U
Umberto Mura
Researcher at University of Pisa
Publications - 111
Citations - 2094
Umberto Mura is an academic researcher from University of Pisa. The author has contributed to research in topics: Aldose reductase & Aldehyde Reductase. The author has an hindex of 25, co-authored 106 publications receiving 1912 citations. Previous affiliations of Umberto Mura include University of Somalia & University of Santiago de Compostela.
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Journal ArticleDOI
Synthesis, activity, and molecular modeling of a new series of tricyclic pyridazinones as selective aldose reductase inhibitors
Luca Costantino,Giulio Rastelli,K. Vescovini,Giorgio Cignarella,Paola Vianello,A Del Corso,Mario Cappiello,Umberto Mura,Daniela Barlocco +8 more
TL;DR: Three new series of tricyclic pyridazinones synthesized and tested in vitro give indications of specific interaction sites responsible for the binding of the ALR2-inhibitor complex, thus providing information for the design of new inhibitors with improved affinity for the enzyme.
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Identification of 5-arylidene-4-thiazolidinone derivatives endowed with dual activity as aldose reductase inhibitors and antioxidant agents for the treatment of diabetic complications
Rosaria Ottanà,Rosanna Maccari,Marco Giglio,Antonella Del Corso,Mario Cappiello,Umberto Mura,Sandro Cosconati,Luciana Marinelli,Ettore Novellino,Stefania Sartini,Concettina La Motta,Federico Da Settimo +11 more
TL;DR: Acetic acids 5, particularly 5a and 5h, proved to be interesting inhibitors of the enzyme as well as excellent antioxidant agents that are potentially able to counteract the oxidative stress associated with both diabetic complications and other pathologies.
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Specifically targeted modification of human aldose reductase by physiological disulfides
Mario Cappiello,Margaret Voltarelli,I Cecconi,Pier Giuseppe Vilardo,Massimo Dal Monte,I Marini,Antonella Del Corso,David K. Wilson,Florante A. Quiocho,J. Mark Petrash,Umberto Mura +10 more
TL;DR: Cystamine inactivated the wild-type enzyme as well as all three cysteine mutants, suggesting that cystamine-induced inactivation of aldose reductase does not involve modification of cysteines exclusively at position 80, 298, or 303.
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Oxidative modification of aldose reductase induced by copper ion. Definition of the metal-protein interaction mechanism.
I Cecconi,Andrea Scaloni,Giulio Rastelli,Maria Cristina Moroni,Pier Giuseppe Vilardo,Luca Costantino,Mario Cappiello,Donita Garland,Deborah Carper,J. Mark Petrash,Antonella Del Corso,Umberto Mura +11 more
TL;DR: The mechanism underlying the reversible modification of ALR2 was studied by mass spectrometry, circular dichroism, and molecular modeling approaches on the enzyme purified from bovine lens and on wild type and mutant recombinant forms of the human placental and rat lens ALR 2 as discussed by the authors.
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Structure-activity relationships and molecular modelling of new 5-arylidene-4-thiazolidinone derivatives as aldose reductase inhibitors and potential anti-inflammatory agents.
Rosanna Maccari,Rosa Maria Vitale,Rosaria Ottanà,Marco Rocchiccioli,Agostino Marrazzo,Venera Cardile,Adriana Carol Eleonora Graziano,Pietro Amodeo,Umberto Mura,Antonella Del Corso +9 more
TL;DR: Molecular docking and molecular dynamics simulations were undertaken to investigate the binding modes of selected compounds into the active site of AR in order to rationalize the inhibitory effectiveness of these derivatives.