3.4.23.47: HIV-2 retropepsin
This is an abbreviated version!
For detailed information about HIV-2 retropepsin, go to the full flat file.
Word Map on EC 3.4.23.47
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3.4.23.47
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polyproteins
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antiretroviral
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medicine
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darunavir
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saquinavir
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amprenavir
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lopinavir
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myeloblastosis
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nelfinavir
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hiv-2-infected
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drv
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drug development
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molecular biology
- 3.4.23.47
- polyproteins
-
antiretroviral
- medicine
- darunavir
- saquinavir
- amprenavir
- lopinavir
-
myeloblastosis
- nelfinavir
-
hiv-2-infected
- drv
- drug development
- molecular biology
Reaction
Endopeptidase for which the P1 residue is preferably hydrophobic =
Synonyms
HIV-2 protease, HIV-2 proteinase, human immunodeficiency virus 2 retropepsin, More, PR, PR2, retroviral aspartic proteinase, retroviral proteinase
ECTree
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Application
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drug development
HIV-2 protease is an important drug target
medicine
molecular biology
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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
medicine
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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
medicine
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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
medicine
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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
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