fadrozole has been researched along with furafylline in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 1 (25.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Birk, B; Grombein, CM; Hartmann, RW; Heim, R; Lucas, S; Müller-Vieira, U; Negri, M; Ries, C; Schewe, KE | 1 |
Antes, I; Bisi, A; Gobbi, S; Hartmann, RW; Heim, R; Lucas, S; Negri, M; Ries, C; Schewe, KE | 1 |
Birk, B; Hartmann, RW; Heim, R; Lucas, S; Ries, C; Schewe, KE | 1 |
Hartmann, RW; Heim, R; Lucas, S; Negri, M; Zimmer, C | 1 |
4 other study(ies) available for fadrozole and furafylline
Article | Year |
---|---|
Overcoming undesirable CYP1A2 inhibition of pyridylnaphthalene-type aldosterone synthase inhibitors: influence of heteroaryl derivatization on potency and selectivity.
Topics: Animals; Cytochrome P-450 CYP11B2; Cytochrome P-450 CYP1A2; Cytochrome P-450 CYP1A2 Inhibitors; Fibrosis; Heart Failure; Humans; Male; Myocardium; Naphthalenes; Rats; Rats, Wistar; Structure-Activity Relationship | 2008 |
Novel aldosterone synthase inhibitors with extended carbocyclic skeleton by a combined ligand-based and structure-based drug design approach.
Topics: Acids, Carbocyclic; Binding Sites; Computer Simulation; Crystallography, X-Ray; Cytochrome P-450 CYP11B2; Dose-Response Relationship, Drug; Drug Design; Humans; Ligands; Models, Chemical; Models, Molecular; Molecular Structure; Naphthalenes; Stereoisomerism; Structure-Activity Relationship | 2008 |
In vivo active aldosterone synthase inhibitors with improved selectivity: lead optimization providing a series of pyridine substituted 3,4-dihydro-1H-quinolin-2-one derivatives.
Topics: Animals; Carbon; Chemistry, Pharmaceutical; Cytochrome P-450 CYP11B2; Cytochrome P-450 CYP1A2; Drug Design; Enzyme Inhibitors; Humans; Inhibitory Concentration 50; Liver; Pyridines; Quinolones; Rats; Temperature; U937 Cells | 2008 |
Fine-tuning the selectivity of aldosterone synthase inhibitors: structure-activity and structure-selectivity insights from studies of heteroaryl substituted 1,2,5,6-tetrahydropyrrolo[3,2,1-ij]quinolin-4-one derivatives.
Topics: Animals; Cytochrome P-450 CYP11B2; Drug Design; Enzyme Inhibitors; Humans; Male; Models, Molecular; Protein Conformation; Quinolines; Rats; Rats, Wistar; Structure-Activity Relationship; Substrate Specificity | 2011 |