메뉴 건너뛰기




Volumn 11, Issue 11, 2009, Pages 2655-2671

Hydrogen peroxide as a cell-survival signaling molecule

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CYSTEINE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PHOSPHOTRANSFERASE; PROTEIN P53; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TRANSCRIPTION FACTOR AP 1;

EID: 73449129394     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2009.2728     Document Type: Review
Times cited : (271)

References (169)
  • 2
    • 0027136031 scopus 로고
    • Nanomolar arachidonicacid influences the respiratory burst in eosinophils and neutrophils induced by Gtp-binding protein: A comparative study of the respiratory burst in bovine eosinophils and neutrophils
    • Aebischer CP, Pasche I, and Jorg A. nanomolar arachidonicacid influences the respiratory burst in eosinophils and neutrophils induced by Gtp-binding protein: a comparative study of the respiratory burst in bovine eosinophils and neutrophils. Eur J Biochem 218: 669-677, 1993.
    • (1993) Eur J Biochem , vol.218 , pp. 669-677
    • Aebischer, C.P.1    Pasche, I.2    Jorg, A.3
  • 4
    • 8544270180 scopus 로고    scopus 로고
    • Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase
    • Ambasta RK, Kumar P, Griendling KK, Schmidt H, Busse R, and Brandes RP. Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase. J Biol Chem 279: 45935-45941, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 45935-45941
    • Ambasta, R.K.1    Kumar, P.2    Griendling, K.K.3    Schmidt, H.4    Busse, R.5    Brandes, R.P.6
  • 6
    • 0025720735 scopus 로고
    • The role of Jun, Fos and the AP-1 complex in cell proliferation and transformation
    • Angel P and Karin M. The role of Jun, Fos and the AP-1 complex in cell proliferation and transformation. Biochim Biophys Acta 1072: 129-157, 1991.
    • (1991) Biochim Biophys Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 8
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • Banfi B, Clark RA, Steger K, and Krause KH. Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J Biol Chem 278: 3510-3513, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 3510-3513
    • Banfi, B.1    Clark, R.A.2    Steger, K.3    Krause, K.H.4
  • 13
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROSgenerating NADPH oxidases: Physiology and pathophysiology
    • Bedard K and Krause KH. The NOX family of ROSgenerating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87: 245-313, 2007.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 14
    • 0029143425 scopus 로고
    • Involvement of proteinkinase-c and of protein phosphatase-1 and=or phosphatase-2a in p47 phox phosphorylation in formylmet-Leu-phe stimulated neutrophils: Studies with selective inhibitors ro-31-8220 and alyculin-A
    • Bengisgarber C and Gruener N. Involvement of proteinkinase-c and of protein phosphatase-1 and=or phosphatase-2a in p47 phox phosphorylation in formylmet-Leu-phe stimulated neutrophils: studies with selective inhibitors ro-31-8220 and alyculin-A. Cell Signal 7: 721-732, 1995.
    • (1995) Cell Signal , vol.7 , pp. 721-732
    • Bengisgarber, C.1    Gruener, N.2
  • 15
    • 0032514915 scopus 로고    scopus 로고
    • P40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase: Implication of a protein kinase C type kinase in the phosphorylation process
    • Bouin AP, Grandvaux N. Vignais PV, and Fuchs A. p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase: implication of a protein kinase C type kinase in the phosphorylation process. J Biol Chem 273: 30097-30103, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 30097-30103
    • Bouin, A.P.1    Grandvaux, N.2    Vignais, P.V.3    Fuchs, A.4
  • 17
    • 0037262072 scopus 로고    scopus 로고
    • The role of nitric oxide (NO) in stability regulation of hypoxia inducible factor-1alpha (HIF-1alpha)
    • Brune B and Zhou J. The role of nitric oxide (NO) in stability regulation of hypoxia inducible factor-1alpha (HIF-1alpha). Curr Med Chem 10: 845-855, 2003.
    • (2003) Curr Med Chem , vol.10 , pp. 845-855
    • Brune, B.1    Zhou, J.2
  • 19
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • Chen K, Kirber MT, Xiao H, Yang Y, and Keaney JF. Regulation of ROS signal transduction by NADPH oxidase 4 localization. J Cell Biol 181: 1129-1139, 2008.
    • (2008) J Cell Biol , vol.181 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney, J.F.5
  • 20
    • 33745815084 scopus 로고    scopus 로고
    • Nox1-dependent reactive oxygen generation is regulated by Rac1
    • Cheng G, Diebold BA, Hughes Y, and Lambeth JD. Nox1-dependent reactive oxygen generation is regulated by Rac1. J Biol Chem 281: 17718-17726, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 17718-17726
    • Cheng, G.1    Diebold, B.A.2    Hughes, Y.3    Lambeth, J.D.4
  • 21
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • Cheng GJ, Cao ZH, Xu XX,Van Meir EG, and Lambeth JD. Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 269: 131-140, 2001.
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.J.1    Zh, C.2    Xu, X.X.3    Van Meir, E.G.4    Lambeth, J.D.5
  • 22
    • 1042289744 scopus 로고    scopus 로고
    • NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the phox homology (PX) domain
    • Cheng GJ and Lambeth JD. NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the phox homology (PX) domain. J Biol Chem 279: 4737-4742, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 4737-4742
    • Cheng, G.J.1    Lambeth, J.D.2
  • 23
    • 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 ML, Talini D, Giannoni E, Raugei G, and Ramponi G. 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.
    • (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
  • 24
    • 55949128465 scopus 로고    scopus 로고
    • Anoikis: A necessary death program for anchorage-dependent cells
    • Chiarugi P and Giannoni E. Anoikis: a necessary death program for anchorage-dependent cells. Biochem Pharmacol 76: 1352-1364, 2008.
    • (2008) Biochem Pharmacol , vol.76 , pp. 1352-1364
    • Chiarugi, P.1    Giannoni, E.2
  • 26
    • 0025259712 scopus 로고
    • Cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma-membrane during cell activation
    • Clark RA, Volpp BD, Leidal KG, and Nauseef WM. Cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma-membrane during cell activation. J Clin Invest 85: 714-721, 1990.
    • (1990) J Clin Invest , vol.85 , pp. 714-721
    • Clark, R.A.1    Volpp, B.D.2    Leidal, K.G.3    Nauseef, W.M.4
  • 27
    • 0028321912 scopus 로고
    • Reciprocal interactions between protein-kinase-c and components of the NADPH oxidase complex may regulate superoxide production by neutrophils stimulated with a phorbol ester
    • Curnutte JT, Erickson RW, Ding JB, and Badwey JA. Reciprocal interactions between protein-kinase-c and components of the NADPH oxidase complex may regulate superoxide production by neutrophils stimulated with a phorbol ester. J Biol Chem 269: 10813-10819, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 10813-10819
    • Curnutte, J.T.1    Erickson, R.W.2    Ding, J.B.3    Badwey, J.A.4
  • 29
    • 27144535425 scopus 로고    scopus 로고
    • Regulation and termination of NADPH oxidase activity
    • DeCoursey TE and Ligeti E. Regulation and termination of NADPH oxidase activity. Cell Mol Life Sci 62: 2173-2193, 2005.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2173-2193
    • Decoursey, T.E.1    Ligeti, E.2
  • 30
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu JM and Dixon JE. Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr Opin Chem Biol 2: 633-641, 1998.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 633-641
    • Denu, J.M.1    Dixon, J.E.2
  • 33
    • 0033601327 scopus 로고    scopus 로고
    • Purification of a novel flavoprotein involved in the thyroid NADPH oxidase: Cloning of the porcine and human cDNAs
    • Dupuy C, Ohayon R, Valent A, Noel-Hudson MS, Deme D, and Virion A. Purification of a novel flavoprotein involved in the thyroid NADPH oxidase: cloning of the porcine and human cDNAs. J Biol Chem 274: 37265-37269, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 37265-37269
    • Dupuy, C.1    Ohayon, R.2    Valent, A.3    Noel-Hudson, M.S.4    Deme, D.5    Virion, A.6
  • 34
    • 0027364858 scopus 로고
    • Activation of NADPH oxidase of human neutrophils involves the phosphorylation and the translocation of cytosolic p67phox
    • Dusi S and Rossi F. Activation of NADPH oxidase of human neutrophils involves the phosphorylation and the translocation of cytosolic p67phox. Biochem J 296: 367-371, 1993.
    • (1993) Biochem J , vol.296 , pp. 367-371
    • Dusi, S.1    Rossi, F.2
  • 38
    • 0030764621 scopus 로고    scopus 로고
    • Phosphorylation of the respiratory burst oxidase subunit p67(phox) during human neutrophil activation: Regulation by protein kinase Cdependent and independent pathways
    • El Benna J, Dang PMC, Gaudry M, Fay M, Morel F, Hakim J, and Gougerot Pocidalo M.A. Phosphorylation of the respiratory burst oxidase subunit p67(phox) during human neutrophil activation: regulation by protein kinase Cdependent and independent pathways. J Biol Chem 272: 17204-17208, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 17204-17208
    • El Benna, J.1    Pmc, D.2    Gaudry, M.3    Fay, M.4    Morel, F.5    Hakim, J.6    Gougerot Pocidalo, M.A.7
  • 39
    • 0032843737 scopus 로고    scopus 로고
    • Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine=threonine protein phosphatase-1 subfamily
    • Fetrow JS, Siew N, and Skolnick J. Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine=threonine protein phosphatase-1 subfamily. FASEB J 13: 1866-1874, 1999.
    • (1999) FASEB J , vol.13 , pp. 1866-1874
    • Fetrow, J.S.1    Siew, N.2    Skolnick, J.3
  • 40
    • 13244288043 scopus 로고    scopus 로고
    • Regulation of H2O2 generation in thyroid cells does not involve Rac1 activation
    • Fortemaison N, Miot F, Dumont JE, and Dremier S. Regulation of H2O2 generation in thyroid cells does not involve Rac1 activation. Eur J Endocrinol 152: 127-133, 2005.
    • (2005) Eur J Endocrinol , vol.152 , pp. 127-133
    • Fortemaison, N.1    Miot, F.2    Dumont, J.E.3    Dremier, S.4
  • 41
    • 0030959894 scopus 로고    scopus 로고
    • NADPH oxidase activity is independent of p47(phox) in vitro (vol 271, pg 22578, 1996)
    • Freeman JL and Lambeth JD. NADPH oxidase activity is independent of p47(phox) in vitro (vol 271, pg 22578, 1996). J Biol Chem 272: 7566-7566, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 7566-7566
    • Freeman, J.L.1    Lambeth, J.D.2
  • 42
    • 0030694534 scopus 로고    scopus 로고
    • The 40-kDa component of the phagocyte NADPH oxidase (p40phox) is phosphorylated during activation in differentiated HL60 cells
    • Fuchs A, Bouin AP, Rabilloud T, and Vignais PV. The 40-kDa component of the phagocyte NADPH oxidase (p40phox) is phosphorylated during activation in differentiated HL60 cells. Eur J Biochem 249: 531-539, 1997.
    • (1997) Eur J Biochem , vol.249 , pp. 531-539
    • Fuchs, A.1    Bouin, A.P.2    Rabilloud, T.3    Vignais, P.V.4
  • 43
    • 15244339921 scopus 로고    scopus 로고
    • Overexpression of a novel superoxideproducing enzyme, NADPH oxidase 1, in adenoma and well differentiated adenocarcinoma of the human colon
    • Fukuyama M, Rokutan K, Sano T, Miyake H, Shimada M, and Tashiro S. Overexpression of a novel superoxideproducing enzyme, NADPH oxidase 1, in adenoma and well differentiated adenocarcinoma of the human colon. Cancer Lett 221: 97-104, 2005.
    • (2005) Cancer Lett , vol.221 , pp. 97-104
    • Fukuyama, M.1    Rokutan, K.2    Sano, T.3    Miyake, H.4    Shimada, M.5    Tashiro, S.6
  • 44
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • Gao T, Furnari F, and Newton AC. PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol Cell 18: 13-24, 2005.
    • (2005) Mol Cell , vol.18 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 46
    • 0036141212 scopus 로고    scopus 로고
    • AP-1 is essential for p67(phox) promoter activity
    • Gauss KA, Bunger PL, and Quinn MT. AP-1 is essential for p67(phox) promoter activity. J Leukoc Biol 71: 163-172, 2002.
    • (2002) J Leukoc Biol , vol.71 , pp. 163-172
    • Gauss, K.A.1    Bunger, P.L.2    Quinn, M.T.3
  • 48
    • 0042203535 scopus 로고    scopus 로고
    • Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense
    • Geiszt M, Witta J, Baffi J, Lekstrom K, and Leto TL. Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. FASEB J 17: 1502-1504, 2003.
    • (2003) FASEB J , vol.17 , pp. 1502-1504
    • Geiszt, M.1    Witta, J.2    Baffi, J.3    Lekstrom, K.4    Leto, T.L.5
  • 50
    • 1242316987 scopus 로고    scopus 로고
    • H2O2-dependent activation of GCLC-ARE4 reporter occurs by mitogen-activated protein kinase pathways without oxidation of cellular glutathione or thioredoxin-1
    • Go YM, Gipp JJ, Mulcahy RT, and Jones DP. H2O2-dependent activation of GCLC-ARE4 reporter occurs by mitogen-activated protein kinase pathways without oxidation of cellular glutathione or thioredoxin-1. J Biol Chem 279: 5837-5845, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 5837-5845
    • Go, Y.M.1    Gipp, J.J.2    Mulcahy, R.T.3    Jones, D.P.4
  • 51
    • 77957139430 scopus 로고    scopus 로고
    • Nox4 mediates angiotensin II-induced mesangial cell hypertrophy via activation of Akt=protein kinase B
    • Gorin Y, Ricono JM, Kim NH, Bhandari B, Choudhury GG, and Abboud HE. Nox4 mediates angiotensin II-induced mesangial cell hypertrophy via activation of Akt=protein kinase B. J Am Soc Nephrol 14: 91A-91A, 2003.
    • (2003) J Am Soc Nephrol , vol.14
    • Gorin, Y.1    Ricono, J.M.2    Kim, N.H.3    Bhandari, B.4    Choudhury, G.G.5    Abboud, H.E.6
  • 52
    • 0035816732 scopus 로고    scopus 로고
    • Thrombin activates the hypoxia-inducible factor-1 signaling pathway in vascular smooth muscle cells: Role of the p22(phox)-containing NADPH oxidase
    • Gorlach A, Diebold I, Schini-Kerth VB, Berchner-Pfannschmidt U, Roth U, Brandes RP, Kietzmann T, and Busse R. Thrombin activates the hypoxia-inducible factor-1 signaling pathway in vascular smooth muscle cells: role of the p22(phox)-containing NADPH oxidase. Circ Res 89: 47-54, 2001.
    • (2001) Circ Res , vol.89 , pp. 47-54
    • Gorlach, A.1    Diebold, I.2    Schini-Kerth, V.B.3    Berchner-Pfannschmidt, U.4    Roth, U.5    Brandes, R.P.6    Kietzmann, T.7    Busse, R.8
  • 53
    • 33745821178 scopus 로고    scopus 로고
    • Identification of the maturation factor for dual oxidase: Evolution of a eukaryotic operon equivalent
    • Grasberger H and Refetoff S. Identification of the maturation factor for dual oxidase: evolution of a eukaryotic operon equivalent. J Biol Chem 281: 18269-18272, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 18269-18272
    • Grasberger, H.1    Refetoff, S.2
  • 54
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y, Lapouge K, Smerdon SJ, and Rittinger K. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113: 343-355, 2003.
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 55
    • 85047692201 scopus 로고
    • Activation of protein kinases and the inactivation of protein phosphatase 2A in tumour necrosis factor and interleukin-1 signaltransduction pathways
    • Guy GR, Philp R, and Tan YH. Activation of protein kinases and the inactivation of protein phosphatase 2A in tumour necrosis factor and interleukin-1 signaltransduction pathways. Eur J Biochem 229: 503-511, 1995.
    • (1995) Eur J Biochem , vol.229 , pp. 503-511
    • Guy, G.R.1    Philp, R.2    Tan, Y.H.3
  • 56
    • 28544448737 scopus 로고    scopus 로고
    • Reactive oxygen species amplify glucose signalling in renal cells cultured under high glucose and in diabetic kidney
    • DOI 10.1111/j.1440-1797.2005.00448.x
    • Ha H and Lee HB. Reactive oxygen species amplify glucose signaling in renal cells cultured under high glucose and in diabetic kidney. Nephrology (Carlton) 10(suppl): S7-S10, 2005. (Pubitemid 41743468)
    • (2005) Nephrology , vol.10 , Issue.SUPPL. 2
    • Ha, H.1    Lee, H.B.2
  • 57
    • 0029846572 scopus 로고    scopus 로고
    • Involvement of superoxide and myeloperoxidase in oxygendependent killing of Staphylococcus aureus by neutrophils
    • Hampton MB, Kettle AJ, and Winterbourn CC. Involvement of superoxide and myeloperoxidase in oxygendependent killing of Staphylococcus aureus by neutrophils. Infect Immun 64: 3512-3517, 1996.
    • (1996) Infect Immun , vol.64 , pp. 3512-3517
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 58
    • 0030865646 scopus 로고    scopus 로고
    • Dual regulation of caspase activity by hydrogen peroxide: Implications for apoptosis
    • Hampton MB and Orrenius S. Dual regulation of caspase activity by hydrogen peroxide: implications for apoptosis. FEBS Lett 414: 552-556, 1997.
    • (1997) FEBS Lett , vol.414 , pp. 552-556
    • Hampton, M.B.1    Orrenius, S.2
  • 60
    • 0032540225 scopus 로고    scopus 로고
    • Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47(phox) on serine 303 or 304
    • Inanami O, Johnson JL, McAdara JK, El Benna J, Faust LRP, Newburger PE, and Babior BM, Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47(phox) on serine 303 or 304. J Biol Chem 273: 9539-9543, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 9539-9543
    • Inanami, O.1    Johnson, J.L.2    McAdara, J.K.3    El Benna, J.4    Lrp, F.5    Newburger, P.E.6    Babior, B.M.7
  • 61
    • 0000725406 scopus 로고
    • Biochemical aspects of phagocytosis
    • Iyer GY, Islam MF, and Quastel JH. Biochemical aspects of phagocytosis. Nature 192: 535-542, 1961.
    • (1961) Nature , vol.192 , pp. 535-542
    • Iyer, G.Y.1    Islam, M.F.2    Quastel, J.H.3
  • 62
    • 0027964491 scopus 로고
    • Evidence for a readily dissociable complex of p47phox and p67phox in cytosol of unstimulated human neutrophils
    • Iyer SS, Pearson DW, Nauseef WM, and Clark RA. Evidence for a readily dissociable complex of p47phox and p67phox in cytosol of unstimulated human neutrophils. J Biol Chem 269: 22405-22411, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 22405-22411
    • Iyer, S.S.1    Pearson, D.W.2    Nauseef, W.M.3    Clark, R.A.4
  • 63
    • 33847697219 scopus 로고    scopus 로고
    • Novel mechanism of activation of NADPH oxidase 5: Calcium sensitization via phosphorylation
    • Jagnandan D, Church JE, Banfi B, Stuehr DJ, Marrero MB, and Fulton DJR. Novel mechanism of activation of NADPH oxidase 5: calcium sensitization via phosphorylation. J Biol Chem 282: 6494-6507, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 6494-6507
    • Jagnandan, D.1    Church, J.E.2    Banfi, B.3    Stuehr, D.J.4    Marrero, M.B.5    Fulton, D.J.R.6
  • 64
    • 0037157177 scopus 로고    scopus 로고
    • Hydrogen peroxide activates IkappaB kinases through phosphorylation of serine residues in the activation loops
    • Kamata H, Manabe T, Oka S, Kamata K, and Hirata H. Hydrogen peroxide activates IkappaB kinases through phosphorylation of serine residues in the activation loops. FEBS Lett 519: 231-237, 2002.
    • (2002) FEBS Lett , vol.519 , pp. 231-237
    • Kamata, H.1    Manabe, T.2    Oka, S.3    Kamata, K.4    Hirata, H.5
  • 67
    • 45149112512 scopus 로고    scopus 로고
    • Identification of a conserved Rac-binding site on NADPH oxidases supports a direct GTPase regulatory mechanism
    • Kao YY, Gianni D, Bohl B, Taylor RM, and Bokoch GM. Identification of a conserved Rac-binding site on NADPH oxidases supports a direct GTPase regulatory mechanism. J Biol Chem 283: 12736-12746, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 12736-12746
    • Kao, Y.Y.1    Gianni, D.2    Bohl, B.3    Taylor, R.M.4    Bokoch, G.M.5
  • 68
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogenactivated protein kinases
    • Karin M. The regulation of AP-1 activity by mitogenactivated protein kinases. J Biol Chem 270: 16483-16486, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 69
    • 0037134506 scopus 로고    scopus 로고
    • NADPH oxidase is involved in prostaglandin F2alpha-induced hypertrophy of vascular smooth muscle cells: Induction of NOX1 by PGF2alpha
    • Katsuyama M, Fan C, and Yabe-Nishimura C. NADPH oxidase is involved in prostaglandin F2alpha-induced hypertrophy of vascular smooth muscle cells: induction of NOX1 by PGF2alpha. J Biol Chem 277: 13438-13442, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 13438-13442
    • Katsuyama, M.1    Fan, C.2    Yabe-Nishimura, C.3
  • 70
    • 24744468043 scopus 로고    scopus 로고
    • Point mutations in the proline-rich region of p22(phox) are dominant inhibitors of Nox1-and Nox2-dependent reactive oxygen generation
    • Kawahara T, Ritsick D, Cheng GJ, and Lambeth JD. Point mutations in the proline-rich region of p22(phox) are dominant inhibitors of Nox1-and Nox2-dependent reactive oxygen generation. J Biol Chem 280: 31859-31869, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 31859-31869
    • Kawahara, T.1    Ritsick, D.2    Cheng, G.J.3    Lambeth, J.D.4
  • 71
    • 34547697113 scopus 로고    scopus 로고
    • Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox=Duox) family of enzymes
    • Kawahara T, Quinn MT, and Lambeth JD. Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox=Duox) family of enzymes. BMC Evol Biol 7: 104, 2007.
    • (2007) BMC Evol Biol , vol.7 , pp. 104
    • Kawahara, T.1    Quinn, M.T.2    Lambeth, J.D.3
  • 72
    • 0029029066 scopus 로고
    • Arachidonic-acid and free fatty-acids as 2nd-messengers and the role of proteinkinase-C
    • Khan WA, Blob E, and Hannun YA. Arachidonic-acid and free fatty-acids as 2nd-messengers and the role of proteinkinase-C. Cell Signal 7: 171-184, 1995.
    • (1995) Cell Signal , vol.7 , pp. 171-184
    • Khan, W.A.1    Blob, E.2    Hannun, Y.A.3
  • 73
    • 36849030223 scopus 로고    scopus 로고
    • Regulation of Nox1 activity via protein kinase Amediated phosphorylation of NoxA1 and 14-3-3 binding
    • Kim JS, Diebold BA, Babior BM, Knaus UG, and Bokoch UG. Regulation of Nox1 activity via protein kinase Amediated phosphorylation of NoxA1 and 14-3-3 binding. J Biol Chem 282: 34787-34800, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 34787-34800
    • Kim, J.S.1    Diebold, B.A.2    Babior, B.M.3    Knaus, U.G.4    Bokoch, U.G.5
  • 75
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff SJ. Myeloperoxidase: friend and foe. J Leukoc Biol 77: 598-625, 2005.
    • (2005) J Leukoc Biol , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 77
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles HJ, Raval RR, Harris AL, and Ratcliffe PJ. Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res 63: 1764-1768, 2003.
    • (2003) Cancer Res , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 78
    • 0033609785 scopus 로고    scopus 로고
    • Tetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase
    • Koga H, Terasawa H, Nunoi H, Takeshige K, Inagaki F, and Sumimoto H. Tetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase. J Biol Chem 274: 25051-25060, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 25051-25060
    • Koga, H.1    Terasawa, H.2    Nunoi, H.3    Takeshige, K.4    Inagaki, F.5    Sumimoto, H.6
  • 79
    • 0029828538 scopus 로고    scopus 로고
    • The cytosolic component p47(phox) is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production
    • Koshkin V, Lotan O, and Pick E. The cytosolic component p47(phox) is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production. J Biol Chem 271: 30326-30329, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 30326-30329
    • Koshkin, V.1    Lotan, O.2    Pick, E.3
  • 80
    • 0032911057 scopus 로고    scopus 로고
    • The diversity of the lipoxygenase family: Many sequence data but little information on biological significance
    • Kuhn H and Thiele BJ. The diversity of the lipoxygenase family: many sequence data but little information on biological significance. FEBS Lett 449: 7-11, 1999.
    • (1999) FEBS Lett , vol.449 , pp. 7-11
    • Kuhn, H.1    Thiele, B.J.2
  • 83
    • 56349142515 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha activates transcription of the NADPH oxidase organizer 1 (NOXO1) gene and upregulates superoxide production in colon epithelial cells
    • Kuwano Y, Tominaga K, Kawahara T, Sasaki H, Takeo K, Nishida K, Masuda K, Kawai T, Teshima-Kondo S, and Rokutan K. Tumor necrosis factor alpha activates transcription of the NADPH oxidase organizer 1 (NOXO1) gene and upregulates superoxide production in colon epithelial cells. Free Radic Biol Med 45: 1642-1652, 2008.
    • (2008) Free Radic Biol Med , vol.45 , pp. 1642-1652
    • Kuwano, Y.1    Tominaga, K.2    Kawahara, T.3    Sasaki, H.4    Takeo, K.5    Nishida, K.6    Masuda, K.7    Kawai, T.8    Teshima-Kondo, S.9    Rokutan, K.10
  • 84
    • 34250888056 scopus 로고    scopus 로고
    • Regulation of Nox and Duox enzymatic activity and expression
    • Lambeth JD, Kawahara T, and Diebold B. Regulation of Nox and Duox enzymatic activity and expression. Free Radic Biol Med 43: 319-331, 2007.
    • (2007) Free Radic Biol Med , vol.43 , pp. 319-331
    • Lambeth, J.D.1    Kawahara, T.2    Diebold, B.3
  • 87
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee SR, Kwon KS, Kim SR, and Rhee SG. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273: 15366-15372, 1998.
    • (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
  • 88
    • 20444464441 scopus 로고    scopus 로고
    • Membrane depolarization induces the undulating phosphorylation= dephosphorylation of glycogen synthase kinase 3beta, and this dephosphorylation involves protein phosphatases 2A and 2B in SH-SY5Y human neuroblastoma cells
    • Lee YI, Seo M, Kim Y, Kim SY, Kang UG, Kim YS, and Juhnn YS. Membrane depolarization induces the undulating phosphorylation=dephosphorylation of glycogen synthase kinase 3beta, and this dephosphorylation involves protein phosphatases 2A and 2B in SH-SY5Y human neuroblastoma cells. J Biol Chem 280: 22044-22252, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 22044-22252
    • Lee, Y.I.1    Seo, M.2    Kim, Y.3    Kim, S.Y.4    Kang, U.G.5    Kim, Y.S.6    Juhnn, Y.S.7
  • 89
    • 44449129056 scopus 로고    scopus 로고
    • Inorganic arsenic activates reduced NADPH oxidase in human primary macrophages through a Rho kinase=p38 kinase pathway
    • Lemarie A, Bourdonnay E, Morzadec C, Fardel O, and Lernhet L. Inorganic arsenic activates reduced NADPH oxidase in human primary macrophages through a Rho kinase=p38 kinase pathway. J Immunol 180: 6010-6017, 2008.
    • (2008) J Immunol , vol.180 , pp. 6010-6017
    • Lemarie, A.1    Bourdonnay, E.2    Morzadec, C.3    Fardel, O.4    Lernhet, L.5
  • 90
    • 0027973549 scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Binding of Src homology-3 domains to proline-rich targets
    • Leto TL, Adams AG, and Demendez I. Assembly of the phagocyte NADPH oxidase: binding of Src homology-3 domains to proline-rich targets. Proc Natl Acad Sci U S A 91: 10650-10654, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10650-10654
    • Leto, T.L.1    Adams, A.G.2    Demendez, I.3
  • 91
    • 34547813240 scopus 로고    scopus 로고
    • Nox2 regulates endothelial cell cycle arrest and apoptosis via p21cip1 and p53
    • Li JM, Fan LM, George VT, and Brooks G. Nox2 regulates endothelial cell cycle arrest and apoptosis via p21cip1 and p53. Free Radic Biol Med 43: 976-986, 2007.
    • (2007) Free Radic Biol Med , vol.43 , pp. 976-986
    • Li, J.M.1    Fan, L.M.2    George, V.T.3    Brooks, G.4
  • 92
    • 0035914325 scopus 로고    scopus 로고
    • Transcriptional regulation of the p67phox gene: Role of AP-1 in concert with myeloid-specific transcription factors
    • Li SL, Valente AJ, Wang L, Gamez MJ, and Clark RA. Transcriptional regulation of the p67phox gene: role of AP-1 in concert with myeloid-specific transcription factors. J Biol Chem 276: 39368-39378, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 39368-39378
    • Li, S.L.1    Valente, A.J.2    Wang, L.3    Gamez, M.J.4    Clark, R.A.5
  • 94
    • 14944361889 scopus 로고    scopus 로고
    • NADPH oxidase produces reactive oxygen species and maintains survival of rat astrocytes
    • Liu Q, Kang JH, and Zheng RL. NADPH oxidase produces reactive oxygen species and maintains survival of rat astrocytes. Cell Biochem Funct 23: 93-100, 2005.
    • (2005) Cell Biochem Funct , vol.23 , pp. 93-100
    • Liu, Q.1    Kang, J.H.2    Zheng, R.L.3
  • 95
    • 0024376120 scopus 로고
    • Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease
    • Lomax KJ, Leto TL, Nunoi H, Gallin JI, and Malech HL. Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease. Science 245: 409-412, 1989.
    • (1989) Science , vol.245 , pp. 409-412
    • Lomax, K.J.1    Leto, T.L.2    Nunoi, H.3    Gallin, J.I.4    Malech, H.L.5
  • 97
    • 0035877633 scopus 로고    scopus 로고
    • Insulinstimulated hydrogen peroxide reversibly inhibits proteintyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • Mahadev K, Zilbering A, Zhu L, and Goldstein BJ. Insulinstimulated hydrogen peroxide reversibly inhibits proteintyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J Biol Chem 276: 21938-21942, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 99
    • 26244444476 scopus 로고    scopus 로고
    • Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
    • Martyn KD, Frederick LM, von Loehneysen K, Dinauer MC, and Knaus UG. Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell Signal 18: 69-82, 2006.
    • (2006) Cell Signal , vol.18 , pp. 69-82
    • Martyn, K.D.1    Frederick, L.M.2    Von Loehneysen, K.3    Dinauer, M.C.4    Knaus, U.G.5
  • 100
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng TC, Fukada T, and Tonks NK. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol Cell 9: 387-399, 2002.
    • (2002) Mol Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 102
    • 33845451723 scopus 로고    scopus 로고
    • ROS-induced histone modifications and their role in cell survival and cell death
    • Monks TJ, Xie R, Tikoo K, and Lau SS. ROS-induced histone modifications and their role in cell survival and cell death. Drug Metab Rev 38: 755-767, 2006.
    • (2006) Drug Metab Rev , vol.38 , pp. 755-767
    • Monks, T.J.1    Xie, R.2    Tikoo, K.3    Lau, S.S.4
  • 103
    • 34447122529 scopus 로고    scopus 로고
    • Activation of NADPH oxidase by transforming growth factorbeta in hepatocytes mediates up-regulation of epidermal growth factor receptor ligands through a nuclear factorkappa B-dependent mechanism
    • Murillo MM, Carmona-Cuenca I, Del Castillo G, Ortiz C, Roncero C, Sanchez A, Fernandez M, and Fabregat I. Activation of NADPH oxidase by transforming growth factorbeta in hepatocytes mediates up-regulation of epidermal growth factor receptor ligands through a nuclear factorkappa B-dependent mechanism. Biochem J 405: 251-259, 2007.
    • (2007) Biochem J , vol.405 , pp. 251-259
    • Murillo, M.M.1    Carmona-Cuenca, I.2    Del Castillo, G.3    Ortiz, C.4    Roncero, C.5    Sanchez, A.6    Fernandez, M.7    Fabregat, I.8
  • 104
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • Murry CE, Jennings RB, and Reimer KA. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 74: 1124-1136, 1986.
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 105
    • 0023440635 scopus 로고
    • Activation by Atp of calcium-dependent NADPH-oxidase generating hydrogenperoxide in thyroid plasma-membranes
    • Nakamura Y, Ogihara S, and Ohtaki S. Activation by Atp of calcium-dependent NADPH-oxidase generating hydrogenperoxide in thyroid plasma-membranes. J Biochem (Tokyo) 102: 1121-1132, 1987.
    • (1987) J Biochem (Tokyo) , vol.102 , pp. 1121-1132
    • Nakamura, Y.1    Ogihara, S.2    Ohtaki, S.3
  • 106
    • 0025923304 scopus 로고
    • Mechanism of H2O2 production in porcine thyroid-cells: Evidence for intermediary formation of superoxide anion by NADPH-dependent H2O2-generating machinery
    • Nakamura Y, Makino R, Tanaka T, Ishimura I, and Ohtaki S, Mechanism of H2O2 production in porcine thyroid-cells: evidence for intermediary formation of superoxide anion by NADPH-dependent H2O2-generating machinery. Biochemistry 30: 4880-4886, 1991.
    • (1991) Biochemistry , vol.30 , pp. 4880-4886
    • Nakamura, Y.1    Makino, R.2    Tanaka, T.3    Ishimura, I.4    Ohtaki, S.5
  • 107
    • 0345304900 scopus 로고    scopus 로고
    • MEK kinase 1 mediates the antiapoptotic effect of the Bcr-Abl oncogene through NFkappaB activation
    • Nawata R, Yujiri T, Nakamura Y, Ariyoshi K, Takahashi T, Sato Y, Oka Y, and Tanizawa Y. MEK kinase 1 mediates the antiapoptotic effect of the Bcr-Abl oncogene through NFkappaB activation. Oncogene 22: 7774-7780, 2003.
    • (2003) Oncogene , vol.22 , pp. 7774-7780
    • Nawata, R.1    Yujiri, T.2    Nakamura, Y.3    Ariyoshi, K.4    Takahashi, T.5    Sato, Y.6    Oka, Y.7    Tanizawa, Y.8
  • 108
    • 0028961293 scopus 로고
    • Rho Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD and Hall A. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81: 53-62, 1995.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 109
    • 53449086160 scopus 로고    scopus 로고
    • A novel antioxidant function for the tumor-suppressor gene p53 in the retinal ganglion cell
    • O'Connor JC, Wallace DM, O'Brien CJ, and Cotter TJ. A novel antioxidant function for the tumor-suppressor gene p53 in the retinal ganglion cell. Invest Ophthalmol Vis Sci 49: 4237-4244, 2008.
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 4237-4244
    • O'Connor, J.C.1    Wallace, D.M.2    O'Brien, C.J.3    Cotter, T.J.4
  • 110
    • 0042163035 scopus 로고    scopus 로고
    • Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide: Potential regulation of eIF2 alpha phosphorylation in differentiated PC12 cells
    • O'Loghlen A, Perez-Morgado MI, Salinas M, and Martin ME. Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide: potential regulation of eIF2 alpha phosphorylation in differentiated PC12 cells. Arch Biochem Biophys 417: 194-202, 2003.
    • (2003) Arch Biochem Biophys , vol.417 , pp. 194-202
    • O'Loghlen, A.1    Perez-Morgado, M.I.2    Salinas, M.3    Martin, M.E.4
  • 112
    • 4644350365 scopus 로고    scopus 로고
    • Cutting edge: Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharideinduced production of reactive oxygen species and activation of NF-kappa B
    • Park HS, Jung HY, Park EY, Kim J, Lee WJ, and Bae YS. Cutting edge: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharideinduced production of reactive oxygen species and activation of NF-kappa B. J Immunol 173: 3589-3593, 2004.
    • (2004) J Immunol , vol.173 , pp. 3589-3593
    • Park, H.S.1    Jung, H.Y.2    Park, E.Y.3    Kim, J.4    Lee, W.J.5    Bae, Y.S.6
  • 113
    • 2942628119 scopus 로고    scopus 로고
    • Sequential activation of phosphatidylinositol 3-kinase, beta Pix, Rac1, and Nox1 in growth factor-induced production of H2O2
    • Park HS, Lee SH, Park D, Lee JS, Ryu HS, Lee WJ, Rhee SG, and Bae YS. Sequential activation of phosphatidylinositol 3-kinase, beta Pix, Rac1, and Nox1 in growth factor-induced production of H2O2. Mol Cell Biol 24: 4384-4394, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 4384-4394
    • Park, H.S.1    Lee, S.H.2    Park, D.3    Lee, J.S.4    Ryu, H.S.5    Lee, W.J.6    Rhee, S.G.7    Bae, Y.S.8
  • 114
    • 28844479984 scopus 로고    scopus 로고
    • Molecular interaction of NADPH oxidase 1 with beta Pix and Nox organizer 1
    • Park HS, Park D, and Bae YS. Molecular interaction of NADPH oxidase 1 with beta Pix and Nox organizer 1. Biochem Biophys Res Commun 339: 985-990, 2006.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 985-990
    • Park, H.S.1    Park, D.2    Bae, Y.S.3
  • 115
    • 0030963249 scopus 로고    scopus 로고
    • Activation of the leukocyte NADPH oxidase subunit p47(phox) by protein kinase C: A phosphorylation-dependent change in the conformation of the C-terminal end of p47(phox)
    • Park JW and Babior BM. Activation of the leukocyte NADPH oxidase subunit p47(phox) by protein kinase C: a phosphorylation-dependent change in the conformation of the C-terminal end of p47(phox). Biochemistry 36: 11292-11292, 1997.
    • (1997) Biochemistry , vol.36 , pp. 11292-11292
    • Park, J.W.1    Babior, B.M.2
  • 117
    • 45949086327 scopus 로고    scopus 로고
    • The molecular sources of reactive oxygen species in hypertension
    • Puddu P, Puddu GM, Cravero E, Rosati M, and Muscari A. The molecular sources of reactive oxygen species in hypertension. Blood Press 17: 70-77, 2008.
    • (2008) Blood Press , vol.17 , pp. 70-77
    • Puddu, P.1    Puddu, G.M.2    Cravero, E.3    Rosati, M.4    Muscari, A.5
  • 118
    • 29744453873 scopus 로고    scopus 로고
    • Microglial NADPH oxidase mediates leucine enkephalin dopaminergic neuroprotection
    • DOI 10.1196/annals.1344.009
    • Qin L, Liu Y, Qian X, Hong JS, and Block ML. Microglial NADPH oxidase mediates leucine enkephalin dopaminergic neuroprotection. Ann N Y Acad Sci 1053: 107-120, 2005. (Pubitemid 43031088)
    • (2005) Annals of the New York Academy of Sciences , vol.1053 , pp. 107-120
    • Qin, L.1    Liu, Y.2    Qian, X.3    Hong, J.-S.4    Block, M.L.5
  • 119
    • 2542538216 scopus 로고    scopus 로고
    • Complex regulation of signal transducers and activators of transcription 3 activation in normal and malignant keratinocytes
    • Quadros MR, Peruzzi F, Kari C, and Rodeck U. Complex regulation of signal transducers and activators of transcription 3 activation in normal and malignant keratinocytes. Cancer Res 64: 3934-3939, 2004.
    • (2004) Cancer Res , vol.64 , pp. 3934-3939
    • Quadros, M.R.1    Peruzzi, F.2    Kari, C.3    Rodeck, U.4
  • 120
    • 0036066957 scopus 로고    scopus 로고
    • Oxidative stress and TNF-alpha induce histone acetylation and NF-kappaB=AP-1 activation in alveolar epithelial cells: Potential mechanism in gene transcription in lung inflammation
    • 239-248
    • Rahman I, Gilmour PS, Jimenez LA, and MacNee W. Oxidative stress and TNF-alpha induce histone acetylation and NF-kappaB=AP-1 activation in alveolar epithelial cells: potential mechanism in gene transcription in lung inflammation. Mol Cell Biochem 234-235: 239-248, 2002.
    • (2002) Mol Cell Biochem , pp. 234-235
    • Rahman, I.1    Gilmour, P.S.2    Jimenez, L.A.3    MacNee, W.4
  • 121
    • 4143070452 scopus 로고    scopus 로고
    • Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression
    • Rahman I, Marwick J, and Kirkham P. Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression. Biochem Pharmacol 68: 1255-1267, 2004.
    • (2004) Biochem Pharmacol , vol.68 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 122
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation
    • Rao RK and Clayton LW. Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation. Biochem Biophys Res Commun 293: 610-616, 2002.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 123
    • 0033572857 scopus 로고    scopus 로고
    • Direct interaction between p47(phox) and protein kinase C: Evidence for targeting of protein kinase C by p47(phox) in neutrophils
    • Reeves EP, Dekker LV, Forbes LV, Wientjes FB, Grogan A, Pappin DJC, and Segal AW. Direct interaction between p47(phox) and protein kinase C: evidence for targeting of protein kinase C by p47(phox) in neutrophils. Biochem J 344: 859-866, 1999.
    • (1999) Biochem J , vol.344 , pp. 859-866
    • Reeves, E.P.1    Dekker, L.V.2    Forbes, L.V.3    Wientjes, F.B.4    Grogan, A.5    Djc, P.6    Segal, A.W.7
  • 124
    • 0033579491 scopus 로고    scopus 로고
    • A phosphatidic acid-activated protein kinase and conventional protein kinase C isoforms phosphorylate p22(phox) NADPH oxidase component
    • Regier DS, Waite KA, Wallin R, and McPhail LC. A phosphatidic acid-activated protein kinase and conventional protein kinase C isoforms phosphorylate p22(phox) NADPH oxidase component. J Biol Chem 274: 36601-36608, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 36601-36608
    • Regier, D.S.1    Waite, K.A.2    Wallin, R.3    McPhail, L.C.4
  • 125
    • 0034664253 scopus 로고    scopus 로고
    • Phosphorylation of p22phox is mediated by phospholipase D-dependent and -independent mechanisms: Correlation of NADPH oxidase activity and p22phox phosphorylation
    • Regier DS, Greene DG, Sergeant S, Jesaitis AJ, and McPhail LC. Phosphorylation of p22phox is mediated by phospholipase D-dependent and -independent mechanisms: correlation of NADPH oxidase activity and p22phox phosphorylation. J Biol Chem 275: 28406-28412, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 28406-28412
    • Regier, D.S.1    Greene, D.G.2    Sergeant, S.3    Jesaitis, A.J.4    McPhail, L.C.5
  • 126
    • 33745631769 scopus 로고    scopus 로고
    • H2O2, a necessary evil for cell signaling
    • Rhee SG. H2O2, a necessary evil for cell signaling. Science 312: 1882-1883, 2006.
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 129
    • 44449162944 scopus 로고    scopus 로고
    • The Rac activator Tiam1 prevents keratinocyte apoptosis by controlling ROS-mediated ERK phosphorylation
    • Rygiel TP, Mertens AE, Strumane K, van der Kammen R, and Collard JG. The Rac activator Tiam1 prevents keratinocyte apoptosis by controlling ROS-mediated ERK phosphorylation. J Cell Sci 121: 1183-1192, 2008.
    • (2008) J Cell Sci , vol.121 , pp. 1183-1192
    • Rygiel, T.P.1    Mertens, A.E.2    Strumane, K.3    Van Der Kammen, R.4    Collard, J.G.5
  • 131
    • 17644371347 scopus 로고    scopus 로고
    • Functions and mechanisms of redox regulation of cysteine-based phosphatases
    • Salmeen A and Barford D. Functions and mechanisms of redox regulation of cysteine-based phosphatases. Antioxid Redox Signal 7: 560-577, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 560-577
    • Salmeen, A.1    Barford, D.2
  • 132
    • 63049123598 scopus 로고    scopus 로고
    • Insulin-induced NADPH oxidase activation promotes proliferation and matrix metalloproteinase activation in monocytes=macrophages
    • San Jose G, Bidegain J, Robador PA, Diez J, Fortuno A, and Zalba G. Insulin-induced NADPH oxidase activation promotes proliferation and matrix metalloproteinase activation in monocytes=macrophages. Free Radic Biol Med 46: 1058-1067, 2009.
    • (2009) Free Radic Biol Med , vol.46 , pp. 1058-1067
    • San Jose, G.1    Bidegain, J.2    Robador, P.A.3    Diez, J.4    Fortuno, A.5    Zalba, G.6
  • 133
    • 38849083944 scopus 로고    scopus 로고
    • Exercise and tachycardia increase NADPH oxidase and ryanodine receptor-2 activity: Possible robe in cardioprotection
    • Sanchez G, Escobar M, Pedrozo Z, Macho P, Domenech R, Hartel S, Hidalgo C, and Donoso P. Exercise and tachycardia increase NADPH oxidase and ryanodine receptor-2 activity: possible robe in cardioprotection. Cardiovasc Res 77: 380-386, 2008.
    • (2008) Cardiovasc Res , vol.77 , pp. 380-386
    • Sanchez, G.1    Escobar, M.2    Pedrozo, Z.3    MacHo, P.4    Domenech, R.5    Hartel, S.6    Hidalgo, C.7    Donoso, P.8
  • 134
    • 0037036460 scopus 로고    scopus 로고
    • Redox regulation of Cdc25C
    • Savitsky PA and Finkel T. Redox regulation of Cdc25C. J Biol Chem 277: 20535-20540, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 20535-20540
    • Savitsky, P.A.1    Finkel, T.2
  • 137
    • 0038115172 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein (oxLDL) triggers hypoxia-inducible factor-1alpha (HIF-1alpha) accumulation via redox-dependent mechanisms
    • Shatrov VA, Sumbayev VV, Zhou J, and Brune B. Oxidized low-density lipoprotein (oxLDL) triggers hypoxia-inducible factor-1alpha (HIF-1alpha) accumulation via redox-dependent mechanisms. Blood 101: 4847-4849, 2003.
    • (2003) Blood , vol.101 , pp. 4847-4849
    • Shatrov, V.A.1    Sumbayev, V.V.2    Zhou, J.3    Brune, B.4
  • 140
    • 0032743539 scopus 로고    scopus 로고
    • The biology of 5-lipoxygenase: Function, structure, and regulatory mechanisms
    • Silverman ES and Drazen JM. The biology of 5-lipoxygenase: function, structure, and regulatory mechanisms. Proc Assoc Am Physicians 111: 525-536, 1999.
    • (1999) Proc Assoc Am Physicians , vol.111 , pp. 525-536
    • Silverman, E.S.1    Drazen, J.M.2
  • 141
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre J, Buckingham JA, Roebuck SJ, and Brand MD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277: 44784-44790, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 142
    • 0036485664 scopus 로고    scopus 로고
    • Generation of oxygen free radicals in thyroid cells and inhibition of thyroid peroxidase
    • Sugawara M, Sugawara Y, Wen K, and Giulivi C. Generation of oxygen free radicals in thyroid cells and inhibition of thyroid peroxidase. Exp Biol Med 227: 141-146, 2002.
    • (2002) Exp Biol Med , vol.227 , pp. 141-146
    • Sugawara, M.1    Sugawara, Y.2    Wen, K.3    Giulivi, C.4
  • 144
    • 34548125720 scopus 로고    scopus 로고
    • Antiinflammatory and side effects of cyclooxygenase inhibitors
    • Suleyman, H, Demircan B, and Karagoz Y. Antiinflammatory and side effects of cyclooxygenase inhibitors. Pharmacol Rep 59: 247-258, 2007.
    • (2007) Pharmacol Rep , vol.59 , pp. 247-258
    • Suleyman, H.1    Demircan, B.2    Karagoz, Y.3
  • 145
    • 27544443327 scopus 로고    scopus 로고
    • Molecular composition and regulation of the Nox family NAD(P)H oxidases
    • Sumimoto H, Miyano K, and Takeya R. Molecular composition and regulation of the Nox family NAD(P)H oxidases. Biochem Biophys Res Commun 338: 677-686, 2005.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 677-686
    • Sumimoto, H.1    Miyano, K.2    Takeya, R.3
  • 146
    • 44949106317 scopus 로고    scopus 로고
    • Structure, regulation and evolution of Noxfamily NADPH oxidases that produce reactive oxygen species
    • Sumimoto H. Structure, regulation and evolution of Noxfamily NADPH oxidases that produce reactive oxygen species. FEBS J 275: 3249-3277, 2008.
    • (2008) FEBS J , vol.275 , pp. 3249-3277
    • Sumimoto, H.1
  • 147
    • 0029760957 scopus 로고    scopus 로고
    • Redox regulation of transcriptional activators
    • Sun Y and Oberley LW. Redox regulation of transcriptional activators. Free Radic Biol Med 21: 335-348, 1996.
    • (1996) Free Radic Biol Med , vol.21 , pp. 335-348
    • Sun, Y.1    Oberley, L.W.2
  • 148
    • 0345062252 scopus 로고    scopus 로고
    • Possible role of Rac-GTPase-activating protein in the termination of superoxide production in phagocytic cells
    • Szaszi K, Korda A, Wolfl J, Paclet MH, Morel F, and Ligeti E. Possible role of Rac-GTPase-activating protein in the termination of superoxide production in phagocytic cells. Free Radic Biol Med 27: 764-772, 1999.
    • (1999) Free Radic Biol Med , vol.27 , pp. 764-772
    • Szaszi, K.1    Korda, A.2    Wolfl, J.3    Paclet, M.H.4    Morel, F.5    Ligeti, E.6
  • 149
    • 0042991381 scopus 로고    scopus 로고
    • Novel human homologues of p47(phox) and p67(phox) participate in activation of superoxide-producing NADPH oxidases
    • Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, and Sumimoto H. Novel human homologues of p47(phox) and p67(phox) participate in activation of superoxide-producing NADPH oxidases. J Biol Chem 278: 25234-25246, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 25234-25246
    • Takeya, R.1    Ueno, N.2    Kami, K.3    Taura, M.4    Kohjima, M.5    Izaki, T.6    Nunoi, H.7    Sumimoto, H.8
  • 150
    • 0023191301 scopus 로고
    • The X-linked chronic granulomatous disease gene codes for the beta-chain of cytochrome-b-245
    • Teahan C, Rowe P, Parker P, Totty N, and Segal AW. The X-linked chronic granulomatous disease gene codes for the beta-chain of cytochrome-b-245. Nature 327: 720-721, 1987.
    • (1987) Nature , vol.327 , pp. 720-721
    • Teahan, C.1    Rowe, P.2    Parker, P.3    Totty, N.4    Segal, A.W.5
  • 151
    • 33847731516 scopus 로고    scopus 로고
    • NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin
    • Tirone F and Cox JA. NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin. FEBS Lett 581: 1202-1208, 2007.
    • (2007) FEBS Lett , vol.581 , pp. 1202-1208
    • Tirone, F.1    Cox, J.A.2
  • 152
    • 0031596533 scopus 로고    scopus 로고
    • Distinct phospholipases A(2) regulate the release of arachidonic acid for eicosanoid production and superoxide anion generation in neutrophils
    • Tithof PK, Peters-Golden M, and Ganey PE. Distinct phospholipases A(2) regulate the release of arachidonic acid for eicosanoid production and superoxide anion generation in neutrophils. J Immunol 160: 953-960, 1998.
    • (1998) J Immunol , vol.160 , pp. 953-960
    • Tithof, P.K.1    Peters-Golden, M.2    Ganey, P.E.3
  • 153
    • 0025852479 scopus 로고
    • Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro
    • Toledano MB and Leonard WJ. Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro. Proc Natl Acad Sci U S A 88: 4328-4332, 1991.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 4328-4332
    • Toledano, M.B.1    Leonard, W.J.2
  • 154
    • 0012449739 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways in redox signaling
    • Torres M. Mitogen-activated protein kinase pathways in redox signaling. Front Biosci 8: d369-d391, 2003.
    • (2003) Front Biosci , vol.8
    • Torres, M.1
  • 156
    • 20744440943 scopus 로고    scopus 로고
    • The NADPH oxidase Nox3 constitutively produces superoxide in a p22(Phox)-dependent manner
    • Ueno N, Takeya R, Miyano R, Kikuchi H, and Sumimoto H. The NADPH oxidase Nox3 constitutively produces superoxide in a p22(Phox)-dependent manner. J Biol Chem 280: 23328-23339, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 23328-23339
    • Ueno, N.1    Takeya, R.2    Miyano, R.3    Kikuchi, H.4    Sumimoto, H.5
  • 157
    • 33750310510 scopus 로고    scopus 로고
    • Vav proteins in neutrophils are required for Fc gamma R-mediated signaling to Rac GTPases and nicotinamide adenine dinucleotide phosphate oxidase component p40(phox)
    • Utomo A, Cullere X, Glogauer M, Swat W, and Mayadas TN. Vav proteins in neutrophils are required for Fc gamma R-mediated signaling to Rac GTPases and nicotinamide adenine dinucleotide phosphate oxidase component p40(phox). J Immunol 177: 6388-6397, 2006.
    • (2006) J Immunol , vol.177 , pp. 6388-6397
    • Utomo, A.1    Cullere, X.2    Glogauer, M.3    Swat, W.4    Mayadas, T.N.5
  • 158
    • 22744458796 scopus 로고    scopus 로고
    • The antiapoptotic effect of fibroblast growth factor-2 is mediated through nuclear factor-kappaB activation induced via interaction between Akt and IkappaB kinase-beta in breast cancer cells
    • Vandermoere F, El Yazidi-Belkoura I, Adriaenssens E, Lemoine J, and Hondermarck H. The antiapoptotic effect of fibroblast growth factor-2 is mediated through nuclear factor-kappaB activation induced via interaction between Akt and IkappaB kinase-beta in breast cancer cells. Oncogene 24: 5482-5491, 2005.
    • (2005) Oncogene , vol.24 , pp. 5482-5491
    • Vandermoere, F.1    El Yazidi-Belkoura, I.2    Adriaenssens, E.3    Lemoine, J.4    Hondermarck, H.5
  • 159
    • 4544250814 scopus 로고    scopus 로고
    • Reactive oxygen species produced by NAD(P)H oxidase inhibit apoptosis in pancreatic cancer cells
    • Vaquero EC, Edderkaoui M, Pandol SJ, Gukovsky I, and Gukovskaya AS. Reactive oxygen species produced by NAD(P)H oxidase inhibit apoptosis in pancreatic cancer cells. J Biol Chem 279: 34643-34654, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 34643-34654
    • Vaquero, E.C.1    Edderkaoui, M.2    Pandol, S.J.3    Gukovsky, I.4    Gukovskaya, A.S.5
  • 163
    • 0027787417 scopus 로고
    • P40(phox), a 3rd cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains
    • Wientjes FB, Hsuan JJ, Totty NF, and Segal AW. P40(phox), a 3rd cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem J 296: 557-561, 1993.
    • (1993) Biochem J , vol.296 , pp. 557-561
    • Wientjes, F.B.1    Hsuan, J.J.2    Totty, N.F.3    Segal, A.W.4
  • 165
    • 33644967001 scopus 로고    scopus 로고
    • Delineating the mechanism by which selenium deactivates Akt in prostate cancer cells
    • Wu Y, Zu K, Warren MA, Wallace PK, and Ip C. Delineating the mechanism by which selenium deactivates Akt in prostate cancer cells. Mol Cancer Ther 5: 246-252, 2006.
    • (2006) Mol Cancer Ther , vol.5 , pp. 246-252
    • Wu, Y.1    Zu, K.2    Warren, M.A.3    Wallace, P.K.4    Ip, C.5
  • 166
    • 33846202517 scopus 로고    scopus 로고
    • C-Jun downregulation by HDAC3-dependent transcriptional repression promotes osmotic stress-induced cell apoptosis
    • Xia Y, Wang J, Liu TL, Yung WK, Hunter T, and Lu Z. c-Jun downregulation by HDAC3-dependent transcriptional repression promotes osmotic stress-induced cell apoptosis. Mol Cell 25: 219-232, 2007.
    • (2007) Mol Cell , vol.25 , pp. 219-232
    • Xia, Y.1    Wang, J.2    Liu, T.L.3    Yung, W.K.4    Hunter, T.5    Lu, Z.6
  • 167
    • 33846130923 scopus 로고    scopus 로고
    • MEKK1 mediates the ubiquitination and degradation of c-Jun in response to osmotic stress
    • Xia Y, Wang J, Xu S, Johnson GL, Hunter T, and Lu Z. MEKK1 mediates the ubiquitination and degradation of c-Jun in response to osmotic stress. Mol Cell Biol 27: 510-517, 2007.
    • (2007) Mol Cell Biol , vol.27 , pp. 510-517
    • Xia, Y.1    Wang, J.2    Xu, S.3    Johnson, G.L.4    Hunter, T.5    Lu, Z.6
  • 168
    • 50949103810 scopus 로고    scopus 로고
    • Expression of NADPH oxidases and enhanced H(2)O(2)-generating activity in human coronary artery endothelial cells upon induction with tumor necrosis factor-alpha
    • Yoshida LS and Tsunawaki S. Expression of NADPH oxidases and enhanced H(2)O(2)-generating activity in human coronary artery endothelial cells upon induction with tumor necrosis factor-alpha. Int Immunopharmacol 8: 1377-1385, 2008.
    • (2008) Int Immunopharmacol , vol.8 , pp. 1377-1385
    • Yoshida, L.S.1    Tsunawaki, S.2
  • 169
    • 34548501984 scopus 로고    scopus 로고
    • Diphenyleneiodonium suppresses apoptosis in cerulein-stimulated pancreatic acinar cells
    • Yu JH, Kim KH, Kim DG, and Kim H. Diphenyleneiodonium suppresses apoptosis in cerulein-stimulated pancreatic acinar cells. Int J Biochem Cell Biol 39: 2063-2075, 2007.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 2063-2075
    • Yu, J.H.1    Kim, K.H.2    Kim, D.G.3    Kim, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.