EC Number   |
Inhibitors |
Structure  |
|---|
   3.4.23.16 | more |
design of tight-binding human immunodeficiency virus type 1 protease inhibitors |
 |
| 3.4.23.16 | more |
oxim derivatives containing halogenomethylketone and phenyl moieties are specific HIV-1 protease inhibitors |
|
| 3.4.23.16 | more |
RVL-(reduced peptide bond)-FEA-Nle-NH2 and Ac-TI-Nle-(reduced peptide bond)-Nle-QR-NH2 |
|
| 3.4.23.16 | more |
design of hydrolytically-stable cyclic peptidomimetic inhibitors of HIV-1 protease |
|
| 3.4.23.16 | more |
substrate-based cyclic peptidomimetics of Phe-Ile-Val that inhibit HIV-1 protease using a novel enzyme-binding mode |
|
| 3.4.23.16 | more |
active site inhibitor binding structure analysis, overview |
|
| 3.4.23.16 | more |
synthesis of diverse prodrugs of the water-soluble dipeptide-type HIV-1 protease inhibitors KNI-727, KNI-272, and KNI-279 by O to N acyl migration, and analysis of the water-solubility and stability of the prodrugs, overview |
|
| 3.4.23.16 | more |
molecular basis for substrate recognition and drug resistance, structure analysis of substrate analogue inhibitors bound to wild-type enzyme, mutant V82A enzyme, and mutant I84V enzyme, overview |
|
| 3.4.23.16 | more |
design of enzyme inhibitors active on multidrug-resistant virus, overview |
|
| 3.4.23.16 | more |
inhibition analysis with eight clinically used protease inhibitors reveales that the natural polymorphisms found in subtype C protease, in combination with drug resistance mutations, can influence enzymatic catalytic efficiency and inhibitor resistance |
|
