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Volumn , Issue , 2008, Pages 1-17

Hydrogen peroxide: The good, the bad, and the ugly

Author keywords

ASK1; catalase; DuOX; glutathione peroxidase; Hydrogen peroxide; hydroxyl radical; hypobromous acid; hypochlorous acid; hypothiocyanic acid; lactoperoxidase; mitochondria; myeloperoxidase; NADPH oxidase; NOX; peroxiredoxin; protein tyrosine phosphatase; signal transduction; superoxide; superoxide dismutase; thioredoxin

Indexed keywords


EID: 67649783837     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4020-8399-0_1     Document Type: Chapter
Times cited : (11)

References (106)
  • 2
    • 0003698541 scopus 로고
    • Biological reactivity of hypochlorous acid: Implications for microbicidal mechanisms of leukocyte myeloperoxidase
    • Albrich, J. M., Mccarthy, C. A. & Hurst, J. K. (1981) Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase. Proceedings National Academy of Sciences, USA 78, 210-214.
    • (1981) Proceedings National Academy of Sciences, USA , vol.78 , pp. 210-214
    • Albrich, J.M.1    Mccarthy, C.A.2    Hurst, J.K.3
  • 3
    • 0033231351 scopus 로고    scopus 로고
    • Gene expression and the thiol redox state
    • Arrigo, A. P. (1999) Gene expression and the thiol redox state. Free Radic Biol Med 27, 936-944.
    • (1999) Free Radic Biol Med , vol.27 , pp. 936-944
    • Arrigo, A.P.1
  • 4
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain, J., McLauchlan, H., Elliott, M. & Cohen, P. (2003) The specificities of protein kinase inhibitors: an update. Biochem J 371, 199-204.
    • (2003) Biochem J , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 5
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • Barrett, W. C., Degnore, J. P., Keng, Y. F., Zhang, Z. Y., Yim, M. B. & Chock, P. B. (1999a) Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J Biol Chem 274, 34543-34546.
    • (1999) J Biol Chem , vol.274 , pp. 34543-34546
    • Barrett, W.C.1    Degnore, J.P.2    Keng, Y.F.3    Zhang, Z.Y.4    Yim, M.B.5    Chock, P.B.6
  • 8
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K. & Krause, K. H. (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87, 245-313.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 10
    • 0016681098 scopus 로고
    • Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
    • Boveris, A. & Cadenas, E. (1975) Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration. FEBS Letters 54, 311.
    • (1975) FEBS Letters , vol.54 , pp. 311
    • Boveris, A.1    Cadenas, E.2
  • 11
    • 0002889135 scopus 로고    scopus 로고
    • Cellular sources and steady-state levels of reactive oxygen species
    • Clerch, L. B. & Massaro, D. J. Eds., New York, Marcel Dekker
    • Boveris, A. & Cadenas, E. (1997) Cellular sources and steady-state levels of reactive oxygen species. In Clerch, L. B. & Massaro, D. J. (Eds.) Oxygen, Gene Expression, and Cellular Function, New York, Marcel Dekker.
    • (1997) Oxygen, Gene Expression, and Cellular Function
    • Boveris, A.1    Cadenas, E.2
  • 12
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris, A., Oshino, N. & Chance, B. (1972) The cellular production of hydrogen peroxide. Biochem J 128, 617-630.
    • (1972) Biochem J , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 13
    • 0020624295 scopus 로고
    • Identification and quantitation of glutathione and its relationship to glutathione disulfide
    • Brigelius, R., Muckel, C., Akerboom, T. P. M. & Sies, H. (1983) Identification and quantitation of glutathione and its relationship to glutathione disulfide. Biochemical Pharmacology 32, 2529-2534.
    • (1983) Biochemical Pharmacology , vol.32 , pp. 2529-2534
    • Brigelius, R.1    Muckel, C.2    Akerboom, T.P.M.3    Sies, H.4
  • 14
    • 0037082357 scopus 로고    scopus 로고
    • *) signaling pathway, and the transduction of nitrosative to oxidative cell signals: An alternative function for cytochrome C oxidase
    • *) signaling pathway, and the transduction of nitrosative to oxidative cell signals: an alternative function for cytochrome C oxidase. Free Radic Biol Med 32, 370-374.
    • (2002) Free Radic Biol Med , vol.32 , pp. 370-374
    • Brookes, P.1    Darley-Usmar, V.M.2
  • 15
    • 0029887638 scopus 로고    scopus 로고
    • Effect of eosinophil peroxidase on airway epithelial permeability in the guinea pig
    • Brottman, G. M., Regelmann, W. E., Slungaard, A. & Wangensteen, O. D. (1996) Effect of eosinophil peroxidase on airway epithelial permeability in the guinea pig. Pediatr Pulmonol 21, 159-166.
    • (1996) Pediatr Pulmonol , vol.21 , pp. 159-166
    • Brottman, G.M.1    Regelmann, W.E.2    Slungaard, A.3    Wangensteen, O.D.4
  • 16
    • 33749234188 scopus 로고    scopus 로고
    • A new paradigm: Manganese superoxide dismutase influences the production of H2O2 in cells and thereby their biological state
    • Buettner, G. R., Ng, C. F., Wang, M., Rodgers, V. G. & Schafer, F. Q. (2006) A new paradigm: manganese superoxide dismutase influences the production of H2O2 in cells and thereby their biological state. Free Radic Biol Med 41, 1338-1350.
    • (2006) Free Radic Biol Med , vol.41 , pp. 1338-1350
    • Buettner, G.R.1    Ng, C.F.2    Wang, M.3    Rodgers, V.G.4    Schafer, F.Q.5
  • 17
  • 18
    • 0025616118 scopus 로고
    • Oxidative stress and tumour cell proliferation
    • Burdon, R. H., Gill, V. & Rice-Evans, C. (1990) Oxidative stress and tumour cell proliferation. Free Radic Res Commun 11(1-3), 65-76.
    • (1990) Free Radic Res Commun , vol.11 , Issue.1-3 , pp. 65-76
    • Burdon, R.H.1    Gill, V.2    Rice-Evans, C.3
  • 19
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • Cadenas, E., Boveris, A., Ragan, C. I. & Stoppani, A. O. (1977) Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch Biochem Biophys 180, 248-257.
    • (1977) Arch Biochem Biophys , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 20
    • 0032544309 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx
    • Chang, H. Y., Nishitoh, H., Yang, X., Ichijo, H. & Baltimore, D. (1998) Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx. Science 281, 1860-1863.
    • (1998) Science , vol.281 , pp. 1860-1863
    • Chang, H.Y.1    Nishitoh, H.2    Yang, X.3    Ichijo, H.4    Baltimore, D.5
  • 21
    • 0035823539 scopus 로고    scopus 로고
    • Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation
    • Chiarugi, P., Fiaschi, T., Taddei, M. L., Talini, D., Giannoni, E., Raugei, G. & Ramponi, G. (2001) Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation. J Biol Chem 276, 33478-33487.
    • (2001) J Biol Chem , vol.276 , pp. 33478-33487
    • Chiarugi, P.1    Fiaschi, T.2    Taddei, M.L.3    Talini, D.4    Giannoni, E.5    Raugei, G.6    Ramponi, G.7
  • 22
    • 17644378052 scopus 로고    scopus 로고
    • H2O2 activates Nox4 through PLA2-dependent arachidonic acid production in adult cardiac fibroblasts
    • Colston, J. T., De La Rosa, S. D., Strader, J. R., Anderson, M. A. & Freeman, G. L. (2005) H2O2 activates Nox4 through PLA2-dependent arachidonic acid production in adult cardiac fibroblasts. FEBS Lett 579, 2533-2540.
    • (2005) FEBS Lett , vol.579 , pp. 2533-2540
    • Colston, J.T.1    De La Rosa, S.D.2    Strader, J.R.3    Anderson, M.A.4    Freeman, G.L.5
  • 23
    • 0016240863 scopus 로고
    • Biological defense mechanisms. The effect of bacteria and serum on superoxide production by granulocytes
    • Curnutte, J. T. & Babior, B. M. (1974) Biological defense mechanisms. The effect of bacteria and serum on superoxide production by granulocytes. J Clin Invest 53, 1662-1672.
    • (1974) J Clin Invest , vol.53 , pp. 1662-1672
    • Curnutte, J.T.1    Babior, B.M.2
  • 24
    • 0017261573 scopus 로고
    • Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system
    • Czech, M. P. (1976) Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system. J Biol Chem 251, 1164-1170.
    • (1976) J Biol Chem , vol.251 , pp. 1164-1170
    • Czech, M.P.1
  • 25
    • 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
    • Denu, J. M. & Tanner, K. G. (1998) Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37, 5633-5642.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 26
    • 0031570504 scopus 로고    scopus 로고
    • Mice lacking reduced nicotinamide adenine dinucleotide phosphate oxidase activity show increased susceptibility to early infection with Listeria monocytogenes
    • Dinauer, M. C., Deck, M. B. & Unanue, E. R. (1997) Mice lacking reduced nicotinamide adenine dinucleotide phosphate oxidase activity show increased susceptibility to early infection with Listeria monocytogenes. J Immunol 158, 5581-5583.
    • (1997) J Immunol , vol.158 , pp. 5581-5583
    • Dinauer, M.C.1    Deck, M.B.2    Unanue, E.R.3
  • 28
    • 33750900751 scopus 로고    scopus 로고
    • Intracellular redox regulation by the family of small GTPases
    • Finkel, T. (2006) Intracellular redox regulation by the family of small GTPases. Antioxid Redox Signal 8, 1857-1863.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1857-1863
    • Finkel, T.1
  • 30
    • 33847660853 scopus 로고    scopus 로고
    • Use and abuse of exogenous H2O2 in studies of signal transduction
    • Forman, H. J. (2007) Use and abuse of exogenous H2O2 in studies of signal transduction. Free Radic Biol Med 42, 926-932.
    • (2007) Free Radic Biol Med , vol.42 , pp. 926-932
    • Forman, H.J.1
  • 32
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling - Thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman, H. J., Fukuto, J. & Torres, M. (2004) Redox signaling - thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 287, C246-C256.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Forman, H.J.1    Fukuto, J.2    Torres, M.3
  • 33
    • 0016246294 scopus 로고
    • Role of superoxide radical in mitochondrial dehydrogenase reactions
    • Forman, H. J. & Kennedy, J. A. (1974) Role of superoxide radical in mitochondrial dehydrogenase reactions. Biochem Biophys Res Commun 60, 1044-1050.
    • (1974) Biochem Biophys Res Commun , vol.60 , pp. 1044-1050
    • Forman, H.J.1    Kennedy, J.A.2
  • 34
    • 0034782946 scopus 로고    scopus 로고
    • Redox signaling in macrophages
    • Forman, H. J. & Torres, M. (2001) Redox signaling in macrophages. Mol Aspects Med 22, 189-216.
    • (2001) Mol Aspects Med , vol.22 , pp. 189-216
    • Forman, H.J.1    Torres, M.2
  • 35
    • 0344258132 scopus 로고    scopus 로고
    • Abnormal glutathione transport in cystic fibrosis airway epithelia
    • Gao, L., Kim, K. J., Yankaskas, J. R. & Forman, H. J. (1999) Abnormal glutathione transport in cystic fibrosis airway epithelia. Am J Physiol 277, L113-L118.
    • (1999) Am J Physiol , vol.277
    • Gao, L.1    Kim, K.J.2    Yankaskas, J.R.3    Forman, H.J.4
  • 36
    • 33745209498 scopus 로고    scopus 로고
    • NADPH oxidases: New kids on the block
    • Geiszt, M. (2006) NADPH oxidases: new kids on the block. Cardiovasc Res 71, 289-299.
    • (2006) Cardiovasc Res , vol.71 , pp. 289-299
    • Geiszt, M.1
  • 37
    • 0034677947 scopus 로고    scopus 로고
    • NAD (P) H oxidase: Role in cardiovascular biology and disease
    • Griendling, K. K., Sorescu, D. & Ushio-Fukai, M. (2000) NAD (P) H oxidase: role in cardiovascular biology and disease. Circ Res 86, 494-501.
    • (2000) Circ Res , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 38
    • 0029819752 scopus 로고    scopus 로고
    • Measuring nitric oxide and superoxide: Rate constants for aconitase reactivity
    • Hausladen, A. & Fridovich, I. (1996) Measuring nitric oxide and superoxide: rate constants for aconitase reactivity. Methods Enzymol 269, 37-41.
    • (1996) Methods Enzymol , vol.269 , pp. 37-41
    • Hausladen, A.1    Fridovich, I.2
  • 43
    • 0014010888 scopus 로고
    • Antimycin-insensitive oxidation of succinate and reduced nicotinamideadenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation
    • Jensen, P. K. (1966) Antimycin-insensitive oxidation of succinate and reduced nicotinamideadenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation. Biochim Biophys Acta 122, 157-166.
    • (1966) Biochim Biophys Acta , vol.122 , pp. 157-166
    • Jensen, P.K.1
  • 44
    • 33749993246 scopus 로고    scopus 로고
    • Disruption of mitochondrial redox circuitry in oxidative stress
    • Jones, D. P. (2006) Disruption of mitochondrial redox circuitry in oxidative stress. Chem Biol Interact 163, 38-53.
    • (2006) Chem Biol Interact , vol.163 , pp. 38-53
    • Jones, D.P.1
  • 45
    • 0028138966 scopus 로고
    • The functional expression of p47-phox and p67-phox may contribute to the generation of superoxide by an NADPH oxidase-like system in human fibroblasts
    • Jones, S. A., Wood, J. D., Coffey, M. J. & Jones, O. T. (1994) The functional expression of p47-phox and p67-phox may contribute to the generation of superoxide by an NADPH oxidase-like system in human fibroblasts. FEBS Lett 355, 178-182.
    • (1994) FEBS Lett , vol.355 , pp. 178-182
    • Jones, S.A.1    Wood, J.D.2    Coffey, M.J.3    Jones, O.T.4
  • 46
    • 0032541085 scopus 로고    scopus 로고
    • A Rac1 effector site controlling mitogenesis through superoxide production
    • Joneson, T. & Bar-Sagi, D. (1998) A Rac1 effector site controlling mitogenesis through superoxide production. J Biol Chem 273, 17991-17994.
    • (1998) J Biol Chem , vol.273 , pp. 17991-17994
    • Joneson, T.1    Bar-Sagi, D.2
  • 47
    • 0029760973 scopus 로고    scopus 로고
    • Activation of NF-β by the respiratory burst of macrophages
    • Kaul, N. & Forman, H. J. (1996) Activation of NF-β by the respiratory burst of macrophages. Free Radical Biology & Medicine 21, 401-405.
    • (1996) Free Radical Biology & Medicine , vol.21 , pp. 401-405
    • Kaul, N.1    Forman, H.J.2
  • 48
    • 0020287103 scopus 로고
    • The role of nonenzymatic reactions of glutathione in xenobiotic metabolism
    • Ketterer, B. (1982) The role of nonenzymatic reactions of glutathione in xenobiotic metabolism. Drug Metabolism Reviews 13, 161-187.
    • (1982) Drug Metabolism Reviews , vol.13 , pp. 161-187
    • Ketterer, B.1
  • 49
    • 0015501473 scopus 로고
    • A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis
    • Klug, D., Rabani, J. & Fridovich, I. (1972) A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis. J Biol Chem 247, 4839-4842.
    • (1972) J Biol Chem , vol.247 , pp. 4839-4842
    • Klug, D.1    Rabani, J.2    Fridovich, I.3
  • 51
    • 0030967205 scopus 로고    scopus 로고
    • Role of oxidative stress in the action of vanadium phosphotyrosine phosphatase inhibitors. Redox independent activation of NF-β
    • Krejsa, C. M., Nadler, S. G., Esselstyn, J. M., Kavanagh, T. J., Ledbetter, J. A. & Schieven, G. L. (1997) Role of oxidative stress in the action of vanadium phosphotyrosine phosphatase inhibitors. Redox independent activation of NF-β B. J Biol Chem 272, 11541-11549.
    • (1997) B. J Biol Chem , vol.272 , pp. 11541-11549
    • Krejsa, C.M.1    Nadler, S.G.2    Esselstyn, J.M.3    Kavanagh, T.J.4    Ledbetter, J.A.5    Schieven, G.L.6
  • 52
    • 34347257042 scopus 로고    scopus 로고
    • Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy
    • Lambeth, J. D. (2007) Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy. Free Radic Biol Med 43, 332-347.
    • (2007) Free Radic Biol Med , vol.43 , pp. 332-347
    • Lambeth, J.D.1
  • 54
    • 34250888056 scopus 로고    scopus 로고
    • Regulation of Nox and DuOx enzymatic activity and expression
    • Lambeth, J. D., Kawahara, T. & Diebold, B. (2007) Regulation of Nox and DuOx enzymatic activity and expression Free Radic Biol Med 43, 319-331.
    • (2007) Free Radic Biol Med , vol.43 , pp. 319-331
    • Lambeth, J.D.1    Kawahara, T.2    Diebold, B.3
  • 55
    • 0035844030 scopus 로고    scopus 로고
    • Novel gp91phox homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways
    • Lassegue, B., Sorescu, D., Szocs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D. & Griendling, K. K. (2001) Novel gp91phox homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways. Circ Res 88, 888-894.
    • (2001) Circ Res , vol.88 , pp. 888-894
    • Lassegue, B.1    Sorescu, D.2    Szocs, K.3    Yin, Q.4    Akers, M.5    Zhang, Y.6    Grant, S.L.7    Lambeth, J.D.8    Griendling, K.K.9
  • 56
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee, S. R., Kwon, K. S., Kim, S. R. & Rhee, S. G. (1998) Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273, 15366-15372.
    • (1998) J Biol Chem , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 57
    • 0037443130 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols
    • Li, S. & Whorton, A. R. (2003) Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols. Arch Biochem Biophys 410, 269-279.
    • (2003) Arch Biochem Biophys , vol.410 , pp. 269-279
    • Li, S.1    Whorton, A.R.2
  • 58
    • 33749248371 scopus 로고    scopus 로고
    • The ADP-stimulated NADPH oxidase activates the ASK-1/MKK4/JNK pathway in alveolar macrophages
    • Liu, H., Zhang, H., Iles, K. E., Rinna, A., Merrill, G., Yodoi, J., Torres, M. & Forman, H. J. (2006) The ADP-stimulated NADPH oxidase activates the ASK-1/MKK4/JNK pathway in alveolar macrophages. Free Radic Res 40, 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
  • 59
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • Loschen, G., Azzi, A., Richter, C. & Flohe, L. (1974) Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Letters 42, 68.
    • (1974) FEBS Letters , vol.42 , pp. 68
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohe, L.4
  • 60
    • 0021280371 scopus 로고
    • Properties of extracellular superoxide dismutase from human lung
    • Marklund, S. L. (1984) Properties of extracellular superoxide dismutase from human lung. Biochem J 220, 269-272.
    • (1984) Biochem J , vol.220 , pp. 269-272
    • Marklund, S.L.1
  • 62
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M. & Fridovich, I. (1969) Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244, 6049-6055.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 64
    • 0015523099 scopus 로고
    • The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase
    • Misra, H. P. & Fridovich, I. (1972) The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J Biol Chem 247, 3170.
    • (1972) J Biol Chem , vol.247 , pp. 3170
    • Misra, H.P.1    Fridovich, I.2
  • 67
    • 0028233138 scopus 로고
    • NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium
    • Mohazzab-H, K. M., Kaminski, P. M. & Wolin, M. S. (1994) NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium. Am J Physiol 266, H2568-H2572.
    • (1994) Am J Physiol , vol.266
    • Mohazzab-H, K.M.1    Kaminski, P.M.2    Wolin, M.S.3
  • 68
    • 0017331289 scopus 로고
    • Paraquat toxicity and pulmonary superoxide dismutase: An enzymic deficiency of lung microsomes
    • Montgomery, M. (1977) Paraquat toxicity and pulmonary superoxide dismutase: an enzymic deficiency of lung microsomes. Res Commun Chem Pathol Pharmacol 16, 155.
    • (1977) Res Commun Chem Pathol Pharmacol , vol.16 , pp. 155
    • Montgomery, M.1
  • 69
    • 0018071115 scopus 로고
    • Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents
    • Mukherjee, S. P., Lane, R. H. & Lynn, W. S. (1978) Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents. Biochem Pharmacol 27, 2589-2594.
    • (1978) Biochem Pharmacol , vol.27 , pp. 2589-2594
    • Mukherjee, S.P.1    Lane, R.H.2    Lynn, W.S.3
  • 70
    • 0019948668 scopus 로고
    • Similar activities of nerve growth factor and its homologue proinsulin in intracellular hydrogen peroxide production and metabolism in adipocytes. Transmembrane signalling relative to insulin-mimicking cellular effects
    • Mukherjee, S. P. & Mukherjee, C. (1982) Similar activities of nerve growth factor and its homologue proinsulin in intracellular hydrogen peroxide production and metabolism in adipocytes. Transmembrane signalling relative to insulin-mimicking cellular effects. Biochem Pharmacol 31, 3163-3172.
    • (1982) Biochem Pharmacol , vol.31 , pp. 3163-3172
    • Mukherjee, S.P.1    Mukherjee, C.2
  • 73
    • 0025101590 scopus 로고
    • Effect of superoxide dismutase on the autoxidation of substituted hydro- and semi-naphthoquinones
    • Ollinger, K., Buffinton, G. D., Ernster, L. & Cadenas, E. (1990) Effect of superoxide dismutase on the autoxidation of substituted hydro- and semi-naphthoquinones. Chem Biol Interact 73, 53-76.
    • (1990) Chem Biol Interact , vol.73 , pp. 53-76
    • Ollinger, K.1    Buffinton, G.D.2    Ernster, L.3    Cadenas, E.4
  • 74
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso, J. J., Carreras, M. C., Lisdero, C., Riobo, N., Schopfer, F. & Boveris, A. (1996) Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch Biochem Biophys 328, 85-92.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobo, N.4    Schopfer, F.5    Boveris, A.6
  • 75
    • 0037089309 scopus 로고    scopus 로고
    • Creation of a genetic system for analysis of the phagocyte respiratory burst: High-level reconstitution of the NADPH oxidase in a nonhematopoietic system
    • Price, M. O., Mcphail, L. C., Lambeth, J. D., Han, C. H., Knaus, U. G. & Dinauer, M. C. (2002) Creation of a genetic system for analysis of the phagocyte respiratory burst: high-level reconstitution of the NADPH oxidase in a nonhematopoietic system. Blood 99, 2653-2661.
    • (2002) Blood , vol.99 , pp. 2653-2661
    • Price, M.O.1    Mcphail, L.C.2    Lambeth, J.D.3    Han, C.H.4    Knaus, U.G.5    Dinauer, M.C.6
  • 77
    • 0036305442 scopus 로고    scopus 로고
    • Low molecular weight protein tyrosine phosphatases: Small, but smart
    • Raugei, G., Ramponi, G. & Chiarugi, P. (2002) Low molecular weight protein tyrosine phosphatases: small, but smart. Cell Mol Life Sci 59, 941-949.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 941-949
    • Raugei, G.1    Ramponi, G.2    Chiarugi, P.3
  • 78
    • 33745631769 scopus 로고    scopus 로고
    • Cell signaling. H2O2, a necessary evil for cell signaling
    • Rhee, S. G. (2006) Cell signaling. H2O2, a necessary evil for cell signaling. Science 312, 1882-1883.
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 79
    • 33745006817 scopus 로고    scopus 로고
    • Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B
    • Rinna, A., Torres, M. & Forman, H. J. (2006) Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B. Free Radic Biol Med 41, 86-91.
    • (2006) Free Radic Biol Med , vol.41 , pp. 86-91
    • Rinna, A.1    Torres, M.2    Forman, H.J.3
  • 81
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T. C., Hinks, J. A., Tonks, N. K. & Barford, D. (2003) Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423, 769-773.
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 82
    • 0014020468 scopus 로고
    • Relationship of glycolytic and oxidative metabolism to particle entry and destruction in phagocytosing cells
    • Selvaraj, R. J. & Sbarra, A. J. (1966) Relationship of glycolytic and oxidative metabolism to particle entry and destruction in phagocytosing cells. Nature 211, 1272-1276.
    • (1966) Nature , vol.211 , pp. 1272-1276
    • Selvaraj, R.J.1    Sbarra, A.J.2
  • 83
    • 0018862223 scopus 로고
    • Lung inflammation induced by complement-derived chemotactic fragments in the alveolus
    • Shaw, J. O., Henson, P. M., Henson, J. & Webster, R. O. (1980) Lung inflammation induced by complement-derived chemotactic fragments in the alveolus. Lab Invest 42, 547-558.
    • (1980) Lab Invest , vol.42 , pp. 547-558
    • Shaw, J.O.1    Henson, P.M.2    Henson, J.3    Webster, R.O.4
  • 84
    • 0041323072 scopus 로고    scopus 로고
    • Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction
    • Sohn, J. & Rudolph, J. (2003) Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction. Biochemistry 42, 10060-10070.
    • (2003) Biochemistry , vol.42 , pp. 10060-10070
    • Sohn, J.1    Rudolph, J.2
  • 85
    • 0042068217 scopus 로고    scopus 로고
    • Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1
    • Song, J. J. & Lee, Y. J. (2003) Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1. Biochem J 373, 845-853.
    • (2003) Biochem J , vol.373 , pp. 845-853
    • Song, J.J.1    Lee, Y.J.2
  • 86
    • 0028053726 scopus 로고
    • Modulation of activator protein-1 (AP-1) transcription factor and protein kinase C by hydrogen peroxide and D-α-tocopherol in vascular smooth muscle cells
    • Stauble, B., Boscoboinik, D., Tasinato, A. & Azzi, A. (1994) Modulation of activator protein-1 (AP-1) transcription factor and protein kinase C by hydrogen peroxide and D-α-tocopherol in vascular smooth muscle cells. Eur J Biochem 226, 392-402.
    • (1994) Eur J Biochem , vol.226 , pp. 392-402
    • Stauble, B.1    Boscoboinik, D.2    Tasinato, A.3    Azzi, A.4
  • 87
    • 0842348252 scopus 로고    scopus 로고
    • An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems
    • Stone, J. R. (2004) An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems. Arch Biochem Biophys 422, 119-124.
    • (2004) Arch Biochem Biophys , vol.422 , pp. 119-124
    • Stone, J.R.1
  • 88
    • 0015240625 scopus 로고
    • Effect of superoxide generation and dismutation on hydroxylation reactions catalyzed by liver microsomal cytochrome P-450
    • Strobel, H. W. & Coon, M. J. (1971) Effect of superoxide generation and dismutation on hydroxylation reactions catalyzed by liver microsomal cytochrome P-450. J Biol Chem 246, 7826.
    • (1971) J Biol Chem , vol.246 , pp. 7826
    • Strobel, H.W.1    Coon, M.J.2
  • 90
  • 91
    • 0034737642 scopus 로고    scopus 로고
    • Apoptosis signal-regulating kinase 1 (ASK1) induces neuronal differentiation and survival of PC12 cells
    • Takeda, K., Hatai, T., Hamazaki, T. S., Nishitoh, H., Saitoh, M. & Ichijo, H. (2000) Apoptosis signal-regulating kinase 1 (ASK1) induces neuronal differentiation and survival of PC12 cells. J Biol Chem 275, 9805-9813.
    • (2000) J Biol Chem , vol.275 , pp. 9805-9813
    • Takeda, K.1    Hatai, T.2    Hamazaki, T.S.3    Nishitoh, H.4    Saitoh, M.5    Ichijo, H.6
  • 92
    • 17744417909 scopus 로고    scopus 로고
    • NADPH oxidase contributes directly to oxidative stress and apoptosis in nerve growth factor-deprived sympathetic neurons
    • Tammariello, S. P., Quinn, M. T. & Estus, S. (2000) NADPH oxidase contributes directly to oxidative stress and apoptosis in nerve growth factor-deprived sympathetic neurons. J Neurosci 20, RC53.
    • (2000) J Neurosci , vol.20
    • Tammariello, S.P.1    Quinn, M.T.2    Estus, S.3
  • 93
    • 0013802106 scopus 로고
    • Mechanisms of oxidation with oxygen
    • Taube, H. (1965) Mechanisms of oxidation with oxygen. J. Gen. Physiol 2, 29.
    • (1965) J. Gen. Physiol , vol.2 , pp. 29
    • Taube, H.1
  • 94
    • 0036193169 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer
    • Tobiume, K., Saitoh, M. & Ichijo, H. (2002) Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer. J Cell Physiol 191, 95-104.
    • (2002) J Cell Physiol , vol.191 , pp. 95-104
    • Tobiume, K.1    Saitoh, M.2    Ichijo, H.3
  • 95
    • 0033563866 scopus 로고    scopus 로고
    • Activation of several MAP kinases upon stimulation of rat alveolar macrophages: Role of the NADPH oxidase
    • Torres, M. & Forman, H. J. (1999) Activation of several MAP kinases upon stimulation of rat alveolar macrophages: role of the NADPH oxidase. Arch Biochem Biophys 366, 231-239.
    • (1999) Arch Biochem Biophys , vol.366 , pp. 231-239
    • Torres, M.1    Forman, H.J.2
  • 96
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu, B. P., Ho-Schleyer, S. C., Travers, K. J. & Weissman, J. S. (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290, 1571-1574.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 98
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini, F., Maiorino, M. & Gregolin, C. (1985) The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim Biophys Acta 839, 62-70.
    • (1985) Biochim Biophys Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 99
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity
    • Van der Vliet, A., Eiserich, J. P., Halliwell, B. & Cross, C. E. (1997) Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J Biol Chem 272, 7617-7625.
    • (1997) J Biol Chem , vol.272 , pp. 7617-7625
    • Van Der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 101
    • 30544453606 scopus 로고    scopus 로고
    • Role of eosinophil peroxidase in host defense and disease pathology
    • Wang, J. & Slungaard, A. (2006) Role of eosinophil peroxidase in host defense and disease pathology. Arch Biochem Biophys 445, 256-260.
    • (2006) Arch Biochem Biophys , vol.445 , pp. 256-260
    • Wang, J.1    Slungaard, A.2
  • 102
    • 0029954102 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase
    • Wang, X. S., Diener, K., Jannuzzi, D., Trollinger, D., Tan, T. H., Lichenstein, H., Zukowski, M. & Yao, Z. (1996) Molecular cloning and characterization of a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase. J Biol Chem 271, 31607-31611.
    • (1996) J Biol Chem , vol.271 , pp. 31607-31611
    • Wang, X.S.1    Diener, K.2    Jannuzzi, D.3    Trollinger, D.4    Tan, T.H.5    Lichenstein, H.6    Zukowski, M.7    Yao, Z.8
  • 103
    • 0015694842 scopus 로고
    • Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial localization
    • Weisiger, R. A. & Fridovich, I. (1973) Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial localization. J Biol Chem 248, 4793-4796.
    • (1973) J Biol Chem , vol.248 , pp. 4793-4796
    • Weisiger, R.A.1    Fridovich, I.2
  • 104
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Winterbourn, C. C. & Metodiewa, D. (1999) Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med 27, 322-328.
    • (1999) Free Radic Biol Med , vol.27 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 105
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood, Z. A., Poole, L. B. & Karplus, P. A. (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 106
    • 33846025045 scopus 로고    scopus 로고
    • The oxidation of apocynin catalyzed by myeloperoxidase: Proposal for NADPH oxidase inhibition
    • Ximenes, V. F., Kanegae, M. P., Rissato, S. R. & Galhiane, M. S. (2007) The oxidation of apocynin catalyzed by myeloperoxidase: proposal for NADPH oxidase inhibition. Arch Biochem Biophys 457, 134-141.
    • (2007) Arch Biochem Biophys , vol.457 , pp. 134-141
    • Ximenes, V.F.1    Kanegae, M.P.2    Rissato, S.R.3    Galhiane, M.S.4


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