Oxidative stress

Annual Review of Biochemistry

Volumn 86, Issue , 2017, Pages 715-748

  Sies, Helmut ^a   Berndt, Carsten ^b   Jones, Dean P ^c  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b Department of Orthopedic Surgery   (Germany)

^c EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Antioxidants; Hydrogen peroxide; Oxidants; Oxidative damage; Redox signaling; Redox state

Indexed keywords

ANTINEOPLASTIC AGENT; ANTIOXIDANT; CARBOHYDRATE; FLUORESCENT DYE; FREE RADICAL; HYDROGEN PEROXIDE; HYDROGEN SULFIDE; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KELCH LIKE ECH ASSOCIATED PROTEIN 1; LIPID; NITRIC OXIDE; NUCLEIC ACID; PEROXYNITRITE; PROTEIN; PROTEOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SINGLET OXYGEN; THIOREDOXIN; TRANSCRIPTION FACTOR NRF2; GLUTATHIONE; I KAPPA B KINASE ALPHA; KEAP1 PROTEIN, HUMAN; NFE2L2 PROTEIN, HUMAN; TXN PROTEIN, HUMAN;

ARTICLE; CONFORMATIONAL TRANSITION; CYTOLOGY; DIABETES MELLITUS; GLYCATION; GLYCOSYLATION; HUMAN; NEUROLOGIC DISEASE; NONHUMAN; OBESITY; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PHOTODYNAMIC THERAPY; PHOTOOXIDATION; PRIORITY JOURNAL; SECOND MESSENGER; SIGNAL TRANSDUCTION; WOUND HEALING; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MITOCHONDRION;

GENE EXPRESSION REGULATION; GLUTATHIONE; HUMANS; HYDROGEN PEROXIDE; KELCH-LIKE ECH-ASSOCIATED PROTEIN 1; MITOCHONDRIA; NADPH OXIDASE; NF-E2-RELATED FACTOR 2; NF-KAPPA B; NF-KAPPAB INHIBITOR ALPHA; OXIDATION-REDUCTION; OXIDATIVE STRESS; SIGNAL TRANSDUCTION; SINGLET OXYGEN; THIOREDOXINS;

EID: 85009852867     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-061516-045037     Document Type: Article

References (222)

1. Jones DP, Sies H. (2015). The redox code. Antioxid. Redox Signal. 23: 734-46
2. Kemp M, Go YM, Jones DP. (2008). Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology. Free Radic. Biol. Med. 44: 921-37
3. Bücher T, Sies H. (1969). Steady state relaxation of enolase in vitro and metabolic throughput in vivo of red and white rabbit muscles. Eur. J. Biochem. 8: 273-83
4. Selye H. (1936). A syndrome produced by diverse nocuous agents. Nature 138: 32
5. Selye H. (1976). Forty years of stress research: principal remaining problems and misconceptions. Can. Med. Assoc. J. 115: 53-56
6. McEwen BS. (2016). In pursuit of resilience: stress, epigenetics, and brain plasticity. Ann. N.Y. Acad. Sci. 1373: 56-64
7. Sterling P, Eyer J. (1988). Allostasis: a new paradigm to explain arousal pathology. In Handbook of Life Stress, Cognition and Health, ed. S Fisher, J Reason, pp. 629-49. New York: Wiley
8. Davies KJ. (2016). Adaptive homeostasis. Mol. Asp. Med. 49: 1-7
9. Ore S. (1956). Oxidative stress relaxation of natural rubber vulcanized with di-tertiary-butyl peroxide. Rubber Chem. Technol. 29: 1043-46
10. Paniker NV, Srivastava SK, Beutler E. (1970). Glutathionemetabolism of the red cells.Effect of glutathione reductase deficiency on the stimulation of hexose monophosphate shunt under oxidative stress. Biochim. Biophys. Acta 215: 456-60
11. Sies H, Cadenas E. (1985). Oxidative stress: damage to intact cells and organs. Philos. Trans. R. Soc. B 311: 617-31
12. Sies H. (1985). Oxidative stress: introductory remarks. In Oxidative Stress, ed. H Sies, pp. 1-8. London: Academic
13. Sies H. (1986). Biochemistry of oxidative stress. Angew. Chem. Int. Ed. Engl. 25: 1058-71
14. Jones DP. (2006). Redefining oxidative stress. Antioxid. Redox Signal. 8: 1865-79
15. Sies H, Jones DP. (2007). Oxidative stress. In Encyclopedia of Stress, Vol. 3, ed. G Fink, pp. 45-48. Amsterdam: Elsevier. 2nd ed
16. Azzi A, Davies KJ, Kelly F. (2004). Free radical biology-terminology and critical thinking. FEBS Lett. 558: 3-6
17. Levonen AL, Hill BG, Kansanen E, Zhang J, Darley-Usmar VM. (2014). Redox regulation of antioxidants, autophagy, and the response to stress: implications for electrophile therapeutics. Free Radic. Biol. Med. 71: 196-207
18. Estevam EC, Nasim MJ, Faulstich L, Hakenesch M, Burkholz T, Jacob C. (2015). A historical perspective on oxidative stress and intracellular redox control. In Oxidative Stress in Applied Basic Research and Clinical Practice, ed. SM Roberts, JP Kehrer, LO Klotz, pp. 3-20. Heidelberg: Humana Press
19. Lushchak VI. (2014). Free radicals, reactive oxygen species, oxidative stress and its classification. Chem. Biol. Interact. 224C: 164-75
20. Yan LJ. (2014). Positive oxidative stress in aging and aging-related disease tolerance. Redox Biol. 2C: 165-69
21. Pickering AM, Vojtovich L, Tower J, Davies KJA. (2013). Oxidative stress adaptation with acute, chronic, and repeated stress. Free Radic. Biol. Med. 55: 109-18
22. Ursini F, Maiorino M, Forman HJ. (2016). Redox homeostasis: the golden mean of healthy living. Redox Biol. 8: 205-15
23. Sies H. (2015). Oxidative stress: a concept in redox biology and medicine. Redox Biol. 4: 180-83
24. Lyons TW, Reinhard CT, Planavsky NJ. (2014). The rise of oxygen inEarth's early ocean and atmosphere. Nature 506: 307-15
25. Del Rio LA. (2015). ROS and RNS in plant physiology: an overview. J. Exp. Bot. 66: 2827-37
26. Giles GI, Tasker KM, Jacob C. (2001). Hypothesis: the role of reactive sulfur species in oxidative stress. Free Radic. Biol. Med. 31: 1279-83
27. DeLeon ER, Gao Y, Huang E, Arif M, Arora N, et al. (2016). A case of mistaken identity: Are reactive oxygen species actually reactive sulfide species? Am. J. Physiol. Regul. Integr. Comp. Physiol. 310: R549-60
28. Poole LB. (2015). The basics of thiols and cysteines in redox biology and chemistry. Free Radic. Biol. Med. 80: 148-57
29. Labunskyy VM, Hatfield DL, Gladyshev VN. (2014). Selenoproteins: molecular pathways and physiological roles. Physiol. Rev. 94: 739-77
30. Kappus H, Sies H. (1981). Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia 37: 1233-41
31. Tonner PD, Pittman AM, Gulli JG, Sharma K, Schmid AK. (2015). A regulatory hierarchy controls the dynamic transcriptional response to extreme oxidative stress in archaea. PLOS Genet. 11: e1004912
32. Mishra S, Imlay J. (2012). Why do bacteria use so many enzymes to scavenge hydrogen peroxide? Arch. Biochem. Biophys. 525: 145-60
33. Sies H. (1993). Strategies of antioxidant defense. Eur. J. Biochem. 215: 213-19
34. Berndt C, Lillig CH, Flohé L. (2014). Redox regulation by glutathione needs enzymes. Front. Pharmacol. 5: 168
35. Culp BR, Titus BG, Lands WE. (1979). Inhibition of prostaglandin biosynthesis by eicosapentaenoic acid. Prostaglandins Med. 3: 269-78
36. Jones DP. (2008). Radical-free biology of oxidative stress. Am. J. Physiol. Cell Physiol. 295: C849-68
37. Sies H. (1982). Nicotinamide nucleotide compartmentation. In Metabolic Compartmentation, ed. H Sies, pp. 205-31. London: Academic
38. Massudi H, Grant R, Guillemin GJ, Braidy N. (2012). NAD+ metabolism and oxidative stress: the golden nucleotide on a crown of thorns. Redox Rep. 17: 28-46
39. Mouchiroud L, Houtkooper RH, Moullan N, Katsyuba E, Ryu D, et al. (2013). The NAD+/sirtuin pathwaymodulates longevity through activation ofmitochondrialUPRandFOXOsignaling. Cell 154: 430-41
40. Canto C, Menzies KJ, Auwerx J. (2015). NAD+ metabolism and the control of energy homeostasis: a balancing act between mitochondria and the nucleus. Cell Metab. 22: 31-53
41. Nickel AG, Von Hardenberg A, Hohl M, Löffler JR, Kohlhaas M, et al. (2015). Reversal of mitochondrial transhydrogenase causes oxidative stress in heart failure. Cell Metab. 22: 472-84
42. Warburg OH. (1928). Über die katalytischenWirkungen der lebendigen Substanz [On the catalytic actions of the living substance]. Berlin: Julius Springer
43. Sies H. (2014). Role of metabolic H2O2 generation: redox signaling and oxidative stress. J. Biol. Chem. 289: 8735-41
44. Bücher T, Klingenberg M. (1958). Wege desWasserstoffs in der lebendigen Organisation. [Pathways of hydrogen in the living organization]. Angew. Chem. 70: 552-70
45. Bücher T, Brauser B, Conze A, Klein F, Langguth O, Sies H. (1972). State of oxidation-reduction and state of binding in the cytosolic NADH-system as disclosed by equilibration with extracellular lactate-pyruvate in hemoglobin-free perfused rat liver. Eur. J. Biochem. 27: 301-17
46. Williamson DH, Lund P, Krebs HA. (1967). The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem. J. 103: 514-27
47. Sies H, Chance B. (1970). The steady state level of catalase compound I in isolated hemoglobin-free perfused rat liver. FEBS Lett. 11: 172-76
48. Maulucci G, Bacic G, Bridal L, Schmidt HH, Tavitian B, et al. (2016). Imaging ROS-induced modifications in living systems. Antioxid. Redox Signal. 24: 939-58
49. Hawkins CL, Davies MJ. (2014). Detection and characterisation of radicals in biological materials using EPR methodology. Biochim. Biophys. Acta 1840: 708-21
50. Belousov VV, Fradkov AF, Lukyanov KA, Staroverov DB, Shakhbazov KS, et al. (2006). Genetically encoded fluorescent indicator for intracellular hydrogen peroxide. Nat. Methods 3: 281-86
51. Hanson GT, Aggeler R, Oglesbee D, Cannon M, Capaldi RA, et al. (2004). Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. J. Biol. Chem. 279: 13044-53
52. Gutscher M, Pauleau AL, Marty L, Brach T, Wabnitz GH, et al. (2008). Real-time imaging of the intracellular glutathione redox potential. Nat. Methods 5: 553-59
53. Morgan B, Van LK, Owusu TN, Ezerina D, Pastor-Flores D, et al. (2016). Real-time monitoring of basal H2O2 levels with peroxiredoxin-based probes. Nat. Chem. Biol. 12: 437-43
54. Wagener KC, Kolbrink B, Dietrich K, Kizina KM, Terwitte LS, et al. (2016). Redox indicator mice stably expressing genetically encoded neuronal roGFP: versatile tools to decipher subcellular redox dynamics in neuropathophysiology. Antioxid. Redox Signal. 25: 41-58
55. Brewer TF, Garcia FJ, Onak CS, Carroll KS, Chang CJ. (2015). Chemical approaches to discovery and study of sources and targets of hydrogen peroxide redox signaling through NADPH oxidase proteins. Annu. Rev. Biochem. 84: 765-90
56. Logan A, Cocheme HM, Li Pun PB, Apostolova N, Smith RA, et al. (2013). Using exomarkers to assess mitochondrial reactive species in vivo. Biochim. Biophys. Acta 1840: 923-30
57. Winterbourn CC. (2014). The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells. Biochim. Biophys. Acta 1840: 730-38
58. Karlsson M, Kurz T, Brunk UT, Nilsson SE, Frennesson CI. (2010). What does the commonly usedDCF test for oxidative stress really show? Biochem. J. 428: 183-90
59. Flohé L. (2016). The impact of thiol peroxidases on redox regulation. Free Radic. Res. 50: 126-42
60. Abate C, Patel L, Rauscher FJ III, Curran T. (1990). Redox regulation of fos and jun DNA-binding activity in vitro. Science 249: 1157-61
61. Klotz LO, Sanchez-Ramos C, Prieto-Arroyo I, Urbanek P, Steinbrenner H, Monsalve M. (2015). Redox regulation of FoxO transcription factors. Redox Biol. 6: 51-72
62. Corcoran A, Cotter TG. (2013). Redox regulation of protein kinases. FEBS J. 280: 1944-65
63. Davies MJ. (2016). Protein oxidation and peroxidation. Biochem. J. 473: 805-25
64. Bindoli A, Rigobello MP. (2013). Principles in redox signaling: from chemistry to functional significance. Antioxid. Redox Signal. 18: 1557-93
65. 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
66. Czech MP, Lawrence JC Jr., Lynn WS. (1974). Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin. PNAS 71: 4173-77
67. Buchanan BB, Balmer Y. (2005). Redox regulation: a broadening horizon. Annu. Rev. Plant Biol. 56: 187-220
68. Mieyal JJ, Chock PB. (2012). Posttranslational modification of cysteine in redox signaling and oxidative stress: focus on S-glutathionylation. Antioxid. Redox Signal. 16: 471-75
69. Hanschmann EM, Godoy JR, Berndt C, Hudemann C, Lillig CH. (2013). Thioredoxins, glutaredoxins, and peroxiredoxins-molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling. Antioxid. Redox Signal. 19: 1539-605
70. Bräutigam L, Schutte LD, Godoy JR, Prozorovski T, Gellert M, et al. (2011). Vertebrate-specific glutaredoxin is essential for brain development. PNAS 108: 20532-37
71. Ullevig SL, Kim HS, Short JD, Tavakoli S, Weintraub ST, et al. (2016). Protein S-glutathionylation mediates macrophage responses to metabolic cues from the extracellular environment. Antioxid. Redox Signal. 25: 836-51
72. Forman HJ, Maiorino M, Ursini F. (2010). Signaling functions of reactive oxygen species. Biochemistry 49: 835-42
73. Marinho HS, Real C, Cyrne L, Soares H, Antunes F. (2014). Hydrogen peroxide sensing, signaling and regulation of transcription factors. Redox Biol. 2: 535-62
74. Sies H. (2017). Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: oxidative eustress. Redox Biol. 11: 613-619
75. Winterbourn CC. (2013). The biological chemistry of hydrogen peroxide. Methods Enzymol. 528: 3-25
76. Reczek CR, Chandel NS. (2015). ROS-dependent signal transduction. Curr. Opin. Cell Biol. 33: 8-13
77. Sobotta MC, Liou W, Stocker S, Talwar D, Oehler M, et al. (2015). Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling. Nat. Chem. Biol. 11: 64-70
78. Karplus PA. (2015). A primer on peroxiredoxin biochemistry. Free Radic. Biol. Med. 80: 183-90
79. Jeong W, Bae SH, Toledano MB, Rhee SG. (2012). Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression. Free Radic. Biol. Med. 53: 447-56
80. Chance B, Sies H, Boveris A. (1979). Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59: 527-605
81. Oshino N, Chance B, Sies H, Bücher T. (1973). The role of H2O2 generation in perfused rat liver and the reaction of catalase compound I and hydrogen donors. Arch. Biochem. Biophys. 154: 117-31
82. Henzler T, Steudle E. (2000). Transport and metabolic degradation of hydrogen peroxide in Chara corallina: Model calculations and measurements with the pressure probe suggest transport of H2O2 across water channels. J. Exp. Bot. 51: 2053-66
83. Bienert GP, Moller AL, Kristiansen KA, Schulz A, Moller IM, et al. (2007). Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes. J. Biol. Chem. 282: 1183-92
84. Marchissio MJ, Frances DE, Carnovale CE, Marinelli RA. (2012). Mitochondrial aquaporin-8 knockdown in human hepatomaHepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability. Toxicol. Appl. Pharmacol. 264: 246-54
85. Medrano-Fernandez I, Bestetti S, Bertolotti M, Bienert GP, Bottino C, et al. (2016). Stress regulates aquaporin-8 permeability to impact cell growth and survival. Antioxid. Redox Signal. 24: 1031-44
86. Hara-Chikuma M, Satooka H, Watanabe S, Honda T, Miyachi Y, et al. (2015). Aquaporin-3-mediated hydrogen peroxide transport is required for NF-κB signalling in keratinocytes and development of psoriasis. Nat. Commun. 6: 7454
87. Bienert GP, Chaumont F. (2014). Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide. Biochim. Biophys. Acta 1840: 1596-604
88. Babior BM, Kipnes RS, Curnutte JT. (1973). Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Investig. 52: 741-44
89. Meier B, Radeke HH, Selle S, Younes M, Sies H, et al. (1989). Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-α. Biochem. J. 263: 539-45
90. Nauseef WM. (2014). Detection of superoxide anion and hydrogen peroxide production by cellular NADPH oxidases. Biochim. Biophys. Acta 1840: 757-67
91. Lassegue B, San MA, Griendling KK. (2012). Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system. Circ. Res. 110: 1364-90
92. Schröder K, Zhang M, Benkhoff S, Mieth A, Pliquett R, et al. (2012). Nox4 is a protective reactive oxygen species generating vascular NADPH oxidase. Circ. Res. 110: 1217-25
93. Santos CX, Hafstad AD, Beretta M, Zhang M, Molenaar C, et al. (2016). Targeted redox inhibition of protein phosphatase 1 by Nox4 regulates eIF2α-mediated stress signaling. EMBO J. 35: 319-34
94. Zhang Y, Shimizu H, Siu KL, Mahajan A, Chen JN, Cai H. (2014). NADPH oxidase 4 induces cardiac arrhythmic phenotype in zebrafish. J. Biol. Chem. 289: 23200-8
95. Oakley FD, Abbott D, Li Q, Engelhardt JF. (2009). Signaling components of redox active endosomes: the redoxosomes. Antioxid. Redox Signal. 11: 1313-33
96. Spencer NY, Engelhardt JF. (2014). The basic biology of redoxosomes in cytokine-mediated signal transduction and implications for disease-specific therapies. Biochemistry 53: 1551-64
97. Boveris A, Oshino N, Chance B. (1972). The cellular production of hydrogen peroxide. Biochem. J. 128: 617-30
98. Loschen G, Flohé L, Chance B. (1971). Respiratory chain linked H2O2 production in pigeon heart mitochondria. FEBS Lett. 18: 261-64
99. Bleier L, Wittig I, Heide H, Steger M, Brandt U, Dröse S. (2015). Generator-specific targets of mitochondrial reactive oxygen species. Free Radic. Biol. Med. 78: 1-10
100. Murphy MP. (2009). How mitochondria produce reactive oxygen species. Biochem. J. 417: 1-13
101. Goncalves RL, Quinlan CL, Perevoshchikova IV, Hey-Mogensen M, Brand MD. (2015). Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise. J. Biol. Chem. 290: 209-27
102. Starkov AA, Fiskum G, Chinopoulos C, Lorenzo BJ, Browne SE, et al. (2004). Mitochondrial α-ketoglutarate dehydrogenase complex generates reactive oxygen species. J. Neurosci. 24: 7779-88
103. Mailloux RJ. (2015). Teaching the fundamentals of electron transfer reactions in mitochondria and the production and detection of reactive oxygen species. Redox Biol. 4: 381-98
104. Go YM, Chandler JD, Jones DP. (2015). The cysteine proteome. Free Radic. Biol. Med. 84: 227-45
105. Riemer J, Schwarzländer M, Conrad M, Herrmann JM. (2015). Thiol switches inmitochondria: operation and physiological relevance. Biol. Chem. 396: 465-82
106. Ermakova YG, Bilan DS, Matlashov ME, Mishina NM, Markvicheva KN, et al. (2014). Red fluorescent genetically encoded indicator for intracellular hydrogen peroxide. Nat. Commun. 5: 5222
107. Mailloux RJ, Treberg JR. (2015). Protein S-glutathionylation links energy metabolism to redox signaling in mitochondria. Redox Biol. 8: 110-18
108. Picard M, McManus MJ, Gray JD, Nasca C, Moffat C, et al. (2015). Mitochondrial functions modulate neuroendocrine, metabolic, inflammatory, and transcriptional responses to acute psychological stress. PNAS 112: E6614-23
109. Waypa GB, Smith KA, Schumacker PT. (2016). O2 sensing, mitochondria and ROS signaling: The fog is lifting. Mol. Aspects Med. 47-48: 76-89
110. Guidot DM, Repine JE, Kitlowski AD, Flores SC, Nelson SK, et al. (1995). Mitochondrial respiration scavenges extramitochondrial superoxide anion via a nonenzymaticmechanism. J. Clin. Investig. 96: 1131-36
111. Dey S, Sidor A, O'Rourke B. (2016). Compartment-specific control of reactive oxygen species scavenging by antioxidant pathway enzymes. J. Biol. Chem. 291: 11185-97
112. Winterbourn CC. (2015). Are free radicals involved in thiol-based redox signaling? Free Radic. Biol. Med. 80: 164-70
113. Trujillo M, Alvarez B, Radi R. (2016). One-and two-electron oxidation of thiols: mechanisms, kinetics and biological fates. Free Radic. Res. 50: 150-71
114. Greiner R, Palinkas Z, Basell K, Becher D, Antelmann H, et al. (2013). Polysulfides link H2S to protein thiol oxidation. Antioxid. Redox Signal. 19: 1749-65
115. Mishanina TV, Libiad M, Banerjee R. (2015). Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways. Nat. Chem. Biol. 11: 457-64
116. Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA. (1990). Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. PNAS 87: 1620-24
117. Jacob C, Giles GI, Giles NM, Sies H. (2003). Sulfur and selenium: the role of oxidation state in protein structure and function. Angew. Chem. Int. Ed. Engl. 42: 4742-58
118. Cremers CM, Jakob U. (2013). Oxidant sensing by reversible disulfide bond formation. J. Biol. Chem. 288: 26489-96
119. Go YM, Jones DP. (2013). The redox proteome. J. Biol. Chem. 288: 26512-20
120. Drazic A, Winter J. (2014). The physiological role of reversible methionine oxidation. Biochim. Biophys. Acta 1844: 1367-82
121. Kaya A, Lee BC, Gladyshev VN. (2015). Regulation of protein function by reversiblemethionine oxidation and the role of selenoprotein MsrB1. Antioxid. Redox Signal. 23: 814-22
122. Itoh K, Chiba T, Takahashi S, Ishii T, Igarashi K, et al. (1997). An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem. Biophys. Res. Commun. 236: 313-22
123. Sporn MB, Liby KT. (2012). NRF2 and cancer: the good, the bad and the importance of context. Nat. Rev. Cancer 12: 564-71
124. Cebula M, Schmidt EE, Arner ES. (2015). TrxR1 as a potent regulator of the Nrf2-Keap1 response system. Antioxid. Redox Signal. 23: 823-53
125. Xue M, Momiji H, Rabbani N, Barker G, Bretschneider T, et al. (2015). Frequency modulated translocational oscillations of Nrf2 mediate the antioxidant response element cytoprotective transcriptional response. Antioxid. Redox Signal. 23: 613-29
126. Pan JA, Sun Y, Jiang YP, Bott AJ, Jaber N, et al. (2016). TRIM21 ubiquitylates SQSTM1/p62 and suppresses protein sequestration to regulate redox homeostasis. Mol. Cell 61: 720-33
127. Kubben N, Zhang W, Wang L, Voss TC, Yang J, et al. (2016). Repression of the antioxidant NRF2 pathway in premature aging. Cell 165: 1361-74
128. Schreck R, Rieber P, Baeuerle PA. (1991). Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J. 10: 2247-58
129. Toledano MB, Leonard WJ. (1991). Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro. PNAS 88: 4328-32
130. Hirota K, Murata M, Sachi Y, Nakamura H, Takeuchi J, et al. (1999). Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-κB. J. Biol. Chem. 274: 27891-97
131. Halvey PJ, Hansen JM, Johnson JM, Go YM, Samali A, Jones DP. (2007). Selective oxidative stress in cell nuclei by nuclear-targeted D-amino acid oxidase. Antioxid. Redox Signal. 9: 807-16
132. Zambrano S, De Toma I, Piffer A, Bianchi ME, Agresti A. (2016). NF-κB oscillations translate into functionally related patterns of gene expression. eLife 5: PMID26765569
133. Ganesan A, Hanawalt P. (2016). Photobiological origins of the field of genomic maintenance. Photochem. Photobiol. 92: 52-60
134. Schmitt FJ, Renger G, Friedrich T, Kreslavski VD, Zharmukhamedov SK, et al. (2014). Reactive oxygen species: re-evaluation of generation, monitoring and role in stress-signaling in phototrophic organisms. Biochim. Biophys. Acta 1837: 835-48
135. Berneburg M, Grether-Beck S, Kurten V, Ruzicka T, Briviba K, et al. (1999). Singlet oxygen mediates the UVA-induced generation of the photoaging-associated mitochondrial common deletion. J. Biol. Chem. 274: 15345-49
136. Sies H, Stahl W. (2004). Nutritional protection against skin damage from sunlight. Annu. Rev. Nutr. 24: 173-200
137. Di Mascio P, Kaiser S, Sies H. (1989). Lycopene as the most efficient biological carotenoid singlet oxygen quencher. Arch. Biochem. Biophys. 274: 532-38
138. Premi S, Wallisch S, Mano CM, Weiner AB, Bacchiocchi A, et al. (2015). Chemiexcitation of melanin derivatives induces DNA photoproducts long after UV exposure. Science 347: 842-47
139. Halliwell B, Gutteridge JMC. (2015). Free Radicals in Biology and Medicine. Oxford: Oxford Univ. Press. 5th ed
140. Storz G, Christman MF, Sies H, Ames BN. (1987). Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium. PNAS 84: 8917-21
141. Freudenthal BD, Beard WA, Perera L, Shock DD, Kim T, et al. (2015). Uncovering the polymeraseinduced cytotoxicity of an oxidized nucleotide. Nature 517: 635-39
142. Cadet J, Loft S, Olinski R, Evans MD, Bialkowski K, et al. (2012). Biologically relevant oxidants and terminology, classification and nomenclature of oxidatively generated damage to nucleobases and 2-deoxyribose in nucleic acids. Free Radic. Res. 46: 367-81
143. Leon J, Sakumi K, Castillo E, Sheng Z, Oka S, Nakabeppu Y. (2016). 8-Oxoguanine accumulation in mitochondrial DNA causes mitochondrial dysfunction and impairs neuritogenesis in cultured adult mouse cortical neurons under oxidative conditions. Sci. Rep. 6: 22086
144. Bräutigam L, Pudelko L, Jemth AS, Gad H, Narwal M, et al. (2016). Hypoxic signaling and the cellular redox tumor environment determine sensitivity to MTH1 inhibition. Cancer Res. 76: 2366-75
145. Poulsen HE, Specht E, Broedbaek K, Henriksen T, Ellervik C, et al. (2012). RNA modifications by oxidation: a novel disease mechanism? Free Radic. Biol. Med. 52: 1353-61
146. Cheng X, Ku CH, Siow RC. (2013). Regulation of the Nrf2 antioxidant pathway by microRNAs: new players in micromanaging redox homeostasis. Free Radic. Biol. Med. 64: 4-11
147. Wang JX, Gao J, Ding SL, Wang K, Jiao JQ, et al. (2015). Oxidative modification of miR-184 enables it to target Bcl-xL and Bcl-w. Mol. Cell 59: 50-61
148. Lang A, Grether-Beck S, Singh M, Kuck F, Jakob S, et al. (2016). MicroRNA-15b regulates mitochondrial ROS production and the senescence-associated secretory phenotype through sirtuin 4/SIRT4. Aging 8: 484-505
149. Griffiths HR, Dias IH, Willetts RS, Devitt A. (2014). Redox regulation of protein damage in plasma. Redox. Biol. 2: 430-35
150. Kim HJ, Ha S, Lee HY, Lee KJ. (2015). ROSics: chemistry and proteomics of cysteine modifications in redox biology. Mass Spectrom. Rev. 34: 184-208
151. Oka OB, Bulleid NJ. (2013). Forming disulfides in the endoplasmic reticulum. Biochim. Biophys. Acta 1833: 2425-29
152. Ramming T, Hansen HG, Nagata K, Ellgaard L, Appenzeller-Herzog C. (2014). GPx8 peroxidase prevents leakage of H2O2 from the endoplasmic reticulum. Free Radic. Biol. Med. 70: 106-16
153. Chen YI, Wei PC, Hsu JL, Su FY, Lee WH. (2016). NPGPx (GPx7): a novel oxidative stress sensor/transmitter with multiple roles in redox homeostasis. Am. J. Transl. Res. 8: 1626-40
154. Appenzeller-Herzog C, Banhegyi G, Bogeski I, Davies KJ, Delaunay-Moisan A, et al. (2016). Transit of H2O2 across the endoplasmic reticulum membrane is not sluggish. Free Radic. Biol. Med. 94: 157-60
155. Kirstein J, Morito D, Kakihana T, Sugihara M, Minnen A, et al. (2015). Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments. EMBO J. 34: 2334-49
156. Hartl FU, Bracher A, Hayer-Hartl M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475: 324-32
157. Eletto D, Chevet E, Argon Y, Appenzeller-Herzog C. (2014). Redox controls UPR to control redox. J. Cell Sci. 127: 3649-58
158. Niforou K, Cheimonidou C, Trougakos IP. (2014). Molecular chaperones and proteostasis regulation during redox imbalance. Redox Biol. 2: 323-32
159. Niki E. (2014). Biomarkers of lipid peroxidation in clinical material. Biochim. Biophys. Acta 1840: 809-17
160. Spickett CM, Pitt AR. (2015). Oxidative lipidomics coming of age: advances in analysis of oxidized phospholipids in physiology and pathology. Antioxid. Redox. Signal. 22: 1646-66
161. Davies SS, Pontsler AV, Marathe GK, Harrison KA, Murphy RC, et al. (2001). Oxidized alkyl phospholipids are specific, high affinity peroxisome proliferator-activated receptor γligands and agonists. J. Biol. Chem. 276: 16015-23
162. Robertson RP. (2004). Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes. J. Biol. Chem. 279: 42351-54
163. Monnier VM, Cerami A. (1981). Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science 211: 491-93
164. Zachara NE, Hart GW. (2006). Cell signaling, the essential role of O-GlcNAc Biochim. Biophys. Acta 1761: 599-617
165. Kizuka Y, Nakano M, Kitazume S, Saito T, Saido TC, Taniguchi N. (2016). Bisecting GlcNAc modification stabilizes BACE1 protein under oxidative stress conditions. Biochem. J. 473: 21-30
166. Karababa A, Görg B, Schliess F, Häussinger D. (2014). O-GlcNAcylation as a novel ammonia-induced posttranslational protein modification in cultured rat astrocytes. Metab. Brain Dis. 29: 975-82
167. Griffiths HR, Moller L, Bartosz G, Bast A, Bertoni-Freddari C, et al. (2002). Biomarkers. Mol. Aspects Med. 23: 101-208
168. Frijhoff J, Winyard PG, Zarkovic N, Davies SS, Stocker R, et al. (2015). Clinical relevance of biomarkers of oxidative stress. Antioxid. Redox Signal. 23: 1144-70
169. Van't Erve TJ, Lih FB, Jelsema C, Deterding LJ, Eling TE, et al. (2016). Reinterpreting the best biomarker of oxidative stress: the 8-iso-prostaglandin F2α/prostaglandin F2α ratio shows complex origins of lipid peroxidation biomarkers in animal models. Free Radic. Biol. Med. 95: 65-73
170. Von Zglinicki T. (2002). Oxidative stress shortens telomeres. Trends Biochem. Sci. 27: 339-44
171. Collins AR. (2014). Measuring oxidative damage to DNA and its repair with the comet assay. Biochim. Biophys. Acta 1840: 794-800
172. Patel RS, Ghasemzadeh N, Eapen DJ, Sher S, Arshad S, et al. (2016). Novel biomarker of oxidative stress is associated with risk of death in patients with coronary artery disease. Circulation 133: 361-69
173. Schaefer L. (2014). Complexity of danger: the diverse nature of damage-associated molecular patterns. J. Biol. Chem. 289: 35237-45
174. Shapiro JA. (1998). Thinking about bacterial populations as multicellular organisms. Annu. Rev. Microbiol. 52: 81-104
175. Gambino M, Cappitelli F. (2016). Mini-review: biofilm responses to oxidative stress. Biofouling 32: 167-78
176. Stahl W, Sies H. (2012). β-Carotene and other carotenoids in protection from sunlight. Am. J. Clin. Nutr. 96: 1179S-84S
177. Cunningham GM, Roman MG, Flores LC, Hubbard GB, Salmon AB, et al. (2015). The paradoxical role of thioredoxin on oxidative stress and aging. Arch. Biochem. Biophys. 576: 32-38
178. Lei XG, Zhu JH, Cheng WH, Bao Y, Ho YS, et al. (2016). Paradoxical roles of antioxidant enzymes: basic mechanisms and health implications. Physiol. Rev. 96: 307-64
179. Szypowska AA, Burgering BM. (2011). The peroxide dilemma: opposing and mediating insulin action. Antioxid. Redox Signal. 15: 219-32
180. Lugrin J, Rosenblatt-Velin N, Parapanov R, Liaudet L. (2014). The role of oxidative stress during inflammatory processes. Biol. Chem. 395: 203-30
181. Nathan C, Cunningham-Bussel A. (2013). Beyond oxidative stress: an immunologist's guide to reactive oxygen species. Nat. Rev. Immunol. 13: 349-61
182. Stocker R, Keaney JF Jr. (2004). Role of oxidative modifications in atherosclerosis. Physiol. Rev. 84: 1381-478
183. Serhan CN, Chiang N, Van Dyke TE. (2008). Resolving inflammation: dual anti-inflammatory and proresolution lipid mediators. Nat. Rev. Immunol. 8: 349-61
184. Martinez-Outschoorn UE, Balliet RM, Rivadeneira DB, Chiavarina B, Pavlides S, et al. (2010). Oxidative stress in cancer associated fibroblasts drives tumor-stroma co-evolution: a new paradigm for understanding tumor metabolism, the field effect and genomic instability in cancer cells. Cell Cycle 9: 3256-76
185. Casas AI, Dao VT, Daiber A, Maghzal GJ, Di LF, et al. (2015). Reactive oxygen-related diseases: therapeutic targets and emerging clinical indications. Antioxid. Redox Signal. 23: 1171-85
186. Dao VT, Casas AI, Maghzal GJ, Seredenina T, Kaludercic N, et al. (2015). Pharmacology and clinical drug candidates in redox medicine. Antioxid. Redox Signal. 23: 1113-29
187. O'Neill P, Wardman P. (2009). Radiation chemistry comes before radiation biology. Int. J. Radiat. Biol. 85: 9-25
188. Chen J, Stubbe J. (2005). Bleomycins: towards better therapeutics. Nat. Rev. Cancer 5: 102-12
189. Reczek CR, Chandel NS. (2015). Cancer. Revisiting vitamin C and cancer. Science 350: 1317-18
190. Du J, Cieslak JA, Welsh JL, Sibenaller ZA, Allen BG, et al. (2015). Pharmacological ascorbate radiosensitizes pancreatic cancer. Cancer Res. 75: 3314-3326
191. Dougherty TJ, Gomer CJ, Henderson BW, Jori G, Kessel D, et al. (1998). Photodynamic therapy. J. Natl. Cancer Inst. 90: 889-905
192. Cordeiro JV, Jacinto A. (2013). The role of transcription-independent damage signals in the initiation of epithelial wound healing. Nat. Rev. Mol. Cell Biol. 14: 249-62
193. Toyokuni S. (2016). The origin and future of oxidative stress pathology: from the recognition of carcinogenesis as an iron addiction with ferroptosis-resistance to non-thermal plasma therapy. Pathol. Int. 66: 245-59
194. Isbary G, Morfill G, Schmidt HU, Georgi M, Ramrath K, et al. (2010). A first prospective randomized controlled trial to decrease bacterial load using cold atmospheric argon plasma on chronic wounds in patients. Brit. J. Dermatol. 163: 78-82
195. Harris IS, Treloar AE, Inoue S, Sasaki M, Gorrini C, et al. (2015). Glutathione and thioredoxin antioxidant pathways synergize to drive cancer initiation and progression. Cancer Cell 27: 211-22
196. Tobe R, Carlson BA, Tsuji PA, Lee BJ, Gladyshev VN, Hatfield DL. (2015). Differences in redox regulatory systems in human lung and liver tumors suggest different avenues for therapy. Cancers 7: 2262-76
197. Chun KS, Kundu J, Kundu JK, Surh YJ. (2014). Targeting Nrf2-Keap1 signaling for chemoprevention of skin carcinogenesis with bioactive phytochemicals. Toxicol. Lett. 229: 73-84
198. Buendia I, Michalska P, Navarro E, Gameiro I, Egea J, Leon R. (2016). Nrf2-ARE pathway: an emerging target against oxidative stress and neuroinflammation in neurodegenerative diseases. Pharmacol. Ther. 157: 84-104
199. Esteras N, Dinkova-Kostova AT, Abramov AY. (2016). Nrf2 activation in the treatment of neurodegenerative diseases: a focus on its role in mitochondrial bioenergetics and function. Biol. Chem. 397: 383-400
200. Brennan MS, Patel H, Allaire N, Thai A, Cullen P, et al. (2016). Pharmacodynamics of dimethyl fumarate are tissue specific and involve NRF2-dependent and -independent mechanisms. Antioxid. Redox Signal. 24: 1058-71
201. Lastres-Becker I, Garcia-Yague AJ, Scannevin RH, Casarejos MJ, Kugler S, et al. (2016). Repurposing the NRF2 activator dimethyl fumarate as therapy against synucleinopathy in Parkinson's disease. Antioxid. Redox Signal. 25: 61-77
202. Kaur SJ, McKeown SR, Rashid S. (2016). Mutant SOD1 mediated pathogenesis of amyotrophic lateral sclerosis. Gene 577: 109-18
203. Freitas-Andrade M, Naus CC. (2016). Astrocytes in neuroprotection and neurodegeneration: the role of connexin43 and pannexin1. Neuroscience 323: 207-21
204. Görg B, Schliess F, Häussinger D. (2013). Osmotic and oxidative/nitrosative stress in ammonia toxicity and hepatic encephalopathy. Arch. Biochem. Biophys. 536: 158-63
205. May JM, de Haen C. (1979). The insulin-like effect of hydrogen peroxide on pathways of lipid synthesis in rat adipocytes. J. Biol. Chem. 254: 9017-21
206. Loh K, Deng H, Fukushima A, Cai X, Boivin B, et al. (2009). Reactive oxygen species enhance insulin sensitivity. Cell Metab. 10: 260-72
207. Sies H, Stahl W, Sevanian A. (2005). Nutritional, dietary and postprandial oxidative stress. J. Nutr. 135: 969-72
208. Watson JD. (2014). Type 2 diabetes as a redox disease. Lancet 383: 841-43
209. Bilan DS, Belousov VV. (2017). New tools for redox biology: from imaging to manipulation. Free Radic. Biol. Med. In press. doi: 10.1016/j.freeradbiomed.2016.12.004
210. Valle G, Stanisloo M, Facciorusso A, Carmignani M, Volpe AR. (2009). Mithridates VI Eupator, father of the empirical toxicology. Clin. Toxicol. 47: 433
211. Borzelleca JF. (2000). Paracelsus: herald of modern toxicology. Toxicol. Sci. 53: 2-4
212. Holmes FL. (1986). Claude Bernard, the milieu intérieur, and regulatory physiology. Hist. Phil. Life Sci. 8: 3-25
213. Cannon WB. (1932). The Wisdom of the Body. New York: Norton
214. Oberbaum M, Gropp C. (2015). Update on hormesis and its relation to homeopathy. Homeopathy 105: 227-33
215. Southam CM, Ehrlich J. (1943). Effects of extracts of western red-cedar heartwood on certain wooddecaying fungi in culture. Phytopathology 33: 517-24
216. Calabrese EJ, Bachmann KA, Bailer AJ, Bolger PM, Borak J, et al. (2007). Biological stress response terminology: integrating the concepts of adaptive response and preconditioning stress within a hormetic dose-response framework. Toxicol. Appl. Pharmacol. 222: 122-28
217. Ritossa F. (1962). A new puffing pattern introduced by temperature shock and DNP in Drosophila. Experientia 18: 571-73
218. Christman MF, Morgan RW, Jacobson FS, Ames BN. (1985). Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 41: 753-62
219. Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. (1988). The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-64
220. Semenza GL, Wang GL. (1992). A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation. Mol. Cell. Biol. 12: 5447-54
221. Wondrak GT. (2009). Redox-directed cancer therapeutics: molecular mechanisms and opportunities. Antioxid. Redox Signal. 11: 3013-69
222. Kirkpatrick DL, Powis G. (2017). Clinically evaluated cancer drugs inhibiting redox signaling. Antioxid. Redox Signal. 26: 262-73