about
Ethylmalonic encephalopathy ETHE1 R163W/R163Q mutations alter protein stability and redox properties of the iron centre.Biophysical principles predict fitness landscapes of drug resistance.Reductive elimination of superoxide: Structure and mechanism of superoxide reductases.Purification, crystallization and X-ray crystallographic analysis of Archaeoglobus fulgidus neelaredoxin.Role of flavinylation in a mild variant of multiple acyl-CoA dehydrogenation deficiency: a molecular rationale for the effects of riboflavin supplementation.Mutations at the flavin binding site of ETF:QO yield a MADD-like severe phenotype in Drosophila.Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'.Free Superoxide is an Intermediate in the Production of H2O2 by Copper(I)-Aβ Peptide and O2.Correction to Rational Design of Novel Allosteric Dihydrofolate Reductase Inhibitors Showing Antibacterial Effects on Drug-Resistant Escherichia coli Escape Variants.Differential Enzyme Flexibility Probed Using Solid-State Nanopores.Kinetics of electron transfer from NADH to the Escherichia coli nitric oxide reductase flavorubredoxin.Mechanism of superoxide and hydrogen peroxide generation by human electron-transfer flavoprotein and pathological variants.Cofactors and metabolites as potential stabilizers of mitochondrial acyl-CoA dehydrogenasesStructural–functional evaluation of ionic liquid libraries for the design of co-solvents in lipase-catalysed reactionsProtein stability in an ionic liquid milieu: on the use of differential scanning fluorimetrySuperoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: comparison with neelaredoxinProteostasis Environment Shapes Higher-Order Epistasis Operating on Antibiotic Resistance.Superoxide reduction mechanism of Archaeoglobus fulgidus one-iron superoxide reductaseAdaptation to mutational inactivation of an essential gene converges to an accessible suboptimal fitness peakSimplified 2,4-dinitrophenylhydrazine spectrophotometric assay for quantification of carbonyls in oxidized proteinsChimeric dihydrofolate reductases display properties of modularity and biophysical diversity
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
João V Rodrigues
@es
João V Rodrigues
@nl
João V Rodrigues
@sl
João V. Rodrigues
@en
type
label
João V Rodrigues
@es
João V Rodrigues
@nl
João V Rodrigues
@sl
João V. Rodrigues
@en
prefLabel
João V Rodrigues
@es
João V Rodrigues
@nl
João V Rodrigues
@sl
João V. Rodrigues
@en
P106
P1153
8380828900
P21
P31
P496
0000-0002-5605-656X