about
Identification of mutant Asp251Gly/Gln307His of cytochrome P450 BM3 for the generation of metabolites of diclofenac, ibuprofen and tolbutamide.Site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in CaHydA [FeFe]-hydrogenase.Hydroxylation of non-substituted polycyclic aromatic hydrocarbons by cytochrome P450 BM3 engineered by directed evolution.Human aromatase: perspectives in biochemistry and biotechnology.Catalytic properties of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13 immobilized on nanosponges.Structural roles of the active site iron(III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13.Engineering Macaca fascicularis cytochrome P450 2C20 to reduce animal testing for new drugs.Effects of surface hydrophobicity on the catalytic iron ion retention in the active site of two catechol 1,2-dioxygenase isoenzymes.Engineering heme binding sites in monomeric rop.Protein and electrode engineering for the covalent immobilization of P450 BMP on gold.Toward reduction in animal sacrifice for drugs: molecular modeling of Macaca fascicularis P450 2C20 for virtual screening of Homo sapiens P450 2C8 substrates.Direct spectroscopic evidence for binding of anastrozole to the iron heme of human aromatase. Peering into the mechanism of aromatase inhibitionInfluence of inter-domain dynamics and surrounding environment flexibility on the direct electrochemistry and electrocatalysis of self-sufficient cytochrome P450 3A4-BMR chimerasDrug–drug interactions and cooperative effects detected in electrochemically driven human cytochrome P450 3A4Fluorescence detection of ligand binding to labeled cytochrome P450BM3Activation of RSK by phosphomimetic substitution in the activation loop is prevented by structural constraintsPeroxide-driven catalysis of the heme domain of A. radioresistens cytochrome P450 116B5 for sustainable aromatic rings oxidation and drug metabolites production
P50
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P50
description
researcher ORCID: 0000-0002-4169-2635
@en
wetenschapper
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name
Giovanna Di Nardo
@ast
Giovanna Di Nardo
@en
Giovanna Di Nardo
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Giovanna Di Nardo
@nl
Giovanna Di Nardo
@sl
type
label
Giovanna Di Nardo
@ast
Giovanna Di Nardo
@en
Giovanna Di Nardo
@es
Giovanna Di Nardo
@nl
Giovanna Di Nardo
@sl
prefLabel
Giovanna Di Nardo
@ast
Giovanna Di Nardo
@en
Giovanna Di Nardo
@es
Giovanna Di Nardo
@nl
Giovanna Di Nardo
@sl
P106
P21
P31
P496
0000-0002-4169-2635