Structure-activity relationships for macrocyclic peptidomimetic inhibitors of HIV-1 protease
- 1 November 1996
- journal article
- Published by Elsevier in Bioorganic & Medicinal Chemistry Letters
- Vol. 6 (21) , 2531-2536
- https://doi.org/10.1016/0960-894x(96)00468-4
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- A Novel Bicyclic Enzyme Inhibitor as a Consensus Peptidomimetic for the Receptor-Bound Conformations of 12 Peptidic Inhibitors of HIV-1 ProteaseJournal of the American Chemical Society, 1996
- Regioselective structural and functional mimicry of peptides. Design of hydrolytically-stable cyclic peptidomimetic inhibitors of HIV-1 protease.Journal of the American Chemical Society, 1995
- Targeting HIV-1 protease: A test of drug-design methodologiesTrends in Pharmacological Sciences, 1995
- Design, Synthesis, and Conformational Analysis of a Novel Macrocyclic HIV-Protease InhibitorJournal of Medicinal Chemistry, 1994
- Design, synthesis, and activity of conformationally-constrained macrocyclic peptide-based inhibitors of HIV proteaseBioorganic & Medicinal Chemistry Letters, 1994
- HIV Protease as an Inhibitor Target for the Treatment of AIDSPublished by Elsevier ,1994
- STRUCTURE-BASED INHIBITORS OF HIV-1 PROTEASEAnnual Review of Biochemistry, 1993
- HIV proteinase inhibitorsBiochemical Society Transactions, 1992
- Effect of hydroxyl group configuration in hydroxyethylamine dipeptide isosteres on HIV protease inhibition. Evidence for multiple binding modesJournal of Medicinal Chemistry, 1991