minalrestat has been researched along with carbostyril in 3 studies
Studies (minalrestat) | Trials (minalrestat) | Recent Studies (post-2010) (minalrestat) | Studies (carbostyril) | Trials (carbostyril) | Recent Studies (post-2010) (carbostyril) |
---|---|---|---|---|---|
9 | 0 | 1 | 12,855 | 1,323 | 5,611 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Akamine, EH; Carvalho, MH; de Cássia Tostes, R; Fortes, ZB; Hohman, TC; Nigro, D | 1 |
Darmanin, C; El-Kabbani, O; Hazemann, I; Joachimiak, A; Mitschler, A; Oka, M; Podjarny, A; Ruiz, F; Schneider, TR; Schulze-Briese, C; Tomizaki, T | 1 |
Carbone, V; Chung, R; El-Kabbani, O; Endo, S; Hara, A; Zhao, HT | 1 |
3 other study(ies) available for minalrestat and carbostyril
Article | Year |
---|---|
Minalrestat, an aldose reductase inhibitor, corrects the impaired microvascular reactivity in diabetes.
Topics: Aldehyde Reductase; Animals; Diabetes Mellitus, Experimental; Disease Models, Animal; Drug Interactions; Galactosemias; Imides; Male; Quinolones; Rats; Rats, Wistar; Splanchnic Circulation; Vasoconstrictor Agents | 2003 |
Ultrahigh resolution drug design. II. Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat: implications for the binding of cyclic imide inhibitors.
Topics: Aldehyde Reductase; Binding Sites; Crystallography, X-Ray; Drug Design; Enzyme Inhibitors; Holoenzymes; Imidazoles; Imidazolidines; Imides; Macromolecular Substances; Models, Molecular; Molecular Structure; Quinolones | 2004 |
Correlation of binding constants and molecular modelling of inhibitors in the active sites of aldose reductase and aldehyde reductase.
Topics: Aldehyde Reductase; Animals; Catalytic Domain; Chlorobenzoates; Computer Simulation; Crystallography, X-Ray; Enzyme Inhibitors; Humans; Imides; Inhibitory Concentration 50; Kinetics; Models, Molecular; Naphthalenes; Quercetin; Quinolones; Recombinant Proteins; Salicylates; Structure-Activity Relationship; Swine; Thermodynamics | 2009 |