amprenavir and urea
amprenavir has been researched along with urea in 4 studies
Research
Studies (4)
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Authors
| Authors | Studies |
|---|---|
| Barnes, JC; Bradley, P; Day, NC; Fourches, D; Reed, JZ; Tropsha, A | 1 |
| Bold, G; Capraro, HG; Goutte, G; Klimkait, T; Lazdins, JK; Mestan, J; Walker, MR | 1 |
| Aungst, BJ; Bulgarelli, JP; Nguyen, NH; Oates-Lenz, K | 1 |
| Bagossi, P; Boross, P; Copeland, TD; Fehér, A; Harrison, RW; Louis, JM; Mahalingam, B; Torshin, IY; Tözsér, J; Weber, IT | 1 |
Other Studies
4 other study(ies) available for amprenavir and urea
| Article | Year |
|---|---|
Cheminformatics analysis of assertions mined from literature that describe drug-induced liver injury in different species.
Topics: Animals; Chemical and Drug Induced Liver Injury; Cluster Analysis; Databases, Factual; Humans; MEDLINE; Mice; Models, Chemical; Molecular Conformation; Quantitative Structure-Activity Relationship | 2010 |
In vitro effect of alpha1-acid glycoprotein on the anti-human immunodeficiency virus (HIV) activity of the protease inhibitor CGP 61755: a comparative study with other relevant HIV protease inhibitors.
Topics: Anti-HIV Agents; Carbamates; Cell Line; Cells, Cultured; Ethylenes; Furans; HIV Protease Inhibitors; HIV Seronegativity; HIV-1; Humans; Indinavir; Kinetics; Lymphocytes; Orosomucoid; Ritonavir; Saquinavir; Sulfonamides; Urea; Virus Replication | 1997 |
The influence of donor and reservoir additives on Caco-2 permeability and secretory transport of HIV protease inhibitors and other lipophilic compounds.
Topics: Acetamides; Albumins; Azepines; Caco-2 Cells; Carbamates; Cell Membrane Permeability; Furans; HIV Protease Inhibitors; Humans; Indinavir; Intestinal Absorption; Nelfinavir; Ritonavir; Solvents; Structure-Activity Relationship; Sulfonamides; Urea | 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 |