Abstract
The protease of HIV-1 is considered to be a prime target for the treatment of AIDS with small molecular weight inhibitors. 1,2,3 Many groups have now demonstrated that compounds designed as potent inhibitors of the enzyme in vitro are effective inhibitors of viral polyprotein processing and viral spread in cultured cells.4–7 Continued effort to discover new potent inhibitors with suitable properties for use in humans is thus justified.
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Darke, P.L. et al. (1991). Interaction of Mutant Forms of the HIV-1 Protease with Substrate and Inhibitors. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_61
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_61
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