D
Diego M. Moreno
Researcher at National University of Rosario
Publications - 35
Citations - 705
Diego M. Moreno is an academic researcher from National University of Rosario. The author has contributed to research in topics: Active site & Ligand (biochemistry). The author has an hindex of 13, co-authored 29 publications receiving 565 citations. Previous affiliations of Diego M. Moreno include National Scientific and Technical Research Council & Facultad de Ciencias Exactas y Naturales.
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Journal ArticleDOI
A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
María-Natalia Lisa,Antonela Rocio Palacios,Mahesh Aitha,Mariano M. González,Diego M. Moreno,Michael W. Crowder,Robert A. Bonomo,James Spencer,David L. Tierney,Leticia I. Llarrull,Alejandro J. Vila +10 more
TL;DR: It is shown that different MβLs share the same reaction mechanism, suggesting new strategies for drug design and open avenues for rationally designed inhibitors of all M βLs, notwithstanding the profound differences between these enzymes’ active site structure, β-lactam specificity and metal content.
Journal ArticleDOI
Parallel derivation of isogenic human primed and naive induced pluripotent stem cells
Stéphanie Kilens,Dimitri Meistermann,Diego M. Moreno,Caroline Chariau,Anne Gaignerie,Arnaud Reignier,Yohann Lelièvre,Miguel Casanova,Céline Vallot,Steven Nedellec,Léa Flippe,Julie Firmin,Juan Song,Eric Charpentier,Jenna Lammers,Audrey Donnart,Nadège Marec,Wallid Deb,Audrey Bihouée,Cédric Le Caignec,Claire Pecqueur,Richard Redon,Paul Barrière,Jérémie Bourdon,Vincent Pasque,Magali Soumillon,Tarjei S. Mikkelsen,Claire Rougeulle,Thomas Fréour,Laurent David +29 more
TL;DR: A method to generate naive hiPSCs directly from somatic cells, using OKMS overexpression and specific culture conditions, further enabling parallel generation of their isogenic primed counterparts and confirming the similarity of naiveHiPSCs to their in vivo counterparts.
Journal ArticleDOI
Synthesis, characterization and antioxidant activity of water soluble MnIII complexes of sulphonato-substituted Schiff base ligands.
Diego M. Moreno,Verónica Daier,Claudia Palopoli,Jean Pierre Tuchagues,Jean Pierre Tuchagues,Sandra Signorella +5 more
TL;DR: Two new Mn(III) complexes prepared and characterized show dual superoxide dismutase/catalase activity that renders these compounds particularly attractive as catalytic antioxidants.
Journal ArticleDOI
Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma cruzi iron-superoxide dismutases (Fe-SODs) A and B: disparate susceptibilities due to the repair of Tyr35 radical by Cys83 in Fe-SODB through intramolecular electron transfer
Alejandra Martínez,Gonzalo Peluffo,Ariel Alcides Petruk,Ariel Alcides Petruk,Martín Hugo,Dolores Piñeyro,Dolores Piñeyro,Verónica Demicheli,Diego M. Moreno,Analía Lima,Carlos Batthyány,Carlos Batthyány,Rosario Durán,Carlos Robello,Carlos Robello,Marcelo A. Martí,Nicole Larrieux,Alejandro Buschiazzo,Madia Trujillo,Rafael Radi,Lucía Piacenza +20 more
TL;DR: Mass spectrometry analysis indicating that peroxynitrite-mediated inactivation of T. cruzi Fe-SODs is due to the site-specific nitration of the critical and universally conserved Tyr35 prevents enzyme nitration and inactivation.
Journal ArticleDOI
Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration.
Diego M. Moreno,Marcelo A. Martí,Pablo M. De Biase,Darío A. Estrin,Verónica Demicheli,Rafael Radi,Leonardo Boechi +6 more
TL;DR: The results for the WT and selected mutant proteins confirm that the phenolic moiety of Y34 plays a key role in assisting superoxide migration, and suggests that 3-nitrotyrosine increases drastically the energetic barrier for ligand entry due to the absence of the proton.