EC Number   |
Inhibitors |
Structure |
|---|
   3.4.23.B2 | chymostatin |
- |
   |
| 3.4.23.B2 | H-Val-Ser-Gln-Asn-Leu-PSI[CH(OH)CH2]Val-Ile-Val-OH |
- |
|
| 3.4.23.B2 | more |
development of a more efficient irreversible inhibitor can be achieved by optimizing the interactions of the inhibitor with the protein while preserving the favorable reactivity and orientation of the epoxide moiety |
|
| 3.4.23.B2 | more |
fusion of HIV-2-Vpx with an enzymatically defective proteases mutant, PR. The Vpx-PR-mutant fusion protein, Vpx-PRM is expressed and packaged efficiently into simian immunodeficiency virus. VpxPRM specifically inhibits the function of the viral protease |
|
| 3.4.23.B2 | more |
to design inhibitors that are equally effective against HIV-1 and HIV-2, one must maintain a balance in the size of the side chains at P2, P1, P1', and P2' |
|
| 3.4.23.B2 | more |
several HIV-1 peptomimetic inhibitors also inhibit the SIV retropepsin, inhibitor binding structure |
|
| 3.4.23.B2 | more |
not inhibitory: HIV-protease inhibitors nelfinavir, saquinavir, darunavir |
|
| 3.4.23.B2 | pepstatin A |
- |
|
| 3.4.23.B2 | pepstatin A |
0.01-0.1 mM |
|
| 3.4.23.B2 | pepstatin A |
specific inhibition |
|
