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Volumn 97, Issue , 2016, Pages 398-407

Redox signaling: An evolution from free radicals to aging

Author keywords

Aging; Air pollution; Antioxidant; AP 1; Glutathione; Homeostasis; Hydrogen peroxide; NADPH oxidase; Nrf2; Oxidative stress; Redox signaling; Superoxide; Thiolate

Indexed keywords

ELECTROPHILE; FREE RADICAL; OXYGEN; PARAQUAT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; SUPEROXIDE DISMUTASE;

EID: 84978485739     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2016.07.003     Document Type: Review
Times cited : (131)

References (116)
  • 1
    • 33645999557 scopus 로고
    • Oxygen poisoning and x-irradiation: a mechanism in common
    • [1] Gerschman, R., Gilbert, D.L., Nye, S.W., Dwyer, P., Fenn, W.O., Oxygen poisoning and x-irradiation: a mechanism in common. Science 119 (1954), 623–626.
    • (1954) Science , vol.119 , pp. 623-626
    • Gerschman, R.1    Gilbert, D.L.2    Nye, S.W.3    Dwyer, P.4    Fenn, W.O.5
  • 2
    • 77049308856 scopus 로고
    • Aging: a theory based on free radical and radiation chemistry
    • [2] Harman, D., Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 11 (1956), 298–300.
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 3
    • 0014691242 scopus 로고
    • Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein)
    • [3] McCord, J.M., Fridovich, I., Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 (1969), 6049–6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 4
    • 0002100141 scopus 로고
    • The chemical nature of vitamin C
    • [4] Svirbely, J.L., Szent-Gyorgyi, A., The chemical nature of vitamin C. Biochem. J. 26 (1932), 865–870.
    • (1932) Biochem. J. , vol.26 , pp. 865-870
    • Svirbely, J.L.1    Szent-Gyorgyi, A.2
  • 5
  • 6
    • 0000050242 scopus 로고
    • Detection of free radicals generated during enzymic oxidations by the initiation of sulfite oxidation
    • [6] Fridovich, I., Handler, P., Detection of free radicals generated during enzymic oxidations by the initiation of sulfite oxidation. J. Biol. Chem. 236 (1961), 1836–1840.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1836-1840
    • Fridovich, I.1    Handler, P.2
  • 7
    • 0015207644 scopus 로고
    • Kinetic evidence indicating the absence during catalysis of an unbound ferroprotoporphyrin form of tryptophan oxygenase
    • [7] Forman, H.J., Feigelson, P., Kinetic evidence indicating the absence during catalysis of an unbound ferroprotoporphyrin form of tryptophan oxygenase. Biochemistry 10 (1971), 760–763.
    • (1971) Biochemistry , vol.10 , pp. 760-763
    • Forman, H.J.1    Feigelson, P.2
  • 8
    • 0015219075 scopus 로고
    • The role of superoxide and hydroperoxide in the reductive activation of tryptophan-2,3-dioxygenase
    • [8] Brady, F.O., Forman, H.J., Feigelson, P., The role of superoxide and hydroperoxide in the reductive activation of tryptophan-2,3-dioxygenase. J. Biol. Chem. 246 (1971), 7119–7124.
    • (1971) J. Biol. Chem. , vol.246 , pp. 7119-7124
    • Brady, F.O.1    Forman, H.J.2    Feigelson, P.3
  • 9
    • 0016414528 scopus 로고
    • Superoxide dismutases
    • [9] Fridovich, I., Superoxide dismutases. Annu Rev. Biochem. 44 (1975), 147–159.
    • (1975) Annu Rev. Biochem. , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 10
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • [10] Fridovich, I., The biology of oxygen radicals. Science 201 (1978), 875–880.
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 11
    • 0007486219 scopus 로고
    • Electrolytic univalent reduction of oxygen in aqueous solution demonstrated with superoxide dismutase
    • [11] Forman, H.J., Fridovich, I., Electrolytic univalent reduction of oxygen in aqueous solution demonstrated with superoxide dismutase. Science, 175, 1972, 339.
    • (1972) Science , vol.175 , pp. 339
    • Forman, H.J.1    Fridovich, I.2
  • 12
    • 0015842752 scopus 로고
    • Superoxide dismutase: a comparison of rate constants
    • [12] Forman, H.J., Fridovich, I., Superoxide dismutase: a comparison of rate constants. Arch. Biochem. Biophys. 158 (1973), 396–400.
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 396-400
    • Forman, H.J.1    Fridovich, I.2
  • 13
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. The effects of metals
    • [13] Forman, H.J., Fridovich, I., On the stability of bovine superoxide dismutase. The effects of metals. J. Biol. Chem. 248 (1973), 2645–2649.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 14
    • 0015937128 scopus 로고
    • Histidine at the active site of superoxide dismutase
    • [14] Forman, H.J., Evans, H.J., Hill, R.L., Fridovich, I., Histidine at the active site of superoxide dismutase. Biochemistry 12 (1973), 823–827.
    • (1973) Biochemistry , vol.12 , pp. 823-827
    • Forman, H.J.1    Evans, H.J.2    Hill, R.L.3    Fridovich, I.4
  • 15
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • [15] Crow, J.P., Sampson, J.B., Zhuang, Y., Thompson, J.A., Beckman, J.S., Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69 (1997), 1936–1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 16
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • [16] Boveris, A., Oshino, N., Chance, B., The cellular production of hydrogen peroxide. Biochem. J. 128 (1972), 617–630.
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 17
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • [17] Loschen, G., Azzi, A., Richter, C., Flohé, L., Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett. 42 (1974), 68–72.
    • (1974) FEBS Lett. , vol.42 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohé, L.4
  • 18
    • 0016246294 scopus 로고
    • Role of superoxide radical in mitochondrial dehydrogenase reactions
    • [18] Forman, H.J., Kennedy, J.A., Role of superoxide radical in mitochondrial dehydrogenase reactions. Biochem. Biophys. Res. Commun. 60 (1974), 1044–1050.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 1044-1050
    • Forman, H.J.1    Kennedy, J.A.2
  • 19
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • [19] Boveris, A., Cadenas, E., Stoppani, A.O.M., Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J., 156, 1976, 435.
    • (1976) Biochem. J. , vol.156 , pp. 435
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.M.3
  • 20
    • 0018129988 scopus 로고
    • Superoxide dismutase as an inhibitor of reactions of semiquinone radicals
    • [20] Winterbourn, C.C., French, J.K., Claridge, R.F., Superoxide dismutase as an inhibitor of reactions of semiquinone radicals. FEBS Lett. 94 (1978), 269–272.
    • (1978) FEBS Lett. , vol.94 , pp. 269-272
    • Winterbourn, C.C.1    French, J.K.2    Claridge, R.F.3
  • 21
    • 0030939089 scopus 로고    scopus 로고
    • On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology
    • [21] Forman, H.J., Azzi, A., On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology. FASEB J., 11, 1997, 374.
    • (1997) FASEB J. , vol.11 , pp. 374
    • Forman, H.J.1    Azzi, A.2
  • 22
    • 0027481965 scopus 로고
    • The reaction of NO with superoxide
    • [22] Huie, R.E., Padmaja, S., The reaction of NO with superoxide. Free Radic. Res. Commun. 18 (1993), 195–199.
    • (1993) Free Radic. Res. Commun. , vol.18 , pp. 195-199
    • Huie, R.E.1    Padmaja, S.2
  • 23
    • 84868007565 scopus 로고    scopus 로고
    • Physiological roles of mitochondrial reactive oxygen species
    • [23] Sena, L.A., Chandel, N.S., Physiological roles of mitochondrial reactive oxygen species. Mol. Cell. 48 (2012), 158–167.
    • (2012) Mol. Cell. , vol.48 , pp. 158-167
    • Sena, L.A.1    Chandel, N.S.2
  • 24
    • 0006883461 scopus 로고
    • Effects of oxygen at increased pressure
    • [24] Bean, J.W., Effects of oxygen at increased pressure. Physiol. Rev. 25 (1945), 1–147.
    • (1945) Physiol. Rev. , vol.25 , pp. 1-147
    • Bean, J.W.1
  • 25
    • 0343303413 scopus 로고
    • Oxygen poisoning; the effect of high oxygen pressure upon enzymes; succinic dehydrogenase and cytochrome oxidase
    • [25] Stadie, W.C., Haugaard, N., Oxygen poisoning; the effect of high oxygen pressure upon enzymes; succinic dehydrogenase and cytochrome oxidase. J. Biol. Chem. 161 (1945), 153–174.
    • (1945) J. Biol. Chem. , vol.161 , pp. 153-174
    • Stadie, W.C.1    Haugaard, N.2
  • 26
    • 0016188423 scopus 로고
    • Superoxide dismutase and pulmonary oxygen toxicity
    • [26] Crapo, J.D., Tierney, D.F., Superoxide dismutase and pulmonary oxygen toxicity. Am. J. Physiol. 226 (1974), 1401–1407.
    • (1974) Am. J. Physiol. , vol.226 , pp. 1401-1407
    • Crapo, J.D.1    Tierney, D.F.2
  • 27
    • 0016153291 scopus 로고
    • Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity
    • [27] Bus, J.S., Aust, S.D., Gibson, J.E., Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity. Biochem. Biophys. Res. Commun. 58 (1974), 749–755.
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 749-755
    • Bus, J.S.1    Aust, S.D.2    Gibson, J.E.3
  • 28
    • 0019520675 scopus 로고
    • Antioxidant enzymes of rat granular pneumocytes. Constitutive levels and effect of hypoxia
    • [28] Forman, H.J., Fisher, A.B., Antioxidant enzymes of rat granular pneumocytes. Constitutive levels and effect of hypoxia. Lab. Invest. 45 (1981), 1–6.
    • (1981) Lab. Invest. , vol.45 , pp. 1-6
    • Forman, H.J.1    Fisher, A.B.2
  • 29
    • 0019940951 scopus 로고
    • Differential paraquat (PO) accumulation and redox kinetics in rat lung cells
    • [29] Forman, H.J., Aldrich, T.K., Posner, M.A., Fisher, A.B., Differential paraquat (PO) accumulation and redox kinetics in rat lung cells. Fed. Proc., 41, 1982.
    • (1982) Fed. Proc. , vol.41
    • Forman, H.J.1    Aldrich, T.K.2    Posner, M.A.3    Fisher, A.B.4
  • 30
    • 0015596284 scopus 로고
    • The production by leukocytes of superoxide, a potential bactericidal agent
    • [30] Babior, B.M., Kipnes, R.S., Curnutte, J.T., The production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Invest., 52, 1973, 741.
    • (1973) J. Clin. Invest. , vol.52 , pp. 741
    • Babior, B.M.1    Kipnes, R.S.2    Curnutte, J.T.3
  • 31
    • 0019163463 scopus 로고
    • Rat alveolar macrophages require NADPH for superoxide production in the respiratory burst. Effect of NADPH depletion by paraquat
    • [31] Forman, H.J., Nelson, J., Fisher, A.B., Rat alveolar macrophages require NADPH for superoxide production in the respiratory burst. Effect of NADPH depletion by paraquat. J. Biol. Chem. 255 (1980), 9879–9883.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9879-9883
    • Forman, H.J.1    Nelson, J.2    Fisher, A.B.3
  • 32
  • 33
    • 0022407995 scopus 로고
    • Effects of t-butyl hydroperoxide on NADPH, glutathione, and the respiratory burst of rat alveolar macrophages
    • [33] Sutherland, M.W., Nelson, J., Harrison, G., Forman, H.J., Effects of t-butyl hydroperoxide on NADPH, glutathione, and the respiratory burst of rat alveolar macrophages. Arch. Biochem. Biophys. 243 (1985), 325–331.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 325-331
    • Sutherland, M.W.1    Nelson, J.2    Harrison, G.3    Forman, H.J.4
  • 34
    • 0014876254 scopus 로고
    • y-Glutamyl cycle : a possible transport system for amino acids
    • [34] Orlowski, M., Meister, A., y-Glutamyl cycle : a possible transport system for amino acids. Proc. Natl. Acad. Sci. USA 67 (1970), 1248–1255.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 1248-1255
    • Orlowski, M.1    Meister, A.2
  • 35
    • 0022294173 scopus 로고
    • Oxidative stress: excited oxygen species and enzyme activity
    • [35] Cadenas, E., Sies, H., Oxidative stress: excited oxygen species and enzyme activity. Adv. Enzym. Regul. 23 (1985), 217–237.
    • (1985) Adv. Enzym. Regul. , vol.23 , pp. 217-237
    • Cadenas, E.1    Sies, H.2
  • 36
    • 84968813794 scopus 로고    scopus 로고
    • Glutathione - from antioxidant to post-translational modifier
    • [36] Forman, H.J., Glutathione - from antioxidant to post-translational modifier. Arch. Biochem. Biophys. 595 (2016), 64–67.
    • (2016) Arch. Biochem. Biophys. , vol.595 , pp. 64-67
    • Forman, H.J.1
  • 37
    • 0028075841 scopus 로고
    • Quinone-induced oxidative stress elevates glutathione and induces γ-Glutamylcysteine synthetase activity in rat lung epithelial L2 cells
    • [37] Shi, M.M., Kugelman, A., Iwamoto, T., Tian, L., Forman, H.J., Quinone-induced oxidative stress elevates glutathione and induces γ-Glutamylcysteine synthetase activity in rat lung epithelial L2 cells. J. Biol. Chem. 269 (1994), 26512–26517.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26512-26517
    • Shi, M.M.1    Kugelman, A.2    Iwamoto, T.3    Tian, L.4    Forman, H.J.5
  • 38
    • 0028081526 scopus 로고
    • γ-Glutamylcysteine synthetase and GSH increase in quinone-induced oxidative stress in BPAEC
    • [38] Shi, M.M., Iwamoto, T., Forman, H.J., γ-Glutamylcysteine synthetase and GSH increase in quinone-induced oxidative stress in BPAEC. Am. J. Physiol. - Lung Cell. Mol. Physiol., 267, 1994.
    • (1994) Am. J. Physiol. - Lung Cell. Mol. Physiol. , vol.267
    • Shi, M.M.1    Iwamoto, T.2    Forman, H.J.3
  • 39
    • 0031172884 scopus 로고    scopus 로고
    • Increased transcription of the regulatory subunit of gamma-glutamylcysteine synthetase in rat lung epithelial L2 cells exposed to oxidative stress or glutathione depletion
    • [39] Tian, L., Shi, M.M., Forman, H.J., Increased transcription of the regulatory subunit of gamma-glutamylcysteine synthetase in rat lung epithelial L2 cells exposed to oxidative stress or glutathione depletion. Arch. Biochem. Biophys. 342 (1997), 126–133.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 126-133
    • Tian, L.1    Shi, M.M.2    Forman, H.J.3
  • 40
    • 0028534953 scopus 로고
    • Gamma-Glutamyl transpeptidase is increased by oxidative stress in rat alveolar L2 epithelial cells
    • [40] Kugelman, A., Choy, H.A., Liu, R., Shi, M.M., Gozal, E., Forman, H.J., Gamma-Glutamyl transpeptidase is increased by oxidative stress in rat alveolar L2 epithelial cells. Am. J. Respir. Cell Mol. Biol. 11 (1994), 586–592.
    • (1994) Am. J. Respir. Cell Mol. Biol. , vol.11 , pp. 586-592
    • Kugelman, A.1    Choy, H.A.2    Liu, R.3    Shi, M.M.4    Gozal, E.5    Forman, H.J.6
  • 41
    • 0018071115 scopus 로고
    • Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents
    • [41] Mukherjee, S.P., Lane, R.H., Lynn, W.S., Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents. Biochem. Pharmacol.. 27 (1978), 2589–2594.
    • (1978) Biochem. Pharmacol.. , vol.27 , pp. 2589-2594
    • Mukherjee, S.P.1    Lane, R.H.2    Lynn, W.S.3
  • 42
    • 0017261573 scopus 로고
    • Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system
    • [42] Czech, M.P., Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system. J. Biol. Chem. 251 (1976), 1164–1170.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1164-1170
    • Czech, M.P.1
  • 43
    • 0024724936 scopus 로고
    • 2+- and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain
    • 2+- and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain. Proc. Natl. Acad. Sci. USA 86 (1989), 6758–6762.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6758-6762
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 44
    • 0020539966 scopus 로고
    • Requirements for hydroperoxide by the cyclooxygenase and peroxidase activities of prostaglandin H synthase
    • [44] Kulmacz, R.J., Lands, W.E., Requirements for hydroperoxide by the cyclooxygenase and peroxidase activities of prostaglandin H synthase. Prostaglandins 25 (1983), 531–540.
    • (1983) Prostaglandins , vol.25 , pp. 531-540
    • Kulmacz, R.J.1    Lands, W.E.2
  • 45
    • 0023013502 scopus 로고
    • Modulation of the 5-lipoxygenase activity of MC-9 mast cells: activation by hydroperoxides
    • [45] Bryant, R.W., She, H.S., Ng, K.J., Siegel, M.I., Modulation of the 5-lipoxygenase activity of MC-9 mast cells: activation by hydroperoxides. Prostaglandins. 32 (1986), 615–627.
    • (1986) Prostaglandins. , vol.32 , pp. 615-627
    • Bryant, R.W.1    She, H.S.2    Ng, K.J.3    Siegel, M.I.4
  • 46
    • 0030062726 scopus 로고    scopus 로고
    • Modulation of the rat alveolar macrophage respiratory burst by hydroperoxides is calcium dependent
    • [46] Hoyal, C.R., Gozal, E., Zhou, H., Foldenauer, K., Forman, H.J., Modulation of the rat alveolar macrophage respiratory burst by hydroperoxides is calcium dependent. Arch. Biochem. Biophys. 326 (1996), 166–171.
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 166-171
    • Hoyal, C.R.1    Gozal, E.2    Zhou, H.3    Foldenauer, K.4    Forman, H.J.5
  • 47
    • 0027689975 scopus 로고
    • Stimulation of the rat alveolar macrophage respiratory burst by extracellular adenine nucleotides
    • [47] Murphy, J.K., Livingston, F.R., Gozal, E., Torres, M., Forman, H.J., Stimulation of the rat alveolar macrophage respiratory burst by extracellular adenine nucleotides. Am. J. Respir. Cell Mol. Biol. 9 (1993), 505–510.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.9 , pp. 505-510
    • Murphy, J.K.1    Livingston, F.R.2    Gozal, E.3    Torres, M.4    Forman, H.J.5
  • 49
    • 0036131211 scopus 로고    scopus 로고
    • 2 is prevented by phosphatidylcholine-specific phospholipase C inhibitor Tricyclodecan-9-yl-xanthate (D609)
    • 2 is prevented by phosphatidylcholine-specific phospholipase C inhibitor Tricyclodecan-9-yl-xanthate (D609). J. Pharmacol. Exp. Ther. 301 (2002), 87–94.
    • (2002) J. Pharmacol. Exp. Ther. , vol.301 , pp. 87-94
    • Giron-Calle, J.1
  • 50
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • [50] Schreck, R., Rieber, P., Baeuerle, P.A., Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J. 10 (1991), 2247–2258.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 51
    • 0029760973 scopus 로고    scopus 로고
    • Activation of NFκB by the respiratory burst of macrophages
    • [51] Kaul, N., Forman, H.J., Activation of NFκB by the respiratory burst of macrophages. Free Radic. Biol. Med. 21 (1996), 401–405.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 401-405
    • Kaul, N.1    Forman, H.J.2
  • 52
    • 0031825098 scopus 로고    scopus 로고
    • Role of protein kinase C in basal and hydrogen peroxide-stimulated NF-kappa B activation in the murine macrophage J774A.1 cell line
    • [52] Kaul, N., Gopalakrishna, R., Gundimeda, U., Choi, J., Forman, H.J., Role of protein kinase C in basal and hydrogen peroxide-stimulated NF-kappa B activation in the murine macrophage J774A.1 cell line. Arch. Biochem. Biophys. 350 (1998), 79–86.
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 79-86
    • Kaul, N.1    Gopalakrishna, R.2    Gundimeda, U.3    Choi, J.4    Forman, H.J.5
  • 53
    • 0033563866 scopus 로고    scopus 로고
    • Activation of several MAP kinases upon stimulation of rat alveolar macrophages: role of the NADPH oxidase
    • [53] Torres, M., Forman, H.J., Activation of several MAP kinases upon stimulation of rat alveolar macrophages: role of the NADPH oxidase. Arch. Biochem. Biophys. 366 (1999), 231–239.
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 231-239
    • Torres, M.1    Forman, H.J.2
  • 55
    • 3242657766 scopus 로고    scopus 로고
    • The Nox enzymes and the regulated generation of reactive oxygen species
    • in: H.J. Forman, J. Fukuto, M. Torres (Eds.), Kluwer Academic Publishers, Dordrecht ; Boston
    • [55] W.P. Arnold, J.D. Lambeth, The Nox enzymes and the regulated generation of reactive oxygen species, in: H.J. Forman, J. Fukuto, M. Torres (Eds.), Signal Transduct. by React. Oxyg. Nitrogen Species Pathways Chem. Princ., Kluwer Academic Publishers, Dordrecht ; Boston, 2003: pp. 102–118.
    • (2003) Signal Transduct. by React. Oxyg. Nitrogen Species Pathways Chem. Princ. , pp. 102-118
    • Arnold, W.P.1    Lambeth, J.D.2
  • 57
    • 0004078316 scopus 로고    scopus 로고
    • Oxidative Stress and Signal Transduction
    • Springer Verlag New York
    • [57] Forman, H.J.J., Cadenas, E., Oxidative Stress and Signal Transduction. 1997, Springer Verlag, New York.
    • (1997)
    • Forman, H.J.J.1    Cadenas, E.2
  • 59
    • 0018665496 scopus 로고
    • Inhibition of prostaglandin biosynthesis by eicosapentaenoic acid
    • [59] Culp, B.R., Titus, B.G., Lands, W.E., Inhibition of prostaglandin biosynthesis by eicosapentaenoic acid. Prostaglandins Med. 3 (1979), 269–278.
    • (1979) Prostaglandins Med. , vol.3 , pp. 269-278
    • Culp, B.R.1    Titus, B.G.2    Lands, W.E.3
  • 60
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • [60] Forman, H.J., Maiorino, M., Ursini, F., Signaling functions of reactive oxygen species. Biochemistry 49 (2010), 835–842.
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 64
    • 33749248371 scopus 로고    scopus 로고
    • The ADP-stimulated NADPH oxidase activates the ASK-1/MKK4/JNK pathway in alveolar macrophages
    • [64] Liu, H., Zhang, H., Iles, K.E., Rinna, A., Merrill, G., Yodoi, J., Torres, M., Forman, H.J., The ADP-stimulated NADPH oxidase activates the ASK-1/MKK4/JNK pathway in alveolar macrophages. Free Radic. Res. 40 (2006), 865–874.
    • (2006) Free Radic. Res. , vol.40 , pp. 865-874
    • Liu, H.1    Zhang, H.2    Iles, K.E.3    Rinna, A.4    Merrill, G.5    Yodoi, J.6    Torres, M.7    Forman, H.J.8
  • 65
    • 77953363542 scopus 로고    scopus 로고
    • DJ-1 protects against oxidative damage by regulating the thioredoxin/ASK1 complex
    • [65] Im, J.Y., Lee, K.W., Junn, E., Mouradian, M.M., DJ-1 protects against oxidative damage by regulating the thioredoxin/ASK1 complex. Neurosci. Res. 67 (2010), 203–208.
    • (2010) Neurosci. Res. , vol.67 , pp. 203-208
    • Im, J.Y.1    Lee, K.W.2    Junn, E.3    Mouradian, M.M.4
  • 67
    • 0021842533 scopus 로고
    • Separation and characterization of the aldehydic products of lipid peroxidation stimulated by carbon tetrachloride or ADP- iron in isolated rat hepatocytes and rat liver microsomal suspension
    • [67] Poli, G., Dianzani, M.U., Cheeseman, K.H., Slater, T.F., Lang, J., Esterbauer, H., Separation and characterization of the aldehydic products of lipid peroxidation stimulated by carbon tetrachloride or ADP- iron in isolated rat hepatocytes and rat liver microsomal suspension. Biochem. J., 227, 1985, 629.
    • (1985) Biochem. J. , vol.227 , pp. 629
    • Poli, G.1    Dianzani, M.U.2    Cheeseman, K.H.3    Slater, T.F.4    Lang, J.5    Esterbauer, H.6
  • 69
    • 0027959220 scopus 로고
    • Postischemic accumulation of the lipid peroxidation product 4-hydroxynonenal in rat small intestine
    • [69] Grune, T., Siems, W.G., Kowalewski, J., Esterbauer, H., Postischemic accumulation of the lipid peroxidation product 4-hydroxynonenal in rat small intestine. Life Sci. 55 (1994), 693–699.
    • (1994) Life Sci. , vol.55 , pp. 693-699
    • Grune, T.1    Siems, W.G.2    Kowalewski, J.3    Esterbauer, H.4
  • 70
    • 0021758483 scopus 로고
    • Cytotoxic aldehydes originating from the peroxidation of liver microsomal lipids
    • [70] Benedetti, A., Comporti, M., Fulceri, R., Esterbauer, H., Cytotoxic aldehydes originating from the peroxidation of liver microsomal lipids. Biochim. Biophys. Acta, 792, 1984, 172.
    • (1984) Biochim. Biophys. Acta , vol.792 , pp. 172
    • Benedetti, A.1    Comporti, M.2    Fulceri, R.3    Esterbauer, H.4
  • 71
    • 0019193338 scopus 로고
    • Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids
    • [71] Benedetti, A., Comporti, M., Esterbauer, H., Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids. Biochim. Biophys. Acta 620 (1980), 281–296.
    • (1980) Biochim. Biophys. Acta , vol.620 , pp. 281-296
    • Benedetti, A.1    Comporti, M.2    Esterbauer, H.3
  • 72
    • 0030756676 scopus 로고    scopus 로고
    • The lipid peroxidation end product 4-hydroxy-2,3-nonenal up-regulates transforming growth factor b1 expression in the macrophage lineage: a link between oxidative injury and fibrosclerosis
    • [72] Leonarduzzi, G., Scavazza, A., Biasi, F., Chiarpotto, E., Camandola, S., Vogl, S., Dargel, R., Poli, G., The lipid peroxidation end product 4-hydroxy-2,3-nonenal up-regulates transforming growth factor b1 expression in the macrophage lineage: a link between oxidative injury and fibrosclerosis. FASEB J. 11 (1997), 851–857.
    • (1997) FASEB J. , vol.11 , pp. 851-857
    • Leonarduzzi, G.1    Scavazza, A.2    Biasi, F.3    Chiarpotto, E.4    Camandola, S.5    Vogl, S.6    Dargel, R.7    Poli, G.8
  • 74
    • 0033985185 scopus 로고    scopus 로고
    • The lipid peroxidation product 4-hydroxy-2,3-nonenal increases AP-1-binding activity through caspase activation in neurons
    • [74] Camandola, S., Poli, G., Mattson, M.P., The lipid peroxidation product 4-hydroxy-2,3-nonenal increases AP-1-binding activity through caspase activation in neurons. J. Neurochem. 74 (2000), 159–168.
    • (2000) J. Neurochem. , vol.74 , pp. 159-168
    • Camandola, S.1    Poli, G.2    Mattson, M.P.3
  • 75
    • 0029035346 scopus 로고
    • Release of aldehydes from rat alveolar macrophages exposed in vitro to low concentrations of nitrogen dioxide
    • [75] Robison, T.W., Forman, H.J., Thomas, M.J., Release of aldehydes from rat alveolar macrophages exposed in vitro to low concentrations of nitrogen dioxide. Biochim. Biophys. Acta - Lipids Lipid Metab. 1256 (1995), 334–340.
    • (1995) Biochim. Biophys. Acta - Lipids Lipid Metab. , vol.1256 , pp. 334-340
    • Robison, T.W.1    Forman, H.J.2    Thomas, M.J.3
  • 76
    • 13844272420 scopus 로고    scopus 로고
    • 4-Hydroxynonenal increases gamma-glutamyl transpeptidase gene expression through mitogen-activated protein kinase pathways
    • [76] Zhang, H., Dickinson, D.A., Liu, R.-M., Forman, H.J., 4-Hydroxynonenal increases gamma-glutamyl transpeptidase gene expression through mitogen-activated protein kinase pathways. Free Radic. Biol. Med. 38 (2005), 463–471.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 463-471
    • Zhang, H.1    Dickinson, D.A.2    Liu, R.-M.3    Forman, H.J.4
  • 77
    • 33846849624 scopus 로고    scopus 로고
    • Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cells
    • [77] Zhang, H., Court, N., Forman, H.J., Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cells. Redox Rep. 12 (2007), 101–106.
    • (2007) Redox Rep. , vol.12 , pp. 101-106
    • Zhang, H.1    Court, N.2    Forman, H.J.3
  • 79
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • [79] Rushmore, T.H., Morton, M.R., Pickett, C.B., The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J. Biol. Chem. 266 (1991), 11632–11639.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 80
    • 0026571238 scopus 로고
    • Two adjacent AP-1 binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene
    • [80] Friling, R.S., Bergelson, S., Daniel, V., Two adjacent AP-1 binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene. Proc. Natl. Acad. Sci. USA. 89 (1992), 668–672.
    • (1992) Proc. Natl. Acad. Sci. USA. , vol.89 , pp. 668-672
    • Friling, R.S.1    Bergelson, S.2    Daniel, V.3
  • 81
    • 0028914295 scopus 로고
    • Identification of a putative antioxidant response element in the 5′-flanking region of the human g-glutamylcycteine synthetase heavy subunit gene
    • [81] Mulcahy, R.T., Gipp, J.J., Identification of a putative antioxidant response element in the 5′-flanking region of the human g-glutamylcycteine synthetase heavy subunit gene. Biochem. Biophys. Res. Commun. 209 (1995), 227–233.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 227-233
    • Mulcahy, R.T.1    Gipp, J.J.2
  • 82
    • 0033546686 scopus 로고    scopus 로고
    • Up-regulation of the human gamma-glutamylcysteine synthetase regulatory subunit gene involves binding of Nrf-2 to an electrophile responsive element
    • [82] Moinova, H.R., Mulcahy, R.T., Up-regulation of the human gamma-glutamylcysteine synthetase regulatory subunit gene involves binding of Nrf-2 to an electrophile responsive element. Biochem. Biophys. Res Commun. 261 (1999), 661–668.
    • (1999) Biochem. Biophys. Res Commun. , vol.261 , pp. 661-668
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 84
    • 0037366092 scopus 로고    scopus 로고
    • Curcumin alters EpRE and AP-1 binding complexes and elevates glutamate-cysteine ligase gene expression
    • [84] Dickinson, D.A., Iles, K.E., Zhang, H., Blank, V., Forman, H.J., Curcumin alters EpRE and AP-1 binding complexes and elevates glutamate-cysteine ligase gene expression. FASEB J. 17 (2003), 473–475.
    • (2003) FASEB J. , vol.17 , pp. 473-475
    • Dickinson, D.A.1    Iles, K.E.2    Zhang, H.3    Blank, V.4    Forman, H.J.5
  • 87
    • 77951105782 scopus 로고    scopus 로고
    • C-Myc is a Nrf2-interacting protein that negatively regulates phase II genes through their electrophile responsive elements
    • [87] Levy, S., Forman, H.J., C-Myc is a Nrf2-interacting protein that negatively regulates phase II genes through their electrophile responsive elements. IUBMB Life 62 (2010), 237–246.
    • (2010) IUBMB Life , vol.62 , pp. 237-246
    • Levy, S.1    Forman, H.J.2
  • 88
    • 67349089075 scopus 로고    scopus 로고
    • Multidrug-resistant protein-3 gene regulation by the transcription factor Nrf2 in human bronchial epithelial and non-small-cell lung carcinoma
    • [88] Mahaffey, C.M., Zhang, H., Rinna, A., Holland, W., Mack, P.C., Forman, H.J., Multidrug-resistant protein-3 gene regulation by the transcription factor Nrf2 in human bronchial epithelial and non-small-cell lung carcinoma. Free Radic. Biol. Med. 46 (2009), 1650–1657.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1650-1657
    • Mahaffey, C.M.1    Zhang, H.2    Rinna, A.3    Holland, W.4    Mack, P.C.5    Forman, H.J.6
  • 90
    • 33745006817 scopus 로고    scopus 로고
    • Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B
    • [90] Rinna, A., Torres, M., Forman, H.J., Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B. Free Radic. Biol. Med. 41 (2006), 86–91.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 86-91
    • Rinna, A.1    Torres, M.2    Forman, H.J.3
  • 91
    • 45849089850 scopus 로고    scopus 로고
    • SHP-1 inhibition by 4-hydroxynonenal activates Jun N-terminal kinase and glutamate cysteine ligase
    • [91] Rinna, A., Forman, H.J., SHP-1 inhibition by 4-hydroxynonenal activates Jun N-terminal kinase and glutamate cysteine ligase. Am. J. Respir. Cell Mol. Biol. 39 (2008), 97–104.
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.39 , pp. 97-104
    • Rinna, A.1    Forman, H.J.2
  • 94
    • 0037029043 scopus 로고    scopus 로고
    • Lung cancer, cardiopulmonary mortality, and long-term exposure to fine particulate air pollution
    • [94] Pope, C.A., Burnett, R.T., Thun, M.J., Calle, E.E., Krewski, D., Ito, K., Thurston, G.D., Lung cancer, cardiopulmonary mortality, and long-term exposure to fine particulate air pollution. JAMA 287 (2002), 1132–1141.
    • (2002) JAMA , vol.287 , pp. 1132-1141
    • Pope, C.A.1    Burnett, R.T.2    Thun, M.J.3    Calle, E.E.4    Krewski, D.5    Ito, K.6    Thurston, G.D.7
  • 95
    • 20644449754 scopus 로고    scopus 로고
    • Nanotoxicology: an emerging discipline evolving from studies of ultrafine particles
    • [95] Oberdorster, G., Oberdorster, E., Oberdorster, J., Nanotoxicology: an emerging discipline evolving from studies of ultrafine particles. Environ. Health Perspect. 113 (2005), 823–839.
    • (2005) Environ. Health Perspect. , vol.113 , pp. 823-839
    • Oberdorster, G.1    Oberdorster, E.2    Oberdorster, J.3
  • 96
    • 41549129392 scopus 로고    scopus 로고
    • The role of oxidative stress in ambient particulate matter-induced lung diseases and its implications in the toxicity of engineered nanoparticles
    • [96] Li, N., Xia, T., Nel, A.E., The role of oxidative stress in ambient particulate matter-induced lung diseases and its implications in the toxicity of engineered nanoparticles. Free Radic. Biol. Med. 44 (2008), 1689–1699.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1689-1699
    • Li, N.1    Xia, T.2    Nel, A.E.3
  • 97
    • 40949129640 scopus 로고    scopus 로고
    • Silica binding and toxicity in alveolar macrophages
    • [97] Hamilton, R.F., Thakur, S.A., Holian, A., Silica binding and toxicity in alveolar macrophages. Free Radic. Biol. Med. 44 (2008), 1246–1258.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1246-1258
    • Hamilton, R.F.1    Thakur, S.A.2    Holian, A.3
  • 98
    • 34247600505 scopus 로고    scopus 로고
    • Silica induces macrophage cytokines through phosphatidylcholine-specific phospholipase C with hydrogen peroxide
    • [98] Liu, H., Zhang, H., Forman, H.J., Silica induces macrophage cytokines through phosphatidylcholine-specific phospholipase C with hydrogen peroxide. Am. J. Respir. Cell Mol. Biol. 36 (2007), 594–599.
    • (2007) Am. J. Respir. Cell Mol. Biol. , vol.36 , pp. 594-599
    • Liu, H.1    Zhang, H.2    Forman, H.J.3
  • 99
    • 80051788903 scopus 로고    scopus 로고
    • Iron-mediated lipid peroxidation and lipid raft disruption in low-dose silica-induced macrophage cytokine production
    • [99] Premasekharan, G., Nguyen, K., Contreras, J., Ramon, V., Leppert, V.J., Forman, H.J., Iron-mediated lipid peroxidation and lipid raft disruption in low-dose silica-induced macrophage cytokine production. Free Radic. Biol. Med. 51 (2011), 1184–1194.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1184-1194
    • Premasekharan, G.1    Nguyen, K.2    Contreras, J.3    Ramon, V.4    Leppert, V.J.5    Forman, H.J.6
  • 100
    • 1542723493 scopus 로고    scopus 로고
    • Decline in transcriptional activity of Nrf2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid
    • [100] Suh, J.H., Shenvi, S.V., Dixon, B.M., Liu, H., Jaiswal, A.K., Liu, R.M., Hagen, T.M., Decline in transcriptional activity of Nrf2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid. Proc. Natl. Acad. Sci. USA 101 (2004), 3381–3386.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3381-3386
    • Suh, J.H.1    Shenvi, S.V.2    Dixon, B.M.3    Liu, H.4    Jaiswal, A.K.5    Liu, R.M.6    Hagen, T.M.7
  • 101
    • 84860471609 scopus 로고    scopus 로고
    • Nrf2-regulated phase II enzymes are induced by chronic ambient nanoparticle exposure in young mice with age-related impairments
    • [101] Zhang, H., Liu, H., Davies, K.J.A., Sioutas, C., Finch, C.E., Morgan, T.E., Forman, H.J., Nrf2-regulated phase II enzymes are induced by chronic ambient nanoparticle exposure in young mice with age-related impairments. Free Radic. Biol. Med. 52 (2012), 2038–2046.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 2038-2046
    • Zhang, H.1    Liu, H.2    Davies, K.J.A.3    Sioutas, C.4    Finch, C.E.5    Morgan, T.E.6    Forman, H.J.7
  • 102
    • 84892369382 scopus 로고    scopus 로고
    • How do nutritional antioxidants really work: nucleophilic tone and para-hormesis versus free radical scavenging in vivo
    • [102] Forman, H.J., Davies, K.J.A., Ursini, F., How do nutritional antioxidants really work: nucleophilic tone and para-hormesis versus free radical scavenging in vivo. Free Radic. Biol. Med. 66 (2014), 24–35.
    • (2014) Free Radic. Biol. Med. , vol.66 , pp. 24-35
    • Forman, H.J.1    Davies, K.J.A.2    Ursini, F.3
  • 104
    • 84955279653 scopus 로고    scopus 로고
    • Redox homeostasis: the Golden Mean of healthy living
    • [104] Ursini, F., Maiorino, M., Forman, H.J., Redox homeostasis: the Golden Mean of healthy living. Redox Biol. 8 (2016), 205–215.
    • (2016) Redox Biol. , vol.8 , pp. 205-215
    • Ursini, F.1    Maiorino, M.2    Forman, H.J.3
  • 105
    • 84921449543 scopus 로고    scopus 로고
    • TGFβ1 rapidly activates Src through a non-canonical redox signaling mechanism
    • [105] Zhang, H., Davies, K.J.A., Forman, H.J., TGFβ1 rapidly activates Src through a non-canonical redox signaling mechanism. Arch. Biochem. Biophys. 568 (2015), 1–7.
    • (2015) Arch. Biochem. Biophys. , vol.568 , pp. 1-7
    • Zhang, H.1    Davies, K.J.A.2    Forman, H.J.3
  • 106
    • 0000707453 scopus 로고
    • Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate levels in various tissue preparations
    • [106] Arnold, W.P., Mittal, C.K., Katsuki, S., Murad, F., Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate levels in various tissue preparations. Proc. Natl. Acad. Sci. U S A 74 (1977), 3203–3207.
    • (1977) Proc. Natl. Acad. Sci. U S A , vol.74 , pp. 3203-3207
    • Arnold, W.P.1    Mittal, C.K.2    Katsuki, S.3    Murad, F.4
  • 107
    • 0018311634 scopus 로고
    • Relaxation of bovine coronary artery and activation of coronary arterial guanylate cyclase by nitric oxide, nitroprusside and a carcinogenic nitrosoamine
    • [107] Gruetter, C.A., Barry, B.K., McNamara, D.B., Gruetter, D.Y., Kadowitz, P.J., Ignarro, L., Relaxation of bovine coronary artery and activation of coronary arterial guanylate cyclase by nitric oxide, nitroprusside and a carcinogenic nitrosoamine. J. Cycl. Nucleotide Res 5 (1979), 211–224.
    • (1979) J. Cycl. Nucleotide Res , vol.5 , pp. 211-224
    • Gruetter, C.A.1    Barry, B.K.2    McNamara, D.B.3    Gruetter, D.Y.4    Kadowitz, P.J.5    Ignarro, L.6
  • 109
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H: quinone oxidoreductase1 gene
    • [109] Venugopal, R., Jaiswal, A.K., Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H: quinone oxidoreductase1 gene. J. Clin. Invest. 93 (1996), 14960–14965.
    • (1996) J. Clin. Invest. , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 110
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation
    • [110] Denu, J.M., Tanner, K.G., Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochem 37 (1998), 5633–5642.
    • (1998) Biochem , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 112
    • 0035853157 scopus 로고    scopus 로고
    • Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice
    • [112] Ramos-Gomez, M., Kwak, M.K., Dolan, P.M., Itoh, K., Yamamoto, M., Talalay, P., Kensler, T.W., Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc. Natl. Acad. Sci. USA 98 (2001), 3410–3415.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3410-3415
    • Ramos-Gomez, M.1    Kwak, M.K.2    Dolan, P.M.3    Itoh, K.4    Yamamoto, M.5    Talalay, P.6    Kensler, T.W.7
  • 113
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • [113] Dinkova-Kostova, A.T., Holtzclaw, W.D., Cole, R.N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., Talalay, P., Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl. Acad. Sci. USA 99 (2002), 11908–11913.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 114
    • 0034284232 scopus 로고    scopus 로고
    • The role of a mitochondrial pathway in the induction of apoptosis by chemicals extracted from diesel exhaust particles
    • [114] Hiura, T.S., Li, N., Kaplan, R., Horwitz, M., Seagrave, J.C., Nel, A.E., The role of a mitochondrial pathway in the induction of apoptosis by chemicals extracted from diesel exhaust particles. J. Immunol. 165 (2000), 2703–2711.
    • (2000) J. Immunol. , vol.165 , pp. 2703-2711
    • Hiura, T.S.1    Li, N.2    Kaplan, R.3    Horwitz, M.4    Seagrave, J.C.5    Nel, A.E.6
  • 115
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • [115] McMahon, M., Itoh, K., Yamamoto, M., Hayes, J.D., Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J. Biol. Chem. 278 (2003), 21592–21600.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 116
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • [116] Levonen, A.L., Landar, A., Ramachandran, A., Ceaser, E.K., Dickinson, D.A., Zanoni, G., Morrow, J.D., Darley-Usmar, V.M., Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem. J. 378 (2004), 373–382.
    • (2004) Biochem. J. , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8


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