Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
Author:
Affiliation:
1. Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, United States
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja2095766
Reference30 articles.
1. Active human immunodeficiency virus protease is required for viral infectivity.
2. HTLV-III gag Protein Is Processed in Yeast Cells by the Virus pol -Protease
3. A Major Role for a Set of Non-Active Site Mutations in the Development of HIV-1 Protease Drug Resistance
4. Multidrug Resistance to HIV-1 Protease Inhibition Requires Cooperative Coupling between Distal Mutations
5. Comparing the Accumulation of Active- and Nonactive-Site Mutations in the HIV-1 Protease
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