Design, synthesis, and characterization of dipeptide isostere containing cis-epoxide for the irreversible inactivation of HIV protease
- 19 March 1996
- journal article
- Published by Elsevier in Bioorganic & Medicinal Chemistry Letters
- Vol. 6 (6) , 589-594
- https://doi.org/10.1016/0960-894x(96)00087-x
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Inactivation of HIV-1 protease by a tripeptidyl epoxideBioorganic & Medicinal Chemistry Letters, 1992
- Two-step binding mechanism for HIV protease inhibitorsBiochemistry, 1992
- Human immunodeficiency virus-1 protease. 1. Initial velocity studies and kinetic characterization of reaction intermediates by oxygen-18 isotope exchangeBiochemistry, 1991
- Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanismBiochemistry, 1991
- Structure-based, C2 symmetric inhibitors of HIV proteaseJournal of Medicinal Chemistry, 1990
- The Structure and Function of the Aspartic ProteinasesAnnual Review of Biophysics, 1990
- Rational Design of Peptide-Based HIV Proteinase InhibitorsScience, 1990
- In vitro inhibition of HIV‐1 proteinase by ceruleninFEBS Letters, 1990
- Pepstatin-derived inhibitors of aspartic proteinases. A close look at an apparent transition-state analog inhibitorJournal of Medicinal Chemistry, 1985
- Suicide substrates: mechanism-based enzyme inactivatorsTetrahedron, 1982