about
Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): structural and computational studyStructural 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 intrSynthesis, characterization and antioxidant activity of water soluble MnIII complexes of sulphonato-substituted Schiff base ligands.Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.Protein dynamics and ligand migration interplay as studied by computer simulation.Mechanism of the Reaction of Human Manganese Superoxide Dismutase with Peroxynitrite: Nitration of Critical Tyrosine 34.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Shaping substrate selectivity in a broad spectrum metallo-β-lactamase.Tuning the MnII2/MnIII2 redox cycle of a phenoxo-bridged diMn catalase mimic with terminal carboxylate donors.Synthesis, characterization and activity of imidazolate-bridged and Schiff-base dinuclear complexes as models of Cu,Zn-SOD. A comparative study.dsRNA-protein interactions studied by molecular dynamics techniques. Unravelling dsRNA recognition by DCL1.Synthesis, structure and catalase-like activity of dimanganese(III) complexes of 1,5-bis(X-salicylidenamino)pentan-3-ol (X = 3- and 5-methyl). Influence of phenyl-ring substituents on catalytic activityExploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitrationHuman Mn-superoxide dismutase inactivation by peroxynitrite: a paradigm of metal-catalyzed tyrosine nitration in vitro and in vivoStudy of the role of Mg2+ in dsRNA processing mechanism by bacterial RNase III through QM/MM simulations
P50
Q27675520-98E91FC7-0AB8-4256-B9F2-6E473B5D1E99Q27682069-DFAE7EE9-0B4A-40AC-A5BD-0FA9A6EB9725Q33529340-A16DB088-6ABC-4D70-8280-F29DAB72008EQ37287914-C1AC77FF-DE87-40BF-ADF1-712C785F05F4Q37783384-A9064778-24B7-432D-A1BF-420568FAF243Q39734660-D12CBF21-C040-44FF-BBA8-9E64F5F1FF29Q40040050-BBD9F2FD-0ACA-4546-8A5B-C3161016D32CQ49874620-70340D10-6A49-48F9-870D-F6111591F476Q50058876-2D61BF14-C89A-4DCB-8964-5A70B5458248Q52841456-5BACC325-C086-4C5D-BC82-CF364BC38E6EQ52880156-D7EE22F9-8E1E-4147-A59B-B8C112C3166FQ79320329-14701F1B-6091-4A5D-AD6B-439A7AFFE11CQ82936138-5557AE84-F364-4F79-B27E-0BD1D3DBBBB8Q88600849-0E779A41-156B-41B8-95FA-B8ADBD1CCD29Q91389238-DE19E46F-FDC7-4989-8BB4-5B4761390618
P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0001-5493-8537
@en
name
Diego M Moreno
@ast
Diego M Moreno
@en
Diego M Moreno
@es
Diego M Moreno
@nl
type
label
Diego M Moreno
@ast
Diego M Moreno
@en
Diego M Moreno
@es
Diego M Moreno
@nl
prefLabel
Diego M Moreno
@ast
Diego M Moreno
@en
Diego M Moreno
@es
Diego M Moreno
@nl
P106
P1153
55418218200
P21
P31
P496
0000-0001-5493-8537