2008
DOI: 10.1002/ardp.200700267
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Design of Potent Aspartic Protease Inhibitors to Treat Various Diseases

Abstract: In this retrospective, personal review covering our research from the late 1980s until 2007, we outline nearly two-decade worth of our own work on several aspartic protease inhibitors including those affecting renin, HIV-1 protease, plasmepsins, b-secretase, and HTLV-I protease and we report on aspartic protease inhibitors as potential drugs to treat hypertension, AIDS, malaria, Alzheimer's disease and adult T-cell leukemia, HTLV-I associated myelopathy / tropical spastic paraparesis, and various, respectively… Show more

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Cited by 66 publications
(39 citation statements)
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“…This study examines the PScatalyzed folding of pepsin, which serves as a model for understanding the nature of folding/unfolding barriers and the folding mechanism of related APs and proteases from other families. Using what is known about structure-function relationships could provide further critical information in the development of APs as targets in pharmaceutical intervention in human diseases such as hypertension (renin), breast cancer (cathepsin D), Alzheimer disease (beta-secretase), AIDS (HIV protease), and malaria (plasmepsins) (17,18).…”
mentioning
confidence: 99%
“…This study examines the PScatalyzed folding of pepsin, which serves as a model for understanding the nature of folding/unfolding barriers and the folding mechanism of related APs and proteases from other families. Using what is known about structure-function relationships could provide further critical information in the development of APs as targets in pharmaceutical intervention in human diseases such as hypertension (renin), breast cancer (cathepsin D), Alzheimer disease (beta-secretase), AIDS (HIV protease), and malaria (plasmepsins) (17,18).…”
mentioning
confidence: 99%
“…Currently, the main approach has been to obtain good inhibitors of the target protease, in the belief that inhibition of the activity will be therapeutic. In this context, our research group has published some works that corroborate this premise [1][2][3][4][5][6]10,[29][30][31][32][33][34][35][36][37][38][39] .…”
Section: Tripeptidyl Peptidases Dipeptidyl Peptidasesmentioning
confidence: 97%
“…Aspartic peptidases are characteristically inhibited by the microbial peptide pepstatin A (Fig. 13.6), which contains the .5 Catalytic mechanism of aspartic-type peptidases proposed by Nguyen et al (2008). A water molecule tightly bond to the aspartates in the native enzyme is proposed to nucleophilically attack the scissile bond carbonyl.…”
Section: Proteolytic Enzymes and Proteolytic Inhibitorsmentioning
confidence: 99%