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These protease inhibitors prevent viral replication by selectively binding to viral proteases (e.g. HIV-1 protease) and blocking proteolytic cleavage of protein precursors that are necessary for the production of infectious viral particles. Protease inhibitors that have been developed and are currently used in clinical practice include:
Protease inhibitors may be classified either by the type of protease they inhibit, or by their mechanism of action. In 2004 Rawlings and colleagues introduced a classification of protease inhibitors based on similarities detectable at the level of amino acid sequence. [ 4 ]
TPCK is an irreversible inhibitor of chymotrypsin. Also inhibits some cysteine proteases such as caspase, papain, bromelain or ficin. [1] It does not inhibit trypsin or zymogens. TPCK is observed covalently bound in the active site of Caspase 3 in the crystal structure of the complex solved in 2010. [2]
Pages in category "Protease inhibitors" The following 27 pages are in this category, out of 27 total. This list may not reflect recent changes. ...
Tipranavir is a nonpeptidic HIV-1 protease inhibitor [11] and reached the market in 2005. [18] Unlike other HIV protease inhibitors on the market, tipranavir was developed from a nonpeptidic coumarin template and its antiprotease activity was discovered by high-throughput screening. [23]
[11] [12] CLIP-CHIP™, developed by the Overall Lab, is a complete protease and inhibitor DNA microarray for all 1561 human and murine proteases, non-proteolytic homologues, and their inhibitors. [13] [14] [15] Both of these tools allow comparison of expression patterns between normal and diseased samples and tissues.