(Q27636175)

1

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Michael Scheiwein

2

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Catharina C Bohme

3

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Gavin E Arteel

4

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P Andrew Karplus

5

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R Heiner Schirmer

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

25 January 2002

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published in

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volume

277

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issue

4

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page(s)

2779-84

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cites work

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Helicobacter pylori urease suppresses bactericidal activity of peroxynitrite via carbon dioxide production

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High plasma levels of nitrogen oxides are associated with severe disease and correlate with rapid parasitological and clinical cure in Plasmodium falciparum malaria.

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Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme

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Tyrosine modification by reactive nitrogen species: a closer look

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Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: Lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide

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Peroxynitrite activates the phosphoinositide 3-kinase/Akt pathway in human skin primary fibroblasts

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Immunolocalization of glutathione reductase in the murine brain.

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Glutathione, oxidative stress and neurodegeneration

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Peroxynitrite plays a role in methamphetamine-induced dopaminergic neurotoxicity: evidence from mice lacking neuronal nitric oxide synthase gene or overexpressing copper-zinc superoxide dismutase

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Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species

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Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation

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Erratum: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

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Amperometric ultramicrosensors for peroxynitrite detection and its application toward single myocardial cells

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Inactivation of antioxidant enzymes by peroxynitrite

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Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues

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Disulfide-Reductase Inhibitors as Chemotherapeutic Agents: The Design of Drugs for Trypanosomiasis and Malaria

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Peroxynitrite modification of glutathione reductase: modeling studies and kinetic evidence suggest the modification of tyrosines at the glutathione disulfide binding site

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Oxidative chemistry of peroxynitrite

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Role of active site tyrosine residues in catalysis by human glutathione reductase

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Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite

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Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide

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Factors determining the selectivity of protein tyrosine nitration

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Nitration of internal tyrosine of cytochromec probed by resonance Raman scattering

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Charge is the major discriminating factor for glutathione reductase versus trypanothione reductase inhibitors

21 January 2018

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A novel procedure for generating both nitric oxide and superoxide in situ from chemical sources at any chosen mole ratio. First application: tyrosine oxidation and a comparison with preformed peroxynitrite

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