amprenavir and g 52
amprenavir has been researched along with g 52 in 3 studies
Research
Studies (3)
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 3 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Authors
| Authors | Studies |
|---|---|
| Agniswamy, J; Ghosh, AK; Louis, JM; Rao, KV; Sayer, JM; Shen, CH; Wang, YF; Weber, IT; Xu, CX | 1 |
| Agniswamy, J; Amano, M; Ghosh, AK; Martyr, CD; Mitsuya, H; Nyalapatla, PR; Osswald, HL; Parham, GL; Wang, YF; Weber, IT | 1 |
| Amano, M; Aoki, M; Campbell, JR; Das, D; Ghosh, AK; Mitsuya, H; Rao, KV; Salcedo-Gómez, PM; Tojo, Y; Xu, CX | 1 |
Other Studies
3 other study(ies) available for amprenavir and g 52
| Article | Year |
|---|---|
Extreme multidrug resistant HIV-1 protease with 20 mutations is resistant to novel protease inhibitors with P1'-pyrrolidinone or P2-tris-tetrahydrofuran.
Topics: Binding Sites; Calorimetry, Differential Scanning; Carbamates; Crystallization; Darunavir; Drug Resistance, Multiple; Drug Resistance, Viral; Escherichia coli; Furans; Genes, Synthetic; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Models, Molecular; Mutation; Pyrrolidinones; Structure-Activity Relationship; Sulfonamides | 2013 |
Highly potent HIV-1 protease inhibitors with novel tricyclic P2 ligands: design, synthesis, and protein-ligand X-ray studies.
Topics: Crystallography, X-Ray; HIV Protease; HIV Protease Inhibitors; Ligands; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Molecular | 2013 |
GRL-0519, a novel oxatricyclic ligand-containing nonpeptidic HIV-1 protease inhibitor (PI), potently suppresses replication of a wide spectrum of multi-PI-resistant HIV-1 variants in vitro.
Topics: Amino Acid Sequence; Atazanavir Sulfate; Binding Sites; Carbamates; Cell Line, Tumor; Darunavir; Drug Resistance, Viral; Furans; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Inhibitory Concentration 50; Lopinavir; Molecular Docking Simulation; Molecular Sequence Data; Oligopeptides; Protein Binding; Pyridines; Ritonavir; Structure-Activity Relationship; Sulfonamides; T-Lymphocytes; Virus Replication | 2013 |