechanism and Active Site Expansion in HIV-1 Protease Drug Resistant Variant Gly48Thr/Leu89Met: Mechanisms for the Loss of Saquinavir Binding Potency

Published:2015-01-07 Issue:2 Volume:54 Page:422-433
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Goldfarb Nathan E.¹,Ohanessian Meray¹,Biswas Shyamasri¹,McGee T. Dwight¹,Mahon Brian P.¹,Ostrov David A.¹,Garcia Jose¹,Tang Yan¹,McKenna Robert¹,Roitberg Adrian¹,Dunn Ben M.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, ‡Department of Chemistry, and §Departments of Pathology, Immunology, and Laboratory Medicine, University of Florida, Gainesville, Florida 32601-0245, United States

Funder

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi501088e

Reference70 articles.

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3. HIV Inhibitors: Problems and Reality

4. A Controlled Trial of Two Nucleoside Analogues plus Indinavir in Persons with Human Immunodeficiency Virus Infection and CD4 Cell Counts of 200 per Cubic Millimeter or Less

5. In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors

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