Redox regulation of protein kinases

References

• Abe J, Takahashi M, Ishida M, et al. (1997). c-Src is required for oxidative stress-mediated activation of big mitogen-activated protein kinase 1. J Biol Chem 272:20389–94
   PubMed Web of Science ®Google Scholar
• Abid MR, Kachra Z, Spokes KC, Aird WC. (2000). NADPH oxidase activity is required for endothelial cell proliferation and migration. FEBS Lett 486:252–6
   PubMed Web of Science ®Google Scholar
• Abid MR, Spokes KC, Shih SC, Aird WC. (2007). NADPH oxidase activity selectively modulates vascular endothelial growth factor signaling pathways. J Biol Chem 282:35373–85
   PubMed Web of Science ®Google Scholar
• Akhand AA, Pu M, Senga T, et al. (1999). Nitric oxide controls src kinase activity through a sulfhydryl group modification-mediated Tyr-527-independent and Tyr-416-linked mechanism. J Biol Chem 274:25821–6
   PubMed Web of Science ®Google Scholar
• Anastasiou D, Poulogiannis G, Asara JM, et al. (2011). Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science 334:1278–83
   PubMed Web of Science ®Google Scholar
• Anderson TA, Sauer RT. (2003). Role of an N(cap) residue in determining the stability and operator-binding affinity of Arc repressor. Biophys Chem 100:341–50
   Google Scholar
• Andrae J, Gallini R, Betsholtz C. (2008). Role of platelet-derived growth factors in physiology and medicine. Genes Dev 22:1276–312
   PubMed Web of Science ®Google Scholar
• Arbiser JL, Petros J, Klafter R, et al. (2002). Reactive oxygen generated by Nox1 triggers the angiogenic switch. Proc Natl Acad Sci USA 99:715–20
   PubMed Web of Science ®Google Scholar
• Aslan M, Ozben T. (2003). Oxidants in receptor tyrosine kinase signal transduction pathways. Antioxid Redox Signal 5:781–8
   PubMed Web of Science ®Google Scholar
• Avruch J. (1998). Insulin signal transduction through protein kinase cascades. Mol Cell Biochem 182:31–48
   PubMed Web of Science ®Google Scholar
• Babior BM. (2000). The NADPH oxidase of endothelial cells. IUBMB Life 50:267–9
   PubMed Web of Science ®Google Scholar
• Bae YS, Kang SW, Seo MS, et al. (1997). Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem 272:217–21
   PubMed Web of Science ®Google Scholar
• Bae YS, Sung JY, Kim OS, et al. (2000). Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase. J Biol Chem 275:10527–31
   PubMed Web of Science ®Google Scholar
• Banerjee R, ed. (2008). Redox biochemistry. Hoboken (NJ): John Wiley & Sons
   Google Scholar
• Barnham KJ, Masters CL, Bush AI. (2004). Neurodegenerative diseases and oxidative stress. Nat Rev Drug Discov 3:205–14
   PubMed Web of Science ®Google Scholar
• Benitez LV, Allison WS. (1974). The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins. J Biol Chem 249:6234–43
   PubMed Web of Science ®Google Scholar
• Bienert GP, Moller AL, Kristiansen KA, et al. (2007). Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes. J Biol Chem 282:1183–92
   PubMed Web of Science ®Google Scholar
• Bienert GP, Schjoerring JK, Jahn TP. (2006). Membrane transport of hydrogen peroxide. Biochim Biophys Acta 1758:994–1003
   PubMed Web of Science ®Google Scholar
• Blume-Jensen P, Hunter T. (2001). Oncogenic kinase signalling. Nature 411:355–65
   PubMed Web of Science ®Google Scholar
• Boivin B, Zhang S, Arbiser JL, et al. (2008). A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells. Proc Natl Acad Sci USA 105:9959–64
   PubMed Web of Science ®Google Scholar
• Buhrow SA, Cohen S, Staros JV. (1982). Affinity labeling of the protein kinase associated with the epidermal growth factor receptor in membrane vesicles from A431 cells. J Biol Chem 257:4019–22
   PubMed Web of Science ®Google Scholar
• Cantley LC, Neel BG. (1999). New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci USA 96:4240–5
   PubMed Web of Science ®Google Scholar
• Carpenter G, King L Jr, Cohen S. (1978). Epidermal growth factor stimulates phosphorylation in membrane preparations in vitro. Nature 276:409–10
   PubMed Web of Science ®Google Scholar
• Carvalho-Filho MA, Ueno M, Hirabara SM, et al. (2005). S-nitrosation of the insulin receptor, insulin receptor substrate 1, and protein kinase B/Akt: a novel mechanism of insulin resistance. Diabetes 54:959–67
   PubMed Web of Science ®Google Scholar
• Caselli A, Marzocchini R, Camici G, et al. (1998). The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J Biol Chem 273:32554–60
   PubMed Web of Science ®Google Scholar
• Chan TO, Rittenhouse SE, Tsichlis PN. (1999). AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation. Annu Rev Biochem 68:965–1014
   PubMed Web of Science ®Google Scholar
• Chen K, Kirber MT, Xiao H, et al. (2008). Regulation of ROS signal transduction by NADPH oxidase 4 localization. J Cell Biol 181:1129–39
   PubMed Web of Science ®Google Scholar
• Chen Q, Olashaw N, Wu J. (1995). Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway. J Biol Chem 270:28499–502
   PubMed Web of Science ®Google Scholar
• Chen K, Thomas SR, Albano A, et al. (2004). Mitochondrial function is required for hydrogen peroxide-induced growth factor receptor transactivation and downstream signaling. J Biol Chem 279:35079–86
   PubMedGoogle Scholar
• Chen K, Vita JA, Berk BC, Keaney JF Jr. (2001a). c-Jun N-terminal kinase activation by hydrogen peroxide in endothelial cells involves SRC-dependent epidermal growth factor receptor transactivation. J Biol Chem 276:16045–50
   PubMed Web of Science ®Google Scholar
• Chen WS, Xu PZ, Gottlob K, et al. (2001b). Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene. Genes Dev 15:2203–8
   PubMed Web of Science ®Google Scholar
• Cheng G, Cao Z, Xu X, et al. (2001). Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 269:131–40
   PubMed Web of Science ®Google Scholar
• Chiarugi P, Buricchi F. (2007). Protein tyrosine phosphorylation and reversible oxidation: two cross-talking posttranslation modifications. Antioxid Redox Signal 9:1–24
   PubMed Web of Science ®Google Scholar
• Chiarugi P, Cirri P, Raugei G, et al. (1995). PDGF receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase. FEBS Lett 372:49–53
   PubMedGoogle Scholar
• Chiarugi P, Cirri P, Taddei ML, et al. (2002). New perspectives in PDGF receptor downregulation: the main role of phosphotyrosine phosphatases. J Cell Sci 115:2219–32
   PubMed Web of Science ®Google Scholar
• Chiarugi P, Fiaschi T, Taddei ML, et al. (2001). Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation. J Biol Chem 276:33478–87
   PubMed Web of Science ®Google Scholar
• Cho H, Mu J, Kim JK, et al. (2001a). Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Science 292:1728–31
   PubMed Web of Science ®Google Scholar
• Cho H, Thorvaldsen JL, Chu Q, et al. (2001b). Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice. J Biol Chem 276:38349–52
   PubMed Web of Science ®Google Scholar
• Choi MH, Lee IK, Kim GW, et al. (2005). Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II. Nature 435:347–53
   PubMed Web of Science ®Google Scholar
• Chua CC, Hamdy RC, Chua BH. (1998). Upregulation of vascular endothelial growth factor by H2O2 in rat heart endothelial cells. Free Radic Biol Med 25:891–7
   PubMed Web of Science ®Google Scholar
• Clark S, Konstantopoulos N. (1993). Sulphydryl agents modulate insulin- and epidermal growth factor (EGF)-receptor kinase via reaction with intracellular receptor domains: differential effects on basal versus activated receptors. Biochem J 292:217–23
   Google Scholar
• Cohen S. (2008). Origins of growth factors: NGF and EGF. J Biol Chem 283:33793–7
   PubMed Web of Science ®Google Scholar
• Cohen S, Carpenter G, King L Jr. (1980). Epidermal growth factor-receptor-protein kinase interactions. Co-purification of receptor and epidermal growth factor-enhanced phosphorylation activity. J Biol Chem 255:4834–42
   PubMed Web of Science ®Google Scholar
• Colavitti R, Pani G, Bedogni B, et al. (2002). Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR. J Biol Chem 277:3101–8
   PubMed Web of Science ®Google Scholar
• Cross DA, Alessi DR, Cohen P, et al. (1995). Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378:785–9
   PubMed Web of Science ®Google Scholar
• Cross JV, Templeton DJ. (2004). Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain. Biochem J 381:675–83
   PubMed Web of Science ®Google Scholar
• Cunnick JM, Dorsey JF, Standley T, et al. (1998). Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway. J Biol Chem 273:14468–75
   PubMedGoogle Scholar
• D'Autreaux B, Toledano MB. (2007). ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 8:813–24
   PubMed Web of Science ®Google Scholar
• De Deken X, Wang D, Many MC, et al. (2000). Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J Biol Chem 275:23227–33
   PubMed Web of Science ®Google Scholar
• Denu JM, Tanner KG. (1998). Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37:5633–42
   PubMed Web of Science ®Google Scholar
• Depuydt M, Messens J, Collet JF. (2011). How proteins form disulfide bonds. Antioxid Redox Signal 15:49–66
   PubMed Web of Science ®Google Scholar
• Devary Y, Gottlieb RA, Lau LF, Karin M. (1991). Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol Cell Biol 11:2804–11
   PubMed Web of Science ®Google Scholar
• DeYulia GJ Jr, Carcamo JM. (2005). EGF receptor-ligand interaction generates extracellular hydrogen peroxide that inhibits EGFR-associated protein tyrosine phosphatases. Biochem Biophys Res Commun 334:38–42
   Google Scholar
• DeYulia GJ Jr, Carcamo JM, Borquez-Ojeda O, et al. (2005). Hydrogen peroxide generated extracellularly by receptor-ligand interaction facilitates cell signaling. Proc Natl Acad Sci USA 102:5044–9
   PubMed Web of Science ®Google Scholar
• Diao Y, Liu W, Wong CC, et al. (2010). Oxidation-induced intramolecular disulfide bond inactivates mitogen-activated protein kinase kinase 6 by inhibiting ATP binding. Proc Natl Acad Sci USA 107:20974–9
   Google Scholar
• Dickinson BC, Chang CJ. (2011). Chemistry and biology of reactive oxygen species in signaling or stress responses. Nat Chem Biol 7:504–11
   PubMed Web of Science ®Google Scholar
• Dolfi F, Garcia-Guzman M, Ojaniemi M, et al. (1998). The adaptor protein Crk connects multiple cellular stimuli to the JNK signaling pathway. Proc Natl Acad Sci USA 95:15394–9
   PubMed Web of Science ®Google Scholar
• Elchebly M, Payette P, Michaliszyn E, et al. (1999). Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283:1544–8
   PubMed Web of Science ®Google Scholar
• Engelman JA, Luo J, Cantley LC. (2006). The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat Rev Genet 7:606–19
   PubMed Web of Science ®Google Scholar
• Esposito F, Chirico G, Montesano Gesualdi N, et al. (2003). Protein kinase B activation by reactive oxygen species is independent of tyrosine kinase receptor phosphorylation and requires SRC activity. J Biol Chem 278:20828–34
   PubMed Web of Science ®Google Scholar
• Ferrara N, Gerber HP, Lecouter J. (2003). The biology of VEGF and its receptors. Nat Med 9:669–76
   PubMed Web of Science ®Google Scholar
• Finkel T. (2011). Signal transduction by reactive oxygen species. J Cell Biol 194:7–15
   PubMed Web of Science ®Google Scholar
• Finkel T. (2012). From sulfenylation to sulfhydration: what a thiolate needs to tolerate. Sci Signal 5:pe10
   PubMedGoogle Scholar
• Finkel T, Serrano M, Blasco MA. (2007). The common biology of cancer and ageing. Nature 448:767–74
   PubMed Web of Science ®Google Scholar
• Flint AJ, Tiganis T, Barford D, Tonks NK. (1997). Development of “substrate-trapping” mutants to identify physiological substrates of protein tyrosine phosphatases. Proc Natl Acad Sci USA 94:1680–5
   PubMed Web of Science ®Google Scholar
• Franke TF, Kaplan DR, Cantley LC, Toker A. (1997). Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275:665–8
   PubMed Web of Science ®Google Scholar
• Fridovich I. (1995). Superoxide radical and superoxide dismutases. Annu Rev Biochem 64:97–112
   PubMed Web of Science ®Google Scholar
• Gamou S, Shimizu N. (1995). Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor. FEBS Lett 357:161–4
   PubMed Web of Science ®Google Scholar
• Gardner PR, Raineri I, Epstein LB, White CW. (1995). Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem 270:13399–405
   PubMed Web of Science ®Google Scholar
• Gianni D, Bohl B, Courtneidge SA, Bokoch GM. (2008). The involvement of the tyrosine kinase c-Src in the regulation of reactive oxygen species generation mediated by NADPH oxidase-1. Mol Biol Cell 19:2984–94
   PubMed Web of Science ®Google Scholar
• Giannoni E, Buricchi F, Grimaldi G, et al. (2008). Redox regulation of anoikis: reactive oxygen species as essential mediators of cell survival. Cell Death Differ 15:867–78
   Google Scholar
• Giannoni E, Buricchi F, Raugei G, et al. (2005). Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth. Mol Cell Biol 25:6391–403
   PubMed Web of Science ®Google Scholar
• Giannoni E, Taddei ML, Chiarugi P. (2010). Src redox regulation: again in the front line. Free Radic Biol Med 49:516–27
   PubMed Web of Science ®Google Scholar
• Giorgio M, Migliaccio E, Orsini F, et al. (2005). Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 122:221–33
   PubMed Web of Science ®Google Scholar
• Giorgio M, Trinei M, Migliaccio E, Pelicci PG. (2007). Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? Nat Rev Mol Cell Biol 8:722–8
   PubMed Web of Science ®Google Scholar
• Go YM, Jones DP. (2013). Thiol/disulfide redox states in signaling and sensing. Crit Rev Biochem Mol Biol 48:173--81
   PubMed Web of Science ®Google Scholar
• Goldkorn T, Balaban N, Matsukuma K, et al. (1998). EGF-Receptor phosphorylation and signaling are targeted by H2O2 redox stress. Am J Respir Cell Mol Biol 19:786–98
   PubMedGoogle Scholar
• Gonzalez E, Mcgraw TE. (2009a). The Akt kinases: isoform specificity in metabolism and cancer. Cell Cycle 8:2502–8
   PubMed Web of Science ®Google Scholar
• Gonzalez E, Mcgraw TE. (2009b). Insulin-modulated Akt subcellular localization determines Akt isoform-specific signaling. Proc Natl Acad Sci USA 106:7004–9
   PubMed Web of Science ®Google Scholar
• Gonzalez-Pacheco FR, Deudero JJ, Castellanos MC, et al. (2006). Mechanisms of endothelial response to oxidative aggression: protective role of autologous VEGF and induction of VEGFR2 by H2O2. Am J Physiol Heart Circ Physiol 291:H1395–401
   PubMed Web of Science ®Google Scholar
• Gorlach A, Brandes RP, Nguyen K, et al. (2000). A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall. Circ Res 87:26–32
   PubMed Web of Science ®Google Scholar
• Grazia Lampugnani M, Zanetti A, Corada M, et al. (2003). Contact inhibition of VEGF-induced proliferation requires vascular endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148. J Cell Biol 161:793–804
   PubMed Web of Science ®Google Scholar
• Guo Z, Deshpande R, Paull TT. (2010a). ATM activation in the presence of oxidative stress. Cell Cycle 9:4805–11
   PubMed Web of Science ®Google Scholar
• Guo Z, Kozlov S, Lavin MF, et al. (2010b). ATM activation by oxidative stress. Science 330:517–21
   PubMed Web of Science ®Google Scholar
• Guyton KZ, Liu Y, Gorospe M, et al. (1996). Activation of mitogen-activated protein kinase by H2O2. Role in cell survival following oxidant injury. J Biol Chem 271:4138–42
   PubMed Web of Science ®Google Scholar
• Haj FG, Markova B, Klaman LD, et al. (2003). Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatase-1B. J Biol Chem 278:739–44
   PubMed Web of Science ®Google Scholar
• Haj FG, Verveer PJ, Squire A, et al. (2002). Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 295:1708–11
   PubMed Web of Science ®Google Scholar
• Hall A, Karplus PA, Poole LB. (2009). Typical 2-Cys peroxiredoxins–structures, mechanisms and functions. FEBS J 276:2469–77
   PubMed Web of Science ®Google Scholar
• Halvey PJ, Watson WH, Hansen JM, et al. (2005). Compartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling. Biochem J 386:215–19
   PubMed Web of Science ®Google Scholar
• Handy DE, Lubos E, Yang Y, et al. (2009). Glutathione peroxidase-1 regulates mitochondrial function to modulate redox-dependent cellular responses. J Biol Chem 284:11913–21
   PubMed Web of Science ®Google Scholar
• Haque A, Andersen JN, Salmeen A, et al. (2011). Conformation-sensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity. Cell 147:185–98
   PubMed Web of Science ®Google Scholar
• Heeneman S, Haendeler J, Saito Y, et al. (2000). Angiotensin II induces transactivation of two different populations of the platelet-derived growth factor beta receptor. Key role for the p66 adaptor protein Shc. J Biol Chem 275:15926–32
   PubMed Web of Science ®Google Scholar
• Heldin CH, Westermark B. (1999). Mechanism of action and in vivo role of platelet-derived growth factor. Physiol Rev 79:1283–316
   PubMed Web of Science ®Google Scholar
• Herbst RS. (2004). Review of epidermal growth factor receptor biology. Int J Radiat Oncol Biol Phys 59:21–6
   PubMed Web of Science ®Google Scholar
• Hess DT, Stamler JS. (2012). Regulation by S-nitrosylation of protein post-translational modification. J Biol Chem 287:4411–18
   PubMed Web of Science ®Google Scholar
• Houstis N, Rosen ED, Lander ES. (2006). Reactive oxygen species have a causal role in multiple forms of insulin resistance. Nature 440:944–8
   PubMed Web of Science ®Google Scholar
• Hsu JL, Hsieh Y, Tu C, et al. (1996). Catalytic properties of human manganese superoxide dismutase. J Biol Chem 271:17687–91
   PubMed Web of Science ®Google Scholar
• Huang X, Begley M, Morgenstern KA, et al. (2003). Crystal structure of an inactive Akt2 kinase domain. Structure 11:21–30
   PubMed Web of Science ®Google Scholar
• Hubbard SR, Till JH. (2000). Protein tyrosine kinase structure and function. Annu Rev Biochem 69:373–98
   PubMed Web of Science ®Google Scholar
• Ichijo H, Nishida E, Irie K, et al. (1997). Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 275:90–4
   PubMed Web of Science ®Google Scholar
• Ikeda S, Ushio-Fukai M, Zuo L, et al. (2005a). Novel role of ARF6 in vascular endothelial growth factor-induced signaling and angiogenesis. Circ Res 96:467–75
   PubMedGoogle Scholar
• Ikeda S, Yamaoka-Tojo M, Hilenski L, et al. (2005b). IQGAP1 regulates reactive oxygen species-dependent endothelial cell migration through interacting with Nox2. Arterioscler Thromb Vasc Biol 25:2295–300
   Google Scholar
• Jacob C, Battaglia E, Burkholz T, et al. (2012). Control of oxidative posttranslational cysteine modifications: from intricate chemistry to widespread biological and medical applications. Chem Res Toxicol 25:588–604
   PubMed Web of Science ®Google Scholar
• Jacob C, Winyard PG, eds. (2009). Redox signaling and regulation in biology and medicine. Weinheim: Wiley-VCH
   Google Scholar
• Jaspers I, Zhang W, Fraser A, et al. (2001). Hydrogen peroxide has opposing effects on IKK activity and IkappaBalpha breakdown in airway epithelial cells. Am J Respir Cell Mol Biol 24:769–77
   PubMed Web of Science ®Google Scholar
• Joneson T, Bar-Sagi D. (1998). A Rac1 effector site controlling mitogenesis through superoxide production. J Biol Chem 273:17991–4
   PubMed Web of Science ®Google Scholar
• Juarez JC, Manuia M, Burnett ME, et al. (2008). Superoxide dismutase 1 (SOD1) is essential for H2O2-mediated oxidation and inactivation of phosphatases in growth factor signaling. Proc Natl Acad Sci USA 105:7147–52
   PubMed Web of Science ®Google Scholar
• Kageyama K, Ihara Y, Goto S, et al. (2002). Overexpression of calreticulin modulates protein kinase B/Akt signaling to promote apoptosis during cardiac differentiation of cardiomyoblast H9c2 cells. J Biol Chem 277:19255–64
   PubMedGoogle Scholar
• Kamata H, Honda S, Maeda S, et al. (2005). Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120:649–61
   PubMed Web of Science ®Google Scholar
• Kamata H, Manabe T, Oka S, et al. (2002). Hydrogen peroxide activates IkappaB kinases through phosphorylation of serine residues in the activation loops. FEBS Lett 519:231–7
   PubMed Web of Science ®Google Scholar
• Kanda M, Ihara Y, Murata H, et al. (2006). Glutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphatase. J Biol Chem 281:28518–28
   PubMed Web of Science ®Google Scholar
• Kang SW, Chae HZ, Seo MS, et al. (1998). Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem 273:6297–302
   PubMed Web of Science ®Google Scholar
• Kang DH, Lee DJ, Lee KW, et al. (2011). Peroxiredoxin II is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells. Mol Cell 44:545–58
   PubMed Web of Science ®Google Scholar
• Kapahi P, Takahashi T, Natoli G, et al. (2000). Inhibition of NF-kappa B activation by arsenite through reaction with a critical cysteine in the activation loop of Ikappa B kinase. J Biol Chem 275:36062–6
   PubMed Web of Science ®Google Scholar
• Kaplan N, Urao N, Furuta E, et al. (2011). Localized cysteine sulfenic acid formation by vascular endothelial growth factor: role in endothelial cell migration and angiogenesis. Free Radic Res 45:1124–35
   PubMed Web of Science ®Google Scholar
• Kemble DJ, Sun G. (2009). Direct and specific inactivation of protein tyrosine kinases in the Src and FGFR families by reversible cysteine oxidation. Proc Natl Acad Sci USA 106:5070–5
   PubMed Web of Science ®Google Scholar
• Kido Y, Nakae J, Accili D. (2001). Clinical review 125: The insulin receptor and its cellular targets. J Clin Endocrinol Metab 86:972–9
   PubMed Web of Science ®Google Scholar
• Klaman LD, Boss O, Peroni OD, et al. (2000). Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol Cell Biol 20:5479–89
   PubMed Web of Science ®Google Scholar
• Klomsiri C, Karplus PA, Poole LB. (2011). Cysteine-based redox switches in enzymes. Antioxid Redox Signal 14:1065–77
   PubMed Web of Science ®Google Scholar
• Kohn AD, Summers SA, Birnbaum MJ, Roth RA. (1996). Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J Biol Chem 271:31372–8
   PubMed Web of Science ®Google Scholar
• Korn SH, Wouters EF, Vos N, Janssen-Heininger YM. (2001). Cytokine-induced activation of nuclear factor-kappa B is inhibited by hydrogen peroxide through oxidative inactivation of IkappaB kinase. J Biol Chem 276:35693–700
   PubMed Web of Science ®Google Scholar
• Krasnowska EK, Pittaluga E, Brunati AM, et al. (2008). N-acetyl-l-cysteine fosters inactivation and transfer to endolysosomes of c-Src. Free Radic Biol Med 45:1566–72
   PubMedGoogle Scholar
• Krieger-Brauer HI, Kather H. (1992). Human fat cells possess a plasma membrane-bound H2O2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase. J Clin Invest 89:1006–13
   PubMed Web of Science ®Google Scholar
• Krieger-Brauer HI, Kather H. (1995). Antagonistic effects of different members of the fibroblast and platelet-derived growth factor families on adipose conversion and NADPH-dependent H2O2 generation in 3T3 L1-cells. Biochem J 307:549–56
   PubMedGoogle Scholar
• Krieger-Brauer HI, Medda PK, Kather H. (1997). Insulin-induced activation of NADPH-dependent H2O2 generation in human adipocyte plasma membranes is mediated by Galphai2. J Biol Chem 272:10135–43
   PubMed Web of Science ®Google Scholar
• Kroviarski Y, Debbabi M, Bachoual R, et al. (2010). Phosphorylation of NADPH oxidase activator 1 (NOXA1) on serine 282 by MAP kinases and on serine 172 by protein kinase C and protein kinase A prevents NOX1 hyperactivation. FASEB J 24:2077–92
   Google Scholar
• Kuroki M, Voest EE, Amano S, et al. (1996). Reactive oxygen intermediates increase vascular endothelial growth factor expression in vitro and in vivo. J Clin Invest 98:1667–75
   PubMed Web of Science ®Google Scholar
• Kwarcinski FE, Fox CC, Steffey ME, Soellner MB. (2012). Irreversible inhibitors of c-Src kinase that target a nonconserved cysteine. ACS Chem Biol 7:1910--17
   Google Scholar
• Kwon J, Lee SR, Yang KS, et al. (2004). Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc Natl Acad Sci USA 101:16419–24
   PubMed Web of Science ®Google Scholar
• Labrecque L, Royal I, Surprenant DS, et al. (2003). Regulation of vascular endothelial growth factor receptor-2 activity by caveolin-1 and plasma membrane cholesterol. Mol Biol Cell 14:334–47
   PubMed Web of Science ®Google Scholar
• Lam YW, Yuan Y, Isaac J, et al. (2010). Comprehensive identification and modified-site mapping of S-nitrosylated targets in prostate epithelial cells. PLoS One 5:e9075
   PubMed Web of Science ®Google Scholar
• Lambeth JD. (2004). NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 4:181–9
   PubMed Web of Science ®Google Scholar
• Lander HM, Milbank AJ, Tauras JM, et al. (1996). Redox regulation of cell signalling. Nature 381:380–1
   PubMed Web of Science ®Google Scholar
• Lassegue B, Sorescu D, Szocs K, et al. (2001). Novel gp91(phox) homologues in vascular smooth muscle cells: nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways. Circ Res 88:888–94
   PubMed Web of Science ®Google Scholar
• Lee JW, Kim JE, Park EJ, et al. (2004). Two conserved cysteine residues are critical for the enzymic function of the human platelet-derived growth factor receptor-beta: evidence for different roles of Cys-822 and Cys-940 in the kinase activity. Biochem J 382:631–9
   Google Scholar
• Lee SR, Kwon KS, Kim SR, Rhee SG. (1998). Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273:15366–72
   PubMed Web of Science ®Google Scholar
• Lee SR, Yang KS, Kwon J, et al. (2002). Reversible inactivation of the tumor suppressor PTEN by H2O2. J Biol Chem 277:20336–42
   PubMed Web of Science ®Google Scholar
• Leonard SE, Garcia FJ, Goodsell DS, Carroll KS. (2011). Redox-based probes for protein tyrosine phosphatases. Angew Chem Int Ed Engl 50:4423–7
   Google Scholar
• Leonard SE, Reddie KG, Carroll KS. (2009). Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem Biol 4:783–99
   PubMed Web of Science ®Google Scholar
• Leonberg AK, Chai YC. (2007). The functional role of cysteine residues for c-Abl kinase activity. Mol Cell Biochem 304:207–12
   PubMed Web of Science ®Google Scholar
• Leslie NR. (2006). The redox regulation of PI 3-kinase-dependent signaling. Antioxid Redox Signal 8:1765–74
   PubMedGoogle Scholar
• Leslie NR, Bennett D, Lindsay YE, et al. (2003). Redox regulation of PI 3-kinase signalling via inactivation of PTEN. EMBO J 22:5501–10
   PubMed Web of Science ®Google Scholar
• Levinson NM, Seeliger MA, Cole PA, Kuriyan J. (2008). Structural basis for the recognition of c-Src by its inactivator Csk. Cell 134:124–34
   PubMed Web of Science ®Google Scholar
• Li W, Schlessinger J. (1991). Platelet-derived growth factor (PDGF)-induced disulfide-linked dimerization of PDGF receptor in living cells. Mol Cell Biol 11:3756–61
   PubMedGoogle Scholar
• Li Q, Zhang Y, Marden JJ, et al. (2008). Endosomal NADPH oxidase regulates c-Src activation following hypoxia/reoxygenation injury. Biochem J 411:531–41
   PubMed Web of Science ®Google Scholar
• Lin Y, Berg AH, Iyengar P, et al. (2005). The hyperglycemia-induced inflammatory response in adipocytes: the role of reactive oxygen species. J Biol Chem 280:4617–26
   PubMed Web of Science ®Google Scholar
• Liu H, Nishitoh H, Ichijo H, Kyriakis JM. (2000). Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol Cell Biol 20:2198–208
   PubMed Web of Science ®Google Scholar
• Liu Q, Sabnis Y, Zhao Z, et al. (2013). Developing irreversible inhibitors of the protein kinase cysteinome. Chem Biol 20:146–59
   PubMed Web of Science ®Google Scholar
• Lo YY, Cruz TF. (1995). Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes. J Biol Chem 270:11727–30
   PubMed Web of Science ®Google Scholar
• Lo YY, Wong JM, Cruz TF. (1996). Reactive oxygen species mediate cytokine activation of c-Jun NH2-terminal kinases. J Biol Chem 271:15703–7
   PubMed Web of Science ®Google Scholar
• Lohse DL, Denu JM, Santoro N, Dixon JE. (1997). Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1. Biochemistry 36:4568–75
   PubMed Web of Science ®Google Scholar
• Lowell BB, Shulman GI. (2005). Mitochondrial dysfunction and type 2 diabetes. Science 307:384–7
   PubMed Web of Science ®Google Scholar
• Lu Y, Yu Q, Liu JH, et al. (2003). Src family protein-tyrosine kinases alter the function of PTEN to regulate phosphatidylinositol 3-kinase/AKT cascades. J Biol Chem 278:40057–66
   PubMed Web of Science ®Google Scholar
• Lu Z, Xu S. (2006). ERK1/2 MAP kinases in cell survival and apoptosis. IUBMB Life 58:621–31
   PubMed Web of Science ®Google Scholar
• Ma YC, Huang XY. (2002). Novel regulation and function of Src tyrosine kinase. Cell Mol Life Sci 59:456–62
   Google Scholar
• Macias A, Azavedo E, Hagerstrom T, et al. (1987). Prognostic significance of the receptor for epidermal growth factor in human mammary carcinomas. Anticancer Res 7:459–64
   PubMed Web of Science ®Google Scholar
• Mahadev K, Motoshima H, Wu X, et al. (2004). The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction. Mol Cell Biol 24:1844–54
   PubMed Web of Science ®Google Scholar
• Mahadev K, Wu X, Zilbering A, et al. (2001a). Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes. J Biol Chem 276:48662–9
   PubMedGoogle Scholar
• Mahadev K, Zilbering A, Zhu L, Goldstein BJ. (2001b). Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J Biol Chem 276:21938–42
   PubMed Web of Science ®Google Scholar
• Maller C, Schroder E, Eaton P. (2011). Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: studies with a novel anti-dimedone sulfenic acid antibody. Antioxid Redox Signal 14:49–60
   PubMed Web of Science ®Google Scholar
• Mamathambika BS, Bardwell JC. (2008). Disulfide-linked protein folding pathways. Annu Rev Cell Dev Biol 24:211–35
   Google Scholar
• Manning BD, Cantley LC. (2007). AKT/PKB signaling: navigating downstream. Cell 129:1261–74
   PubMed Web of Science ®Google Scholar
• Manning G, Whyte DB, Martinez R, et al. (2002). The protein kinase complement of the human genome. Science 298:1912–34
   PubMed Web of Science ®Google Scholar
• Matsuzawa A, Ichijo H. (2005). Stress-responsive protein kinases in redox-regulated apoptosis signaling. Antioxid Redox Signal 7:472–81
   PubMed Web of Science ®Google Scholar
• May JM, de Haen C. (1979a). The insulin-like effect of hydrogen peroxide on pathways of lipid synthesis in rat adipocytes. J Biol Chem 254:9017–21
   PubMed Web of Science ®Google Scholar
• May JM, de Haen C. (1979b). Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells. J Biol Chem 254:2214–20
   PubMed Web of Science ®Google Scholar
• Mccord JM, Fridovich I. (1969). Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244:6049–55
   PubMed Web of Science ®Google Scholar
• McCubrey JA, Lahair MM, Franklin RA. (2006). Reactive oxygen species-induced activation of the MAP kinase signaling pathways. Antioxid Redox Signal 8:1775–89
   PubMed Web of Science ®Google Scholar
• Mebratu Y, Tesfaigzi Y. (2009). How ERK1/2 activation controls cell proliferation and cell death: is subcellular localization the answer? Cell Cycle 8:1168–75
   PubMed Web of Science ®Google Scholar
• Mehdi MZ, Pandey NR, Pandey SK, Srivastava AK. (2005). H2O2-induced phosphorylation of ERK1/2 and PKB requires tyrosine kinase activity of insulin receptor and c-Src. Antioxid Redox Signal 7:1014–20
   Google Scholar
• Meng TC, Fukada T, Tonks NK. (2002). Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol Cell 9:387–99
   PubMed Web of Science ®Google Scholar
• Migliaccio E, Giorgio M, Mele S, et al. (1999). The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 402:309–13
   PubMed Web of Science ®Google Scholar
• Miller EW, Dickinson BC, Chang CJ. (2010). Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc Natl Acad Sci USA 107:15681–6
   PubMed Web of Science ®Google Scholar
• Miller EW, Tulyathan O, Isacoff EY, Chang CJ. (2007). Molecular imaging of hydrogen peroxide produced for cell signaling. Nat Chem Biol 3:263–7
   PubMed Web of Science ®Google Scholar
• Mills JE, Whitford PC, Shaffer J, et al. (2007). A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity. J Mol Biol 365:1460–8
   PubMed Web of Science ®Google Scholar
• Mukherjee SP, Lane RH, Lynn WS. (1978). Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents. Biochem Pharmacol 27:2589–94
   Google Scholar
• Murata H, Ihara Y, Nakamura H, et al. (2003). Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J Biol Chem 278:50226–33
   PubMed Web of Science ®Google Scholar
• Murillo-Carretero M, Torroglosa A, Castro C, et al. (2009). S-Nitrosylation of the epidermal growth factor receptor: a regulatory mechanism of receptor tyrosine kinase activity. Free Radic Biol Med 46:471–9
   Google Scholar
• Nadeau PJ, Charette SJ, Landry J. (2009). REDOX reaction at ASK1-Cys250 is essential for activation of JNK and induction of apoptosis. Mol Biol Cell 20:3628–37
   PubMed Web of Science ®Google Scholar
• Nadeau PJ, Charette SJ, Toledano MB, Landry J. (2007). Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis. Mol Biol Cell 18:3903–13
   PubMed Web of Science ®Google Scholar
• Nakamura Y, Patrushev N, Inomata H, et al. (2008). Role of protein tyrosine phosphatase 1B in vascular endothelial growth factor signaling and cell--cell adhesions in endothelial cells. Circ Res 102:1182–91
   PubMedGoogle Scholar
• Nakashima I, Kato M, Akhand AA, et al. (2002). Redox-linked signal transduction pathways for protein tyrosine kinase activation. Antioxid Redox Signal 4:517–31
   PubMed Web of Science ®Google Scholar
• Nakashima N, Sharma PM, Imamura T, et al. (2000). The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes. J Biol Chem 275:12889–95
   PubMed Web of Science ®Google Scholar
• Nose K, Shibanuma M, Kikuchi K, et al. (1991). Transcriptional activation of early-response genes by hydrogen peroxide in a mouse osteoblastic cell line. Eur J Biochem 201:99–106
   PubMedGoogle Scholar
• Oh H, Jung HY, Kim J, Bae YS. (2010). Phosphorylation of serine282 in NADPH oxidase activator 1 by Erk desensitizes EGF-induced ROS generation. Biochem Biophys Res Commun 394:691–6
   PubMedGoogle Scholar
• Olsson AK, Dimberg A, Kreuger J, Claesson-Welsh L. (2006). VEGF receptor signalling -- in control of vascular function. Nat Rev Mol Cell Biol 7:359–71
   PubMed Web of Science ®Google Scholar
• Oshikawa J, Urao N, Kim HW, et al. (2010). Extracellular SOD-derived H2O2 promotes VEGF signaling in caveolae/lipid rafts and post-ischemic angiogenesis in mice. PLoS One 5:e10189
   PubMed Web of Science ®Google Scholar
• Pantano C, Reynaert NL, Van Der Vliet A, Janssen-Heininger YM. (2006). Redox-sensitive kinases of the nuclear factor-kappaB signaling pathway. Antioxid Redox Signal 8:1791–806
   PubMed Web of Science ®Google Scholar
• Park HS, Huh SH, Kim MS, et al. (2000). Nitric oxide negatively regulates c-Jun N-terminal kinase/stress-activated protein kinase by means of S-nitrosylation. Proc Natl Acad Sci USA 97:14382–7
   PubMedGoogle Scholar
• Park HS, Lee SH, Park D, et al. (2004a). Sequential activation of phosphatidylinositol 3-kinase, beta Pix, Rac1, and Nox1 in growth factor-induced production of H2O2. Mol Cell Biol 24:4384–94
   PubMed Web of Science ®Google Scholar
• Park HS, Yu JW, Cho JH, et al. (2004b). Inhibition of apoptosis signal-regulating kinase 1 by nitric oxide through a thiol redox mechanism. J Biol Chem 279:7584–90
   PubMed Web of Science ®Google Scholar
• Parsonage D, Karplus PA, Poole LB. (2008). Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proc Natl Acad Sci USA 105:8209–14
   PubMed Web of Science ®Google Scholar
• Paulsen CE, Carroll KS. (2010). Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol 5:47–62
   PubMed Web of Science ®Google Scholar
• Paulsen CE, Truong TH, Garcia FJ, et al. (2012). Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity. Nat Chem Biol 8:57–64
   Web of Science ®Google Scholar
• Penel S, Hughes E, Doig AJ. (1999). Side-chain structures in the first turn of the alpha-helix. J Mol Biol 287:127–43
   Google Scholar
• Peskin AV, Low FM, Paton LN, et al. (2007). The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents. J Biol Chem 282:11885–92
   PubMed Web of Science ®Google Scholar
• Poole LB, Klomsiri C, Knaggs SA, et al. (2007). Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins. Bioconjug Chem 18:2004–17
   PubMed Web of Science ®Google Scholar
• Poole LB, Zeng BB, Knaggs SA, et al. (2005). Synthesis of chemical probes to map sulfenic acid modifications on proteins. Bioconjug Chem 16:1624–8
   PubMed Web of Science ®Google Scholar
• Raha S, Robinson BH. (2000). Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem Sci 25:502–8
   PubMed Web of Science ®Google Scholar
• Rahman MA, Senga T, Ito S, et al. (2010). S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion. J Biol Chem 285:3806–14
   PubMed Web of Science ®Google Scholar
• Reddie KG, Carroll KS. (2008). Expanding the functional diversity of proteins through cysteine oxidation. Curr Opin Chem Biol 12:746–54
   PubMed Web of Science ®Google Scholar
• Reddie KG, Seo YH, Muse III, et al. (2008). A chemical approach for detecting sulfenic acid-modified proteins in living cells. Mol Biosyst 4:521–31
   PubMed Web of Science ®Google Scholar
• Reynaert NL, Ckless K, Korn SH, et al. (2004). Nitric oxide represses inhibitory kappaB kinase through S-nitrosylation. Proc Natl Acad Sci USA 101:8945–50
   PubMed Web of Science ®Google Scholar
• Reynaert NL, Van Der Vliet A, Guala AS, et al. (2006). Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta. Proc Natl Acad Sci USA 103:13086–91
   PubMed Web of Science ®Google Scholar
• Reynolds AR, Tischer C, Verveer PJ, et al. (2003). EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation. Nat Cell Biol 5:447–53
   PubMed Web of Science ®Google Scholar
• Rhee SG. (2006). Cell signaling. H2O2, a necessary evil for cell signaling. Science 312:1882–3
   PubMed Web of Science ®Google Scholar
• Roberts PJ, Der CJ. (2007). Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Oncogene 26:3291–310
   PubMed Web of Science ®Google Scholar
• Rostovtsev VV, Green LG, Fokin VV, Sharpless KB. (2002). A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective “ligation” of azides and terminal alkynes. Angew Chem Int Ed Engl 41:2596–9
   PubMed Web of Science ®Google Scholar
• Rudich A, Tirosh A, Potashnik R, et al. (1998). Prolonged oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes. Diabetes 47:1562–9
   PubMed Web of Science ®Google Scholar
• Saito Y, Berk BC. (2001). Transactivation: a novel signaling pathway from angiotensin II to tyrosine kinase receptors. J Mol Cell Cardiol 33:3–7
   PubMed Web of Science ®Google Scholar
• Saito S, Frank GD, Mifune M, et al. (2002). Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase C-delta and c-Src. J Biol Chem 277:44695–700
   PubMed Web of Science ®Google Scholar
• Saitoh M, Nishitoh H, Fujii M, et al. (1998). Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 17:2596–606
   PubMed Web of Science ®Google Scholar
• Salsbury FR Jr., Knutson ST, Poole LB, Fetrow JS. (2008). Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid. Protein Sci 17:299–312
   PubMed Web of Science ®Google Scholar
• Saltiel AR, Kahn CR. (2001). Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414:799–806
   PubMed Web of Science ®Google Scholar
• Saxon E, Bertozzi CR. (2000). Cell surface engineering by a modified Staudinger reaction. Science 287:2007–10
   PubMed Web of Science ®Google Scholar
• Schlessinger J. (2000). Cell signaling by receptor tyrosine kinases. Cell 103:211–25
   PubMed Web of Science ®Google Scholar
• Schlessinger J. (2002). Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110:669–72
   PubMed Web of Science ®Google Scholar
• Schmid E, El Benna J, Galter D, et al. (1998). Redox priming of the insulin receptor beta-chain associated with altered tyrosine kinase activity and insulin responsiveness in the absence of tyrosine autophosphorylation. FASEB J 12:863–70
   PubMedGoogle Scholar
• Schmitt TL, Hotz-Wagenblatt A, Klein H, Droge W. (2005). Interdependent regulation of insulin receptor kinase activity by ADP and hydrogen peroxide. J Biol Chem 280:3795–801
   PubMed Web of Science ®Google Scholar
• Seo JH, Ahn Y, Lee SR, et al. (2005). The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway. Mol Biol Cell 16:348–57
   PubMed Web of Science ®Google Scholar
• Seo YH, Carroll KS. (2009). Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies. Proc Natl Acad Sci USA 106:16163–8
   PubMed Web of Science ®Google Scholar
• Seo YH, Carroll KS. (2011). Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone. Angew Chem Int Ed Engl 50:1342–5
   PubMed Web of Science ®Google Scholar
• Shaw M, Cohen P, Alessi DR. (1998). The activation of protein kinase B by H2O2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2. Biochem J 336:241–6
   PubMed Web of Science ®Google Scholar
• Singh J, Dobrusin EM, Fry DW, et al. (1997). Structure-based design of a potent, selective, and irreversible inhibitor of the catalytic domain of the erbB receptor subfamily of protein tyrosine kinases. J Med Chem 40:1130–5
   Google Scholar
• Singh J, Petter RC, Baillie TA, Whitty A. (2011). The resurgence of covalent drugs. Nat Rev Drug Discov 10:307–17
   PubMed Web of Science ®Google Scholar
• Singh J, Petter RC, Kluge AF. (2010). Targeted covalent drugs of the kinase family. Curr Opin Chem Biol 14:475–80
   PubMed Web of Science ®Google Scholar
• Sondhi D, Xu W, Songyang Z, et al. (1998). Peptide and protein phosphorylation by protein tyrosine kinase Csk: insights into specificity and mechanism. Biochemistry 37:165–72
   PubMed Web of Science ®Google Scholar
• St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD. (2002). Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277:44784–90
   PubMed Web of Science ®Google Scholar
• Stambolic V, Suzuki A, De La Pompa JL, et al. (1998). Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell 95:29–39
   PubMed Web of Science ®Google Scholar
• Stockler-Ipsiroglu S. (1997). Creatine deficiency syndromes: a new perspective on metabolic disorders and a diagnostic challenge. J Pediatr 131:510–11
   Google Scholar
• Stokoe D, Stephens LR, Copeland T, et al. (1997). Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B. Science 277:567–70
   PubMed Web of Science ®Google Scholar
• Stone JR, Yang S. (2006). Hydrogen peroxide: a signaling messenger. Antioxid Redox Signal 8:243–70
   PubMed Web of Science ®Google Scholar
• Suh YA, Arnold RS, Lassegue B, et al. (1999). Cell transformation by the superoxide-generating oxidase Mox1. Nature 401:79–82
   PubMed Web of Science ®Google Scholar
• Sun G, Kemble DJ. (2009). To C or not to C: direct and indirect redox regulation of Src protein tyrosine kinase. Cell Cycle 8:2353–5
   PubMed Web of Science ®Google Scholar
• Sundaresan M, Yu ZX, Ferrans VJ, et al. (1995). Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270:296–9
   PubMed Web of Science ®Google Scholar
• Sundaresan M, Yu ZX, Ferrans VJ, et al. (1996). Regulation of reactive-oxygen-species generation in fibroblasts by Rac1. Biochem J 318:379–82
   PubMed Web of Science ®Google Scholar
• Switzer CH, Glynn SA, Cheng RY, et al. (2012). S-Nitrosylation of EGFR and Src activates an oncogenic signaling network in human basal-like breast cancer. Mol Cancer Res 10:1203–15
   Google Scholar
• Tang H, Hao Q, Rutherford SA, et al. (2005). Inactivation of SRC family tyrosine kinases by reactive oxygen species in vivo. J Biol Chem 280:23918–25
   PubMed Web of Science ®Google Scholar
• Taylor SS, Knighton DR, Zheng J, et al. (1992). Structural framework for the protein kinase family. Annu Rev Cell Biol 8:429–62
   PubMedGoogle Scholar
• Templeton DJ, Aye MS, Rady J, et al. (2010). Purification of reversibly oxidized proteins (PROP) reveals a redox switch controlling p38 MAP kinase activity. PLoS One 5:e15012
   PubMed Web of Science ®Google Scholar
• Thannickal VJ, Day RM, Klinz SG, et al. (2000). Ras-dependent and -independent regulation of reactive oxygen species by mitogenic growth factors and TGF-beta1. FASEB J 14:1741–8
   PubMed Web of Science ®Google Scholar
• Thomas SM, Brugge JS. (1997). Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol 13:513–609
   PubMed Web of Science ®Google Scholar
• Truong TH, Carroll KS. (2012). Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation. Biochemistry 51:9954–65
   PubMed Web of Science ®Google Scholar
• Truong TH, Garcia FJ, Seo YH, Carroll KS. (2011). Isotope-coded chemical reporter and acid-cleavable affinity reagents for monitoring protein sulfenic acids. Bioorg Med Chem Lett 21:5015–20
   PubMed Web of Science ®Google Scholar
• Turner N, Grose R. (2010). Fibroblast growth factor signalling: from development to cancer. Nat Rev Cancer 10:116–29
   PubMed Web of Science ®Google Scholar
• Ueki K, Yamamoto-Honda R, Kaburagi Y, et al. (1998). Potential role of protein kinase B in insulin-induced glucose transport, glycogen synthesis, and protein synthesis. J Biol Chem 273:5315–22
   PubMed Web of Science ®Google Scholar
• Ushio-Fukai M. (2006). Localizing NADPH oxidase-derived ROS. Sci STKE 2006:re8
   PubMedGoogle Scholar
• Ushio-Fukai M. (2007). VEGF signaling through NADPH oxidase-derived ROS. Antioxid Redox Signal 9:731–9
   Google Scholar
• Ushio-Fukai M, Alexander RW, Akers M, Griendling KK. (1998). p38 Mitogen-activated protein kinase is a critical component of the redox-sensitive signaling pathways activated by angiotensin II. Role in vascular smooth muscle cell hypertrophy. J Biol Chem 273:15022–9
   PubMed Web of Science ®Google Scholar
• Ushio-Fukai M, Alexander RW, Akers M, et al. (1999). Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells. J Biol Chem 274:22699–704
   PubMed Web of Science ®Google Scholar
• Ushio-Fukai M, Griendling KK, Becker PL, et al. (2001). Epidermal growth factor receptor transactivation by angiotensin II requires reactive oxygen species in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 21:489–95
   PubMed Web of Science ®Google Scholar
• Ushio-Fukai M, Tang Y, Fukai T, et al. (2002). Novel role of gp91(phox)-containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis. Circ Res 91:1160–7
   PubMed Web of Science ®Google Scholar
• Van der Kaay J, Beck M, Gray A, Downes CP. (1999). Distinct phosphatidylinositol 3-kinase lipid products accumulate upon oxidative and osmotic stress and lead to different cellular responses. J Biol Chem 274:35963–8
   PubMed Web of Science ®Google Scholar
• Veal EA, Findlay VJ, Day AM, et al. (2004). A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase. Mol Cell 15:129–39
   PubMed Web of Science ®Google Scholar
• Vivanco I, Rohle D, Versele M, et al. (2010). The phosphatase and tensin homolog regulates epidermal growth factor receptor (EGFR) inhibitor response by targeting EGFR for degradation. Proc Natl Acad Sci USA 107:6459–64
   PubMed Web of Science ®Google Scholar
• Wagner EF, Nebreda AR. (2009). Signal integration by JNK and p38 MAPK pathways in cancer development. Nat Rev Cancer 9:537–49
   PubMed Web of Science ®Google Scholar
• Wang X, Martindale JL, Liu Y, Holbrook NJ. (1998). The cellular response to oxidative stress: influences of mitogen-activated protein kinase signalling pathways on cell survival. Biochem J 333:291–300
   PubMed Web of Science ®Google Scholar
• Wang X, Mccullough KD, Franke TF, Holbrook NJ. (2000). Epidermal growth factor receptor-dependent Akt activation by oxidative stress enhances cell survival. J Biol Chem 275:14624–31
   PubMed Web of Science ®Google Scholar
• Wani R, Qian J, Yin L, et al. (2011). Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species. Proc Natl Acad Sci USA 108:10550–5
   PubMed Web of Science ®Google Scholar
• Wilden PA, Pessin JE. (1987). Differential sensitivity of the insulin-receptor kinase to thiol and oxidizing agents in the absence and presence of insulin. Biochem J 245:325–31
   PubMedGoogle Scholar
• Winterbourn CC. (2008). Reconciling the chemistry and biology of reactive oxygen species. Nat Chem Biol 4:278–86
   PubMed Web of Science ®Google Scholar
• Winterbourn CC, Metodiewa D. (1999). Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med 27:322–8
   PubMed Web of Science ®Google Scholar
• Woltjer RL, Staros JV. (1997). Effects of sulfhydryl modification reagents on the kinase activity of the epidermal growth factor receptor. Biochemistry 36:9911–16
   Google Scholar
• Woo HA, Yim SH, Shin DH, et al. (2010). Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. Cell 140:517–28
   PubMed Web of Science ®Google Scholar
• Wortzel I, Seger R. (2011). The ERK cascade: distinct functions within various subcellular organelles. Genes Cancer 2:195–209
   PubMedGoogle Scholar
• Xu W, Harrison SC, Eck MJ. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385:595–602
   PubMed Web of Science ®Google Scholar
• Yamaoka-Tojo M, Tojo T, Kim HW, et al. (2006). IQGAP1 mediates VE-cadherin-based cell--cell contacts and VEGF signaling at adherence junctions linked to angiogenesis. Arterioscler Thromb Vasc Biol 26:1991–7
   Google Scholar
• Yamaoka-Tojo M, Ushio-Fukai M, Hilenski L, et al. (2004). IQGAP1, a novel vascular endothelial growth factor receptor binding protein, is involved in reactive oxygen species–dependent endothelial migration and proliferation. Circ Res 95:276–83
   PubMed Web of Science ®Google Scholar
• Yarden Y, Sliwkowski MX. (2001). Untangling the ErbB signalling network. Nat Rev Mol Cell Biol 2:127–37
   PubMed Web of Science ®Google Scholar
• Yasukawa T, Tokunaga E, Ota H, et al. (2005). S-nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance. J Biol Chem 280:7511–18
   PubMed Web of Science ®Google Scholar
• Yeatman TJ. (2004). A renaissance for SRC. Nat Rev Cancer 4:470–80
   PubMed Web of Science ®Google Scholar
• Yellaturu CR, Bhanoori M, Neeli I, Rao GN. (2002). N-Ethylmaleimide inhibits platelet-derived growth factor BB-stimulated Akt phosphorylation via activation of protein phosphatase 2A. J Biol Chem 277:40148–55
   Google Scholar
• Yoo SK, Starnes TW, Deng Q, Huttenlocher, A. (2011). Lyn is a redox sensor that mediates leukocyte wound attraction in vivo. Nature 480:109–12
   PubMed Web of Science ®Google Scholar
• Yoshizumi M, Abe J, Haendeler J, et al. (2000). Src and Cas mediate JNK activation but not ERK1/2 and p38 kinases by reactive oxygen species. J Biol Chem 275:11706–12
   PubMed Web of Science ®Google Scholar
• Youngren JF. (2007). Regulation of insulin receptor function. Cell Mol Life Sci 64:873–91
   PubMed Web of Science ®Google Scholar
• Zhang T, Inesta-Vaquera F, Niepel M, et al. (2012). Discovery of potent and selective covalent inhibitors of JNK. Chem Biol 19:140–54
   PubMed Web of Science ®Google Scholar
• Zhang ZY, Dixon JE. (1993). Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402. Biochemistry 32:9340–5
   PubMed Web of Science ®Google Scholar