Design, synthesis, and activity of conformationally-constrained macrocyclic peptide-based inhibitors of HIV protease
- 22 September 1994
- journal article
- Published by Elsevier in Bioorganic & Medicinal Chemistry Letters
- Vol. 4 (18) , 2217-2222
- https://doi.org/10.1016/s0960-894x(00)80074-8
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Rational Design of Potent, Bioavailable, Nonpeptide Cyclic Ureas as HIV Protease InhibitorsScience, 1994
- Present Status and Future Prospects for HIV TherapiesScience, 1993
- Intriguing structure-activity relations underlie the potent inhibition of HIV protease by norstatine-based peptidesJournal of Medicinal Chemistry, 1992
- Kynostatin (KNI-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine.CHEMICAL & PHARMACEUTICAL BULLETIN, 1992
- Inhibitors of HIV-1 ProteaseJournal of Enzyme Inhibition, 1992
- The design and synthesis of cyclic renin inhibitorsTetrahedron Letters, 1991
- HIV protease: a novel chemotherapeutic target for AIDSJournal of Medicinal Chemistry, 1991
- Structure-based, C2 symmetric inhibitors of HIV proteaseJournal of Medicinal Chemistry, 1990
- Potent human renin inhibitors containing novel small cyclic peptides and stable to chymotrypsin degradationJournal of the Chemical Society, Chemical Communications, 1990
- Renin inhibitors. Design and synthesis of a new class of conformationally restricted analogs of angiotensinogenJournal of Medicinal Chemistry, 1988