FEBS Letters · 1989 · 28 citations · 5 references
Life SciencesBiochemistryMolecular BiologyEnzymologyMolecular VirologyVirologyEnzyme InhibitionEnzyme KineticsMichaelis-menten KineticsProtein Interaction KineticsProteolytic EnzymesAntiviral Mechanisms Of ActionAspartic ProteasesEnzyme Inhibition KineticsInhibition ConstantsViral Protease Inhibition
Kinetic constants were determined for the interaction of the HIV-2 aspartic proteinase with a synthetic substrate and a number of inhibitors at several pH values. Acetyl-pepstatin was more effective towards HIV-2 proteinase than the renin inhibitor, H-261; this effect is exactly the opposite from that observed previously for the proteinase from the HIV-1 AIDS virus.
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Genome organization and transactivation of the human immunodeficiency virus type 2
Mireille Guyader, Michael Emerman, P. Sonigo et al. · Nature · 1987 · 837 citations
Molecular Modeling of the HIV-1 Protease and Its Substrate Binding Site
Irene T. Weber, Maria Miller, Mariusz Jaskólski et al. · Science · 1989 · 170 citations