Brief communicationEffects of H2O2 on protein tyrosine phosphatase activity in HER14 cells
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Analysis of protein phosphorylation sites in the hypothalamus tissues of pubescent goats
2022, Journal of ProteomicsRedox signaling in the pathogenesis of human disease and the regulatory role of autophagy
2020, International Review of Cell and Molecular BiologyCitation Excerpt :Intracellular O2− is readily converted to the non-radical product H2O2 by the action of the various superoxide dismutase (cytosolic Cu/ZnSOD and mitochondrial MnSOD). Hydrogen peroxide has a much longer lifespan and ability to diffuse through membranes and as such most of the secondary messenger function attributed to intracellular ROS is believed to be mediated by the oxidizing activity of H2O2, such as observed with the post-translational modification(s) of kinases (Akt/PKB, MAPK) and phosphatases (PTPase, PTEN) (Bae et al., 1997; Chiarugi, 2003; Denu and Dixon, 1998; Finkel, 2012; Heffetz et al., 1992; Lo and Cruz, 1995; Sullivan et al., 1994; Sundaresan et al., 1995; Ushio-Fukai et al., 2002). It is also noteworthy that a second critical factor in the overall readout of redox signaling is the involvement of reactive nitrogen species (RNS), in particular nitric oxide (NO), and more importantly its reactivity with O2− to generate peroxynitrite (OONO−), which has a better and more selective reactivity with biomolecules (Beckman and Koppenol, 1996).
Role of protein tyrosine phosphatase 1B in cardiovascular diseases
2016, Journal of Molecular and Cellular CardiologyHelmut Sies: A continuous presence in my scientific development
2016, Archives of Biochemistry and BiophysicsThe myeloperoxidase-derived oxidant hypothiocyanous acid inhibits protein tyrosine phosphatases via oxidation of key cysteine residues
2016, Free Radical Biology and MedicineCitation Excerpt :Oxidation can modulate these processes, and hence signaling, as both PTPs and kinases contain redox-sensitive amino acids, and particularly low pKa Cys residues [35,36]. H2O2, other peroxides present on amino acids and proteins, peroxynitrous acid, singlet oxygen and some MPO-derived oxidants, are all known to inactivate members of the PTP family [21,39–42]. For kinases, oxidation has been reported to result in either activation or inactivation depending on the enzyme and oxidant; this may occur either by Cys modification or alternative mechanisms [35,43].
A possible role for oxidation stress in lymphoid leukaemias and therapeutic failure
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