- Kinetics of reaction of nitrogen dioxide with dihydrorhodamine and the reaction of the dihydrorhodamine radical with oxygen: Implications for quantifying peroxynitrite formation in cells
[作者:Folkes, LK; Patel, KB; Wardman, P; Wrona, M,期刊:Archives of Biochemistry and Biophysics , 页码:122-126 , 文章类型: Article,,卷期:2009年484-2]
- Dihydrorhodamine 123 (RhH2) has been used to detect 'reactive nitrogen species', including peroxynitrite and its radical decomposition products, peroxynitrite probably oxidizing RhH2 to rhodamine (Rh) via radical product...
- Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase
[作者:Vaz, SM; Prado, FM; Di Mascio, P; Augusto, O,期刊:Archives of Biochemistry and Biophysics , 页码:127-133 , 文章类型: Article,,卷期:2009年484-2]
- In spite of the many studies on protein modifications by reactive species, knowledge about the products resulting from the oxidation of protein-aromatic residues, including protein-derived radicals and their stable produ...
- The effect of neighboring methionine residue on tyrosine nitration and oxidation in peptides treated with MPO, H2O2, and NO2- or peroxynitrite and bicarbonate: Role of intramolecular electron transfer mechanism?
[作者:Zhang, H; Zielonka, J; Sikora, A; Joseph, J; Xu, YK; Kalyanaraman, B,期刊:Archives of Biochemistry and Biophysics , 页码:134-145 , 文章类型: Article,,卷期:2009年484-2]
- Recent reports suggest that intramolecular electron transfer reactions can profoundly affect the site and specificity of tyrosyl nitration and oxidation in peptides and proteins. Here we investigated the effects of methi...
- The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2
[作者:Manta, B; Hugo, M; Ortiz, C; Ferrer-Sueta, G; Trujillo, M; Denicola, A,期刊:Archives of Biochemistry and Biophysics , 页码:146-154 , 文章类型: Article,,卷期:2009年484-2]
- Peroxiredoxin 2 (Prx2) is a 2-Cys peroxiredoxin extremely abundant in the erythrocyte. The peroxidase activity was studied in a steady-state approach yielding an apparent K-M of 2.4 mu M for human thioredoxin and a very ...
- Inactivation of rabbit muscle glycogen phosphorylase b by peroxynitrite revisited: Does the nitration of Tyr(613) in the allosteric inhibition site control enzymatic function?
[作者:Sharov, VS; Galeva, NA; Dremina, ES; Williams, TD; Schoneich, C,期刊:Archives of Biochemistry and Biophysics , 页码:155-166 , 文章类型: Article,,卷期:2009年484-2]
- There is increasing evidence that sequence-specific formation of 3-nitrotyrosine (3-NT) may cause functional changes in target proteins. Recently, the nitration of Tyr residues in glycogen phosphorylase b (Phb) was impli...
- Peroxynitrite signaling in human erythrocytes: Synergistic role of hemoglobin oxidation and band 3 tyrosine phosphorylation
[作者:Metere, A; Iorio, E; Pietraforte, D; Podo, F; Minetti, M,期刊:Archives of Biochemistry and Biophysics , 页码:173-182 , 文章类型: Article,,卷期:2009年484-2]
- Peroxynitrite crosses the red blood cell (RBC) membrane and reacts with hemoglobin (Hb) producing mainly metHb, which is reduced back to ferrousHb by NADH- and NADPH-dependent reductases. Peroxynitrite also induces band ...
- Nitric oxide and airway epithelial barrier function: Regulation of tight junction proteins and epithelial permeability
[作者:Olson, N; Greul, AK; Hristova, M; Bove, PF; Kasahara, DI; van der Vliet, A,期刊:Archives of Biochemistry and Biophysics , 页码:205-213 , 文章类型: Article,,卷期:2009年484-2]
- Acute airway inflammation is associated with enhanced production of nitric oxide (NO center dot) and altered airway epithelial barrier function, suggesting a role of NO center dot or its metabolites in epithelial permeab...
- Glucose-modulated tyrosine nitration in beta cells: Targets and consequences
[作者:Koeck, T; Corbett, JA; Crabb, JW; Stuehr, DJ; Aulak, KS,期刊:Archives of Biochemistry and Biophysics , 页码:221-231 , 文章类型: Article,,卷期:2009年484-2]
- Hyperglycemia, key factor of the pre-diabetic and diabetic pathology, is associated with cellular oxidative stress that promotes oxidative Protein modifications. We report that protein nitration is responsive to changes ...
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