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Volumn 98, Issue , 2016, Pages 2-12

Going retro: Oxidative stress biomarkers in modern redox biology

Author keywords

Biomarkers; Oxidative stress; Pathology; Physiology; Redox signaling

Indexed keywords

BIOLOGICAL MARKER;

EID: 84958191682     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2016.02.005     Document Type: Article
Times cited : (71)

References (184)
  • 2
    • 23844540597 scopus 로고    scopus 로고
    • Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats
    • [2] Gomez-Cabrera, M.C., Borras, C., Pallardo, F.V., Sastre, J., Ji, L.L., Vina, J., Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats. J. Physiol. 567 (2005), 113–120.
    • (2005) J. Physiol. , vol.567 , pp. 113-120
    • Gomez-Cabrera, M.C.1    Borras, C.2    Pallardo, F.V.3    Sastre, J.4    Ji, L.L.5    Vina, J.6
  • 5
    • 0033042955 scopus 로고    scopus 로고
    • Establishing the significance and optimal intake of dietary antioxidants: the biomarker concept
    • [5] Halliwell, B., Establishing the significance and optimal intake of dietary antioxidants: the biomarker concept. Nutr. Rev. 57 (1999), 104–113.
    • (1999) Nutr. Rev. , vol.57 , pp. 104-113
    • Halliwell, B.1
  • 7
    • 84929493137 scopus 로고    scopus 로고
    • Influence of vitamin C and vitamin E on redox signaling: implications for exercise adaptations
    • [7] Cobley, J.N., McHardy, H., Morton, J.P., Nikolaidis, M.G., Close, G.L., Influence of vitamin C and vitamin E on redox signaling: implications for exercise adaptations. Free Radic. Biol. Med. 84 (2015), 65–76.
    • (2015) Free Radic. Biol. Med. , vol.84 , pp. 65-76
    • Cobley, J.N.1    McHardy, H.2    Morton, J.P.3    Nikolaidis, M.G.4    Close, G.L.5
  • 8
    • 84961347689 scopus 로고    scopus 로고
    • Principles for integrating reactive species into in vivo biological processes: examples from exercise physiology, Cell. Signal., pii: S0898−6568(15)30016−4. 10.1016/j.cellsig.2015.12.011.
    • [8] N.V. Margaritelis, J.N. Cobley, V. Paschalis, A.S. Veskoukis, A.A. Theodorou, A. Kyparos, M.G. Nikolaidis, Principles for integrating reactive species into in vivo biological processes: examples from exercise physiology, Cell. Signal., pii: S0898−6568(15)30016−4. 10.1016/j.cellsig.2015.12.011.
    • Margaritelis, N.V.1    Cobley, J.N.2    Paschalis, V.3    Veskoukis, A.S.4    Theodorou, A.A.5    Kyparos, A.6    Nikolaidis, M.G.7
  • 9
    • 0035100888 scopus 로고    scopus 로고
    • Biomarkers and surrogate endpoints: preferred definitions and conceptual framework
    • [9] Biomarkers Definitions Working, G. Biomarkers and surrogate endpoints: preferred definitions and conceptual framework. Clin. Pharmacol. Ther. 69 (2001), 89–95.
    • (2001) Clin. Pharmacol. Ther. , vol.69 , pp. 89-95
  • 10
    • 0036129318 scopus 로고    scopus 로고
    • Biomarkers in molecular epidemiology studies for health risk prediction
    • [10] Bonassi, S., Au, W.W., Biomarkers in molecular epidemiology studies for health risk prediction. Mutat. Res. 511 (2002), 73–86.
    • (2002) Mutat. Res. , vol.511 , pp. 73-86
    • Bonassi, S.1    Au, W.W.2
  • 11
    • 33747334038 scopus 로고    scopus 로고
    • Molecular epidemiology: new rules for new tools?
    • [11] Merlo, D.F., Sormani, M.P., Bruzzi, P., Molecular epidemiology: new rules for new tools?. Mutat. Res. 600 (2006), 3–11.
    • (2006) Mutat. Res. , vol.600 , pp. 3-11
    • Merlo, D.F.1    Sormani, M.P.2    Bruzzi, P.3
  • 12
    • 35448941232 scopus 로고    scopus 로고
    • Molecular epidemiology and biomarkers in etiologic cancer research: the new in light of the old
    • [12] Vineis, P., Perera, F., Molecular epidemiology and biomarkers in etiologic cancer research: the new in light of the old. Cancer Epidemiol. Biomark. Prev. 16 (2007), 1954–1965.
    • (2007) Cancer Epidemiol. Biomark. Prev. , vol.16 , pp. 1954-1965
    • Vineis, P.1    Perera, F.2
  • 13
    • 48249093095 scopus 로고    scopus 로고
    • Integration and use of biomarkers in drug development, regulation and clinical practice: a US regulatory perspective
    • [13] Amur, S., Frueh, F.W., Lesko, L.J., Huang, S.M., Integration and use of biomarkers in drug development, regulation and clinical practice: a US regulatory perspective. Biomark. Med. 2 (2008), 305–311.
    • (2008) Biomark. Med. , vol.2 , pp. 305-311
    • Amur, S.1    Frueh, F.W.2    Lesko, L.J.3    Huang, S.M.4
  • 14
    • 80052774208 scopus 로고    scopus 로고
    • Translational research: what does it mean, what has it delivered and what might it deliver?
    • [14] Proudfoot, A.G., McAuley, D.F., Hind, M., Griffiths, M.J., Translational research: what does it mean, what has it delivered and what might it deliver?. Curr. Opin. Crit. Care 17 (2011), 495–503.
    • (2011) Curr. Opin. Crit. Care , vol.17 , pp. 495-503
    • Proudfoot, A.G.1    McAuley, D.F.2    Hind, M.3    Griffiths, M.J.4
  • 15
    • 84876461744 scopus 로고    scopus 로고
    • Nutritional countermeasures targeting reactive oxygen species in cancer: from mechanisms to biomarkers and clinical evidence
    • [15] Samoylenko, A., Hossain, J.A., Mennerich, D., Kellokumpu, S., Hiltunen, J.K., Kietzmann, T., Nutritional countermeasures targeting reactive oxygen species in cancer: from mechanisms to biomarkers and clinical evidence. Antioxid. Redox Signal. 19 (2013), 2157–2196.
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 2157-2196
    • Samoylenko, A.1    Hossain, J.A.2    Mennerich, D.3    Kellokumpu, S.4    Hiltunen, J.K.5    Kietzmann, T.6
  • 17
    • 0006198863 scopus 로고    scopus 로고
    • Biomarkers of free radical damage applications in experimental animals and in humans
    • [17] de Zwart, L.L., Meerman, J.H., Commandeur, J.N., Vermeulen, N.P., Biomarkers of free radical damage applications in experimental animals and in humans. Free Radic. Biol. Med. 26 (1999), 202–226.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 202-226
    • de Zwart, L.L.1    Meerman, J.H.2    Commandeur, J.N.3    Vermeulen, N.P.4
  • 19
    • 84973508753 scopus 로고    scopus 로고
    • Protein oxidation products as biomarkers
    • [19] Grune, T., Protein oxidation products as biomarkers. Free Radic. Biol. Med., 75(Suppl. 1), 2014, S7.
    • (2014) Free Radic. Biol. Med. , vol.75 , pp. S7
    • Grune, T.1
  • 23
    • 13244279737 scopus 로고    scopus 로고
    • Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans
    • [23] Morrow, J.D., Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans. Arterioscler. Thromb. Vasc. Biol. 25 (2005), 279–286.
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 279-286
    • Morrow, J.D.1
  • 24
    • 84902369665 scopus 로고    scopus 로고
    • Mass spectrometry and 3-nitrotyrosine: strategies, controversies, and our current perspective
    • [24] Tsikas, D., Duncan, M.W., Mass spectrometry and 3-nitrotyrosine: strategies, controversies, and our current perspective. Mass Spectrom. Rev. 33 (2014), 237–276.
    • (2014) Mass Spectrom. Rev. , vol.33 , pp. 237-276
    • Tsikas, D.1    Duncan, M.W.2
  • 25
    • 84943276168 scopus 로고    scopus 로고
    • Tripping up Trp: modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences
    • [25] Ehrenshaft, M., Deterding, L.J., Mason, R.P., Tripping up Trp: modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences. Free Radic. Biol. Med. 89 (2015), 220–228.
    • (2015) Free Radic. Biol. Med. , vol.89 , pp. 220-228
    • Ehrenshaft, M.1    Deterding, L.J.2    Mason, R.P.3
  • 26
    • 50049091026 scopus 로고    scopus 로고
    • Repeated bouts of aerobic exercise lead to reductions in skeletal muscle free radical generation and nuclear factor kappaB activation
    • [26] Brooks, S.V., Vasilaki, A., Larkin, L.M., McArdle, A., Jackson, M.J., Repeated bouts of aerobic exercise lead to reductions in skeletal muscle free radical generation and nuclear factor kappaB activation. J. Physiol. 586 (2008), 3979–3990.
    • (2008) J. Physiol. , vol.586 , pp. 3979-3990
    • Brooks, S.V.1    Vasilaki, A.2    Larkin, L.M.3    McArdle, A.4    Jackson, M.J.5
  • 28
    • 84925536798 scopus 로고    scopus 로고
    • Exercise improves mitochondrial and redox-regulated stress responses in the elderly: better late than never!
    • [28] Cobley, J.N., Moult, P.R., Burniston, J.G., Morton, J.P., Close, G.L., Exercise improves mitochondrial and redox-regulated stress responses in the elderly: better late than never!. Biogerontology 16 (2015), 249–264.
    • (2015) Biogerontology , vol.16 , pp. 249-264
    • Cobley, J.N.1    Moult, P.R.2    Burniston, J.G.3    Morton, J.P.4    Close, G.L.5
  • 30
    • 37849021505 scopus 로고    scopus 로고
    • Moderate exercise is an antioxidant: upregulation of antioxidant genes by training
    • [30] Gomez-Cabrera, M.C., Domenech, E., Vina, J., Moderate exercise is an antioxidant: upregulation of antioxidant genes by training. Free Radic. Biol. Med. 44 (2008), 126–131.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 126-131
    • Gomez-Cabrera, M.C.1    Domenech, E.2    Vina, J.3
  • 31
    • 37849002320 scopus 로고    scopus 로고
    • Modulation of skeletal muscle antioxidant defense by exercise: role of redox signaling
    • [31] Ji, L.L., Modulation of skeletal muscle antioxidant defense by exercise: role of redox signaling. Free Radic. Biol. Med. 44 (2008), 142–152.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 142-152
    • Ji, L.L.1
  • 32
    • 78650699249 scopus 로고    scopus 로고
    • F(2)-isoprostane formation, measurement and interpretation: the role of exercise
    • [32] Nikolaidis, M.G., Kyparos, A., Vrabas, I.S., F(2)-isoprostane formation, measurement and interpretation: the role of exercise. Prog. Lipid Res. 50 (2011), 89–103.
    • (2011) Prog. Lipid Res. , vol.50 , pp. 89-103
    • Nikolaidis, M.G.1    Kyparos, A.2    Vrabas, I.S.3
  • 33
    • 38149131289 scopus 로고    scopus 로고
    • Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance
    • [33] Gomez-Cabrera, M.C., Domenech, E., Romagnoli, M., Arduini, A., Borras, C., Pallardo, F.V., Sastre, J., Vina, J., Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance. Am. J. Clin. Nutr. 87 (2008), 142–149.
    • (2008) Am. J. Clin. Nutr. , vol.87 , pp. 142-149
    • Gomez-Cabrera, M.C.1    Domenech, E.2    Romagnoli, M.3    Arduini, A.4    Borras, C.5    Pallardo, F.V.6    Sastre, J.7    Vina, J.8
  • 34
    • 79959479021 scopus 로고    scopus 로고
    • The dual role of p53: DNA protection and antioxidant
    • [34] Borras, C., Gomez-Cabrera, M.C., Vina, J., The dual role of p53: DNA protection and antioxidant. Free Radic. Res. 45 (2011), 643–652.
    • (2011) Free Radic. Res. , vol.45 , pp. 643-652
    • Borras, C.1    Gomez-Cabrera, M.C.2    Vina, J.3
  • 35
    • 84939789855 scopus 로고    scopus 로고
    • Redox regulation of muscle adaptations to contractile activity and aging
    • [35] Jackson, M.J., Redox regulation of muscle adaptations to contractile activity and aging. J. Appl. Physiol. (1985) 119 (2015), 163–171.
    • (2015) J. Appl. Physiol. (1985) , vol.119 , pp. 163-171
    • Jackson, M.J.1
  • 36
    • 33750161128 scopus 로고    scopus 로고
    • Adaptive responses of mouse skeletal muscle to contractile activity: the effect of age
    • [36] Vasilaki, A., McArdle, F., Iwanejko, L.M., McArdle, A., Adaptive responses of mouse skeletal muscle to contractile activity: the effect of age. Mech. Ageing Dev. 127 (2006), 830–839.
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 830-839
    • Vasilaki, A.1    McArdle, F.2    Iwanejko, L.M.3    McArdle, A.4
  • 38
    • 32244436294 scopus 로고    scopus 로고
    • The role of NF-kappaB in protein breakdown in immobilization, aging, and exercise: from basic processes to promotion of health
    • [38] Bar-Shai, M., Carmeli, E., Reznick, A.Z., The role of NF-kappaB in protein breakdown in immobilization, aging, and exercise: from basic processes to promotion of health. Ann. N. Y. Acad. Sci. 1057 (2005), 431–447.
    • (2005) Ann. N. Y. Acad. Sci. , vol.1057 , pp. 431-447
    • Bar-Shai, M.1    Carmeli, E.2    Reznick, A.Z.3
  • 39
    • 76149090178 scopus 로고    scopus 로고
    • Interplay of oxidants and antioxidants during exercise: implications for muscle health
    • [39] Gomez-Cabrera, M.C., Vina, J., Ji, L.L., Interplay of oxidants and antioxidants during exercise: implications for muscle health. Phys. Sportsmed. 37 (2009), 116–123.
    • (2009) Phys. Sportsmed. , vol.37 , pp. 116-123
    • Gomez-Cabrera, M.C.1    Vina, J.2    Ji, L.L.3
  • 40
    • 59649104233 scopus 로고    scopus 로고
    • The IkappaB kinases IKKalpha and IKKbeta are necessary and sufficient for skeletal muscle atrophy
    • [40] Van Gammeren, D., Damrauer, J.S., Jackman, R.W., Kandarian, S.C., The IkappaB kinases IKKalpha and IKKbeta are necessary and sufficient for skeletal muscle atrophy. FASEB J. 23 (2009), 362–370.
    • (2009) FASEB J. , vol.23 , pp. 362-370
    • Van Gammeren, D.1    Damrauer, J.S.2    Jackman, R.W.3    Kandarian, S.C.4
  • 41
    • 84940041547 scopus 로고    scopus 로고
    • The basic chemistry of exercise-induced DNA oxidation: oxidative damage, redox signaling, and their interplay
    • [41] Cobley, J.N., Margaritelis, N.V., Morton, J.P., Close, G.L., Nikolaidis, M.G., Malone, J.K., The basic chemistry of exercise-induced DNA oxidation: oxidative damage, redox signaling, and their interplay. Front. Physiol., 6, 2015, 182.
    • (2015) Front. Physiol. , vol.6 , pp. 182
    • Cobley, J.N.1    Margaritelis, N.V.2    Morton, J.P.3    Close, G.L.4    Nikolaidis, M.G.5    Malone, J.K.6
  • 43
    • 79954590152 scopus 로고    scopus 로고
    • Variability in training-induced skeletal muscle adaptation
    • [43] Timmons, J.A., Variability in training-induced skeletal muscle adaptation. J. Appl. Physiol. (1985) 110 (2011), 846–853.
    • (2011) J. Appl. Physiol. (1985) , vol.110 , pp. 846-853
    • Timmons, J.A.1
  • 46
    • 71849114694 scopus 로고    scopus 로고
    • Oxidative stress and human diseases: origin, link, measurement, mechanisms, and biomarkers
    • [46] Giustarini, D., Dalle-Donne, I., Tsikas, D., Rossi, R., Oxidative stress and human diseases: origin, link, measurement, mechanisms, and biomarkers. Crit. Rev. Clin. Lab. Sci. 46 (2009), 241–281.
    • (2009) Crit. Rev. Clin. Lab. Sci. , vol.46 , pp. 241-281
    • Giustarini, D.1    Dalle-Donne, I.2    Tsikas, D.3    Rossi, R.4
  • 47
    • 0034525341 scopus 로고    scopus 로고
    • Review of human studies on oxidative damage and antioxidant protection related to cardiovascular diseases
    • [47] Aviram, M., Review of human studies on oxidative damage and antioxidant protection related to cardiovascular diseases. Free Radic. Res. 33:Suppl. (2000), S85–S97.
    • (2000) Free Radic. Res. , vol.33 , pp. S85-S97
    • Aviram, M.1
  • 48
    • 0037093739 scopus 로고    scopus 로고
    • Effect of diet on cancer development: is oxidative DNA damage a biomarker?
    • [48] Halliwell, B., Effect of diet on cancer development: is oxidative DNA damage a biomarker?. Free Radic. Biol. Med. 32 (2002), 968–974.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 968-974
    • Halliwell, B.1
  • 50
    • 43149108399 scopus 로고    scopus 로고
    • Antioxidant vitamins and cancer risk: is oxidative damage to DNA a relevant biomarker?
    • [50] Loft, S., Moller, P., Cooke, M.S., Rozalski, R., Olinski, R., Antioxidant vitamins and cancer risk: is oxidative damage to DNA a relevant biomarker?. Eur. J. Nutr. 47:Suppl. 2 (2008), 19–28.
    • (2008) Eur. J. Nutr. , vol.47 , pp. 19-28
    • Loft, S.1    Moller, P.2    Cooke, M.S.3    Rozalski, R.4    Olinski, R.5
  • 51
    • 27744440994 scopus 로고    scopus 로고
    • Effect of daily fruit ingestion on angiotensin converting enzyme activity, blood pressure, and oxidative stress in chronic smokers
    • [51] McAnulty, S.R., McAnulty, L.S., Morrow, J.D., Khardouni, D., Shooter, L., Monk, J., Gross, S., Brown, V., Effect of daily fruit ingestion on angiotensin converting enzyme activity, blood pressure, and oxidative stress in chronic smokers. Free Radic. Res. 39 (2005), 1241–1248.
    • (2005) Free Radic. Res. , vol.39 , pp. 1241-1248
    • McAnulty, S.R.1    McAnulty, L.S.2    Morrow, J.D.3    Khardouni, D.4    Shooter, L.5    Monk, J.6    Gross, S.7    Brown, V.8
  • 52
    • 84934926971 scopus 로고    scopus 로고
    • Plasma F2-isoprostane class VI isomers at 12−18 weeks of pregnancy are associated with later occurrence of preeclampsia
    • [52] Bilodeau, J.F., Qin Wei, S., Larose, J., Greffard, K., Moisan, V., Audibert, F., Fraser, W.D., Julien, P., Plasma F2-isoprostane class VI isomers at 12−18 weeks of pregnancy are associated with later occurrence of preeclampsia. Free Radic. Biol. Med. 85 (2015), 282–287.
    • (2015) Free Radic. Biol. Med. , vol.85 , pp. 282-287
    • Bilodeau, J.F.1    Qin Wei, S.2    Larose, J.3    Greffard, K.4    Moisan, V.5    Audibert, F.6    Fraser, W.D.7    Julien, P.8
  • 53
    • 0036196952 scopus 로고    scopus 로고
    • Effects of alpha-tocopherol supplementation and continuous subcutaneous insulin infusion on oxidative stress in Korean patients with type 2 diabetes
    • [53] Park, S., Choi, S.B., Effects of alpha-tocopherol supplementation and continuous subcutaneous insulin infusion on oxidative stress in Korean patients with type 2 diabetes. Am. J. Clin. Nutr. 75 (2002), 728–733.
    • (2002) Am. J. Clin. Nutr. , vol.75 , pp. 728-733
    • Park, S.1    Choi, S.B.2
  • 56
  • 58
    • 0034906822 scopus 로고    scopus 로고
    • Training practices and overtraining syndrome in Swedish age-group athletes
    • [58] Kentta, G., Hassmen, P., Raglin, J.S., Training practices and overtraining syndrome in Swedish age-group athletes. Int. J. Sports Med. 22 (2001), 460–465.
    • (2001) Int. J. Sports Med. , vol.22 , pp. 460-465
    • Kentta, G.1    Hassmen, P.2    Raglin, J.S.3
  • 59
    • 0031043740 scopus 로고    scopus 로고
    • Resistance exercise overtraining and overreaching. Neuroendocrine responses
    • [59] Fry, A.C., Kraemer, W.J., Resistance exercise overtraining and overreaching. Neuroendocrine responses. Sports Med. 23 (1997), 106–129.
    • (1997) Sports Med. , vol.23 , pp. 106-129
    • Fry, A.C.1    Kraemer, W.J.2
  • 60
    • 28444468750 scopus 로고    scopus 로고
    • Biochemical and immunological markers of over-training
    • [60] Gleeson, M., Biochemical and immunological markers of over-training. J. Sports Sci. Med. 1 (2002), 31–41.
    • (2002) J. Sports Sci. Med. , vol.1 , pp. 31-41
    • Gleeson, M.1
  • 62
    • 79961014440 scopus 로고    scopus 로고
    • NADPH oxidase: a target for the modulation of the excessive oxidase damage induced by overtraining in rat neutrophils
    • [62] Dong, J., Chen, P., Wang, R., Yu, D., Zhang, Y., Xiao, W., NADPH oxidase: a target for the modulation of the excessive oxidase damage induced by overtraining in rat neutrophils. Int. J. Biol. Sci. 7 (2011), 881–891.
    • (2011) Int. J. Biol. Sci. , vol.7 , pp. 881-891
    • Dong, J.1    Chen, P.2    Wang, R.3    Yu, D.4    Zhang, Y.5    Xiao, W.6
  • 63
    • 33344460250 scopus 로고    scopus 로고
    • Antioxidant status and oxidative stress in professional rugby players: evolution throughout a season
    • [63] Finaud, J., Scislowski, V., Lac, G., Durand, D., Vidalin, H., Robert, A., Filaire, E., Antioxidant status and oxidative stress in professional rugby players: evolution throughout a season. Int. J. Sports Med. 27 (2006), 87–93.
    • (2006) Int. J. Sports Med. , vol.27 , pp. 87-93
    • Finaud, J.1    Scislowski, V.2    Lac, G.3    Durand, D.4    Vidalin, H.5    Robert, A.6    Filaire, E.7
  • 67
    • 77949391048 scopus 로고    scopus 로고
    • Altered oxidative stress in overtrained athletes
    • [67] Tanskanen, M., Atalay, M., Uusitalo, A., Altered oxidative stress in overtrained athletes. J. Sports Sci. 28 (2010), 309–317.
    • (2010) J. Sports Sci. , vol.28 , pp. 309-317
    • Tanskanen, M.1    Atalay, M.2    Uusitalo, A.3
  • 68
    • 33745819984 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress in overload training and tapering
    • [68] Vollaard, N.B., Cooper, C.E., Shearman, J.P., Exercise-induced oxidative stress in overload training and tapering. Med. Sci. Sports Exerc. 38 (2006), 1335–1341.
    • (2006) Med. Sci. Sports Exerc. , vol.38 , pp. 1335-1341
    • Vollaard, N.B.1    Cooper, C.E.2    Shearman, J.P.3
  • 69
    • 84980374828 scopus 로고    scopus 로고
    • Low vitamin C values are linked with decreased physical performance and increased oxidative stress: reversal by vitamin C supplementation. Eur. J. Nutr.
    • [69] V. Paschalis, A.A. Theodorou, A. Kyparos, K. Dipla, A. Zafeiridis, G. Panayiotou, I.S. Vrabas, M.G. Nikolaidis, Low vitamin C values are linked with decreased physical performance and increased oxidative stress: reversal by vitamin C supplementation. Eur. J. Nutr. (2014).
    • (2014)
    • Paschalis, V.1    Theodorou, A.A.2    Kyparos, A.3    Dipla, K.4    Zafeiridis, A.5    Panayiotou, G.6    Vrabas, I.S.7    Nikolaidis, M.G.8
  • 71
    • 84910146693 scopus 로고    scopus 로고
    • Passive smoking reduces and vitamin C increases exercise-induced oxidative stress: does this make passive smoking an anti-oxidant and vitamin C a pro-oxidant stimulus?
    • [71] Theodorou, A.A., Paschalis, V., Kyparos, A., Panayiotou, G., Nikolaidis, M.G., Passive smoking reduces and vitamin C increases exercise-induced oxidative stress: does this make passive smoking an anti-oxidant and vitamin C a pro-oxidant stimulus?. Biochem. Biophys. Res. Commun. 454 (2014), 131–136.
    • (2014) Biochem. Biophys. Res. Commun. , vol.454 , pp. 131-136
    • Theodorou, A.A.1    Paschalis, V.2    Kyparos, A.3    Panayiotou, G.4    Nikolaidis, M.G.5
  • 72
    • 84930941319 scopus 로고    scopus 로고
    • Redox modulation of mitochondriogenesis in exercise. Does antioxidant supplementation blunt the benefits of exercise training?
    • [72] Gomez-Cabrera, M.C., Salvador-Pascual, A., Cabo, H., Ferrando, B., Vina, J., Redox modulation of mitochondriogenesis in exercise. Does antioxidant supplementation blunt the benefits of exercise training?. Free Radic. Biol. Med. 86 (2015), 37–46.
    • (2015) Free Radic. Biol. Med. , vol.86 , pp. 37-46
    • Gomez-Cabrera, M.C.1    Salvador-Pascual, A.2    Cabo, H.3    Ferrando, B.4    Vina, J.5
  • 73
    • 84961343826 scopus 로고    scopus 로고
    • Antioxidants in Athlete's Basic Nutrition: Considerations towards a Guideline for the Intake of Vitamin C and Vitamin E
    • M. Lamprecht
    • [73] Neubauer, O., Yfanti, C., Antioxidants in Athlete's Basic Nutrition: Considerations towards a Guideline for the Intake of Vitamin C and Vitamin E. Lamprecht, M., (eds.) Antioxidants in Sport Nutrition. Boca Raton, FL, 2015.
    • (2015) Antioxidants in Sport Nutrition. Boca Raton, FL
    • Neubauer, O.1    Yfanti, C.2
  • 76
    • 77954973280 scopus 로고    scopus 로고
    • Efficacy of antioxidant vitamins and selenium supplement in prostate cancer prevention: a meta-analysis of randomized controlled trials
    • [76] Jiang, L., Yang, K.H., Tian, J.H., Guan, Q.L., Yao, N., Cao, N., Mi, D.H., Wu, J., Ma, B., Yang, S.H., Efficacy of antioxidant vitamins and selenium supplement in prostate cancer prevention: a meta-analysis of randomized controlled trials. Nutr. Cancer 62 (2010), 719–727.
    • (2010) Nutr. Cancer , vol.62 , pp. 719-727
    • Jiang, L.1    Yang, K.H.2    Tian, J.H.3    Guan, Q.L.4    Yao, N.5    Cao, N.6    Mi, D.H.7    Wu, J.8    Ma, B.9    Yang, S.H.10
  • 77
    • 84866157093 scopus 로고    scopus 로고
    • Does vitamin C and E supplementation impair the favorable adaptations of regular exercise?
    • [77] Nikolaidis, M.G., Kerksick, C.M., Lamprecht, M., McAnulty, S.R., Does vitamin C and E supplementation impair the favorable adaptations of regular exercise?. Oxid. Med. Cell Longev., 2012, 707941.
    • (2012) Oxid. Med. Cell Longev. , pp. 707941
    • Nikolaidis, M.G.1    Kerksick, C.M.2    Lamprecht, M.3    McAnulty, S.R.4
  • 78
    • 84860331697 scopus 로고    scopus 로고
    • Free radicals and antioxidants: updating a personal view
    • [78] Halliwell, B., Free radicals and antioxidants: updating a personal view. Nutr. Rev. 70 (2012), 257–265.
    • (2012) Nutr. Rev. , vol.70 , pp. 257-265
    • Halliwell, B.1
  • 79
    • 0027603748 scopus 로고
    • Measurement of oxidative stress status in humans
    • [79] Pryor, W.A., Measurement of oxidative stress status in humans. Cancer Epidemiol. Biomark. Prev. 2 (1993), 289–292.
    • (1993) Cancer Epidemiol. Biomark. Prev. , vol.2 , pp. 289-292
    • Pryor, W.A.1
  • 81
  • 84
    • 84890084174 scopus 로고    scopus 로고
    • Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases
    • [84] Sakellariou, G.K., Jackson, M.J., Vasilaki, A., Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases. Free Radic. Res. 48 (2014), 12–29.
    • (2014) Free Radic. Res. , vol.48 , pp. 12-29
    • Sakellariou, G.K.1    Jackson, M.J.2    Vasilaki, A.3
  • 85
    • 79954504166 scopus 로고    scopus 로고
    • Basic principles and emerging concepts in the redox control of transcription factors
    • [85] Brigelius-Flohe, R., Flohe, L., Basic principles and emerging concepts in the redox control of transcription factors. Antioxid. Redox Signal. 15 (2011), 2335–2381.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 2335-2381
    • Brigelius-Flohe, R.1    Flohe, L.2
  • 86
    • 84867361927 scopus 로고    scopus 로고
    • Redox biology on the rise
    • [86] Herrmann, J.M., Dick, T.P., Redox biology on the rise. Biol. Chem. 393 (2012), 999–1004.
    • (2012) Biol. Chem. , vol.393 , pp. 999-1004
    • Herrmann, J.M.1    Dick, T.P.2
  • 87
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • [87] Winterbourn, C.C., Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 4 (2008), 278–286.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 91
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • [91] Wood, Z.A., Poole, L.B., Karplus, P.A., Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300 (2003), 650–653.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 92
    • 0015240146 scopus 로고
    • Lipids and fatty acids of sarcolemma, sarcoplasmic reticulum, and mitochondria from rat skeletal muscle
    • [92] Fiehn, W., Peter, J.B., Mead, J.F., Gan-Elepano, M., Lipids and fatty acids of sarcolemma, sarcoplasmic reticulum, and mitochondria from rat skeletal muscle. J. Biol. Chem. 246 (1971), 5617–5620.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5617-5620
    • Fiehn, W.1    Peter, J.B.2    Mead, J.F.3    Gan-Elepano, M.4
  • 93
    • 70349840473 scopus 로고    scopus 로고
    • Blood as a reactive species generator and redox status regulator during exercise
    • [93] Nikolaidis, M.G., Jamurtas, A.Z., Blood as a reactive species generator and redox status regulator during exercise. Arch. Biochem. Biophys. 490 (2009), 77–84.
    • (2009) Arch. Biochem. Biophys. , vol.490 , pp. 77-84
    • Nikolaidis, M.G.1    Jamurtas, A.Z.2
  • 94
    • 0033405521 scopus 로고    scopus 로고
    • Oxidative stress status: OSS, BOSS, and “Wild Bill” Donovan
    • [94] Pryor, W.A., Oxidative stress status: OSS, BOSS, and “Wild Bill” Donovan. Free Radic. Biol. Med. 27 (1999), 1135–1136.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1135-1136
    • Pryor, W.A.1
  • 95
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: the long and uncertain path to clinical utility
    • [95] Rifai, N., Gillette, M.A., Carr, S.A., Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat. Biotechnol. 24 (2006), 971–983.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 96
    • 0034659128 scopus 로고    scopus 로고
    • FORUM: oxidation and atherosclerosis
    • [96] Pryor, W.A., FORUM: oxidation and atherosclerosis. Free Radic. Biol. Med. 28 (2000), 1681–1682.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1681-1682
    • Pryor, W.A.1
  • 97
    • 0030827263 scopus 로고    scopus 로고
    • Autoantibodies against oxidized LDL. A potential marker for atherosclerosis
    • [97] Wu, J.T., Wu, L.L., Autoantibodies against oxidized LDL. A potential marker for atherosclerosis. Clin. Lab. Med. 17 (1997), 595–604.
    • (1997) Clin. Lab. Med. , vol.17 , pp. 595-604
    • Wu, J.T.1    Wu, L.L.2
  • 99
    • 70350128251 scopus 로고    scopus 로고
    • Blood reflects tissue oxidative stress depending on biomarker and tissue studied
    • [99] Veskoukis, A.S., Nikolaidis, M.G., Kyparos, A., Kouretas, D., Blood reflects tissue oxidative stress depending on biomarker and tissue studied. Free Radic. Biol. Med. 47 (2009), 1371–1374.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1371-1374
    • Veskoukis, A.S.1    Nikolaidis, M.G.2    Kyparos, A.3    Kouretas, D.4
  • 105
    • 48249118740 scopus 로고    scopus 로고
    • A targetable fluorescent probe for imaging hydrogen peroxide in the mitochondria of living cells
    • [105] Dickinson, B.C., Chang, C.J., A targetable fluorescent probe for imaging hydrogen peroxide in the mitochondria of living cells. J. Am. Chem. Soc. 130 (2008), 9638–9639.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9638-9639
    • Dickinson, B.C.1    Chang, C.J.2
  • 106
    • 84891778532 scopus 로고    scopus 로고
    • Methods for detection of mitochondrial and cellular reactive oxygen species
    • [106] Dikalov, S.I., Harrison, D.G., Methods for detection of mitochondrial and cellular reactive oxygen species. Antioxid. Redox Signal. 20 (2014), 372–382.
    • (2014) Antioxid. Redox Signal. , vol.20 , pp. 372-382
    • Dikalov, S.I.1    Harrison, D.G.2
  • 107
    • 77954356493 scopus 로고    scopus 로고
    • Fluorescent protein-based redox probes
    • [107] Meyer, A.J., Dick, T.P., Fluorescent protein-based redox probes. Antioxid. Redox Signal. 13 (2010), 621–650.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 621-650
    • Meyer, A.J.1    Dick, T.P.2
  • 108
    • 28444495141 scopus 로고    scopus 로고
    • Boronate-based fluorescent probes for imaging cellular hydrogen peroxide
    • [108] Miller, E.W., Albers, A.E., Pralle, A., Isacoff, E.Y., Chang, C.J., Boronate-based fluorescent probes for imaging cellular hydrogen peroxide. J. Am. Chem. Soc. 127 (2005), 16652–16659.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16652-16659
    • Miller, E.W.1    Albers, A.E.2    Pralle, A.3    Isacoff, E.Y.4    Chang, C.J.5
  • 109
    • 77952542916 scopus 로고    scopus 로고
    • Application of the Amplex red/horseradish peroxidase assay to measure hydrogen peroxide generation by recombinant microsomal enzymes
    • [109] Mishin, V., Gray, J.P., Heck, D.E., Laskin, D.L., Laskin, J.D., Application of the Amplex red/horseradish peroxidase assay to measure hydrogen peroxide generation by recombinant microsomal enzymes. Free Radic. Biol. Med. 48 (2010), 1485–1491.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 1485-1491
    • Mishin, V.1    Gray, J.P.2    Heck, D.E.3    Laskin, D.L.4    Laskin, J.D.5
  • 110
    • 0035891533 scopus 로고    scopus 로고
    • Detection of reactive oxygen and reactive nitrogen species in skeletal muscle
    • [110] Murrant, C.L., Reid, M.B., Detection of reactive oxygen and reactive nitrogen species in skeletal muscle. Microsc. Res. Tech. 55 (2001), 236–248.
    • (2001) Microsc. Res. Tech. , vol.55 , pp. 236-248
    • Murrant, C.L.1    Reid, M.B.2
  • 111
    • 84893470593 scopus 로고    scopus 로고
    • Genetically encoded reactive oxygen species (ROS) and redox indicators
    • [111] Pouvreau, S., Genetically encoded reactive oxygen species (ROS) and redox indicators. Biotechnol. J 9 (2014), 282–293.
    • (2014) Biotechnol. J , vol.9 , pp. 282-293
    • Pouvreau, S.1
  • 112
    • 80155167926 scopus 로고    scopus 로고
    • Mitochondria-targeted small molecule therapeutics and probes
    • [112] Smith, R.A., Hartley, R.C., Murphy, M.P., Mitochondria-targeted small molecule therapeutics and probes. Antioxid. Redox Signal. 15 (2011), 3021–3038.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 3021-3038
    • Smith, R.A.1    Hartley, R.C.2    Murphy, M.P.3
  • 113
    • 84890114880 scopus 로고    scopus 로고
    • The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells
    • [113] Winterbourn, C.C., The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells. Biochim. Biophys. Acta 1840 (2014), 730–738.
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 730-738
    • Winterbourn, C.C.1
  • 114
    • 0035143723 scopus 로고    scopus 로고
    • Invited review: redox modulation of skeletal muscle contraction: what we know and what we don't
    • [114] Reid, M.B., Invited review: redox modulation of skeletal muscle contraction: what we know and what we don't. J. Appl. Physiol. (1985) 90 (2001), 724–731.
    • (2001) J. Appl. Physiol. (1985) , vol.90 , pp. 724-731
    • Reid, M.B.1
  • 115
    • 34147152905 scopus 로고    scopus 로고
    • The role of free radicals in the pathophysiology of muscular dystrophy
    • [115] Tidball, J.G., Wehling-Henricks, M., The role of free radicals in the pathophysiology of muscular dystrophy. J. Appl. Physiol. (1985) 102 (2007), 1677–1686.
    • (2007) J. Appl. Physiol. (1985) , vol.102 , pp. 1677-1686
    • Tidball, J.G.1    Wehling-Henricks, M.2
  • 116
    • 78650877942 scopus 로고    scopus 로고
    • Skeletal muscle NADPH oxidase is increased and triggers stretch-induced damage in the mdx mouse
    • [116] Whitehead, N.P., Yeung, E.W., Froehner, S.C., Allen, D.G., Skeletal muscle NADPH oxidase is increased and triggers stretch-induced damage in the mdx mouse. PLoS One, 5, 2010, e15354.
    • (2010) PLoS One , vol.5 , pp. e15354
    • Whitehead, N.P.1    Yeung, E.W.2    Froehner, S.C.3    Allen, D.G.4
  • 117
    • 84944745220 scopus 로고    scopus 로고
    • Potential molecular mechanisms underlying muscle fatigue mediated by reactive oxygen and nitrogen species
    • [117] Debold, E.P., Potential molecular mechanisms underlying muscle fatigue mediated by reactive oxygen and nitrogen species. Front. Physiol., 6, 2015, 239.
    • (2015) Front. Physiol. , vol.6 , pp. 239
    • Debold, E.P.1
  • 118
    • 80052985519 scopus 로고    scopus 로고
    • Emerging roles of ROS/RNS in muscle function and fatigue
    • [118] Westerblad, H., Allen, D.G., Emerging roles of ROS/RNS in muscle function and fatigue. Antioxid. Redox Signal. 15 (2011), 2487–2499.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 2487-2499
    • Westerblad, H.1    Allen, D.G.2
  • 119
    • 81855199913 scopus 로고    scopus 로고
    • Structural and functional impact of site-directed methionine oxidation in myosin
    • [119] Klein, J.C., Moen, R.J., Smith, E.A., Titus, M.A., Thomas, D.D., Structural and functional impact of site-directed methionine oxidation in myosin. Biochemistry 50 (2011), 10318–10327.
    • (2011) Biochemistry , vol.50 , pp. 10318-10327
    • Klein, J.C.1    Moen, R.J.2    Smith, E.A.3    Titus, M.A.4    Thomas, D.D.5
  • 123
    • 42449110720 scopus 로고    scopus 로고
    • Rapid and extensive uptake and activation of hydrophobic triphenylphosphonium cations within cells
    • [123] Ross, M.F., Prime, T.A., Abakumova, I., James, A.M., Porteous, C.M., Smith, R.A., Murphy, M.P., Rapid and extensive uptake and activation of hydrophobic triphenylphosphonium cations within cells. Biochem. J. 411 (2008), 633–645.
    • (2008) Biochem. J. , vol.411 , pp. 633-645
    • Ross, M.F.1    Prime, T.A.2    Abakumova, I.3    James, A.M.4    Porteous, C.M.5    Smith, R.A.6    Murphy, M.P.7
  • 124
    • 84958622777 scopus 로고    scopus 로고
    • Targeting mitochondria with small molecules: the preparation of MitoB and MitoP as exomarkers of mitochondrial hydrogen peroxide
    • [124] Cairns, A.G., McQuaker, S.J., Murphy, M.P., Hartley, R.C., Targeting mitochondria with small molecules: the preparation of MitoB and MitoP as exomarkers of mitochondrial hydrogen peroxide. Methods Mol. Biol. 1265 (2015), 25–50.
    • (2015) Methods Mol. Biol. , vol.1265 , pp. 25-50
    • Cairns, A.G.1    McQuaker, S.J.2    Murphy, M.P.3    Hartley, R.C.4
  • 125
    • 34548507495 scopus 로고    scopus 로고
    • Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications
    • [125] Ying, J., Clavreul, N., Sethuraman, M., Adachi, T., Cohen, R.A., Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications. Free Radic. Biol. Med. 43 (2007), 1099–1108.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1099-1108
    • Ying, J.1    Clavreul, N.2    Sethuraman, M.3    Adachi, T.4    Cohen, R.A.5
  • 126
    • 84872254434 scopus 로고    scopus 로고
    • Redox proteomics: chemical principles, methodological approaches and biological/biomedical promises
    • [126] Bachi, A., Dalle-Donne, I., Scaloni, A., Redox proteomics: chemical principles, methodological approaches and biological/biomedical promises. Chem. Rev. 113 (2013), 596–698.
    • (2013) Chem. Rev. , vol.113 , pp. 596-698
    • Bachi, A.1    Dalle-Donne, I.2    Scaloni, A.3
  • 127
    • 79959438797 scopus 로고    scopus 로고
    • Proteomic responses of skeletal and cardiac muscle to exercise
    • [127] Burniston, J.G., Hoffman, E.P., Proteomic responses of skeletal and cardiac muscle to exercise. Expert Rev. Proteom. 8 (2011), 361–377.
    • (2011) Expert Rev. Proteom. , vol.8 , pp. 361-377
    • Burniston, J.G.1    Hoffman, E.P.2
  • 129
    • 43249093987 scopus 로고    scopus 로고
    • Oxidized phospholipids: emerging lipid mediators in pathophysiology
    • [129] Deigner, H.P., Hermetter, A., Oxidized phospholipids: emerging lipid mediators in pathophysiology. Curr. Opin. Lipidol. 19 (2008), 289–294.
    • (2008) Curr. Opin. Lipidol. , vol.19 , pp. 289-294
    • Deigner, H.P.1    Hermetter, A.2
  • 130
    • 84937731185 scopus 로고    scopus 로고
    • Site-specific proteomic mapping identifies selectively modified regulatory cysteine residues in functionally distinct protein networks
    • [130] Gould, N.S., Evans, P., Martinez-Acedo, P., Marino, S.M., Gladyshev, V.N., Carroll, K.S., Ischiropoulos, H., Site-specific proteomic mapping identifies selectively modified regulatory cysteine residues in functionally distinct protein networks. Chem. Biol. 22 (2015), 965–975.
    • (2015) Chem. Biol. , vol.22 , pp. 965-975
    • Gould, N.S.1    Evans, P.2    Martinez-Acedo, P.3    Marino, S.M.4    Gladyshev, V.N.5    Carroll, K.S.6    Ischiropoulos, H.7
  • 131
    • 84905826571 scopus 로고    scopus 로고
    • Application of redox proteomics to skeletal muscle aging and exercise
    • [131] McDonagh, B., Sakellariou, G.K., Jackson, M.J., Application of redox proteomics to skeletal muscle aging and exercise. Biochem. Soc. Trans. 42 (2014), 965–970.
    • (2014) Biochem. Soc. Trans. , vol.42 , pp. 965-970
    • McDonagh, B.1    Sakellariou, G.K.2    Jackson, M.J.3
  • 132
    • 84930677412 scopus 로고    scopus 로고
    • Oxidative lipidomics coming of age: advances in analysis of oxidized phospholipids in physiology and pathology
    • [132] Spickett, C.M., Pitt, A.R., Oxidative lipidomics coming of age: advances in analysis of oxidized phospholipids in physiology and pathology. Antioxid. Redox Signal. 22 (2015), 1646–1666.
    • (2015) Antioxid. Redox Signal. , vol.22 , pp. 1646-1666
    • Spickett, C.M.1    Pitt, A.R.2
  • 135
    • 84897916912 scopus 로고    scopus 로고
    • Protein carbonylation and muscle function in COPD and other conditions
    • [135] Barreiro, E., Protein carbonylation and muscle function in COPD and other conditions. Mass Spectrom. Rev. 33 (2014), 219–236.
    • (2014) Mass Spectrom. Rev. , vol.33 , pp. 219-236
    • Barreiro, E.1
  • 136
    • 75149149380 scopus 로고    scopus 로고
    • Protein carbonylation in skeletal muscles: impact on function
    • [136] Barreiro, E., Hussain, S.N., Protein carbonylation in skeletal muscles: impact on function. Antioxid. Redox Signal. 12 (2010), 417–429.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 417-429
    • Barreiro, E.1    Hussain, S.N.2
  • 137
    • 84893775972 scopus 로고    scopus 로고
    • Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies
    • [137] Fedorova, M., Bollineni, R.C., Hoffmann, R., Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies. Mass Spectrom. Rev. 33 (2014), 79–97.
    • (2014) Mass Spectrom. Rev. , vol.33 , pp. 79-97
    • Fedorova, M.1    Bollineni, R.C.2    Hoffmann, R.3
  • 140
    • 73349102177 scopus 로고    scopus 로고
    • Transduction of redox signaling by electrophile-protein reactions
    • [140] Rudolph, T.K., Freeman, B.A., Transduction of redox signaling by electrophile-protein reactions. Sci. Signal., 2, 2009, re7.
    • (2009) Sci. Signal. , vol.2 , pp. re7
    • Rudolph, T.K.1    Freeman, B.A.2
  • 141
    • 62349112779 scopus 로고    scopus 로고
    • Oxidized phospholipids in control of inflammation and endothelial barrier
    • [141] Fu, P., Birukov, K.G., Oxidized phospholipids in control of inflammation and endothelial barrier. Transl. Res. 153 (2009), 166–176.
    • (2009) Transl. Res. , vol.153 , pp. 166-176
    • Fu, P.1    Birukov, K.G.2
  • 142
    • 84855432213 scopus 로고    scopus 로고
    • Physiological effects of oxidized phospholipids and their cellular signaling mechanisms in inflammation
    • [142] Greig, F.H., Kennedy, S., Spickett, C.M., Physiological effects of oxidized phospholipids and their cellular signaling mechanisms in inflammation. Free Radic. Biol. Med. 52 (2012), 266–280.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 266-280
    • Greig, F.H.1    Kennedy, S.2    Spickett, C.M.3
  • 143
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: new concepts and molecular mechanisms
    • [143] Higdon, A., Diers, A.R., Oh, J.Y., Landar, A., Darley-Usmar, V.M., Cell signalling by reactive lipid species: new concepts and molecular mechanisms. Biochem. J. 442 (2012), 453–464.
    • (2012) Biochem. J. , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.R.2    Oh, J.Y.3    Landar, A.4    Darley-Usmar, V.M.5
  • 144
    • 84874081337 scopus 로고    scopus 로고
    • Diverse functional roles of reactive cysteines
    • [144] Pace, N.J., Weerapana, E., Diverse functional roles of reactive cysteines. ACS Chem. Biol. 8 (2013), 283–296.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 283-296
    • Pace, N.J.1    Weerapana, E.2
  • 145
    • 84864393985 scopus 로고    scopus 로고
    • The electrophile responsive proteome: integrating proteomics and lipidomics with cellular function
    • [145] Higdon, A.N., Landar, A., Barnes, S., Darley-Usmar, V.M., The electrophile responsive proteome: integrating proteomics and lipidomics with cellular function. Antioxid. Redox Signal. 17 (2012), 1580–1589.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1580-1589
    • Higdon, A.N.1    Landar, A.2    Barnes, S.3    Darley-Usmar, V.M.4
  • 146
    • 77956234404 scopus 로고    scopus 로고
    • Reactive oxygen species and alpha,beta-unsaturated aldehydes as second messengers in signal transduction
    • [146] Forman, H.J., Reactive oxygen species and alpha,beta-unsaturated aldehydes as second messengers in signal transduction. Ann. N. Y. Acad. Sci. 1203 (2010), 35–44.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1203 , pp. 35-44
    • Forman, H.J.1
  • 147
    • 80054075348 scopus 로고    scopus 로고
    • Exploring protein lipidation with chemical biology
    • [147] Hang, H.C., Linder, M.E., Exploring protein lipidation with chemical biology. Chem. Rev. 111 (2011), 6341–6358.
    • (2011) Chem. Rev. , vol.111 , pp. 6341-6358
    • Hang, H.C.1    Linder, M.E.2
  • 148
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • [148] Martin, B.R., Cravatt, B.F., Large-scale profiling of protein palmitoylation in mammalian cells. Nat. Methods 6 (2009), 135–138.
    • (2009) Nat. Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 149
    • 41649118986 scopus 로고    scopus 로고
    • Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives
    • [149] Vila, A., Tallman, K.A., Jacobs, A.T., Liebler, D.C., Porter, N.A., Marnett, L.J., Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives. Chem. Res. Toxicol. 21 (2008), 432–444.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 432-444
    • Vila, A.1    Tallman, K.A.2    Jacobs, A.T.3    Liebler, D.C.4    Porter, N.A.5    Marnett, L.J.6
  • 150
    • 84980392480 scopus 로고    scopus 로고
    • Spectrophotometric assays for measuring redox biomarkers in blood
    • [150] Veskoukis, A.S., Kyparos, A., Paschalis, V., Nikolaidis, M.G., Spectrophotometric assays for measuring redox biomarkers in blood. Biomarkers 26 (2016), 1–10.
    • (2016) Biomarkers , vol.26 , pp. 1-10
    • Veskoukis, A.S.1    Kyparos, A.2    Paschalis, V.3    Nikolaidis, M.G.4
  • 152
    • 84903535662 scopus 로고    scopus 로고
    • Analysis of eicosanoids by LC–MS/MS and GC–MS/MS: a historical retrospect and a discussion
    • [152] Tsikas, D., Zoerner, A.A., Analysis of eicosanoids by LC–MS/MS and GC–MS/MS: a historical retrospect and a discussion. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 964 (2014), 79–88.
    • (2014) J. Chromatogr. B Anal. Technol. Biomed. Life Sci. , vol.964 , pp. 79-88
    • Tsikas, D.1    Zoerner, A.A.2
  • 153
    • 77953313356 scopus 로고    scopus 로고
    • Using isoprostanes as biomarkers of oxidative stress: some rarely considered issues
    • [153] Halliwell, B., Lee, C.Y., Using isoprostanes as biomarkers of oxidative stress: some rarely considered issues. Antioxid. Redox Signal. 13 (2010), 145–156.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 145-156
    • Halliwell, B.1    Lee, C.Y.2
  • 154
    • 84928143241 scopus 로고    scopus 로고
    • Reinterpreting the best biomarker of oxidative stress: the 8-iso-PGF(2alpha)/PGF(2alpha) ratio distinguishes chemical from enzymatic lipid peroxidation
    • [154] van 't Erve, T.J., Lih, F.B., Kadiiska, M.B., Deterding, L.J., Eling, T.E., Mason, R.P., Reinterpreting the best biomarker of oxidative stress: the 8-iso-PGF(2alpha)/PGF(2alpha) ratio distinguishes chemical from enzymatic lipid peroxidation. Free Radic. Biol. Med. 83 (2015), 245–251.
    • (2015) Free Radic. Biol. Med. , vol.83 , pp. 245-251
    • van 't Erve, T.J.1    Lih, F.B.2    Kadiiska, M.B.3    Deterding, L.J.4    Eling, T.E.5    Mason, R.P.6
  • 163
    • 84923675740 scopus 로고    scopus 로고
    • Biomarkers of oxidative stress study VI. Endogenous plasma antioxidants fail as useful biomarkers of endotoxin-induced oxidative stress
    • [163] Kadiiska, M.B., Peddada, S., Herbert, R.A., Basu, S., Hensley, K., Jones, D.P., Hatch, G.E., Mason, R.P., Biomarkers of oxidative stress study VI. Endogenous plasma antioxidants fail as useful biomarkers of endotoxin-induced oxidative stress. Free Radic. Biol. Med. 81 (2015), 100–106.
    • (2015) Free Radic. Biol. Med. , vol.81 , pp. 100-106
    • Kadiiska, M.B.1    Peddada, S.2    Herbert, R.A.3    Basu, S.4    Hensley, K.5    Jones, D.P.6    Hatch, G.E.7    Mason, R.P.8
  • 164
    • 0032461797 scopus 로고    scopus 로고
    • ESCODD: European Standards Committee on Oxidative DNA Damage
    • [164] Lunec, J., ESCODD: European Standards Committee on Oxidative DNA Damage. Free Radic. Res. 29 (1998), 601–608.
    • (1998) Free Radic. Res. , vol.29 , pp. 601-608
    • Lunec, J.1
  • 165
    • 0036605773 scopus 로고    scopus 로고
    • Comparison of results from different laboratories in measuring 8-oxo−2′-deoxyguanosine in synthetic oligonucleotides
    • [165] Riis, B., Comparison of results from different laboratories in measuring 8-oxo−2′-deoxyguanosine in synthetic oligonucleotides. Free Radic. Res. 36 (2002), 649–659.
    • (2002) Free Radic. Res. , vol.36 , pp. 649-659
    • Riis, B.1
  • 166
    • 0037446180 scopus 로고    scopus 로고
    • European; Standards; Committee; on; Oxidative; DNA; Damage. Measurement of DNA oxidation in human cells by chromatographic and enzymic methods
    • [166] ESCODD. European; Standards; Committee; on; Oxidative; DNA; Damage. Measurement of DNA oxidation in human cells by chromatographic and enzymic methods. Free Radic. Biol. Med. 34 (2003), 1089–1099.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1089-1099
  • 167
    • 0036521853 scopus 로고    scopus 로고
    • European; Standards; Committee; on; Oxidative; DNA; Damage. Inter-laboratory validation of procedures for measuring 8-oxo-7,8-dihydroguanine/8-oxo-7,8-dihydro-2′-deoxyguanosine in DNA
    • [167] ESCODD. European; Standards; Committee; on; Oxidative; DNA; Damage. Inter-laboratory validation of procedures for measuring 8-oxo-7,8-dihydroguanine/8-oxo-7,8-dihydro-2′-deoxyguanosine in DNA. Free Radic. Res. 36 (2002), 239–245.
    • (2002) Free Radic. Res. , vol.36 , pp. 239-245
  • 168
    • 0034065401 scopus 로고    scopus 로고
    • European; Standards; Committee; on; Oxidative; DNA; Damage. Comparison of different methods of measuring 8-oxoguanine as a marker of oxidative DNA damage
    • [168] ESCODD. European; Standards; Committee; on; Oxidative; DNA; Damage. Comparison of different methods of measuring 8-oxoguanine as a marker of oxidative DNA damage. Free Radic. Res. 32 (2000), 333–341.
    • (2000) Free Radic. Res. , vol.32 , pp. 333-341
  • 169
    • 0034023134 scopus 로고    scopus 로고
    • The steady-state levels of oxidative DNA damage and of lipid peroxidation (F2-isoprostanes) are not correlated in healthy human subjects
    • [169] England, T., Beatty, E., Rehman, A., Nourooz-Zadeh, J., Pereira, P., O'Reilly, J., Wiseman, H., Geissler, C., Halliwell, B., The steady-state levels of oxidative DNA damage and of lipid peroxidation (F2-isoprostanes) are not correlated in healthy human subjects. Free Radic. Res. 32 (2000), 355–362.
    • (2000) Free Radic. Res. , vol.32 , pp. 355-362
    • England, T.1    Beatty, E.2    Rehman, A.3    Nourooz-Zadeh, J.4    Pereira, P.5    O'Reilly, J.6    Wiseman, H.7    Geissler, C.8    Halliwell, B.9
  • 172
    • 79551488948 scopus 로고    scopus 로고
    • F2-isoprostanes as an indicator and risk factor for coronary heart disease
    • [172] Davies, S.S., Roberts, L.J. 2nd, F2-isoprostanes as an indicator and risk factor for coronary heart disease. Free Radic. Biol. Med. 50 (2011), 559–566.
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 559-566
    • Davies, S.S.1    Roberts, L.J.2
  • 173
    • 55449120824 scopus 로고    scopus 로고
    • Isoprostanes inhibit vascular endothelial growth factor-induced endothelial cell migration, tube formation, and cardiac vessel sprouting in vitro, as well as angiogenesis in vivo via activation of the thromboxane A(2) receptor: a potential link between oxidative stress and impaired angiogenesis
    • [173] Benndorf, R.A., Schwedhelm, E., Gnann, A., Taheri, R., Kom, G., Didie, M., Steenpass, A., Ergun, S., Boger, R.H., Isoprostanes inhibit vascular endothelial growth factor-induced endothelial cell migration, tube formation, and cardiac vessel sprouting in vitro, as well as angiogenesis in vivo via activation of the thromboxane A(2) receptor: a potential link between oxidative stress and impaired angiogenesis. Circ. Res. 103 (2008), 1037–1046.
    • (2008) Circ. Res. , vol.103 , pp. 1037-1046
    • Benndorf, R.A.1    Schwedhelm, E.2    Gnann, A.3    Taheri, R.4    Kom, G.5    Didie, M.6    Steenpass, A.7    Ergun, S.8    Boger, R.H.9
  • 175
    • 10044235066 scopus 로고    scopus 로고
    • Isoprostanes: markers and mediators of oxidative stress
    • [175] Montuschi, P., Barnes, P.J., Roberts, L.J. II, Isoprostanes: markers and mediators of oxidative stress. FASEB J. 18 (2004), 1791–1800.
    • (2004) FASEB J. , vol.18 , pp. 1791-1800
    • Montuschi, P.1    Barnes, P.J.2    Roberts, L.J.3
  • 176
    • 0035902957 scopus 로고    scopus 로고
    • Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn
    • [176] Mallozzi, C., Di Stasi, A.M., Minetti, M., Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn. FEBS Lett. 503 (2001), 189–195.
    • (2001) FEBS Lett. , vol.503 , pp. 189-195
    • Mallozzi, C.1    Di Stasi, A.M.2    Minetti, M.3
  • 177
    • 0034681114 scopus 로고    scopus 로고
    • Modifications of proteins by polyunsaturated fatty acid peroxidation products
    • [177] Refsgaard, H.H., Tsai, L., Stadtman, E.R., Modifications of proteins by polyunsaturated fatty acid peroxidation products. Proc. Natl. Acad. Sci. USA 97 (2000), 611–616.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 611-616
    • Refsgaard, H.H.1    Tsai, L.2    Stadtman, E.R.3
  • 178
    • 0034032816 scopus 로고    scopus 로고
    • The importance of lipid-derived malondialdehyde in diabetes mellitus
    • [178] Slatter, D.A., Bolton, C.H., Bailey, A.J., The importance of lipid-derived malondialdehyde in diabetes mellitus. Diabetologia 43 (2000), 550–557.
    • (2000) Diabetologia , vol.43 , pp. 550-557
    • Slatter, D.A.1    Bolton, C.H.2    Bailey, A.J.3
  • 180
    • 0032586084 scopus 로고    scopus 로고
    • F2-isoprostane excretion rate and diurnal variation in human urine
    • [180] Helmersson, J., Basu, S., F2-isoprostane excretion rate and diurnal variation in human urine. Prostaglandins Leukot. Essent. Fatty Acids 61 (1999), 203–205.
    • (1999) Prostaglandins Leukot. Essent. Fatty Acids , vol.61 , pp. 203-205
    • Helmersson, J.1    Basu, S.2
  • 181
    • 61449089652 scopus 로고    scopus 로고
    • Diurnal variations in salivary protein carbonyl levels in normal and cognitively impaired human subjects
    • [181] Su, H., Gornitsky, M., Geng, G., Velly, A.M., Chertkow, H., Schipper, H.M., Diurnal variations in salivary protein carbonyl levels in normal and cognitively impaired human subjects. Age (Dordr) 30 (2008), 1–9.
    • (2008) Age (Dordr) , vol.30 , pp. 1-9
    • Su, H.1    Gornitsky, M.2    Geng, G.3    Velly, A.M.4    Chertkow, H.5    Schipper, H.M.6
  • 182
    • 0034866745 scopus 로고    scopus 로고
    • Circadian rhythmicity of whole-blood glutathione in healthy subjects
    • [182] Valencia, E., Marin, A., Hardy, G., Circadian rhythmicity of whole-blood glutathione in healthy subjects. Nutrition 17 (2001), 731–733.
    • (2001) Nutrition , vol.17 , pp. 731-733
    • Valencia, E.1    Marin, A.2    Hardy, G.3
  • 183
    • 33745898848 scopus 로고    scopus 로고
    • Dietary antioxidants and beneficial effect on oxidatively damaged DNA
    • [183] Moller, P., Loft, S., Dietary antioxidants and beneficial effect on oxidatively damaged DNA. Free Radic. Biol. Med. 41 (2006), 388–415.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 388-415
    • Moller, P.1    Loft, S.2


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