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23M. Doi, T. Kimura, T. Ishida and Y. Kiso.
Rigid backbone moiety of KNI-272, a highly selective HIV protease inhibitor: methanol, acetone and dimethylsulfoxide solvated forms of 3-[3-benzyl-2-hydroxy-9-(isoquinolin-5-yloxy)-6-methylsulfanylmet
hyl-5,8-dioxo-4,7-diazanonanoyl]-N-tert-butyl-1,3-thiazolidine-4-carboxamide, Acta Cryst. (2004). B60, 433-437Â Â Â Â Design of small peptidomimetic HIV-1 protease inhibitors and prodrug forms, Letters in Peptide Science Developments in peptide synthesis and peptidomimetic chemistry: HIV protease analogs and substrate-based inhibitors, Peptide Science ? Present and Future Potent dipeptide HIV protease inhibitors containing the hydroxymethylcarbonyl isostere as an ideal transition-state mimetic, Peptides Frontiers of Peptide Science Structure of HIV-1 Protease with KNI-272: A Transition State mimetic Inhibitor Containing Allophenylnorstatine, Aspartic Proteinases Design and Synthesis of HIV Protease Inhibitors Containing Allophenylnorstatine as a Transition-State Mimic, Aspartic Proteinases ?O, N-Acyl migration?-type prodrugs of dipeptide HIV protease inhibitors, Peptides Frontiers of Peptide Science Allophenylnorstatine containing HIV-1 protease inhibitors: design, synthesis and structure-activity relationships for selected P2 ligands, Peptide Science ? Present and Future KNI-764, A novel dipeptide-based HIV protease inhibitor containing allophenylnorstatine, Peptide Science ? Present and Future K, AIDS Taschenw??rterbuch