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Biochemistry|March 8, 2006
Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidaseMario Cappiello, Vincenzo Alterio, Pietro Amodeo, et al.
Free Radical Biology & Medicine|February 15, 2015
NADP(+)-dependent dehydrogenase activity of carbonyl reductase on glutathionylhydroxynonanal as a new pathway for hydroxynonenal detoxificationRoberta Moschini, Eleonora Peroni, Rossella Rotondo, et al.
Molecules (Basel, Switzerland)|January 13, 2021
In Search for Multi-Target Ligands as Potential Agents for Diabetes Mellitus and Its Complications-A Structure-Activity Relationship Study on Inhibitors of Aldose Reductase and Protein Tyrosine Phosphatase 1BRosaria Ottanà, Paolo Paoli, Mario Cappiello, et al.
The Journal of Biological Chemistry|August 17, 2002
Oxidative modification of aldose reductase induced by copper ion. Definition of the metal-protein interaction mechanismIlaria Cecconi, Andrea Scaloni, Giulio Rastelli, et al.
European Journal of Medicinal Chemistry|May 3, 2011
Identification of 5-arylidene-4-thiazolidinone derivatives endowed with dual activity as aldose reductase inhibitors and antioxidant agents for the treatment of diabetic complicationsRosaria Ottanà, Rosanna Maccari, Marco Giglio, et al.
Antioxidants (Basel, Switzerland)|October 27, 2019
Stereoselectivity of Aldose Reductase in the Reduction of Glutathionyl-Hydroxynonanal AdductFrancesco Balestri, Vito Barracco, Giovanni Renzone, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry|February 9, 2019
Soyasaponins from Zolfino bean as aldose reductase differential inhibitorsFrancesco Balestri, Marinella De Leo, Carlo Sorce, et al.
Molecules (Basel, Switzerland)|February 9, 2018
Design, Synthesis and in Combo Antidiabetic Bioevaluation of Multitarget Phenylpropanoic AcidsBlanca Colín-Lozano, Samuel Estrada-Soto, Fabiola Chávez-Silva, et al.
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