Principles in redox signaling: From chemistry to functional significance

Antioxidants and Redox Signaling

Volumn 18, Issue 13, 2013, Pages 1557-1593

  Bindoli, Alberto ^a   Rigobello, Maria Pia ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE PEROXIDASE 3; GUANYLATE CYCLASE; HYDROGEN PEROXIDE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; OXYR PROTEIN; PEROXIREDOXIN; PHOSPHATASE; PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SINGLET OXYGEN; SULFENIC ACID DERIVATIVE; SULFINIC ACID DERIVATIVE; SULFONIC ACID DERIVATIVE; SUPEROXIDE; SUPEROXIDE DISMUTASE; THIOL; THIOREDOXIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; XANTHINE DEHYDROGENASE; XANTHINE OXIDASE;

AMINO ACID SEQUENCE; APOPTOSIS; AUTOPHAGY; CATALYSIS; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; FENTON REACTION; GENE EXPRESSION; HUMAN; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PH; PHAGOCYTE; PRIORITY JOURNAL; PROTEIN FOLDING; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; HUMANS; OXIDATION-REDUCTION; PEROXIDES; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN SPECIES; SIGNAL TRANSDUCTION; THIOREDOXINS;

EID: 84875716554     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4655     Document Type: Review

References (383)

1. Al Ghouleh I, Khoo NKH, Knaus UG, Griendling KK, Touyz RM, Thannickal VJ, Barchowsky A, Nauseef WM, Kelley EE, Bauer PM, Darley-Usmar V, Shiva S, Cifuentes-Pagano E, Freeman BA, Gladwin MT, and Pagano PJ. Oxidases and peroxidases in cardiovascular and lung disease: new concepts in reactive oxygen species signaling. Free Radic Biol Med 51: 1271-1288, 2011.
2. Allison WS. Formation and reactions of sulfenic acids in proteins. Acc Chem Res 9: 293-299, 1976.
3. Alvarez B and Radi R. Peroxynitrite reactivity with amino acids and proteins. Amino Acids 25: 295-311, 2003. (Pubitemid 38041267)
4. 2-generating activity. J Biol Chem 280: 30046-30054, 2005. (Pubitemid 41216180)
5. Andreyev AY, Kushnareva YE, and Starkov AA. Mitochondrial metabolism of reactive oxygen species. Biochemistry (Moscow) 70: 200-214, 2005. (Pubitemid 40512329)
6. Anesta l K, Prast-Nielsen S, Cenas N, and Arnér ESJ. Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells. PLoS One 3: e1846, 2008.
7. 2 gradients across biomembranes. FEBS Lett 475: 121-126, 2000. (Pubitemid 30365063)
8. Appenzeller-Herzog C. Glutathione-and non-glutathionebased oxidant control in the endoplasmic reticulum. J Cell Sci 124: 847-855, 2011.
9. Arnér ESJ. Focus on mammalian thioredoxin reductases-Important selenoproteins with versatile functions. Biochim Biophys Acta 1790: 495-526, 2009.
10. Aslund F, Zheng M, Beckwith J, and Storz G. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci U S A 96: 6161-6165, 1999. (Pubitemid 29256636)
11. Awasthi YC, Yang Y, Tiwari NK, Patrick B, Sharma A, Li J, and Awasthi S. Regulation of 4-hydroxynonenal-mediated signaling by glutathione S-transferases. Free Radic Biol Med 37: 607-619, 2004. (Pubitemid 38993509)
12. Backos DS, Franklin CC, and Reigan P. The role of glutathione in brain tumor drug resistance. Biochem Pharmacol 83: 1005-1012, 2012.
13. Bae YS, Kang SW, Seo MS, Baines IC, Tekle E, Chock PB, and Rhee SG. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem 272: 217-221, 1997. (Pubitemid 27021147)
14. Baines CP, Kaiser RA, Purcell NH, Blair NS, Osinska H, Hambleton MA, Brunskill EW, Sayen MR, Gottlieb RA, Dorn GW, Robbins J, and Molkentin JD. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434: 658-662, 2005. (Pubitemid 40488559)
15. Baird L and Dinkova-Kostova AT. The cytoprotective role of the Keap1-Nrf2 pathway. Arch Toxicol 85: 241-272, 2011.
16. 2+ -activated NADPH oxidase in testis, spleen, and lymph nodes. J Biol Chem 276: 37594-37601, 2001.
17. Barrett WC, DeGnore JP, Keng YF, Zhang ZY, Yim MB, and Chock PB. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of proteintyrosine phosphatase 1B. J Biol Chem 274: 34543-34546, 1999. (Pubitemid 129509489)
18. Barrett WC, DeGnore JP, Konig S, Fales HM, Keng YF, Zhang ZY, Yim MB, and Chock PB. Regulation of PTP1B via glutathionylation of the active site cysteine 215. Biochemistry 38: 6699-6705, 1999.
19. Beck CF. Signaling pathways from the chloroplast to the nucleus. Planta 222: 743-756, 2005. (Pubitemid 41660821)
20. Bedard K and Krause KH. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87: 245-313, 2007. (Pubitemid 46209993)
21. Beer SM, Taylor ER, Brown SE, Dahm CC, Costa NJ, Runswick MJ, and Murphy MP. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins. Implications for mitochondrial redox regulation and antioxidant defense. J Biol Chem 279: 47939-47951, 2004. (Pubitemid 39540945)
22. Bell EL, Klimova TA, Eisenbart J, Moraes CT, Murphy MP, Budinger GRS, and Chandel NS. The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production. J Cell Biol 177: 1029-1036, 2007. (Pubitemid 46955707)
23. Benhar M, Forrester MT, Hess DT, and Stamler JS. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320: 1050-1054, 2008. (Pubitemid 351929542)
24. Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol Rev 79: 1127-1155, 1999. (Pubitemid 29473313)
25. Berndt C, Lillig CH, and Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol 292: H1227-H1236, 2007. (Pubitemid 46377107)
26. Berners-Price SJ and Filipovska A. Gold compounds as therapeutic agents for human diseases. Metallomics 3: 863-873, 2011.
27. Berra E, Benizri E, Ginouves A, Volmat V, Roux D, and Pouyssegur J. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J 22: 4082-4090, 2003. (Pubitemid 37021737)
28. Bienert GP, Møller AL, Kristiansen KA, Schulz A, Møller IM, Schjoerring JK, and Jahn TP. Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes. J Biol Chem 282: 1183-1192, 2007. (Pubitemid 47076557)
29. Bienert GP, Schjoerring JK, and Jahn TP. Membrane transport of hydrogen peroxide. Biochim Biophys Acta 1758: 994-1003, 2006. (Pubitemid 44373854)
30. Bindoli A, Callegaro MT, Barzon E, Benetti M, and Rigobello MP. Influence of the redox state of pyridine nucleotides on mitochondrial sulfhydryl groups and permeability transition. Arch Biochem Biophys 342: 22-28, 1997. (Pubitemid 27217098)
31. Bindoli A, Cavallini L, Rigobello MP, Coassin M, and Di Lisa F. Modification of the xanthine-converting enzyme of perfused rat heart during ischemia and oxidative stress. Free Radic Biol Med 4: 163-167, 1988. (Pubitemid 18052531)
32. Bindoli A, Deeble DJ, Rigobello MP, and Galzigna L. Direct and respiratory chain-mediated redox cycling of adrenochrome. Biochim Biophys Acta 1016: 349-356, 1990.
33. 2+ release in skeletal muscle sarcoplasmic reticulum by sulfhydryl reagents and chlorpromazine. Arch Biochem Biophys 221: 458-466, 1983. (Pubitemid 13135507)
34. Bindoli A, Fukuto JM, and Forman HJ. Thiol chemistry in peroxidase catalysis and redox signaling. Antioxid Redox Signal 10: 1549-1564, 2008. (Pubitemid 351931936)
35. Bindoli A, Rigobello MP, and Deeble DJ. Biochemical and toxicological properties of the oxidation products of catecholamines. Free Radic Biol Med 13: 391-405, 1992.
36. Bindoli A, Rigobello MP, Scutari G, Gabbiani C, Casini A, and Messori L. Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs. Coordin Chem Rev 253: 1692-1707, 2009.
37. Biswas SK and Rahman I. Environmental toxicity, redox signaling and lung inflammation: the role of glutathione. Mol Aspects Med 30: 60-76, 2009.
38. Biteau B, Labarre J, and Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425: 980-984, 2003. (Pubitemid 37376931)
39. Block K, Gorin Y, and Abboud HE. Subcellular localization of Nox4 and regulation in diabetes. Proc Natl Acad Sci U S A 106: 14385-14390, 2009.
40. Bloom D, Dhakshinamoorthy S, and Jaiswal AK. Sitedirected mutagenesis of cysteine to serine in the DNA binding region of Nrf2 decreases its capacity to upregulate antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase1 gene. Oncogene 21: 2191-2200, 2002. (Pubitemid 34311373)
41. Bragadin M, Scutari G, Folda A, Bindoli A, and Rigobello MP. Effect of metal complexes on thioredoxin reductase and the regulation of mitochondrial permeability conditions. Ann N Y Acad Sci 1030: 348-354, 2004. (Pubitemid 40378932)
42. Brand MD. The sites and topology of mitochondrial superoxide production. Exp Gerontol 45: 466-472, 2010.
43. Brigelius-Flohé R. Tissue-specific functions of individual glutathione peroxidases. Free Radic Biol Med 27: 951-965, 1999. (Pubitemid 29507469)
44. Brigelius-Flohé R and Banning A. Part of the series: from dietary antioxidants to regulators in cellular signaling and gene regulation. Sulforaphane and selenium, partners in adaptive response and prevention of cancer. Free Radic Res 40: 775-787, 2006. (Pubitemid 44480488)
45. Brigelius-Flohé R and Flohé L. Basic principles and emerging concepts in the redox control of transcription factors. Antioxid Redox Signal 15: 2335-2381, 2011.
46. Brigelius-Flohé R, Müller M, Lippmann D, and Kipp AP. The yin and yang of nrf2-regulated selenoproteins in carcinogenesis. Int J Cell Biol 2012: 486147, 2012.
47. Briviba K, Kissner R, Koppenol WH, and Sies H. Kinetic study of the reaction of glutathione peroxidase with peroxynitrite. Chem Res Toxicol 11: 1398-1401, 1998. (Pubitemid 29013611)
48. Broniowska KA and Hogg N. The chemical biology of Snitrosothiols. Antioxid Redox Signal 17: 969-980, 2012.
49. Broniowska KA, Keszler A, Basu S, Kim-Shapiro DB, and Hogg N. Cytochrome c-mediated formation of S-nitrosothiol in cells. Biochem J 442: 191-197, 2012.
50. Brown GC and Borutaite V. There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells. Mitochondrion 12: 1-4, 2012.
51. Brown KK, Cox AG, and Hampton MB. Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin. FEBS Lett 584: 1257-1262, 2010.
52. Bryk R, Griffin P, and Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407: 211-215, 2000.
53. Bulleid NJ and Ellgaard L. Multiple ways to make disulfides. Trends Biochem Sci 36: 485-492, 2011.
54. Cadenas E. Mitochondrial free radical production and cell signaling. Mol Aspects Med 25: 17-26, 2004. (Pubitemid 38401928)
55. Cai W, Zhang L, Song Y, Wang B, Zhang B, Cui X, Hu G, Liu Y, Wu J, and Fang J. Small molecule inhibitors of mammalian thioredoxin reductase. Free Radic Biol Med 52: 257-265, 2012.
56. Casagrande S, Bonetto V, Fratelli M, Gianazza E, Eberini I, Massignan T, Salmona M, Chang G, Holmgren A, and Ghezzi P. Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems. Proc Natl Acad Sci U S A 99: 9745-9749, 2002. (Pubitemid 34831118)
57. Cash TP, Pan Y, and Simon MC. Reactive oxygen species and cellular oxygen sensing. Free Radic Biol Med 43: 1219-1225, 2007. (Pubitemid 47429935)
58. Cederbaum AI. Cytochrome P450 2E1-dependent oxidant stress and upregulation of anti-oxidant defense in liver cells. J Gastroenterol Hepatol 21 Suppl 3: S22-S25, 2006. (Pubitemid 44266544)
59. Chakravarthi S, Jessop CE, and Bulleid NJ. The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress. EMBO Rep 7: 271-275, 2006.
60. Chance B, Sies H, and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 59: 527-605, 1979. (Pubitemid 9236599)
61. Chen C and Kong AN. Dietary chemopreventive compounds and ARE/EpRE signaling. Free Radic Biol Med 36: 1505-1516, 2004. (Pubitemid 38746559)
62. Chen Y, Cai J, and Jones DP. Mitochondrial thioredoxin in regulation of oxidant-induced cell death. FEBS Lett 580: 6596-6602, 2006. (Pubitemid 44830129)
63. Cheng Q, Sandalova T, Lindqvist Y, and Arnér ESJ. Crystal structure and catalysis of the selenoprotein thioredoxin reductase. J Biol Chem 284: 3998-4008, 2009.
64. Chernyak BV and Bernardi P. The mitochondrial permeability transition pore is modulated by oxidative agents through both pyridine nucleotides and glutathione at two separate sites. Eur J Biochem 238: 623-630, 1996. (Pubitemid 26235100)
65. Chiarugi P. PTPs versus PTKs: the redox side of the coin. Free Radic Res 39: 353-364, 2005. (Pubitemid 40613714)
66. Chung YM, Kim JS, and Yoo YD. A novel protein, Romo1, induces ROS production in the mitochondria. Biochem Biophys Res Commun 347: 649-655, 2006. (Pubitemid 44109674)
67. Claiborne A, Miller H, Parsonage D, and Ross RP. Proteinsulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J 7: 1483-1490, 1993. (Pubitemid 24003268)
68. Connern CP and Halestrap AP. Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel. Biochem J 302 (Pt 2): 321-324, 1994. (Pubitemid 24280079)
69. Conrad M. Transgenic mouse models for the vital selenoenzymes cytosolic thioredoxin reductase, mitochondrial thioredoxin reductase and glutathione peroxidase 4. Biochim Biophys Acta 1790: 1575-1585, 2009.
70. Conrad M, Jakupoglu C, Moreno SG, Lippl S, Banjac A, Schneider M, Beck H, Hatzopoulos AK, Just U, Sinowatz F, Schmahl W, Chien KR, Wurst W, Bornkamm GW, and Brielmeier M. Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function. Mol Cell Biol 24: 9414-9423, 2004. (Pubitemid 39391679)
71. Conrad M, Sandin A, Forster H, Seiler A, Frijhoff J, Dagnell M, Bornkamm GW, Radmark O, Hooft van Huijsduijnen R, Aspenström P, Böhmer F, and Östman A. 12/15-lipoxygenasederived lipid peroxides control receptor tyrosine kinase signaling through oxidation of protein tyrosine phosphatases. Proc Natl Acad Sci U S A 107: 15774-15779, 2010.
72. Coppock DL and Thorpe C. Multidomain flavin-dependent sulfhydryl oxidases. Antioxid Redox Signal 8: 300-311, 2006. (Pubitemid 43741301)
73. Costa VM, Carvalho F, Bastos ML, Carvalho RA, Carvalho M, and Remiao F. Contribution of catecholamine reactive intermediates and oxidative stress to the pathologic features of heart diseases. Curr Med Chem 18: 2272-2314, 2011.
74. Costantini P, Belzacq AS, Vieira HL, Larochette N, de Pablo MA, Zamzami N, Susin SA, Brenner C, and Kroemer G. Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene 19: 307-314, 2000. (Pubitemid 30077228)
75. Costantini P, Chernyak BV, Petronilli V, and Bernardi P. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J Biol Chem 271: 6746-6751, 1996. (Pubitemid 26104106)
76. Cox AG, Brown KK, Arner ESJ, and Hampton MB. The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation. Biochem Pharmacol 76: 1097-1109, 2008.
77. Cuozzo JW and Kaiser CA. Competition between glutathione and protein thiols for disulphide-bond formation. Nat Cell Biol 1: 130-135, 1999. (Pubitemid 129656016)
78. D'Autréaux B and Toledano MB. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 8: 813-824, 2007. (Pubitemid 47462134)
79. Daiber A. Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species. Biochim Biophys Acta 1797: 897-906, 2010.
80. Dalle-Donne I, Colombo G, Gagliano N, Colombo R, Giustarini D, Rossi R, and Milzani A. S-glutathiolation in life and death decisions of the cell. Free Radic Res 45: 3-15, 2011.
81. Dalle-Donne I, Milzani A, Gagliano N, Colombo R, Giustarini D, and Rossi R. Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid Redox Signal 10: 445-473, 2008.
82. Damdimopoulos AE, Miranda-Vizuete A, Pelto-Huikko M, Gustafsson JA, and Spyrou G. Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death. J Biol Chem 277: 33249-33257, 2002. (Pubitemid 34984845)
83. Davis FA, Jenkins LA, and Billmers RL. Chemistry of sulfenic acids.7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogenbonding and electronegativity effects. J Org Chem 51: 1033-1040, 1986.
84. 2-generating system. Exp Cell Res 273: 187-196, 2002. (Pubitemid 34920669)
85. 2 receptor and redoxtransducer in gene activation. Cell 111: 471-481, 2002. (Pubitemid 35356554)
86. Della Corte E and Stirpe F. The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem J 126: 739-745, 1972.
87. Denu JM and Tanner KG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37: 5633-5642, 1998. (Pubitemid 28241948)
88. DeYulia GJ, Jr., Cárcamo JM, Bórquez-Ojeda O, Shelton CC, and Golde DW. Hydrogen peroxide generated extracellularly by receptor-ligand interaction facilitates cell signaling. Proc Natl Acad Sci U S A 102: 5044-5049, 2005.
89. Dickinson DA and Forman HJ. Cellular glutathione and thiols metabolism. Biochem Pharmacol 64: 1019-1026, 2002. (Pubitemid 35238033)
90. Dikalov S. Cross talk between mitochondria and NADPH oxidases. Free Radic Biol Med 51: 1289-1301, 2011.
91. Dinkova-Kostova AT, Holtzclaw WD, Cole RN, Itoh K, Wakabayashi N, Katoh Y, Yamamoto M, and Talalay P. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc Natl Acad Sci U S A 99: 11908-11913, 2002. (Pubitemid 34994497)
92. Ellis HR and Poole LB. Novel application of 7-chloro-4-nitrobenzo-2-oxa- 1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry 36: 15013-15018, 1997. (Pubitemid 27524428)
93. Epstein ACR, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, Mole DR, Mukherji M, Metzen E, Wilson MI, Dhanda A, Tian YM, Masson N, Hamilton DL, Jaakkola P, Barstead R, Hodgkin J, Maxwell PH, Pugh CW, Schofield CJ, and Ratcliffe PJ. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107: 43-54, 2001. (Pubitemid 32972036)
94. Esworthy RS, Ho YS, and Chu FF. The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver. Arch Biochem Biophys 340: 59-63, 1997. (Pubitemid 27200274)
95. Faccio G, Nivala O, Kruus K, Buchert J, and Saloheimo M. Sulfhydryl oxidases: sources, properties, production and applications. Appl Microbiol Biotechnol 91: 957-966, 2011.
96. Fang J, Lu J, and Holmgren A. Thioredoxin reductase is irreversibly modified by curcumin: a novel molecularmechanism for its anticancer activity. J Biol Chem 280: 25284-25290, 2005. (Pubitemid 40934623)
97. Fass D. Hunting for alternative disulfide bond formation pathways: endoplasmic reticulum janitor turns professor and teaches a lesson. Mol Cell 40: 685-686, 2010.
98. Ferrer-Sueta G, Manta B, Botti H, Radi R, Trujillo M, and Denicola A. Factors affecting protein thiol reactivity and specificity in peroxide reduction. Chem Res Toxicol 24: 434-450, 2011.
99. Ferrer-Sueta G and Radi R. Chemical biology of peroxynitrite: kinetics, diffusion, and radicals. ACS Chem Biol 4: 161-177, 2009.
100. Fill M and Copello JA. Ryanodine receptor calcium release channels. Physiol Rev 82: 893-922, 2002.
101. Filomeni G, Rotilio G, and Ciriolo MR. Disulfide relays and phosphorylative cascades: partners in redox-mediated signaling pathways. Cell Death Differ 12: 1555-1563, 2005. (Pubitemid 41679161)
102. Finkel T. Oxygen radicals and signaling. Curr Opin Cell Biol 10: 248-253, 1998. (Pubitemid 28174767)
103. Finkel T. Redox-dependent signal transduction. FEBS Lett 476: 52-54, 2000. (Pubitemid 30394649)
104. Finkel T. Signal transduction by mitochondrial oxidants. J Biol Chem 287: 4434-4440, 2012.
105. Flohé L. Changing paradigms in thiology from antioxidant defense toward redox regulation. Methods Enzymol 473: 1-39, 2010.
106. Flohé L, Brigelius-Flohé R, Saliou C, Traber MG, and Packer L. Redox regulation of NF-kappa B activation. Free Radic Biol Med 22: 1115-1126, 1997. (Pubitemid 27084148)
107. Flohé L, Toppo S, Cozza G, and Ursini F. A comparison of thiol peroxidase mechanisms. Antioxid Redox Signal 15: 763-780, 2011.
108. 2 in studies of signal transduction. Free Radic Biol Med 42: 926-932, 2007. (Pubitemid 46356902)
109. Forman HJ and Fridovich I. Superoxide dismutase: a comparison of rate constants. Arch Biochem Biophys 158: 396-400, 1973.
110. Forman HJ, Fukuto JM, Miller T, Zhang H, Rinna A, and Levy S. The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal. Arch Biochem Biophys 477: 183-195, 2008.
111. Forman HJ, Fukuto JM, and Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 287: C246-C256, 2004. (Pubitemid 38955213)
112. Forman HJ and Kennedy JA. Role of superoxide radical in mitochondrial dehydrogenase reactions. Biochem Biophys Res Commun 60: 1044-1050, 1974.
113. Forman HJ, Maiorino M, and Ursini F. Signaling functions of reactive oxygen species. Biochemistry 49: 835-842, 2010.
114. Foster DB, Van Eyk JE, Marbán E, and O'Rourke B. Redox signaling and protein phosphorylation in mitochondria: progress and prospects. J Bioenerg Biomembr 41: 159-168, 2009.
115. 2 involves KEAP1 disulfide formation. J Biol Chem 285: 8463-8471, 2010.
116. 2 scavenging and signaling. Antioxid Redox Signal 10: 1565-1576, 2008.
117. Fraga CG and Oteiza PI. Dietary flavonoids: Role of (-)-epicatechin and related procyanidins in cell signaling. Free Radic Biol Med 51: 813-823, 2011.
118. Fransen M, Nordgren M, Wang B, and Apanasets O. Role of peroxisomes in ROS/RNS-metabolism: Implications for human disease. Biochim Biophys Acta 1822: 1363-1373, 2012.
119. Fratelli M, Demol H, Puype M, Casagrande S, Villa P, Eberini I, Vandekerckhove J, Gianazza E, and Ghezzi P. Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells. Proteomics 3: 1154-1161, 2003. (Pubitemid 36929537)
120. Fridovich I. Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J Biol Chem 245: 4053-4057, 1970.
121. Fridovich I. The biology of oxygen radicals. Science 201: 875-880, 1978.
122. Friesen C, Kiess Y, and Debatin KM. A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells. Cell Death Differ 11 Suppl 1: S73-S85, 2004. (Pubitemid 39136800)
123. Fujimoto M and Hayashi T. New insights into the role of mitochondria-associated endoplasmic reticulum membrane. Int Rev Cell Mol Biol 292: 73-117, 2011.
124. Geiszt M and Leto TL. The Nox family of NAD(P)H oxidases: host defense and beyond. J Biol Chem 279: 51715-51718, 2004. (Pubitemid 39656535)
125. Gertz M and Steegborn C. The lifespan-regulator p66Shc in mitochondria: redox enzyme or redox sensor? Antioxid Redox Signal 13: 1417-1428, 2010.
126. Giannoni E, Buricchi F, Raugei G, Ramponi G, and Chiarugi P. Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchoragedependent cell growth. Mol Cell Biol 25: 6391-6403, 2005. (Pubitemid 41023216)
127. Giorgio M, Migliaccio E, Orsini F, Paolucci D, Moroni M, Contursi C, Pelliccia G, Luzi L, Minucci S, Marcaccio M, Pinton P, Rizzuto R, Bernardi P, Paolucci F, and Pelicci PG. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 122: 221-233, 2005. (Pubitemid 41032986)
128. Giorgio M, Trinei M, Migliaccio E, and Pelicci PG. Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? Nat Rev Mol Cell Biol 8: 722-728, 2007. (Pubitemid 47312827)
129. Girotti AW. Translocation as a means of disseminating lipid hydroperoxide-induced oxidative damage and effector action. Free Radic Biol Med 44: 956-968, 2008.
130. Girotti AW and Kriska T. Role of lipid hydroperoxides in photo-oxidative stress signaling. Antioxid Redox Signal 6: 301-310, 2004. (Pubitemid 38332587)
131. Gitler C, Zarmi B, Kalef E, Meller R, Zor U, and Goldman R. Calcium-dependent oxidation of thioredoxin during cellular growth initiation. Biochem Biophys Res Commun 290: 624-628, 2002. (Pubitemid 34687485)
132. Gloire G, Legrand-Poels S, and Piette J. NF-jB activation by reactive oxygen species: fifteen years later. Biochem Pharmacol 72: 1493-1505, 2006. (Pubitemid 44666727)
133. Go YM and Jones DP. Redox compartmentalization in eukaryotic cells. Biochim Biophys Acta 1780: 1273-1290, 2008.
134. Go YM and Jones DP. Redox control systems in the nucleus: mechanisms and functions. Antioxid Redox Signal 13: 489-509, 2010.
135. Goossens V, De Vos K, Vercammen D, Steemans M, Vancompernolle K, Fiers W, Vandenabeele P, and Grooten J. Redox regulation of TNF signaling. Biofactors 10: 145-156, 1999. (Pubitemid 29533823)
136. Goto K, Holler M, and Okazaki R. Synthesis, structure, and reactions of a sulfenic acid bearing a novel bowl-type substituent: the first synthesis of a stable sulfenic acid by direct oxidation of a thiol. J Am Chem Soc 119: 1460-1461, 1997. (Pubitemid 27122079)
137. Gow AJ, Buerk DG, and Ischiropoulos H. A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J Biol Chem 272: 2841-2845, 1997. (Pubitemid 27053331)
138. Graham KA, Kulawiec M, Owens KM, Li X, Desouki MM, Chandra D, and Singh KK. NADPH oxidase 4 is an oncoprotein localized to mitochondria. Cancer Biol Ther 10: 223-231, 2010.
139. Gromer S, Arscott LD, Williams CH, Jr., Schirmer RH, and Becker K. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem 273: 20096-20101, 1998. (Pubitemid 28377564)
140. Gromer S, Urig S, and Becker K. The thioredoxin system-From science to clinic. Med Res Rev 24: 40-89, 2004.
141. Guengerich FP. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem Res Toxicol 14: 611-650, 2001. (Pubitemid 32565712)
142. Guidot DM, Repine JE, Kitlowski AD, Flores SC, Nelson SK, Wright RM, and McCord JM. Mitochondrial respiration scavenges extramitochondrial superoxide anion via a nonenzymatic mechanism. J Clin Invest 96: 1131-1136, 1995.
143. Halestrap AP. What is the mitochondrial permeability transition pore? J Mol Cell Cardiol 46: 821-831, 2009.
144. 2+ -induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase. Biochem J 268: 153-160, 1990. (Pubitemid 20166664)
145. Hall A, Parsonage D, Poole LB, and Karplus PA. Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J Mol Biol 402: 194-209, 2010.
146. Halliwell B and Gutteridge JMC. Free Radicals in Biology and Medicine. New York: Oxford University Press, 2007, p.
147. Halvey PJ, Watson WH, Hansen JM, Go YM, Samali A, and Jones DP. Compartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling. Biochem J 386: 215-219, 2005. (Pubitemid 40343778)
148. Hanschmann EM, Lonn ME, Schutte LD, Funke M, Godoy JR, Eitner S, Hudemann C, and Lillig CH. Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3. J Biol Chem 285: 40699-40705, 2010.
149. Hansen JM, Watson WH, and Jones DP. Compartmentation of Nrf-2 redox control: regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1. Toxicol Sci 82: 308-317, 2004. (Pubitemid 39485343)
150. Hansen JM, Zhang H, and Jones DP. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic Biol Med 40: 138-145, 2006. (Pubitemid 41759411)
151. Hansen JM, Zhang H, and Jones DP. Mitochondrial thioredoxin-2 has a key role in determining tumor necrosis factor-a-induced reactive oxygen species generation, NF-jB activation, and apoptosis. Toxicol Sci 91: 643-650, 2006. (Pubitemid 43827316)
152. Hatahet F and Ruddock LW. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal 11: 2807-2850, 2009.
153. Hawkins BJ, Madesh M, Kirkpatrick CJ, and Fisher AB. Superoxide flux in endothelial cells via the chloride channel-3 mediates intracellular signaling. Mol Biol Cell 18: 2002-2012, 2007. (Pubitemid 46911353)
154. He M, Cai J, Go YM, Johnson JM, Martin WD, Hansen JM, and Jones DP. Identification of thioredoxin-2 as a regulator of the mitochondrial permeability transition. Toxicol Sci 105: 44-50, 2008.
155. Hell K. The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria. Biochim Biophys Acta 1783: 601-609, 2008.
156. Hess DT, Matsumoto A, Kim SO, Marshall HE, and Stamler JS. Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol 6: 150-166, 2005.
157. Hickey JL, Ruhayel RA, Barnard PJ, Baker MV, Berners-Price SJ, and Filipovska A. Mitochondria-targeted chemotherapeutics: the rational design of gold(I) N-heterocyclic carbene complexes that are selectively toxic to cancer cells and target protein selenols in preference to thiols. J Am Chem Soc 130: 12570-12571, 2008.
158. Hidalgo C and Donoso P. Crosstalk between calcium and redox signaling: from molecular mechanisms to health implications. Antioxid Redox Signal 10: 1275-1312, 2008. (Pubitemid 351634396)
159. Hidalgo C and Donoso P. Cell signaling. Getting to the heart of mechanotransduction. Science 333: 1388-1390, 2011.
160. Hill KE, McCollum GW, Boeglin ME, and Burk RF. Thioredoxin reductase activity is decreased by selenium deficiency. Biochem Biophys Res Commun 234: 293-295, 1997. (Pubitemid 27243893)
161. Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, and Yodoi J. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci U S A 94: 3633-3638, 1997. (Pubitemid 27180424)
162. Hobbs AJ. Soluble guanylate cyclase: the forgotten sibling. Trends Pharmacol Sci 18: 484-491, 1997.
163. Hoffstrom BG, Kaplan A, Letso R, Schmid RS, Turmel GJ, Lo DC, and Stockwell BR. Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins. Nat Chem Biol 6: 900-906, 2010.
164. Hogg DR. Chemistry of sulphenic acids and esters. In: The Chemistry of Sulphenic Acids and Their Derivatives, edited by Patai S. New York: John Wiley and Sons, 1990, pp. 361-402.
165. Holland R and Fishbein JC. Chemistry of the cysteine sensors in Kelch-like ECH-associated protein. Antioxid Redox Signal 13: 1749-1761, 2010.
166. Holmgren A. Thioredoxin. Annu Rev Biochem 54: 237-271, 1985. (Pubitemid 15073647)
167. Holmgren A and Lu J. Thioredoxin and thioredoxin reductase: current research with special reference to human disease. Biochem Biophys Res Commun 396: 120-124, 2010.
168. Holmgren A and Luthman M. Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay. Biochemistry 17: 4071-4077, 1978. (Pubitemid 9036527)
169. Hwang C, Sinskey AJ, and Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502, 1992.
170. Inarrea P, Moini H, Han D, Rettori D, Aguiló I, Alava MA, Iturralde M, and Cadenas E. Mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu, Zn-superoxide dismutase activity: implications for mitochondrial energy metabolism and apoptosis. Biochem J 405: 173-179, 2007. (Pubitemid 46999938)
171. In? arrea P, Moini H, Rettori D, Han D, Martínez J, García I, Fernández-Vizarra E, Iturralde M, and Cadenas E. Redox activation of mitochondrial intermembrane space Cu, Znsuperoxide dismutase. Biochem J 387: 203-209, 2005. (Pubitemid 40524090)
172. Ishii T, Mori T, Tanaka T, Mizuno D, Yamaji R, Kumazawa S, Nakayama T, and Akagawa M. Covalent modification of proteins by green tea polyphenol (-)-epigallocatechin-3-gallate through autoxidation. Free Radic Biol Med 45: 1384-1394, 2008.
173. Isogai Y, Iizuka T, and Shiro Y. The mechanism of electron donation to molecular oxygen by phagocytic cytochrome b558. J Biol Chem 270: 7853-7857, 1995.
174. Ivashchenko O, Van Veldhoven PP, Brees C, Ho YS, Terlecky SR, and Fransen M. Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk. Mol Biol Cell 22: 1440-1451, 2011.
175. Jacob C, Knight I, and Winyard PG. Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways. Biol Chem 387: 1385-1397, 2006. (Pubitemid 44691419)
176. Jakupoglu C, Przemeck GKH, Schneider M, Moreno SG, Mayr N, Hatzopoulos AK, de Angelis MH, Wurst W, Bornkamm GW, Brielmeier M, and Conrad M. Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development. Mol Cell Biol 25: 1980-1988, 2005. (Pubitemid 40280160)
177. Jäschke A, Mi H, and Tropschug M. Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity. J Mol Biol 277: 763-769, 1998. (Pubitemid 28195979)
178. Jeong W, Jung Y, Kim H, Park SJ, and Rhee SG. Thioredoxin-related protein 14, a new member of the thioredoxin family with disulfide reductase activity: Implication in the redox regulation of TNF-a signaling. Free Radic Biol Med 47: 1294-1303, 2009.
179. Jeong W, Park SJ, Chang TS, Lee DY, and Rhee SG. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J Biol Chem 281: 14400-14407, 2006. (Pubitemid 43848370)
180. Jewett SL, Eddy LJ, and Hochstein P. Is the autoxidation of catecholamines involved in ischemia-reperfusion injury? Free Radic Biol Med 6: 185-188, 1989. (Pubitemid 19054669)
181. Jocelyn PC. Biochemistry of the SH Group; the Occurrence, Chemical Properties, Metabolism and Biological Function of Thiols and Disulphides. London, NY: Academic Press, 1972, p.404
182. Johansson C, Lillig CH, and Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons fromeither glutathione or thioredoxin reductase. J Biol Chem 279: 7537-7543, 2004. (Pubitemid 38294632)
183. Jones DP. Redefining oxidative stress. Antioxid Redox Signal 8: 1865-1879, 2006. (Pubitemid 44726359)
184. Joseph SK, Nakao SK, and Sukumvanich S. Reactivity of free thiol groups in type-I inositol trisphosphate receptors. Biochem J 393: 575-582, 2006. (Pubitemid 43099097)
185. Kabe Y, Ando K, Hirao S, Yoshida M, and Handa H. Redox regulation of NF-jB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal 7: 395-403, 2005. (Pubitemid 40279807)
186. Kaludercic N, Carpi A, Menabò R, Di Lisa F, and Paolocci N. Monoamine oxidases (MAO) in the pathogenesis of heart failure and ischemia/reperfusion injury. Biochim Biophys Acta 1813: 1323-1332, 2011.
187. Kelley EE, Khoo NKH, Hundley NJ, Malik UZ, Freeman BA, and Tarpey MM. Hydrogen peroxide is the major oxidant product of xanthine oxidase. Free Radic Biol Med 48: 493-498, 2010.
188. Kensler TW and Wakabayashi N. Nrf2: friend or foe for chemoprevention? Carcinogenesis 31: 90-99, 2010.
189. Kensler TW, Wakabayashi N, and Biswal S. Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol 47: 89-116, 2007.
190. Kettenhofen NJ and Wood MJ. Formation, reactivity, and detection of protein sulfenic acids. Chem Res Toxicol 23: 1633-1646, 2010.
191. Kice JL. Mechanisms and reactivity in reactions of organic oxyacids of sulfur and their anhydrides. In: Avances in Physical Organic Chemistry, vol. 17, edited by Gold V and Bethell D. London: Academic Press, 1980, pp. 65-181.
192. Kiley PJ and BeinertH. The role of Fe-S proteins in sensing and regulation in bacteria. Curr Opin Microbiol 6: 181-185, 2003. (Pubitemid 36628663)
193. Kim JJ, Lee SB, Park JK, and Yoo YD. TNF-a-induced ROS production triggering apoptosis is directly linked to Romo1 and Bcl-XL. Cell Death Differ 17: 1420-1434, 2010.
194. Kim SO, Merchant K, Nudelman R, Beyer WF, Jr., Keng T, DeAngelo J, Hausladen A, and Stamler JS. OxyR: a molecular code for redox-related signaling. Cell 109: 383-396, 2002. (Pubitemid 34606880)
195. Klotz LO, Kröncke KD, and Sies H. Singlet oxygen-induced signaling effects in mammalian cells. Photochem Photobiol Sci 2: 88-94, 2003. (Pubitemid 41646723)
196. Knock GA and Ward JP. Redox regulation of protein kinases as a modulator of vascular function. Antioxid Redox Signal 15: 1531-1547, 2011.
197. Kodali VK and Thorpe C. Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins. Antioxid Redox Signal 13: 1217-1230, 2010.
198. Kroemer G, Galluzzi L, and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 87: 99-163, 2007. (Pubitemid 46209992)
199. Kukreja RC, Kontos HA, Hess ML, and Ellis EF. PGH synthase and lipoxygenase generate superoxide in the presence of NADH or NADPH. Circ Res 59: 612-619, 1986. (Pubitemid 17035305)
200. Kundu JK and Surh YJ. Nrf2-Keap1 signaling as a potential target for chemoprevention of inflammation-associated carcinogenesis. Pharm Res 27: 999-1013, 2010.
201. Lambeth JD. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 4: 181-189, 2004. (Pubitemid 38339084)
202. Lambeth JD, Kawahara T, and Diebold B. Regulation of Nox and Duox enzymatic activity and expression. Free Radic Biol Med 43: 319-331, 2007. (Pubitemid 46978416)
203. Landmesser U, Dikalov S, Price SR, McCann L, Fukai T, Holland SM, Mitch WE, and Harrison DG. Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension. J Clin Invest 111: 1201-1209, 2003. (Pubitemid 36519937)
204. Lane P and Gross SS. Cell signaling by nitric oxide. Semin Nephrol 19: 215-229, 1999. (Pubitemid 29200830)
205. Lee SP, Hwang YS, Kim YJ, Kwon KS, Kim HJ, Kim K, and ChaeHZ. CyclophilinAbinds to peroxiredoxins and activates its peroxidase activity. J Biol Chem 276: 29826-29832, 2001.
206. Lee SR, Kwon KS, Kim SR, and Rhee SG. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273: 15366-15372, 1998. (Pubitemid 28298140)
207. Lee WK and Thévenod F. A role for mitochondrial aquaporins in cellular life-and-death decisions? Am J Physiol Cell Physiol 291: C195-C202, 2006. (Pubitemid 44148141)
208. Levonen AL, Landar A, Ramachandran A, Ceaser EK, Dickinson DA, Zanoni G, Morrow JD, and Darley-Usmar VM. Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem J 378: 373-382, 2004. (Pubitemid 38367228)
209. Li N, Ragheb K, Lawler G, Sturgis J, Rajwa B, Melendez JA, and Robinson JP. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J Biol Chem 278: 8516-8525, 2003. (Pubitemid 36800604)
210. Lillig CH, Berndt C, and Holmgren A. Glutaredoxin systems. Biochim Biophys Acta 1780: 1304-1317, 2008.
211. Lillig CH and Holmgren A. Thioredoxin and related molecules-From biology to health and disease. Antioxid Redox Signal 9: 25-47, 2007. (Pubitemid 44901873)
212. Lim MD, Lorkovic IM, and Ford PC. NO and NOx interactions with group 8 metalloporphyrins. J Inorg Biochem 99: 151-165, 2005.
213. Linard D, Kandlbinder A, Degand H, Morsomme P, Dietz KJ, and Knoops B. Redox characterization of human cyclophilin D: identification of a new mammalian mitochondrial redox sensor? Arch Biochem Biophys 491: 39-45, 2009.
214. Linnewiel K, Ernst H, Caris-Veyrat C, Ben-Dor A, Kampf A, Salman H, Danilenko M, Levy J, and Sharoni Y. Structure activity relationship of carotenoid derivatives in activation of the electrophile/antioxidant response element transcription system. Free Radic Biol Med 47: 659-667, 2009.
215. Little C and O'Brien PJ. Mechanism of peroxide-inactivation of the sulphydryl enzyme glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem 10: 533-538, 1969.
216. Liu H, Zhang H, Iles KE, Rinna A, Merrill G, Yodoi J, Torres M, and Forman HJ. The ADP-stimulated NADPH oxidase activates the ASK-1/MKK4/JNK pathway in alveolar macrophages. Free Radic Res 40: 865-874, 2006. (Pubitemid 44480497)
217. Liu L, Hausladen A, Zeng M, Que L, Heitman J, and Stamler JS. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410: 490-494, 2001. (Pubitemid 32240051)
218. Lohse DL, Denu JM, Santoro N, and Dixon JE. Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1. Biochemistry 36: 4568-4575, 1997. (Pubitemid 27180305)
219. Loschen G, Azzi A, Richter C, and Flohé L. Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett 42: 68-72, 1974.
220. Lu J, Chew EH, and Holmgren A. Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proc Natl Acad Sci U S A 104: 12288-12293, 2007. (Pubitemid 47206130)
221. Lundström J, Krause G, and Holmgren A. A Pro to His mutation in active site of thioredoxin increases its disulfideisomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease. J Biol Chem 267: 9047-9052, 1992.
222. Ma X, Zhang J, Liu S, Huang Y, Chen B, and Wang D. Nrf2 knockdown by shRNA inhibits tumor growth and increases efficacy of chemotherapy in cervical cancer. Cancer Chemother Pharmacol 69: 485-494, 2012.
223. Maejima Y, Kuroda J, Matsushima S, Ago T, and Sadoshima J. Regulation of myocardial growth and death by NADPH oxidase. J Mol Cell Cardiol 50: 408-416, 2011.
224. Mahadev K, Wu X, Zilbering A, Zhu L, Lawrence JTR, and Goldstein BJ. 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: 48662-48669, 2001.
225. Maiorino M, Roveri A, Benazzi L, Bosello V, Mauri P, Toppo S, Tosatto SC, and Ursini F. Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase. J Biol Chem 280: 38395-38402, 2005. (Pubitemid 43853736)
226. Mairet-Coello G, Tury A, Esnard-Feve A, Fellmann D, Risold PY, and Griffond B. FAD-linked sulfhydryl oxidase QSOX: topographic, cellular, and subcellular immunolocalization in adult rat central nervous system. J Comp Neurol 473: 334-363, 2004. (Pubitemid 38580455)
227. Makino Y, Yoshikawa N, Okamoto K, Hirota K, Yodoi J, Makino I, and Tanaka H. Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J Biol Chem 274: 3182-3188, 1999. (Pubitemid 29075407)
228. Malinouski M, Zhou Y, Belousov VV, Hatfield DL, and Gladyshev VN. Hydrogen peroxide probes directed to different cellular compartments. PLoS One 6: e14564, 2011.
229. Mandal PK, Schneider M, Kölle P, Kuhlencordt P, Förster H, Beck H, Bornkamm GW, and Conrad M. Loss of thioredoxin reductase 1 renders tumors highly susceptible to pharmacologic glutathione deprivation. Cancer Res 70: 9505-9514, 2010.
230. Manevich Y, Feinstein SI, and Fisher AB. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pGST. Proc Natl Acad Sci U S A 101: 3780-3785, 2004. (Pubitemid 38381055)
231. Marengo JJ, Hidalgo C, and Bull R. Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells. Biophys J 74: 1263-1277, 1998. (Pubitemid 28108536)
232. Martindale JL and Holbrook NJ. Cellular response to oxidative stress: signaling for suicide and survival. J Cell Physiol 192: 1-15, 2002. (Pubitemid 34587382)
233. Matsui M, Oshima M, Oshima H, Takaku K, Maruyama T, Yodoi J, and Taketo MM. Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene. Dev Biol 178: 179-185, 1996. (Pubitemid 26297250)
234. Matthews JR, Wakasugi N, Virelizier JL, Yodoi J, and Hay RT. Thioredoxin regulates the DNA binding activity of NFjB by reduction of a disulphide bond involving cysteine. Nucleic Acids Res 20: 3821-3830, 1992.
235. McIlwain CC, Townsend DM, and Tew KD. Glutathione Stransferase polymorphisms: cancer incidence and therapy. Oncogene 25: 1639-1648, 2006.
236. McMahon M, Thomas N, Itoh K, Yamamoto M, and Hayes JD. Dimerization of substrate adaptors can facilitate cullinmediated ubiquitylation of proteins by a ''tethering'' mechanism: a two-site interaction model for the Nrf2-Keap1 complex. J Biol Chem 281: 24756-24768, 2006. (Pubitemid 44274250)
237. McNally JS, Davis ME, Giddens DP, Saha A, Hwang J, Dikalov S, Jo H, and Harrison DG. Role of xanthine oxidoreductase and NAD(P)H oxidase in endothelial superoxide production in response to oscillatory shear stress. Am J Physiol Heart Circ Physiol 285: H2290-H2297, 2003. (Pubitemid 37443044)
238. McStay GP, Clarke SJ, and Halestrap AP. Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore. Biochem J 367: 541-548, 2002. (Pubitemid 35216831)
239. Meier B, Radeke HH, Selle S, Younes M, Sies H, Resch K, and Habermehl GG. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-a. Biochem J 263: 539-545, 1989. (Pubitemid 19254159)
240. Mesecke N, Terziyska N, Kozany C, Baumann F, Neupert W, Hell K, and Herrmann JM. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121: 1059-1069, 2005. (Pubitemid 40884396)
241. Mieyal JJ, Gallogly MM, Qanungo S, Sabens EA, and Shelton MD. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid Redox Signal 10: 1941-1988, 2008.
242. Morel Y and Barouki R. Repression of gene expression by oxidative stress. Biochem J 342 Pt 3: 481-496, 1999. (Pubitemid 29452631)
243. Morgan BA and Veal EA. Functions of typical 2-Cys peroxiredoxins in yeast. Subcell Biochem 44: 253-265, 2007.
244. Motohashi K, Koyama F, Nakanishi Y, Ueoka-Nakanishi H, and Hisabori T. Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cistrans isomerase activity. J Biol Chem 278: 31848-31852, 2003. (Pubitemid 37048368)
245. Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 417: 1-13, 2009.
246. Na HK and Surh YJ. Modulation of Nrf2-mediated antioxidant and detoxifying enzyme induction by the green tea polyphenol EGCG. Food Chem Toxicol 46: 1271-1278, 2008.
247. Nagy P, Karton A, Betz A, Peskin AV, Pace P, O'Reilly RJ, Hampton MB, Radom L, and Winterbourn CC. Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study. J Biol Chem 286: 18048-18055, 2011.
248. Nakagawa T, Shimizu S, Watanabe T, Yamaguchi O, Otsu K, Yamagata H, Inohara H, Kubo T, and Tsujimoto Y. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434: 652-658, 2005. (Pubitemid 40488558)
249. Nakamura T and Lipton SA. Emerging role of proteinprotein transnitrosylation in cell signaling pathways. Antioxid Redox Signal 18: 239-249, 2013.
250. Nakashima I, Takeda K, Kawamoto Y, Okuno Y, Kato M, and Suzuki H. Redox control of catalytic activities of membrane-associated protein tyrosine kinases. Arch Biochem Biophys 434: 3-10, 2005. (Pubitemid 40040464)
251. Nauser T and Koppenol WH. The rate constant of the reaction of superoxide with nitrogen monoxide: Approaching the diffusion limit. J Phys Chem A 106: 4084-4086, 2002. (Pubitemid 35290100)
252. Nguyen TT, Stevens MV, Kohr M, Steenbergen C, Sack MN, and Murphy E. Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore. J Biol Chem 286: 40184-40192, 2011.
253. 2-induced apoptosis. J Biol Chem 283: 15359-15369, 2008.
254. Niecknig H, Tug S, Reyes BD, Kirsch M, Fandrey J, and Berchner-Pfannschmidt U. Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia. Free Radic Res 46: 705-717, 2012.
255. Nishi T, Shimizu N, Hiramoto M, Sato I, Yamaguchi Y, Hasegawa M, Aizawa S, Tanaka H, Kataoka K, Watanabe H, and Handa H. Spatial redox regulation of a critical cysteine residue of NF-jB in vivo. J Biol Chem 277: 44548-44556, 2002. (Pubitemid 36157890)
256. Nishino T, Okamoto K, Eger BT, Pai EF and Nishino T. Mammalian xanthine oxidoreductase -mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J 275: 3278-3289, 2008. (Pubitemid 351813552)
257. Nonn L, Williams RR, Erickson RP, and Powis G. The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice. Mol Cell Biol 23: 916-922, 2003. (Pubitemid 36133510)
258. Okado-Matsumoto A and Fridovich I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria. J Biol Chem 276: 38388-38393, 2001.
259. Pani G, Bedogni B, Colavitti R, Anzevino R, Borrello S, and Galeotti T. Cell compartmentalization in redox signaling. IUBMB Life 52: 7-16, 2001. (Pubitemid 33769663)
260. Park SJ and Kim IS. The role of p38 MAPK activation in auranofin-induced apoptosis of human promyelocytic leukaemia HL-60 cells. Br J Pharmacol 146: 506-513, 2005.
261. Parsonage D, Karplus PA, and Poole LB. Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proc Natl Acad Sci U S A 105: 8209-8214, 2008. (Pubitemid 351904736)
262. Pascal I and Tarbell DS. The kinetics of the oxidation of a mercaptan to the corresponding disulfide by aqueous hydrogen peroxide. J Am Chem Soc 79: 6015-6020, 1957.
263. Patwari P and Lee RT. Thioredoxins, mitochondria, and hypertension. Am J Pathol 170: 805-808, 2007. (Pubitemid 47339350)
264. Paulsen CE and Carroll KS. Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol 5: 47-62, 2010.
265. Peshenko IV and Shichi H. Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite. Free Radic Biol Med 31: 292-303, 2001. (Pubitemid 32675334)
266. 2 is not reflected in its reaction with other oxidants and thiol reagents. J Biol Chem 282: 11885-11892, 2007. (Pubitemid 47100684)
267. Peskin AV and Winterbourn CC. Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Radic Biol Med 30: 572-579, 2001. (Pubitemid 32162964)
268. Piantadosi CA. Regulation of mitochondrial processes by protein S-nitrosylation. Biochim Biophys Acta 1820: 712-721, 2012.
269. Pigiet VP and Schuster BJ. Thioredoxin-catalyzed refolding of disulfide-containing proteins. Proc Natl Acad Sci U S A 83: 7643-7647, 1986. (Pubitemid 17183904)
270. Pomposiello PJ and Demple B. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 19: 109-114, 2001. (Pubitemid 32155431)
271. Poole LB and Claiborne A. The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. J Biol Chem 264: 12330-12338, 1989. (Pubitemid 19191121)
272. Poole LB, Karplus PA, and Claiborne A. Protein sulfenic acids in redox signaling. Annu Rev Pharmacol Toxicol 44: 325-347, 2004. (Pubitemid 38263844)
273. Powis G and Montfort WR. Properties and biological activities of thioredoxins. Annu Rev Pharmacol Toxicol 41: 261-295, 2001. (Pubitemid 32385890)
274. Powis G, Mustacich D, and Coon A. The role of the redox protein thioredoxin in cell growth and cancer. Free Radic Biol Med 29: 312-322, 2000.
275. Prigge JR, Eriksson S, Iverson SV, Meade TA, Capecchi MR, Arnér ESJ, and Schmidt EE. Hepatocyte DNA replication in growing liver requires either glutathione or a single allele of txnrd1. Free Radic Biol Med 52: 803-810, 2012.
276. Prosser BL, Ward CW, and Lederer WJ. X-ROS signaling: rapid mechano-chemo transduction in heart. Science 333: 1440-1445, 2011.
277. Prütz WA. Interactions of hypochlorous acid with pyrimidine nucleotides, and secondary reactions of chlorinated pyrimidines with GSH, NADH, and other substrates. Arch Biochem Biophys 349: 183-191, 1998. (Pubitemid 28368405)
278. Pushpa-Rekha TR, Burdsall AL, Oleksa LM, Chisolm GM, and Driscoll DM. Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites. J Biol Chem 270: 26993-26999, 1995.
279. Quijano C, Alvarez B, Gatti RM, Augusto O, and Radi R. Pathways of peroxynitrite oxidation of thiol groups. Biochem J 322 (Pt 1): 167-173, 1997. (Pubitemid 27095537)
280. Quillet-Mary A, Jaffrézou JP, Mansat V, Bordier C, Naval J, and Laurent G. Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J Biol Chem 272: 21388-21395, 1997. (Pubitemid 27374008)
281. Rackham O, Nichols SJ, Leedman PJ, Berners-Price SJ, and Filipovska A. A gold(I) phosphine complex selectively induces apoptosis in breast cancer cells: Implications for anticancer therapeutics targeted to mitochondria. Biochem Pharmacol 74: 992-1002, 2007. (Pubitemid 47284014)
282. Radi R, Beckman JS, Bush KM, and Freeman BA. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J Biol Chem 266: 4244-4250, 1991. (Pubitemid 21909347)
283. Ramos-Gomez M, Kwak MK, Dolan PM, Itoh K, Yamamoto M, Talalay P, and Kensler TW. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc Natl Acad Sci U S A 98: 3410-3415, 2001. (Pubitemid 32220859)
284. Ren X, Björnstedt M, Shen B, Ericson ML, and Holmgren A. Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione. Biochemistry 32: 9701-9708, 1993. (Pubitemid 23296815)
285. Rhee SG. Redox signaling: hydrogen peroxide as intracellular messenger. Exp Mol Med 31: 53-59, 1999. (Pubitemid 29326708)
286. 2, a necessary evil for cell signaling. Science 312: 1882-1883, 2006. (Pubitemid 43993698)
287. Rhee SG, Chang TS, Bae YS, Lee SR, and Kang SW. Cellular regulation by hydrogen peroxide. J Am Soc Nephrol 14: S211-S215, 2003. (Pubitemid 36903927)
288. 2, and protein chaperones. Antioxid Redox Signal 15: 781-794, 2011.
289. Riemer J, Bulleid N, and Herrmann JM. Disulfide formation in the ER and mitochondria: two solutions to a common process. Science 324: 1284-1287, 2009.
290. Riemer J, Fischer M, and Herrmann JM. Oxidation-driven protein import into mitochondria: insights and blind spots. Biochim Biophys Acta 1808: 981-989, 2011.
291. Rigobello MP, Donella-Deana A, Cesaro L, and Bindoli A. Isolation, purification, and characterization of a rat liver mitochondrial protein disulfide isomerase. Free Radic Biol Med 28: 266-272, 2000. (Pubitemid 30084019)
292. Rigobello MP, Donella-Deana A, Cesaro L, and Bindoli A. Distribution of protein disulphide isomerase in rat liver mitochondria. Biochem J 356: 567-570, 2001. (Pubitemid 32536819)
293. Rigobello MP, Folda A, Baldoin MC, Scutari G, and Bindoli A. Effect of auranofin on the mitochondrial generation of hydrogen peroxide. Role of thioredoxin reductase. Free Radic Res 39: 687-695, 2005. (Pubitemid 40965396)
294. Rigobello MP, Folda A, Scutari G, and Bindoli A. The modulation of thiol redox state affects the production and metabolism of hydrogen peroxide by heart mitochondria. Arch Biochem Biophys 441: 112-122, 2005. (Pubitemid 41568203)
295. RigobelloMP, ScutariG, Boscolo R, and BindoliA. Induction of mitochondrial permeability transition by auranofin, a gold(I)-phosphine derivative. Br J Pharmacol 136: 1162-1168, 2002. (Pubitemid 34970068)
296. Rigobello MP, Scutari G, Folda A, and Bindoli A. Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c. Biochem Pharmacol 67: 689-696, 2004. (Pubitemid 38125252)
297. Rigobello MP, Turcato F, and Bindoli A. Inhibition of rat liver mitochondrial permeability transition by respiratory substrates. Arch Biochem Biophys 319: 225-230, 1995.
298. 2 signaling. Antioxid Redox Signal 14: 459-468, 2011.
299. Rinna A, Torres M, and Forman HJ. Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B. Free Radic Biol Med 41: 86-91, 2006. (Pubitemid 43866455)
300. Roveri A, Casasco A, Maiorino M, Dalan P, Calligaro A, and Ursini F. Phospholipid hydroperoxide glutathione peroxidase of rat testis. Gonadotropin dependence and immunocytochemical identification. J Biol Chem 267: 6142-6146, 1992.
301. Roy S, Khanna S, and Sen CK. Redox regulation of the VEGF signaling path and tissue vascularization: Hydrogen peroxide, the common link between physical exercise and cutaneous wound healing. Free Radic Biol Med 44: 180-192, 2008.
302. Ruoppolo M, Lundström-Ljung J, Talamo F, Pucci P, and Marino G. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A. Biochemistry 36: 12259-12267, 1997. (Pubitemid 27440964)
303. Saggioro D, Rigobello MP, Paloschi L, Folda A, Moggach SA, Parsons S, Ronconi L, Fregona D, and Bindoli A. Gold(III)-dithiocarbamato complexes induce cancer cell death triggered by thioredoxin redox system inhibition and activation of ERK pathway. Chem Biol 14: 1128-1139, 2007. (Pubitemid 47599989)
304. Saitoh M, Nishitoh H, Fujii M, Takeda K, Tobiume K, Sawada Y, Kawabata M, Miyazono K, and Ichijo H. Mammalian thioredoxin is a direct inhibitor of apoptosis signalregulating kinase (ASK). EMBO J 17: 2596-2606, 1998. (Pubitemid 28221195)
305. Sakon S, Xue X, Takekawa M, Sasazuki T, Okazaki T, Kojima Y, Piao JH, Yagita H, Okumura K, Doi T, and Nakano H. NF-jB inhibits TNF-induced accumulation of ROS that mediate prolonged MAPK activation and necrotic cell death. EMBO J 22: 3898-3909, 2003. (Pubitemid 36975716)
306. Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423: 769-773, 2003. (Pubitemid 36735701)
307. Sang S, Lambert JD, Hong J, Tian S, Lee MJ, Stark RE, Ho CT, and Yang CS. Synthesis and structure identification of thiol conjugates of (-)-epigallocatechin gallate and their urinary levels in mice. Chem Res Toxicol 18: 1762-1769, 2005. (Pubitemid 43257759)
308. Santos CXC, Anilkumar N, Zhang M, Brewer AC, and Shah AM. Redox signaling in cardiac myocytes. Free Radic Biol Med 50: 777-793, 2011.
309. Scarbrough PM, Mapuskar KA, Mattson DM, Gius D, Watson WH, and Spitz DR. Simultaneous inhibition of glutathione-and thioredoxin-dependent metabolism is necessary to potentiate 17AAG-induced cancer cell killing via oxidative stress. Free Radic Biol Med 52: 436-443, 2012.
310. Schönbrunner ER, Mayer S, Tropschug M, Fischer G, Takahashi N, and Schmid FX. Catalysis of protein folding by cyclophilins fromdifferent species. J Biol Chem266: 3630-3635, 1991. (Pubitemid 21909259)
311. Schreck R, Rieber P, and Baeuerle PA. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-jB transcription factor and HIV-1. EMBO J 10: 2247-2258, 1991. (Pubitemid 21905698)
312. Seaver LC and Imlay JA. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J Bacteriol 183: 7182-7189, 2001. (Pubitemid 33121852)
313. Semenza GL. Hypoxia-inducible factors in physiology and medicine. Cell 148: 399-408, 2012.
314. Sen CK. Cellular thiols and redox-regulated signal transduction. Curr Top Cell Regul 36: 1-30, 2000.
315. Sengupta R and Holmgren A. The role of thioredoxin in the regulation of cellular processes by S-nitrosylation. Biochim Biophys Acta 1820: 689-700, 2012.
316. Serrander L, Cartier L, Bedard K, Banfi B, Lardy B, Plastre O, Sienkiewicz A, Fórró L, Schlegel W, and Krause KH. NOX4 activity is determined by mRNA levels and reveals a unique pattern of ROS generation. Biochem J 406: 105-114, 2007. (Pubitemid 47264740)
317. Sevier CS and Kaiser CA. Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol 3: 836-847, 2002. (Pubitemid 35285274)
318. Sevier CS and Kaiser CA. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim Biophys Acta 1783: 549-556, 2008.
319. Sies H. Oxidative stress: Introductory remarks. In:Oxidative stress, edited by Sies H. London, Orlando, San Diego, New York, Toronto, Montreal, Sydney, Tokyo: Academic Press, 1985, pp. 1-8.
320. Siliprandi N, Siliprandi D, Bindoli A, and Toninello A. Effect of oxidation of glutathione and membrane thiol groups on mitochondrial functions. In: Functions of Glutathione in Liver and Kidney, edited by Sies H and Wendel A. Berlin, Heidelberg: Springer-Verlag, 1978, pp. 139-147.
321. 2 production and redox signalling? Med Hypotheses 76: 299-301, 2011.
322. Sohn J and Rudolph J. Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction. Biochemistry 42: 10060-10070, 2003. (Pubitemid 37052026)
323. Song JJ and Lee YJ. Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase. Biochem J 373: 845-853, 2003. (Pubitemid 36981094)
324. 2 protects Saccharomyces cerevisiae cells in stationary phase against oxidative stress. FEBS Lett 578: 152-156, 2004. (Pubitemid 39576117)
325. St-Pierre J, Buckingham JA, Roebuck SJ, and Brand MD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277: 44784-44790, 2002. (Pubitemid 36159072)
326. Staal FJ, Roederer M, Herzenberg LA, and Herzenberg LA. Intracellular thiols regulate activation of nuclear factor jB and transcription of human immunodeficiency virus. Proc Natl Acad Sci U S A 87: 9943-9947, 1990. (Pubitemid 120016560)
327. Stamler JS and Hausladen A. Oxidative modifications in nitrosative stress. Nat Struct Biol 5: 247-249, 1998. (Pubitemid 28164870)
328. Stamler JS, Singel DJ, and Loscalzo J. Biochemistry of nitric oxide and its redox-activated forms. Science 258: 1898-1902, 1992. (Pubitemid 23026727)
329. Starkov AA, Fiskum G, Chinopoulos C, Lorenzo BJ, Browne SE, Patel MS, and Beal MF. Mitochondrial a-ketoglutarate dehydrogenase complex generates reactive oxygen species. J Neurosci 24: 7779-7788, 2004. (Pubitemid 39215681)
330. Stewart EJ, Aslund F, and Beckwith J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J 17: 5543-5550, 1998. (Pubitemid 28445966)
331. Stone Jr. An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems. Arch Biochem Biophys 422: 119-124, 2004. (Pubitemid 38169357)
332. Stone JR and Yang S. Hydrogen peroxide: a signaling messenger. Antioxid Redox Signal 8: 243-270, 2006. (Pubitemid 43741296)
333. Storz G and Tartaglia LA. OxyR: a regulator of antioxidant genes. J Nutr 122: 627-630, 1992.
334. 2 for platelet-derived growth factor signal transduction. Science 270: 296-299, 1995.
335. Surh YJ, Kundu JK, and Na HK. Nrf2 as a master redox switch in turning on the cellular signaling involved in the induction of cytoprotective genes by some chemopreventive phytochemicals. Planta Medica 74: 1526-1539, 2008.
336. Tanaka T, Hosoi F, Yamaguchi-Iwai Y, Nakamura H, Masutani H, Ueda S, Nishiyama A, Takeda S, Wada H, Spyrou G, and Yodoi J. Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria-dependent apoptosis. EMBO J 21: 1695-1703, 2002. (Pubitemid 34614625)
337. Tanner JJ, Parsons ZD, Cummings AH, Zhou H, and Gates KS. Redox regulation of protein tyrosine phosphatases: structural and chemical aspects. Antioxid Redox Signal 15: 77-97, 2011.
338. Tavender TJ and Bulleid NJ. Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum. Antioxid Redox Signal 13: 1177-1187, 2010.
339. 2 produced during disulphide formation. J Cell Sci 123: 2672-2679, 2010.
340. Tavender TJ, Springate JJ, and Bulleid NJ. Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J 29: 4185-4197, 2010.
341. 2+ leak in chronic heart failure. Circ Res 103: 1466-1472, 2008.
342. Thannickal VJ and Fanburg BL. Reactive oxygen species in cell signaling. Am J Physiol Lung Cell Mol Physiol 279: L1005-L1028, 2000. (Pubitemid 32009487)
343. Tkachev VO, Menshchikova EB, and Zenkov NK. Mechanism of the Nrf2/Keap1/ARE signaling system. Biochemistry (Moscow) 76: 407-422, 2011.
344. Tong KI, Kobayashi A, Katsuoka F, and YamamotoM. Twosite substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism. Biol Chem 387: 1311-1320, 2006. (Pubitemid 44691409)
345. Tonissen KF and Di Trapani G. Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy. Mol Nutr Food Res 53: 87-103, 2009.
346. Tonks NK. Redox redux: revisiting PTPs and the control of cell signaling. Cell 121: 667-670, 2005. (Pubitemid 40797589)
347. Toppo S, Flohé L, Ursini F, Vanin S, and Maiorino M. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim Biophys Acta 1790: 1486-1500, 2009.
348. Tretter L and Adam-Vizi V. Generation of reactive oxygen species in the reaction catalyzed by a-ketoglutarate dehydrogenase. J Neurosci 24: 7771-7778, 2004. (Pubitemid 39215680)
349. Trotter EW and Grant CM. Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems. EMBO Rep 4: 184-188, 2003. (Pubitemid 36322161)
350. Trujillo M and Radi R. Peroxynitrite reaction with the reduced and the oxidized forms of lipoic acid: new insights into the reaction of peroxynitrite with thiols. Arch Biochem Biophys 397: 91-98, 2002. (Pubitemid 34848253)
351. Tu BP and Weissman JS. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164: 341-346, 2004. (Pubitemid 38174761)
352. Ueno M, Masutani H, Arai RJ, Yamauchi A, Hirota K, Sakai T, Inamoto T, Yamaoka Y, Yodoi J, and Nikaido T. Thioredoxin-dependent redox regulation of p53-mediated p21 activation. J Biol Chem 274: 35809-35815, 1999. (Pubitemid 129512885)
353. Urig S and Becker K. On the potential of thioredoxin reductase inhibitors for cancer therapy. Semin Cancer Biol 16: 452-465, 2006. (Pubitemid 44780136)
354. Ursini F, Heim S, Kiess M, Maiorino M, Roveri A, Wissing J, and Flohé L. Dual function of the selenoprotein PHGPx during sperm maturation. Science 285: 1393-1396, 1999. (Pubitemid 29411669)
355. van der Vliet A. NADPH oxidases in lung biology and pathology: Host defense enzymes, and more. Free Radic Biol Med 44: 938-955, 2008.
356. van Montfort RLM, Congreve M, Tisi D, Carr R, and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423: 773-777, 2003. (Pubitemid 36735702)
357. Vepa S, Scribner WM, and Natarajan V. Activation of protein phosphorylation by oxidants in vascular endothelial cells: identification of tyrosine phosphorylation of caveolin. Free Radic Biol Med 22: 25-35, 1997.
358. Vignais PV. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Life Sci 59: 1428-1459, 2002. (Pubitemid 35239301)
359. Wakabayashi N, Dinkova-Kostova AT, Holtzclaw WD, Kang MI, Kobayashi A, Yamamoto M, Kensler TW, and Talalay P. Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers. Proc Natl Acad Sci U S A 101: 2040-2045, 2004. (Pubitemid 38229011)
360. Welsh SJ, Bellamy WT, Briehl MM, and Powis G. The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1a protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis. Cancer Res 62: 5089-5095, 2002. (Pubitemid 34984438)
361. Wilkinson B and Gilbert HF. Protein disulfide isomerase. Biochim Biophys Acta 1699: 35-44, 2004. (Pubitemid 38680792)
362. Winterbourn CC. Reconciling the chemistry and biology of reactive oxygen species. Nat Chem Biol 4: 278-286, 2008. (Pubitemid 351550893)
363. Winterbourn CC and Hampton MB. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med 45: 549-561, 2008.
364. Winterbourn CC and Metodiewa D. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med 27: 322-328, 1999. (Pubitemid 29395424)
365. Woo HA, Chae HZ, Hwang SC, Yang KS, Kang SW, Kim K, and Rhee SG. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300: 653-656, 2003. (Pubitemid 36520592)
366. Wood ZA, Poole LB, and Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300: 650-653, 2003. (Pubitemid 36520591)
367. Wood ZA, Schroder E, Robin Harris J, and Poole LB. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci 28: 32-40, 2003. (Pubitemid 36051004)
368. Yang KS, Kang SW, Woo HA, Hwang SC, Chae HZ, Kim K, and Rhee SG. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J Biol Chem 277: 38029-38036, 2002. (Pubitemid 35154654)
369. Yeh JI, Claiborne A, and Hol WGJ. Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution. Biochemistry 35: 9951-9957, 1996. (Pubitemid 26269909)
370. 2+ ATPase in diabetic pig aorta. Free Radic Biol Med 45: 756-762, 2008.
371. Zhang DD and Hannink M. Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol Cell Biol 23: 8137-8151, 2003. (Pubitemid 37377505)
372. Zhang DX and Gutterman DD. Mitochondrial reactive oxygen species-mediated signaling in endothelial cells. Am J Physiol Heart Circ Physiol 292: H2023-H2031, 2007. (Pubitemid 47084583)
373. Zhang H, Go YM, and Jones DP. Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress. Arch Biochem Biophys 465: 119-126, 2007. (Pubitemid 47283985)
374. Zhang R, Al-Lamki R, Bai L, Streb JW, Miano JM, Bradley J, and Min W. Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner. Circ Res 94: 1483-1491, 2004. (Pubitemid 38780321)
375. Zhang ZY and Dixon JE. 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: 9340-9345, 1993. (Pubitemid 23292052)
376. Zheng M, Aslund F, and Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721, 1998. (Pubitemid 28164467)
377. 2-mediated inactivation of protein tyrosine phosphatases. JAm Chem Soc 133: 15803-15805, 2011.
378. Zinkevich NS and Gutterman DD. ROS-induced ROS release in vascular biology: redox-redox signaling. Am J Physiol Heart Circ Physiol 301: H647-H653, 2011.
379. Zito E, Melo EP, Yang Y, Wahlander A, Neubert TA, and Ron D. Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol Cell 40: 787-797, 2010.
380. 2+ . J Biol Chem 279: 4166-4174, 2004. (Pubitemid 38199002)
381. Zoratti M and Szabò I. The mitochondrial permeability transition. Biochim Biophys Acta 1241: 139-176, 1995.
382. Zorov DB, Juhaszova M, and Sollott SJ. Mitochondrial ROS-induced ROS release: an update and review. Biochim Biophys Acta 1757: 509-517, 2006.
383. Zorov DB, Juhaszova M, Yaniv Y, Nuss HB, Wang S, and Sollott SJ. Regulation and pharmacology of the mitochondrial permeability transition pore. Cardiovasc Res 83: 213-225, 2009.