dmp 323 has been researched along with amprenavir in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 4 (66.67) | 18.2507 |
2000's | 2 (33.33) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Akamike, E; Cheatham, WW; Collins, RD; DeLucca, I; Hollis, AY; Lam, PY; Ru, Y; Wilkerson, WW | 1 |
Ala, P; Anton, ED; Bacheler, LT; Chang, CH; Garber, SS; Jadhav, PK; Woerner, FJ | 1 |
Cheatham, WW; Dax, S; Wilkerson, WW | 1 |
Anderson, PS; Bacheler, LT; Chang, CH; Cordova, B; Erickson-Viitanen, S; Garber, S; Johnson, BL; Klabe, RM; Ko, SS; Lam, PY; Li, R; Reid, C; Rodgers, JD; Ru, Y; Seitz, SP; Trainor, GL; Wang, H; Wright, MR | 1 |
Alewood, D; Alewood, PF; Bergman, DA; Birch, CJ; Fairlie, DP; Hu, SH; Jardine, DK; March, DR; Martin, JL; Passmore, M; Pattenden, LK; Reid, RC; Todd, B; Tyndall, JD; Tyssen, DP | 1 |
Bagossi, P; Boross, P; Copeland, TD; Fehér, A; Harrison, RW; Louis, JM; Mahalingam, B; Torshin, IY; Tözsér, J; Weber, IT | 1 |
6 other study(ies) available for dmp 323 and amprenavir
Article | Year |
---|---|
HIV protease inhibitory bis-benzamide cyclic ureas: a quantitative structure-activity relationship analysis.
Topics: Anti-HIV Agents; Benzamides; Chromatography, High Pressure Liquid; HIV Protease Inhibitors; HIV-1; Kinetics; RNA, Viral; Structure-Activity Relationship; Urea; Virus Replication | 1996 |
Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV.
Topics: Amides; Anti-HIV Agents; Cells, Cultured; Crystallography, X-Ray; Drug Resistance, Microbial; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Mutation; Protein Conformation; Sensitivity and Specificity; Urea | 1997 |
Nonsymmetrically substituted cyclic urea HIV protease inhibitors.
Topics: Anti-HIV Agents; HIV Protease Inhibitors; RNA, Viral; Structure-Activity Relationship; Urea | 1997 |
Design and selection of DMP 850 and DMP 851: the next generation of cyclic urea HIV protease inhibitors.
Topics: Animals; Anti-HIV Agents; Crystallography, X-Ray; Dogs; Drug Design; HIV; HIV Protease Inhibitors; Molecular Structure; Mutation; Protein Binding; Urea; Virus Replication | 1998 |
Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease.
Topics: Anti-HIV Agents; Cell Line; Crystallography, X-Ray; Heterocyclic Compounds; HIV Protease; HIV Protease Inhibitors; HIV-1; HIV-2; Humans; In Vitro Techniques; Leukocytes, Mononuclear; Models, Molecular; Molecular Mimicry; Peptides; Structure-Activity Relationship; Virus Replication | 2000 |
Effect of sequence polymorphism and drug resistance on two HIV-1 Gag processing sites.
Topics: Amino Acid Sequence; Amino Acid Substitution; Azepines; Binding Sites; Carbamates; Catalysis; Drug Resistance, Viral; Furans; Gene Products, gag; Genes, gag; HIV Protease; HIV Protease Inhibitors; HIV-1; Kinetics; Models, Molecular; Molecular Sequence Data; Oligopeptides; Polymorphism, Genetic; Protein Conformation; Substrate Specificity; Sulfonamides; Urea | 2002 |