EC Number   |
Application |
Reference |
|---|
   3.4.23.47 | drug development |
HIV-2 protease is an important drug target |
754210 |
| 3.4.23.47 | medicine |
- |
644067 |
| 3.4.23.47 | medicine |
potential target for chemotherapy of virus infection and associated diseases, essential for maturation of infectious virions, development of drugs against the protease should be effective against HIV-2 |
644057, 644058, 644059, 644060, 644061, 644063, 644065 |
| 3.4.23.47 | medicine |
the HIV proteases are effective therapeutic targets for treating HIV infection because of the essential role in hydrolysing the viral Gag and Gag-Pol precursor polyprotein during infectious viral particle maturation |
755505 |
| 3.4.23.47 | medicine |
the poly(A)-binding protein is known to be cleaved by several picornaviruses and caliciviruses. The results indicate that retroviruses such as HIV share the capacity to proteolyse poly(A)-binding protein |
667530 |
| 3.4.23.47 | medicine |
the role of natural polymorphisms in the PR gene on the time to the development of resistance to proteinase inhibitors using an HIV-2 tissue culture model are examined. Natural polymorphisms in HIV-2 facilitate the selection of proteinase inhibitor resistance |
677596 |
| 3.4.23.47 | molecular biology |
an experimental model system based on the expression of HIV-2 protease in yeast cells is established: HIV-2 protease activity kills the yeast cell, this process can be abolished by inhibiting the viral enzyme activity |
682827 |
