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Inactivation of human myeloperoxidase by hydrogen peroxideLong-Term Effects of (-)-Epigallocatechin Gallate (EGCG) on Pristane-Induced Arthritis (PIA) in Female Dark Agouti RatsEssential Role of Proximal Histidine-Asparagine Interaction in Mammalian PeroxidasesStructural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium "Candidatus Nitrospira defluvii": identification of a catalytically important amino acid residueUnexpected Diversity of Chlorite Dismutases: a Catalytically Efficient Dimeric Enzyme from Nitrobacter winogradskyiHigh Conformational Stability of Secreted Eukaryotic Catalase-peroxidases: ANSWERS FROM FIRST CRYSTAL STRUCTURE AND UNFOLDING STUDIESManipulating Conserved Heme Cavity Residues of Chlorite Dismutase: Effect on Structure, Redox Chemistry, and ReactivityEukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide DismutationMechanism of reaction of myeloperoxidase with nitriteThe peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune systemIndependent evolution of four heme peroxidase superfamiliesMolecular evolution, structure, and function of peroxidasinsDimeric chlorite dismutase from the nitrogen-fixing cyanobacterium Cyanothece sp. PCC7425Redox thermodynamics of lactoperoxidase and eosinophil peroxidase.Expression and glycoengineering of functionally active heteromultimeric IgM in plants.Redox thermodynamics of high-spin and low-spin forms of chlorite dismutases with diverse subunit and oligomeric structures.Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate.Soluble CuA domain of cyanobacterial cytochrome c oxidase.Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.Active site structure and catalytic mechanisms of human peroxidases.Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties.Mechanisms of catalase activity of heme peroxidases.Interactions of hydrogen sulfide with myeloperoxidaseStructure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes.Evolution of catalases from bacteria to humans.Heme-copper oxidases and their electron donors in cyanobacterial respiratory electron transport.Occurrence, phylogeny, structure, and function of catalases and peroxidases in cyanobacteria.Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of apoB-100.Evolution of structure and function of Class I peroxidases.Molecular evolution of hydrogen peroxide degrading enzymesChlorite dismutases - a heme enzyme family for use in bioremediation and generation of molecular oxygen.Reaction of pyranose dehydrogenase from Agaricus meleagris with its carbohydrate substrates.Nucleotide sequence analysis, overexpression in Escherichia coli and kinetic characterization of Anacystis nidulans catalase-peroxidase.Dynamics of NF kappa B and Ikappa Balpha studied with green fluorescent protein (GFP) fusion proteins. Investigation of GFP-p65 binding to DNa by fluorescence resonance energy transfer.Proline is not uniquely capable of providing the pivot point for domain swapping in 2G12, a broadly neutralizing antibody against HIV-1.The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases.Mechanism of chlorite degradation to chloride and dioxygen by the enzyme chlorite dismutase.Two distinct groups of fungal catalase/peroxidases.Characterization of chemical features of potent myeloperoxidase inhibitors.Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Paul G Furtmüller
@nl
Paul G Furtmüller
@sl
Paul G. Furtmüller
@en
Paul G. Furtmüller
@es
type
label
Paul G Furtmüller
@nl
Paul G Furtmüller
@sl
Paul G. Furtmüller
@en
Paul G. Furtmüller
@es
prefLabel
Paul G Furtmüller
@nl
Paul G Furtmüller
@sl
Paul G. Furtmüller
@en
Paul G. Furtmüller
@es
P106
P1153
6603664473
P21
P31
P3835
paul-furtmller
P496
0000-0002-1199-2469