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3.4.23.47
Analysis of the HIV-2 proteases adaptation to various ligands characterization of backbone asymmetry using a structural alphabet
Human immunodeficiency virus 2
3.4.23.47
Characterizing the structural variability of HIV-2 protease upon the binding of diverse ligands using a structural alphabet approach
Human immunodeficiency virus 2
3.4.23.47
Exploration of the effect of sequence variations located inside the binding pocket of HIV-1 and HIV-2 proteases
Human immunodeficiency virus 2
3.4.23.47
Exploring the reasons for decrease in binding affinity of HIV-2 against HIV-1 protease complex using interaction entropy under polarized force field
Human immunodeficiency virus 2
3.4.23.47
Four amino acid changes in HIV-2 protease confer class-wide sensitivity to protease inhibitors
Human immunodeficiency virus 2
3.4.23.47
Amino acid preferences for a critical substrate binding subsite of retroviral proteases in type 1 cleavage sites
Human immunodeficiency virus 2
3.4.23.47
Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag-Pol polyproteins
Human immunodeficiency virus 2
3.4.23.47
Comparison of the specificity of homo- and heterodimeric linked HIV-1 and HIV-2 proteinase dimers
Human immunodeficiency virus 2
3.4.23.47
Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors
Human immunodeficiency virus 2
3.4.23.47
Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases
Human immunodeficiency virus 2
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