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Volumn 72, Issue 11, 2006, Pages 1493-1505

NF-κB activation by reactive oxygen species: Fifteen years later

Author keywords

Cellular signalling; Cytokines; LPS; NF B; Reactive oxygen species

Indexed keywords

CYTOKINE; EPIGALLOCATECHIN GALLATE; FAS ANTIGEN; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; LIPOPOLYSACCHARIDE; LYMPHOCYTE ANTIGEN RECEPTOR; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; TOLL LIKE RECEPTOR; TROLOX C; TUMOR NECROSIS FACTOR ALPHA;

EID: 33750523632     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.04.011     Document Type: Article
Times cited : (1323)

References (137)
  • 1
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signalling
    • Adler V., Yin Z., Tew K.D., and Ronai Z. Role of redox potential and reactive oxygen species in stress signalling. Oncogene 18 45 (1999) 6104-6111
    • (1999) Oncogene , vol.18 , Issue.45 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 2
    • 0036829062 scopus 로고    scopus 로고
    • Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors
    • Haddad J.J. Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors. Cell Signal 14 11 (2002) 879-897
    • (2002) Cell Signal , vol.14 , Issue.11 , pp. 879-897
    • Haddad, J.J.1
  • 3
    • 1842844732 scopus 로고    scopus 로고
    • Radiation-induced oxidative DNA damage, 8-oxoguanine, in human peripheral T cells
    • Ogawa Y., Kobayashi T., Nishioka A., Kariya S., Hamasato S., Seguchi H., et al. Radiation-induced oxidative DNA damage, 8-oxoguanine, in human peripheral T cells. Int J Mol Med 11 1 (2003) 27-32
    • (2003) Int J Mol Med , vol.11 , Issue.1 , pp. 27-32
    • Ogawa, Y.1    Kobayashi, T.2    Nishioka, A.3    Kariya, S.4    Hamasato, S.5    Seguchi, H.6
  • 4
    • 2342594384 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species in relation to aging and pathology
    • Genova M.L., Pich M.M., Bernacchia A., Bianchi C., Biondi A., Bovina C., et al. The mitochondrial production of reactive oxygen species in relation to aging and pathology. Ann NY Acad Sci 1011 (2004) 86-100
    • (2004) Ann NY Acad Sci , vol.1011 , pp. 86-100
    • Genova, M.L.1    Pich, M.M.2    Bernacchia, A.3    Bianchi, C.4    Biondi, A.5    Bovina, C.6
  • 5
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: an update
    • Babior B.M. NADPH oxidase: an update. Blood 93 5 (1999) 1464-1476
    • (1999) Blood , vol.93 , Issue.5 , pp. 1464-1476
    • Babior, B.M.1
  • 6
    • 0033578648 scopus 로고    scopus 로고
    • Dual role of reactive oxygen species in vascular growth
    • Griendling K.K., and Harrison D.G. Dual role of reactive oxygen species in vascular growth. Circ Res 85 6 (1999) 562-563
    • (1999) Circ Res , vol.85 , Issue.6 , pp. 562-563
    • Griendling, K.K.1    Harrison, D.G.2
  • 7
  • 8
    • 0032911057 scopus 로고    scopus 로고
    • The diversity of the lipoxygenase family. Many sequence data but little information on biological significance
    • Kuhn H., and Thiele B.J. The diversity of the lipoxygenase family. Many sequence data but little information on biological significance. FEBS Lett 449 1 (1999) 7-11
    • (1999) FEBS Lett , vol.449 , Issue.1 , pp. 7-11
    • Kuhn, H.1    Thiele, B.J.2
  • 9
    • 0019195393 scopus 로고
    • Prostaglandins, arachidonic acid, and inflammation
    • Kuehl Jr. F.A., and Egan R.W. Prostaglandins, arachidonic acid, and inflammation. Science 210 4473 (1980) 978-984
    • (1980) Science , vol.210 , Issue.4473 , pp. 978-984
    • Kuehl Jr., F.A.1    Egan, R.W.2
  • 10
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing
    • Hampton M.B., Kettle A.J., and Winterbourn C.C. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92 9 (1998) 3007-3017
    • (1998) Blood , vol.92 , Issue.9 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 11
    • 0036363622 scopus 로고    scopus 로고
    • Involvement of oxidative stress in NF-kappaB activation in endothelial cells treated by photodynamic therapy
    • Volanti C., Matroule J.Y., and Piette J. Involvement of oxidative stress in NF-kappaB activation in endothelial cells treated by photodynamic therapy. Photochem Photobiol 75 1 (2002) 36-45
    • (2002) Photochem Photobiol , vol.75 , Issue.1 , pp. 36-45
    • Volanti, C.1    Matroule, J.Y.2    Piette, J.3
  • 12
    • 0033086310 scopus 로고    scopus 로고
    • Redox-mediated gene therapies for environmental injury: approaches and concepts
    • Engelhardt J.F. Redox-mediated gene therapies for environmental injury: approaches and concepts. Antioxid Redox Signal 1 1 (1999) 5-27
    • (1999) Antioxid Redox Signal , vol.1 , Issue.1 , pp. 5-27
    • Engelhardt, J.F.1
  • 15
    • 0031036917 scopus 로고    scopus 로고
    • An essential role for free radicals and derived species in signal transduction
    • Lander H.M. An essential role for free radicals and derived species in signal transduction. FASEB J 11 2 (1997) 118-124
    • (1997) FASEB J , vol.11 , Issue.2 , pp. 118-124
    • Lander, H.M.1
  • 16
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: revisiting PTPs and the control of cell signalling
    • Tonks N.K. Redox redux: revisiting PTPs and the control of cell signalling. Cell 121 5 (2005) 667-670
    • (2005) Cell , vol.121 , Issue.5 , pp. 667-670
    • Tonks, N.K.1
  • 17
    • 0344827268 scopus 로고    scopus 로고
    • Oxidants in receptor tyrosine kinase signal transduction pathways
    • Aslan M., and Ozben T. Oxidants in receptor tyrosine kinase signal transduction pathways. Antioxid Redox Signal 5 6 (2003) 781-788
    • (2003) Antioxid Redox Signal , vol.5 , Issue.6 , pp. 781-788
    • Aslan, M.1    Ozben, T.2
  • 19
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • Schreck R., Rieber P., and Baeuerle P.A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J 10 8 (1991) 2247-2258
    • (1991) EMBO J , vol.10 , Issue.8 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 21
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden M.S., and Ghosh S. Signaling to NF-kappaB. Genes Dev 18 18 (2004) 2195-2224
    • (2004) Genes Dev , vol.18 , Issue.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 22
    • 0037064536 scopus 로고    scopus 로고
    • Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family
    • Martin M.U., and Wesche H. Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family. Biochim Biophys Acta 1592 3 (2002) 265-280
    • (2002) Biochim Biophys Acta , vol.1592 , Issue.3 , pp. 265-280
    • Martin, M.U.1    Wesche, H.2
  • 23
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin A., Cook A., Lin Y., Rodriguez Y., Kelliher M., and Liu Z. The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 12 4 (2000) 419-429
    • (2000) Immunity , vol.12 , Issue.4 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3    Rodriguez, Y.4    Kelliher, M.5    Liu, Z.6
  • 24
    • 30044442866 scopus 로고    scopus 로고
    • How Toll-like receptors signal: what we know and what we don't know
    • O'Neill L.A. How Toll-like receptors signal: what we know and what we don't know. Curr Opin Immunol 18 1 (2006) 3-9
    • (2006) Curr Opin Immunol , vol.18 , Issue.1 , pp. 3-9
    • O'Neill, L.A.1
  • 25
    • 2342611054 scopus 로고    scopus 로고
    • T-cell-receptor- and B-cell-receptor-mediated activation of NF-kappaB in lymphocytes
    • Weil R., and Israel A. T-cell-receptor- and B-cell-receptor-mediated activation of NF-kappaB in lymphocytes. Curr Opin Immunol 16 3 (2004) 374-381
    • (2004) Curr Opin Immunol , vol.16 , Issue.3 , pp. 374-381
    • Weil, R.1    Israel, A.2
  • 26
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • Bonizzi G., and Karin M. The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol 25 6 (2004) 280-288
    • (2004) Trends Immunol , vol.25 , Issue.6 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 27
    • 33645975534 scopus 로고    scopus 로고
    • Deciphering the pathway from the TCR to NF-kappaB
    • Weil R., and Israel A. Deciphering the pathway from the TCR to NF-kappaB. Cell Death Differ (2006)
    • (2006) Cell Death Differ
    • Weil, R.1    Israel, A.2
  • 28
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation
    • Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., et al. Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 93 7 (1998) 1231-1240
    • (1998) Cell , vol.93 , Issue.7 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6
  • 29
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • Zandi E., Rothwarf D.M., Delhase M., Hayakawa M., and Karin M. The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91 2 (1997) 243-252
    • (1997) Cell , vol.91 , Issue.2 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 30
    • 0036794398 scopus 로고    scopus 로고
    • BAFF-induced NEMO-independent processing of NF-kappa B2 in maturing B cells
    • Claudio E., Brown K., Park S., Wang H., and Siebenlist U. BAFF-induced NEMO-independent processing of NF-kappa B2 in maturing B cells. Nat Immunol 3 10 (2002) 958-965
    • (2002) Nat Immunol , vol.3 , Issue.10 , pp. 958-965
    • Claudio, E.1    Brown, K.2    Park, S.3    Wang, H.4    Siebenlist, U.5
  • 31
    • 18644380147 scopus 로고    scopus 로고
    • The lymphotoxin-beta receptor induces different patterns of gene expression via two NF-kappaB pathways
    • Dejardin E., Droin N.M., Delhase M., Haas E., Cao Y., Makris C., et al. The lymphotoxin-beta receptor induces different patterns of gene expression via two NF-kappaB pathways. Immunity 17 4 (2002) 525-535
    • (2002) Immunity , vol.17 , Issue.4 , pp. 525-535
    • Dejardin, E.1    Droin, N.M.2    Delhase, M.3    Haas, E.4    Cao, Y.5    Makris, C.6
  • 33
    • 0344441264 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded latent infection membrane protein 1 regulates the processing of p100 NF-kappaB2 to p52 via an IKKgamma/NEMO-independent signalling pathway
    • Eliopoulos A.G., Caamano J.H., Flavell J., Reynolds G.M., Murray P.G., Poyet J.L., et al. Epstein-Barr virus-encoded latent infection membrane protein 1 regulates the processing of p100 NF-kappaB2 to p52 via an IKKgamma/NEMO-independent signalling pathway. Oncogene 22 48 (2003) 7557-7569
    • (2003) Oncogene , vol.22 , Issue.48 , pp. 7557-7569
    • Eliopoulos, A.G.1    Caamano, J.H.2    Flavell, J.3    Reynolds, G.M.4    Murray, P.G.5    Poyet, J.L.6
  • 34
    • 0035803392 scopus 로고    scopus 로고
    • Retroviral oncoprotein tax induces processing of NF-kappaB2/p100 in T cells: evidence for the involvement of IKKalpha
    • Xiao G., Cvijic M.E., Fong A., Harhaj E.W., Uhlik M.T., Waterfield M., et al. Retroviral oncoprotein tax induces processing of NF-kappaB2/p100 in T cells: evidence for the involvement of IKKalpha. EMBO J 20 23 (2001) 6805-6815
    • (2001) EMBO J , vol.20 , Issue.23 , pp. 6805-6815
    • Xiao, G.1    Cvijic, M.E.2    Fong, A.3    Harhaj, E.W.4    Uhlik, M.T.5    Waterfield, M.6
  • 35
    • 1642330709 scopus 로고    scopus 로고
    • Oxygen sensing and oxidant/redox-related pathways
    • Haddad J.J. Oxygen sensing and oxidant/redox-related pathways. Biochem Biophys Res Commun 316 4 (2004) 969-977
    • (2004) Biochem Biophys Res Commun , vol.316 , Issue.4 , pp. 969-977
    • Haddad, J.J.1
  • 36
    • 0033163393 scopus 로고    scopus 로고
    • Is NF-kappaB the sensor of oxidative stress?
    • Li N., and Karin M. Is NF-kappaB the sensor of oxidative stress?. FASEB J 13 10 (1999) 1137-1143
    • (1999) FASEB J , vol.13 , Issue.10 , pp. 1137-1143
    • Li, N.1    Karin, M.2
  • 37
    • 0037033433 scopus 로고    scopus 로고
    • Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression
    • Devadas S., Zaritskaya L., Rhee S.G., Oberley L., and Williams M.S. Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression. J Exp Med 195 1 (2002) 59-70
    • (2002) J Exp Med , vol.195 , Issue.1 , pp. 59-70
    • Devadas, S.1    Zaritskaya, L.2    Rhee, S.G.3    Oberley, L.4    Williams, M.S.5
  • 38
    • 2942588874 scopus 로고    scopus 로고
    • Regulation of T-cell apoptosis by reactive oxygen species
    • Hildeman D.A. Regulation of T-cell apoptosis by reactive oxygen species. Free Rad Biol Med 36 12 (2004) 1496-1504
    • (2004) Free Rad Biol Med , vol.36 , Issue.12 , pp. 1496-1504
    • Hildeman, D.A.1
  • 39
    • 14644399197 scopus 로고    scopus 로고
    • Oxidative stress attenuates Fas-mediated apoptosis in Jurkat T cell line through Bfl-1 induction
    • Kim H., Kim Y.N., and Kim C.W. Oxidative stress attenuates Fas-mediated apoptosis in Jurkat T cell line through Bfl-1 induction. Oncogene 24 7 (2005) 1252-1261
    • (2005) Oncogene , vol.24 , Issue.7 , pp. 1252-1261
    • Kim, H.1    Kim, Y.N.2    Kim, C.W.3
  • 40
    • 13244267274 scopus 로고    scopus 로고
    • Acute promyelocytic leukemia: recent advances in therapy and molecular basis of response to arsenic therapies
    • Chou W.C., and Dang C.V. Acute promyelocytic leukemia: recent advances in therapy and molecular basis of response to arsenic therapies. Curr Opin Hematol 12 1 (2005) 1-6
    • (2005) Curr Opin Hematol , vol.12 , Issue.1 , pp. 1-6
    • Chou, W.C.1    Dang, C.V.2
  • 41
    • 10744231785 scopus 로고    scopus 로고
    • Involvement of reactive oxygen species in adaphostin-induced cytotoxicity in human leukemia cells
    • Chandra J., Hackbarth J., Le S., Loegering D., Bone N., Bruzek L.M., et al. Involvement of reactive oxygen species in adaphostin-induced cytotoxicity in human leukemia cells. Blood 102 13 (2003) 4512-4519
    • (2003) Blood , vol.102 , Issue.13 , pp. 4512-4519
    • Chandra, J.1    Hackbarth, J.2    Le, S.3    Loegering, D.4    Bone, N.5    Bruzek, L.M.6
  • 42
    • 0034655179 scopus 로고    scopus 로고
    • Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of I kappa B alpha in NF-kappa B activation by an oxidative stress
    • Schoonbroodt S., Ferreira V., Best-Belpomme M., Boelaert J.R., Legrand-Poels S., Korner M., et al. Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of I kappa B alpha in NF-kappa B activation by an oxidative stress. J Immunol 164 8 (2000) 4292-4300
    • (2000) J Immunol , vol.164 , Issue.8 , pp. 4292-4300
    • Schoonbroodt, S.1    Ferreira, V.2    Best-Belpomme, M.3    Boelaert, J.R.4    Legrand-Poels, S.5    Korner, M.6
  • 43
    • 0037591401 scopus 로고    scopus 로고
    • Hydrogen peroxide activates NF-{kappa}B through tyrosine phosphorylation of I{kappa}B{alpha} and serine phosphorylation of p65: evidence for the involvement of I{kappa}B{alpha} kinase and Syk protein-tyrosine kinase
    • Takada Y., Mukhopadhyay A., Kundu G.C., Mahabeleshwar G.H., Singh S., and Aggarwal B.B. Hydrogen peroxide activates NF-{kappa}B through tyrosine phosphorylation of I{kappa}B{alpha} and serine phosphorylation of p65: evidence for the involvement of I{kappa}B{alpha} kinase and Syk protein-tyrosine kinase. J Biol Chem 278 26 (2003) 24233-24241
    • (2003) J Biol Chem , vol.278 , Issue.26 , pp. 24233-24241
    • Takada, Y.1    Mukhopadhyay, A.2    Kundu, G.C.3    Mahabeleshwar, G.H.4    Singh, S.5    Aggarwal, B.B.6
  • 44
    • 0035082793 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent activation of NF-kappa B. Requirement for p56 LCK and ZAP-70 protein tyrosine kinases
    • Livolsi A., Busuttil V., Imbert V., Abraham R.T., and Peyron J.F. Tyrosine phosphorylation-dependent activation of NF-kappa B. Requirement for p56 LCK and ZAP-70 protein tyrosine kinases. Eur J Biochem 268 5 (2001) 1508-1515
    • (2001) Eur J Biochem , vol.268 , Issue.5 , pp. 1508-1515
    • Livolsi, A.1    Busuttil, V.2    Imbert, V.3    Abraham, R.T.4    Peyron, J.F.5
  • 45
    • 16044365828 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha
    • Imbert V., Rupec R.A., Livolsi A., Pahl H.L., Traenckner E.B., Mueller-Dieckmann C., et al. Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha. Cell 86 5 (1996) 787-798
    • (1996) Cell , vol.86 , Issue.5 , pp. 787-798
    • Imbert, V.1    Rupec, R.A.2    Livolsi, A.3    Pahl, H.L.4    Traenckner, E.B.5    Mueller-Dieckmann, C.6
  • 46
    • 0033582285 scopus 로고    scopus 로고
    • Involvement of regulatory and catalytic subunits of phosphoinositide 3-kinase in NF-kappaB activation
    • Beraud C., Henzel W.J., and Baeuerle P.A. Involvement of regulatory and catalytic subunits of phosphoinositide 3-kinase in NF-kappaB activation. Proc Natl Acad Sci USA 96 2 (1999) 429-434
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.2 , pp. 429-434
    • Beraud, C.1    Henzel, W.J.2    Baeuerle, P.A.3
  • 47
    • 33750516565 scopus 로고    scopus 로고
    • Gloire G, Charlier E, Rahmouni S, Volanti C, Erneux C and Piette J, Restoration of SHIP-1 activity in human leukemic cells modifies NF-kappaB activation pathway and cellular survival upon oxidative stress. Oncogene, in press.
  • 48
    • 0033804532 scopus 로고    scopus 로고
    • Lipid phosphatases in the immune system
    • Krystal G. Lipid phosphatases in the immune system. Semin Immunol 12 4 (2000) 397-403
    • (2000) Semin Immunol , vol.12 , Issue.4 , pp. 397-403
    • Krystal, G.1
  • 49
    • 0037111475 scopus 로고    scopus 로고
    • Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors
    • Freeburn R.W., Wright K.L., Burgess S.J., Astoul E., Cantrell D.A., and Ward S.G. Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors. J Immunol 169 10 (2002) 5441-5450
    • (2002) J Immunol , vol.169 , Issue.10 , pp. 5441-5450
    • Freeburn, R.W.1    Wright, K.L.2    Burgess, S.J.3    Astoul, E.4    Cantrell, D.A.5    Ward, S.G.6
  • 50
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science 296 5573 (2002) 1655-1657
    • (2002) Science , vol.296 , Issue.5573 , pp. 1655-1657
    • Cantley, L.C.1
  • 51
    • 0028006612 scopus 로고
    • Separation of oxidant-initiated and redox-regulated steps in the NF-kappa B signal transduction pathway
    • Anderson M.T., Staal F.J., Gitler C., and Herzenberg L.A. Separation of oxidant-initiated and redox-regulated steps in the NF-kappa B signal transduction pathway. Proc Natl Acad Sci USA 91 24 (1994) 11527-11531
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.24 , pp. 11527-11531
    • Anderson, M.T.1    Staal, F.J.2    Gitler, C.3    Herzenberg, L.A.4
  • 52
    • 0029665048 scopus 로고    scopus 로고
    • Involvement of intracellular Ca2+ in oxidant-induced NF-kappa B activation
    • Sen C.K., Roy S., and Packer L. Involvement of intracellular Ca2+ in oxidant-induced NF-kappa B activation. FEBS Lett 385 1-2 (1996) 58-62
    • (1996) FEBS Lett , vol.385 , Issue.1-2 , pp. 58-62
    • Sen, C.K.1    Roy, S.2    Packer, L.3
  • 53
    • 1642379541 scopus 로고    scopus 로고
    • Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling
    • Storz P., Doppler H., and Toker A. Protein kinase Cdelta selectively regulates protein kinase D-dependent activation of NF-kappaB in oxidative stress signaling. Mol Cell Biol 24 7 (2004) 2614-2626
    • (2004) Mol Cell Biol , vol.24 , Issue.7 , pp. 2614-2626
    • Storz, P.1    Doppler, H.2    Toker, A.3
  • 54
    • 0037413711 scopus 로고    scopus 로고
    • Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway
    • Storz P., and Toker A. Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway. EMBO J 22 1 (2003) 109-120
    • (2003) EMBO J , vol.22 , Issue.1 , pp. 109-120
    • Storz, P.1    Toker, A.2
  • 55
    • 0037449777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of I kappa B alpha activates NF kappa B through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation
    • Fan C., Li Q., Ross D., and Engelhardt J.F. Tyrosine phosphorylation of I kappa B alpha activates NF kappa B through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation. J Biol Chem 278 3 (2003) 2072-2080
    • (2003) J Biol Chem , vol.278 , Issue.3 , pp. 2072-2080
    • Fan, C.1    Li, Q.2    Ross, D.3    Engelhardt, J.F.4
  • 56
    • 0035929670 scopus 로고    scopus 로고
    • Cytokine-induced activation of nuclear factor-kappa B is inhibited by hydrogen peroxide through oxidative inactivation of IkappaB kinase
    • Korn S.H., Wouters E.F., Vos N., and Janssen-Heininger Y.M. Cytokine-induced activation of nuclear factor-kappa B is inhibited by hydrogen peroxide through oxidative inactivation of IkappaB kinase. J Biol Chem 276 38 (2001) 35693-35700
    • (2001) J Biol Chem , vol.276 , Issue.38 , pp. 35693-35700
    • Korn, S.H.1    Wouters, E.F.2    Vos, N.3    Janssen-Heininger, Y.M.4
  • 57
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase
    • Rossi A., Kapahi P., Natoli G., Takahashi T., Chen Y., Karin M., et al. Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403 6765 (2000) 103-108
    • (2000) Nature , vol.403 , Issue.6765 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, G.3    Takahashi, T.4    Chen, Y.5    Karin, M.6
  • 58
    • 0034680928 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B activation by arsenite through reaction with a critical cysteine in the activation loop of Ikappa B kinase
    • Kapahi P., Takahashi T., Natoli G., Adams S.R., Chen Y., Tsien R.Y., et al. Inhibition of NF-kappa B activation by arsenite through reaction with a critical cysteine in the activation loop of Ikappa B kinase. J Biol Chem 275 46 (2000) 36062-36066
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 36062-36066
    • Kapahi, P.1    Takahashi, T.2    Natoli, G.3    Adams, S.R.4    Chen, Y.5    Tsien, R.Y.6
  • 59
    • 10044241543 scopus 로고    scopus 로고
    • Oxidative stress and cigarette smoke alter chromatin remodeling but differentially regulate NF-kappaB activation and proinflammatory cytokine release in alveolar epithelial cells
    • Moodie F.M., Marwick J.A., Anderson C.S., Szulakowski P., Biswas S.K., Bauter M.R., et al. Oxidative stress and cigarette smoke alter chromatin remodeling but differentially regulate NF-kappaB activation and proinflammatory cytokine release in alveolar epithelial cells. FASEB J 18 15 (2004) 1897-1899
    • (2004) FASEB J , vol.18 , Issue.15 , pp. 1897-1899
    • Moodie, F.M.1    Marwick, J.A.2    Anderson, C.S.3    Szulakowski, P.4    Biswas, S.K.5    Bauter, M.R.6
  • 60
    • 0033151902 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation
    • Hawkins C.L., and Davies M.J. Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation. Biochem J 340 Pt. 2 (1999) 539-548
    • (1999) Biochem J , vol.340 , Issue.PART 2 , pp. 539-548
    • Hawkins, C.L.1    Davies, M.J.2
  • 61
    • 0031050027 scopus 로고    scopus 로고
    • Activation of the NF-kappaB transcription factor in a T-lymphocytic cell line by hypochlorous acid
    • Schoonbroodt S., Legrand-Poels S., Best-Belpomme M., and Piette J. Activation of the NF-kappaB transcription factor in a T-lymphocytic cell line by hypochlorous acid. Biochem J 321 Pt. 3 (1997) 777-785
    • (1997) Biochem J , vol.321 , Issue.PART 3 , pp. 777-785
    • Schoonbroodt, S.1    Legrand-Poels, S.2    Best-Belpomme, M.3    Piette, J.4
  • 62
    • 0035881265 scopus 로고    scopus 로고
    • Taurine chloramine inhibits inducible nitric oxide synthase and TNF-alpha gene expression in activated alveolar macrophages: decreased NF-kappaB activation and IkappaB kinase activity
    • Barua M., Liu Y., and Quinn M.R. Taurine chloramine inhibits inducible nitric oxide synthase and TNF-alpha gene expression in activated alveolar macrophages: decreased NF-kappaB activation and IkappaB kinase activity. J Immunol 167 4 (2001) 2275-2281
    • (2001) J Immunol , vol.167 , Issue.4 , pp. 2275-2281
    • Barua, M.1    Liu, Y.2    Quinn, M.R.3
  • 63
    • 0037024693 scopus 로고    scopus 로고
    • Oxidation of Ikappa Balpha at methionine 45 is one cause of taurine chloramine-induced inhibition of NF-kappa B activation
    • Kanayama A., Inoue J., Sugita-Konishi Y., Shimizu M., and Miyamoto Y. Oxidation of Ikappa Balpha at methionine 45 is one cause of taurine chloramine-induced inhibition of NF-kappa B activation. J Biol Chem 277 27 (2002) 24049-24056
    • (2002) J Biol Chem , vol.277 , Issue.27 , pp. 24049-24056
    • Kanayama, A.1    Inoue, J.2    Sugita-Konishi, Y.3    Shimizu, M.4    Miyamoto, Y.5
  • 64
    • 28844507218 scopus 로고    scopus 로고
    • Oxidative modification of IkappaB by monochloramine inhibits tumor necrosis factor alpha-induced NF-kappaB activation
    • Ogino T., Hosako M., Hiramatsu K., Omori M., Ozaki M., and Okada S. Oxidative modification of IkappaB by monochloramine inhibits tumor necrosis factor alpha-induced NF-kappaB activation. Biochim Biophys Acta 1746 2 (2005) 135-142
    • (2005) Biochim Biophys Acta , vol.1746 , Issue.2 , pp. 135-142
    • Ogino, T.1    Hosako, M.2    Hiramatsu, K.3    Omori, M.4    Ozaki, M.5    Okada, S.6
  • 65
    • 0020573713 scopus 로고
    • Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils
    • Thomas E.L., Grisham M.B., and Jefferson M.M. Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils. J Clin Invest 72 2 (1983) 441-454
    • (1983) J Clin Invest , vol.72 , Issue.2 , pp. 441-454
    • Thomas, E.L.1    Grisham, M.B.2    Jefferson, M.M.3
  • 66
    • 33646761969 scopus 로고    scopus 로고
    • IkappaB is a sensitive target for oxidation by cell-permeable chloramines: inhibition of NF-kappaB activity by glycine chloramine through methionine oxidation
    • Midwinter R.G., Cheah F.C., Moskovitz J., Vissers M.C., and Winterbourn C.C. IkappaB is a sensitive target for oxidation by cell-permeable chloramines: inhibition of NF-kappaB activity by glycine chloramine through methionine oxidation. Biochem J 396 May (1) (2006) 71-78
    • (2006) Biochem J , vol.396 , Issue.May 1 , pp. 71-78
    • Midwinter, R.G.1    Cheah, F.C.2    Moskovitz, J.3    Vissers, M.C.4    Winterbourn, C.C.5
  • 67
    • 5344271785 scopus 로고    scopus 로고
    • Chlorine transfer between glycine, taurine, and histamine: reaction rates and impact on cellular reactivity
    • Peskin A.V., Midwinter R.G., Harwood D.T., and Winterbourn C.C. Chlorine transfer between glycine, taurine, and histamine: reaction rates and impact on cellular reactivity. Free Rad Biol Med 37 10 (2004) 1622-1630
    • (2004) Free Rad Biol Med , vol.37 , Issue.10 , pp. 1622-1630
    • Peskin, A.V.1    Midwinter, R.G.2    Harwood, D.T.3    Winterbourn, C.C.4
  • 68
    • 2942562451 scopus 로고    scopus 로고
    • Ultraviolet a radiation-induced immediate iron release is a key modulator of the activation of NF-kappaB in human skin fibroblasts
    • Reelfs O., Tyrrell R.M., and Pourzand C. Ultraviolet a radiation-induced immediate iron release is a key modulator of the activation of NF-kappaB in human skin fibroblasts. J Invest Dermatol 122 6 (2004) 1440-1447
    • (2004) J Invest Dermatol , vol.122 , Issue.6 , pp. 1440-1447
    • Reelfs, O.1    Tyrrell, R.M.2    Pourzand, C.3
  • 69
    • 33750533445 scopus 로고    scopus 로고
    • Matroule JY, Volanti C, Piette J, NF-kappaB in Photodynamic therapy: duality of a master regulator. Photochem Photobiol, in press.
  • 70
    • 2942590657 scopus 로고    scopus 로고
    • U.V.A. and NF-kappaB activity: ironing out the details
    • Swerlick R.A., and Korman N.J. U.V.A. and NF-kappaB activity: ironing out the details. J Invest Dermatol 122 6 (2004) xi-xii
    • (2004) J Invest Dermatol , vol.122 , Issue.6
    • Swerlick, R.A.1    Korman, N.J.2
  • 71
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide
    • Beckman J.S., Beckman T.W., Chen J., Marshall P.A., and Freeman B.A. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA 87 4 (1990) 1620-1624
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.4 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 72
    • 0034059625 scopus 로고    scopus 로고
    • Biology of nitric oxide signaling
    • Liaudet L., Soriano F.G., and Szabo C. Biology of nitric oxide signaling. Crit Care Med 28 4 Suppl. (2000) N37-N52
    • (2000) Crit Care Med , vol.28 , Issue.4 SUPPL
    • Liaudet, L.1    Soriano, F.G.2    Szabo, C.3
  • 73
    • 0035376102 scopus 로고    scopus 로고
    • Myocardial ischemic preconditioning in rodents is dependent on poly (ADP-ribose) synthetase
    • Liaudet L., Yang Z., Al-Affar E.B., and Szabo C. Myocardial ischemic preconditioning in rodents is dependent on poly (ADP-ribose) synthetase. Mol Med 7 6 (2001) 406-417
    • (2001) Mol Med , vol.7 , Issue.6 , pp. 406-417
    • Liaudet, L.1    Yang, Z.2    Al-Affar, E.B.3    Szabo, C.4
  • 74
    • 0037019589 scopus 로고    scopus 로고
    • Pharmacologic inhibition of poly(adenosine diphosphate-ribose) polymerase may represent a novel therapeutic approach in chronic heart failure
    • Pacher P., Liaudet L., Mabley J., Komjati K., and Szabo C. Pharmacologic inhibition of poly(adenosine diphosphate-ribose) polymerase may represent a novel therapeutic approach in chronic heart failure. J Am Coll Cardiol 40 5 (2002) 1006-1016
    • (2002) J Am Coll Cardiol , vol.40 , Issue.5 , pp. 1006-1016
    • Pacher, P.1    Liaudet, L.2    Mabley, J.3    Komjati, K.4    Szabo, C.5
  • 75
    • 0036080603 scopus 로고    scopus 로고
    • Peroxynitrite increases iNOS through NF-kappaB and decreases prostacyclin synthase in endothelial cells
    • Cooke C.L., and Davidge S.T. Peroxynitrite increases iNOS through NF-kappaB and decreases prostacyclin synthase in endothelial cells. Am J Physiol Cell Physiol 282 2 (2002) C395-C402
    • (2002) Am J Physiol Cell Physiol , vol.282 , Issue.2
    • Cooke, C.L.1    Davidge, S.T.2
  • 76
    • 0142231354 scopus 로고    scopus 로고
    • Selenium-containing compounds attenuate peroxynitrite-mediated NF-kappaB and AP-1 activation and interleukin-8 gene and protein expression in human leukocytes
    • Jozsef L., and Filep J.G. Selenium-containing compounds attenuate peroxynitrite-mediated NF-kappaB and AP-1 activation and interleukin-8 gene and protein expression in human leukocytes. Free Rad Biol Med 35 9 (2003) 1018-1027
    • (2003) Free Rad Biol Med , vol.35 , Issue.9 , pp. 1018-1027
    • Jozsef, L.1    Filep, J.G.2
  • 77
    • 2942574528 scopus 로고    scopus 로고
    • NO suppresses while peroxynitrite sustains NF-kappaB: a paradigm to rationalize cytoprotective and cytotoxic actions attributed to NO
    • Hattori Y., Kasai K., and Gross S.S. NO suppresses while peroxynitrite sustains NF-kappaB: a paradigm to rationalize cytoprotective and cytotoxic actions attributed to NO. Cardiovasc Res 63 1 (2004) 31-40
    • (2004) Cardiovasc Res , vol.63 , Issue.1 , pp. 31-40
    • Hattori, Y.1    Kasai, K.2    Gross, S.S.3
  • 78
    • 27144547642 scopus 로고    scopus 로고
    • Peroxynitrite is a potent inhibitor of NF-{kappa}B activation triggered by inflammatory stimuli in cardiac and endothelial cell lines
    • Levrand S., Pesse B., Feihl F., Waeber B., Pacher P., Rolli J., et al. Peroxynitrite is a potent inhibitor of NF-{kappa}B activation triggered by inflammatory stimuli in cardiac and endothelial cell lines. J Biol Chem 280 41 (2005) 34878-34887
    • (2005) J Biol Chem , vol.280 , Issue.41 , pp. 34878-34887
    • Levrand, S.1    Pesse, B.2    Feihl, F.3    Waeber, B.4    Pacher, P.5    Rolli, J.6
  • 79
    • 15944409156 scopus 로고    scopus 로고
    • Tyrosine nitration on p65: a novel mechanism to rapidly inactivate nuclear factor-kappaB
    • Park S.W., Huq M.D., Hu X., and Wei L.N. Tyrosine nitration on p65: a novel mechanism to rapidly inactivate nuclear factor-kappaB. Mol Cell Proteomics 4 3 (2005) 300-309
    • (2005) Mol Cell Proteomics , vol.4 , Issue.3 , pp. 300-309
    • Park, S.W.1    Huq, M.D.2    Hu, X.3    Wei, L.N.4
  • 80
    • 22744431625 scopus 로고    scopus 로고
    • Does peroxynitrite sustain nuclear factor-kappaB?
    • author reply 747-8
    • Biswas S.K., and Lopes de Faria J.B. Does peroxynitrite sustain nuclear factor-kappaB?. Cardiovasc Res 67 4 (2005) 745-746 author reply 747-8
    • (2005) Cardiovasc Res , vol.67 , Issue.4 , pp. 745-746
    • Biswas, S.K.1    Lopes de Faria, J.B.2
  • 81
    • 0029164695 scopus 로고
    • IL-2 gene expression and NF-kappa B activation through CD28 requires reactive oxygen production by 5-lipoxygenase
    • Los M., Schenk H., Hexel K., Baeuerle P.A., Droge W., and Schulze-Osthoff K. IL-2 gene expression and NF-kappa B activation through CD28 requires reactive oxygen production by 5-lipoxygenase. EMBO J 14 15 (1995) 3731-3740
    • (1995) EMBO J , vol.14 , Issue.15 , pp. 3731-3740
    • Los, M.1    Schenk, H.2    Hexel, K.3    Baeuerle, P.A.4    Droge, W.5    Schulze-Osthoff, K.6
  • 82
    • 0033990344 scopus 로고    scopus 로고
    • Cell type-specific role for reactive oxygen species in nuclear factor-kappaB activation by interleukin-1
    • Bonizzi G., Piette J., Merville M.P., and Bours V. Cell type-specific role for reactive oxygen species in nuclear factor-kappaB activation by interleukin-1. Biochem Pharmacol 59 1 (2000) 7-11
    • (2000) Biochem Pharmacol , vol.59 , Issue.1 , pp. 7-11
    • Bonizzi, G.1    Piette, J.2    Merville, M.P.3    Bours, V.4
  • 83
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells
    • Schreck R., Meier B., Mannel D.N., Droge W., and Baeuerle P.A. Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells. J Exp Med 175 5 (1992) 1181-1194
    • (1992) J Exp Med , vol.175 , Issue.5 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3    Droge, W.4    Baeuerle, P.A.5
  • 84
    • 0036889641 scopus 로고    scopus 로고
    • Reactive oxygen intermediates in TNF signaling
    • Garg A.K., and Aggarwal B.B. Reactive oxygen intermediates in TNF signaling. Mol Immunol 39 9 (2002) 509-517
    • (2002) Mol Immunol , vol.39 , Issue.9 , pp. 509-517
    • Garg, A.K.1    Aggarwal, B.B.2
  • 86
    • 0033990345 scopus 로고    scopus 로고
    • Oxidative stress and nuclear factor-kappaB activation: a reassessment of the evidence in the light of recent discoveries
    • Bowie A., and O'Neill L.A. Oxidative stress and nuclear factor-kappaB activation: a reassessment of the evidence in the light of recent discoveries. Biochem Pharmacol 59 1 (2000) 13-23
    • (2000) Biochem Pharmacol , vol.59 , Issue.1 , pp. 13-23
    • Bowie, A.1    O'Neill, L.A.2
  • 87
    • 0038601994 scopus 로고    scopus 로고
    • Evidence that reactive oxygen species do not mediate NF-kappaB activation
    • Hayakawa M., Miyashita H., Sakamoto I., Kitagawa M., Tanaka H., Yasuda H., et al. Evidence that reactive oxygen species do not mediate NF-kappaB activation. EMBO J 22 13 (2003) 3356-3366
    • (2003) EMBO J , vol.22 , Issue.13 , pp. 3356-3366
    • Hayakawa, M.1    Miyashita, H.2    Sakamoto, I.3    Kitagawa, M.4    Tanaka, H.5    Yasuda, H.6
  • 88
    • 0030771914 scopus 로고    scopus 로고
    • 2 in NF-kappaB activation by either cytokine in both primary and transformed endothelial cells
    • 2 in NF-kappaB activation by either cytokine in both primary and transformed endothelial cells. J Biol Chem 272 41 (1997) 25941-25950
    • (1997) J Biol Chem , vol.272 , Issue.41 , pp. 25941-25950
    • Bowie, A.G.1    Moynagh, P.N.2    O'Neill, L.A.3
  • 89
    • 0028924841 scopus 로고
    • Effects of oxidants and antioxidants on nuclear factor kappa B activation in three different cell lines: evidence against a universal hypothesis involving oxygen radicals
    • Brennan P., and O'Neill L.A. Effects of oxidants and antioxidants on nuclear factor kappa B activation in three different cell lines: evidence against a universal hypothesis involving oxygen radicals. Biochim Biophys Acta 1260 2 (1995) 167-175
    • (1995) Biochim Biophys Acta , vol.1260 , Issue.2 , pp. 167-175
    • Brennan, P.1    O'Neill, L.A.2
  • 90
    • 0030694108 scopus 로고    scopus 로고
    • IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling
    • Muzio M., Ni J., Feng P., and Dixit V.M. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science 278 5343 (1997) 1612-1615
    • (1997) Science , vol.278 , Issue.5343 , pp. 1612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 91
    • 0030662372 scopus 로고    scopus 로고
    • Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein
    • Huang J., Gao X., Li S., and Cao Z. Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein. Proc Natl Acad Sci USA 94 24 (1997) 12829-12832
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.24 , pp. 12829-12832
    • Huang, J.1    Gao, X.2    Li, S.3    Cao, Z.4
  • 92
  • 93
    • 0031423761 scopus 로고    scopus 로고
    • MyD88: an adapter that recruits IRAK to the IL-1 receptor complex
    • Wesche H., Henzel W.J., Shillinglaw W., Li S., and Cao Z. MyD88: an adapter that recruits IRAK to the IL-1 receptor complex. Immunity 7 6 (1997) 837-847
    • (1997) Immunity , vol.7 , Issue.6 , pp. 837-847
    • Wesche, H.1    Henzel, W.J.2    Shillinglaw, W.3    Li, S.4    Cao, Z.5
  • 94
    • 0035834672 scopus 로고    scopus 로고
    • IRAK-mediated translocation of TRAF6 and TAB2 in the interleukin-1-induced activation of NFkappa B
    • Qian Y., Commane M., Ninomiya-Tsuji J., Matsumoto K., and Li X. IRAK-mediated translocation of TRAF6 and TAB2 in the interleukin-1-induced activation of NFkappa B. J Biol Chem 276 45 (2001) 41661-41667
    • (2001) J Biol Chem , vol.276 , Issue.45 , pp. 41661-41667
    • Qian, Y.1    Commane, M.2    Ninomiya-Tsuji, J.3    Matsumoto, K.4    Li, X.5
  • 95
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., and Chen Z.J. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412 6844 (2001) 346-351
    • (2001) Nature , vol.412 , Issue.6844 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.5    Chen, Z.J.6
  • 96
    • 0033053617 scopus 로고    scopus 로고
    • Reactive oxygen intermediate-dependent NF-kappaB activation by interleukin-1beta requires 5-lipoxygenase or NADPH oxidase activity
    • Bonizzi G., Piette J., Schoonbroodt S., Greimers R., Havard L., Merville M.P., et al. Reactive oxygen intermediate-dependent NF-kappaB activation by interleukin-1beta requires 5-lipoxygenase or NADPH oxidase activity. Mol Cell Biol 19 3 (1999) 1950-1960
    • (1999) Mol Cell Biol , vol.19 , Issue.3 , pp. 1950-1960
    • Bonizzi, G.1    Piette, J.2    Schoonbroodt, S.3    Greimers, R.4    Havard, L.5    Merville, M.P.6
  • 98
    • 33644990327 scopus 로고    scopus 로고
    • 2-mediated activation of NFkappaB-inducing kinase
    • 2-mediated activation of NFkappaB-inducing kinase. J Biol Chem 281 3 (2006) 1495-1505
    • (2006) J Biol Chem , vol.281 , Issue.3 , pp. 1495-1505
    • Li, Q.1    Engelhardt, J.F.2
  • 99
    • 0035896422 scopus 로고    scopus 로고
    • Defective lymphotoxin-beta receptor-induced NF-kappaB transcriptional activity in NIK-deficient mice
    • Yin L., Wu L., Wesche H., Arthur C.D., White J.M., Goeddel D.V., et al. Defective lymphotoxin-beta receptor-induced NF-kappaB transcriptional activity in NIK-deficient mice. Science 291 5511 (2001) 2162-2165
    • (2001) Science , vol.291 , Issue.5511 , pp. 2162-2165
    • Yin, L.1    Wu, L.2    Wesche, H.3    Arthur, C.D.4    White, J.M.5    Goeddel, D.V.6
  • 100
    • 0027420579 scopus 로고
    • Tumor necrosis factor: an updated review of its biology
    • Tracey K.J., and Cerami A. Tumor necrosis factor: an updated review of its biology. Crit Care Med 21 10 Suppl. (1993) S415-S422
    • (1993) Crit Care Med , vol.21 , Issue.10 SUPPL
    • Tracey, K.J.1    Cerami, A.2
  • 101
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: a double-edged sword
    • Aggarwal B.B. Signalling pathways of the TNF superfamily: a double-edged sword. Nat Rev Immunol 3 9 (2003) 745-756
    • (2003) Nat Rev Immunol , vol.3 , Issue.9 , pp. 745-756
    • Aggarwal, B.B.1
  • 102
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang Y., Woronicz J.D., Liu W., and Goeddel D.V. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 283 5401 (1999) 543-546
    • (1999) Science , vol.283 , Issue.5401 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 103
    • 0038320263 scopus 로고    scopus 로고
    • The signaling adaptors and pathways activated by TNF superfamily
    • Dempsey P.W., Doyle S.E., He J.Q., and Cheng G. The signaling adaptors and pathways activated by TNF superfamily. Cytokine Growth Factor Rev 14 3-4 (2003) 193-209
    • (2003) Cytokine Growth Factor Rev , vol.14 , Issue.3-4 , pp. 193-209
    • Dempsey, P.W.1    Doyle, S.E.2    He, J.Q.3    Cheng, G.4
  • 104
    • 0035965232 scopus 로고    scopus 로고
    • Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-kappa B activation and protection from cell death
    • Tada K., Okazaki T., Sakon S., Kobarai T., Kurosawa K., Yamaoka S., et al. Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-kappa B activation and protection from cell death. J Biol Chem 276 39 (2001) 36530-36534
    • (2001) J Biol Chem , vol.276 , Issue.39 , pp. 36530-36534
    • Tada, K.1    Okazaki, T.2    Sakon, S.3    Kobarai, T.4    Kurosawa, K.5    Yamaoka, S.6
  • 105
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H., Huang J., Shu H.B., Baichwal V., and Goeddel D.V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4 4 (1996) 387-396
    • (1996) Immunity , vol.4 , Issue.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 106
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation
    • Zhang S.Q., Kovalenko A., Cantarella G., and Wallach D. Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation. Immunity 12 3 (2000) 301-311
    • (2000) Immunity , vol.12 , Issue.3 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 107
    • 0033140337 scopus 로고    scopus 로고
    • Antioxidants differentially regulate activation of nuclear factor-kappa B, activator protein-1, c-jun amino-terminal kinases, and apoptosis induced by tumor necrosis factor: evidence that JNK and NF-kappa B activation are not linked to apoptosis
    • Shrivastava A., and Aggarwal B.B. Antioxidants differentially regulate activation of nuclear factor-kappa B, activator protein-1, c-jun amino-terminal kinases, and apoptosis induced by tumor necrosis factor: evidence that JNK and NF-kappa B activation are not linked to apoptosis. Antioxid Redox Signal 1 2 (1999) 181-191
    • (1999) Antioxid Redox Signal , vol.1 , Issue.2 , pp. 181-191
    • Shrivastava, A.1    Aggarwal, B.B.2
  • 108
    • 4143083971 scopus 로고    scopus 로고
    • Regulation at multiple levels of NF-kappaB-mediated transactivation by protein acetylation
    • Quivy V., and Van Lint C. Regulation at multiple levels of NF-kappaB-mediated transactivation by protein acetylation. Biochem Pharmacol 68 6 (2004) 1221-1229
    • (2004) Biochem Pharmacol , vol.68 , Issue.6 , pp. 1221-1229
    • Quivy, V.1    Van Lint, C.2
  • 109
    • 0035315925 scopus 로고    scopus 로고
    • Cigarette smoking reduces histone deacetylase 2 expression, enhances cytokine expression, and inhibits glucocorticoid actions in alveolar macrophages
    • Ito K., Lim S., Caramori G., Chung K.F., Barnes P.J., and Adcock I.M. Cigarette smoking reduces histone deacetylase 2 expression, enhances cytokine expression, and inhibits glucocorticoid actions in alveolar macrophages. FASEB J 15 6 (2001) 1110-1112
    • (2001) FASEB J , vol.15 , Issue.6 , pp. 1110-1112
    • Ito, K.1    Lim, S.2    Caramori, G.3    Chung, K.F.4    Barnes, P.J.5    Adcock, I.M.6
  • 110
    • 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 6 (2004) 1255-1267
    • (2004) Biochem Pharmacol , vol.68 , Issue.6 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 111
    • 0036884292 scopus 로고    scopus 로고
    • A novel mechanism for the inhibition of NF-kappaB activation in vascular endothelial cells by natural antioxidants
    • Schubert S.Y., Neeman I., and Resnick N. A novel mechanism for the inhibition of NF-kappaB activation in vascular endothelial cells by natural antioxidants. FASEB J 16 14 (2002) 1931-1933
    • (2002) FASEB J , vol.16 , Issue.14 , pp. 1931-1933
    • Schubert, S.Y.1    Neeman, I.2    Resnick, N.3
  • 112
    • 21344474327 scopus 로고    scopus 로고
    • From JNK to pay dirt: jun kinases, their biochemistry, physiology and clinical importance
    • Karin M., and Gallagher E. From JNK to pay dirt: jun kinases, their biochemistry, physiology and clinical importance. IUBMB Life 57 4-5 (2005) 283-295
    • (2005) IUBMB Life , vol.57 , Issue.4-5 , pp. 283-295
    • Karin, M.1    Gallagher, E.2
  • 113
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin M., and Lin A. NF-kappaB at the crossroads of life and death. Nat Immunol 3 3 (2002) 221-227
    • (2002) Nat Immunol , vol.3 , Issue.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 114
    • 0035889252 scopus 로고    scopus 로고
    • Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling
    • De Smaele E., Zazzeroni F., Papa S., Nguyen D.U., Jin R., Jones J., et al. Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling. Nature 414 6861 (2001) 308-313
    • (2001) Nature , vol.414 , Issue.6861 , pp. 308-313
    • De Smaele, E.1    Zazzeroni, F.2    Papa, S.3    Nguyen, D.U.4    Jin, R.5    Jones, J.6
  • 115
    • 0035891320 scopus 로고    scopus 로고
    • Inhibition of JNK activation through NF-kappaB target genes
    • Tang G., Minemoto Y., Dibling B., Purcell N.H., Li Z., Karin M., et al. Inhibition of JNK activation through NF-kappaB target genes. Nature 414 6861 (2001) 313-317
    • (2001) Nature , vol.414 , Issue.6861 , pp. 313-317
    • Tang, G.1    Minemoto, Y.2    Dibling, B.3    Purcell, N.H.4    Li, Z.5    Karin, M.6
  • 116
    • 1642602694 scopus 로고    scopus 로고
    • Gadd45 beta mediates the NF-kappa B suppression of JNK signalling by targeting MKK7/JNKK2
    • Papa S., Zazzeroni F., Bubici C., Jayawardena S., Alvarez K., Matsuda S., et al. Gadd45 beta mediates the NF-kappa B suppression of JNK signalling by targeting MKK7/JNKK2. Nat Cell Biol 6 2 (2004) 146-153
    • (2004) Nat Cell Biol , vol.6 , Issue.2 , pp. 146-153
    • Papa, S.1    Zazzeroni, F.2    Bubici, C.3    Jayawardena, S.4    Alvarez, K.5    Matsuda, S.6
  • 117
    • 0042467735 scopus 로고    scopus 로고
    • Cell signalling: cell survival and a Gadd45-factor deficiency
    • discussion 742
    • Amanullah A., Azam N., Balliet A., Hollander C., Hoffman B., Fornace A., et al. Cell signalling: cell survival and a Gadd45-factor deficiency. Nature 424 6950 (2003) 741 discussion 742
    • (2003) Nature , vol.424 , Issue.6950 , pp. 741
    • Amanullah, A.1    Azam, N.2    Balliet, A.3    Hollander, C.4    Hoffman, B.5    Fornace, A.6
  • 118
    • 1642553460 scopus 로고    scopus 로고
    • To be, or not to be: NF-kappaB is the answer--role of Rel/NF-kappaB in the regulation of apoptosis
    • Kucharczak J., Simmons M.J., Fan Y., and Gelinas C. To be, or not to be: NF-kappaB is the answer--role of Rel/NF-kappaB in the regulation of apoptosis. Oncogene 22 56 (2003) 8961-8982
    • (2003) Oncogene , vol.22 , Issue.56 , pp. 8961-8982
    • Kucharczak, J.1    Simmons, M.J.2    Fan, Y.3    Gelinas, C.4
  • 119
    • 0042525938 scopus 로고    scopus 로고
    • NF-kappaB inhibits TNF-induced accumulation of ROS that mediate prolonged MAPK activation and necrotic cell death
    • Sakon S., Xue X., Takekawa M., Sasazuki T., Okazaki T., Kojima Y., et al. NF-kappaB inhibits TNF-induced accumulation of ROS that mediate prolonged MAPK activation and necrotic cell death. EMBO J 22 15 (2003) 3898-3909
    • (2003) EMBO J , vol.22 , Issue.15 , pp. 3898-3909
    • Sakon, S.1    Xue, X.2    Takekawa, M.3    Sasazuki, T.4    Okazaki, T.5    Kojima, Y.6
  • 120
    • 10044265209 scopus 로고    scopus 로고
    • JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species
    • Ventura J.J., Cogswell P., Flavell R.A., Baldwin Jr. A.S., and Davis R.J. JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species. Genes Dev 18 23 (2004) 2905-2915
    • (2004) Genes Dev , vol.18 , Issue.23 , pp. 2905-2915
    • Ventura, J.J.1    Cogswell, P.2    Flavell, R.A.3    Baldwin Jr., A.S.4    Davis, R.J.5
  • 121
    • 8344260568 scopus 로고    scopus 로고
    • Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species
    • Pham C.G., Bubici C., Zazzeroni F., Papa S., Jones J., Alvarez K., et al. Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species. Cell 119 4 (2004) 529-542
    • (2004) Cell , vol.119 , Issue.4 , pp. 529-542
    • Pham, C.G.1    Bubici, C.2    Zazzeroni, F.3    Papa, S.4    Jones, J.5    Alvarez, K.6
  • 122
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H., Honda S., Maeda S., Chang L., Hirata H., and Karin M. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120 5 (2005) 649-661
    • (2005) Cell , vol.120 , Issue.5 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 124
    • 33645983982 scopus 로고    scopus 로고
    • The NF-kappaB-mediated control of the JNK cascade in the antagonism of programmed cell death in health and disease
    • Papa S., Bubici C., Zazzeroni F., Pham C.G., Kuntzen C., Knabb J.R., et al. The NF-kappaB-mediated control of the JNK cascade in the antagonism of programmed cell death in health and disease. Cell Death Differ (2006)
    • (2006) Cell Death Differ
    • Papa, S.1    Bubici, C.2    Zazzeroni, F.3    Pham, C.G.4    Kuntzen, C.5    Knabb, J.R.6
  • 125
    • 2942593988 scopus 로고    scopus 로고
    • Genome wide analysis of TNF-inducible genes reveals that antioxidant enzymes are induced by TNF and responsible for elimination of ROS
    • Sasazuki T., Okazaki T., Tada K., Sakon-Komazawa S., Katano M., Tanaka M., et al. Genome wide analysis of TNF-inducible genes reveals that antioxidant enzymes are induced by TNF and responsible for elimination of ROS. Mol Immunol 41 5 (2004) 547-551
    • (2004) Mol Immunol , vol.41 , Issue.5 , pp. 547-551
    • Sasazuki, T.1    Okazaki, T.2    Tada, K.3    Sakon-Komazawa, S.4    Katano, M.5    Tanaka, M.6
  • 126
    • 0034043956 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: dysregulation of cytokine, chemokine, and toll-like receptor 2 and 4 gene expression
    • Medvedev A.E., Kopydlowski K.M., and Vogel S.N. Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: dysregulation of cytokine, chemokine, and toll-like receptor 2 and 4 gene expression. J Immunol 164 11 (2000) 5564-5574
    • (2000) J Immunol , vol.164 , Issue.11 , pp. 5564-5574
    • Medvedev, A.E.1    Kopydlowski, K.M.2    Vogel, S.N.3
  • 127
    • 0742324860 scopus 로고    scopus 로고
    • TLR signaling pathways
    • Takeda K., and Akira S. TLR signaling pathways. Semin Immunol 16 1 (2004) 3-9
    • (2004) Semin Immunol , vol.16 , Issue.1 , pp. 3-9
    • Takeda, K.1    Akira, S.2
  • 128
    • 0742307236 scopus 로고    scopus 로고
    • Toll receptor families: structure and function
    • Akira S. Toll receptor families: structure and function. Semin Immunol 16 1 (2004) 1-2
    • (2004) Semin Immunol , vol.16 , Issue.1 , pp. 1-2
    • Akira, S.1
  • 129
    • 0025166114 scopus 로고
    • CD14 a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Wright S.D., Ramos R.A., Tobias P.S., Ulevitch R.J., and Mathison J.C. CD14 a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 249 4975 (1990) 1431-1433
    • (1990) Science , vol.249 , Issue.4975 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3    Ulevitch, R.J.4    Mathison, J.C.5
  • 130
    • 0027245548 scopus 로고
    • Involvement of CD14 in lipopolysaccharide-induced tumor necrosis factor-alpha IL-6 and IL-8 release by human monocytes and alveolar macrophages
    • Dentener M.A., Bazil V., Von Asmuth E.J., Ceska M., and Buurman W.A. Involvement of CD14 in lipopolysaccharide-induced tumor necrosis factor-alpha IL-6 and IL-8 release by human monocytes and alveolar macrophages. J Immunol 150 7 (1993) 2885-2891
    • (1993) J Immunol , vol.150 , Issue.7 , pp. 2885-2891
    • Dentener, M.A.1    Bazil, V.2    Von Asmuth, E.J.3    Ceska, M.4    Buurman, W.A.5
  • 132
    • 0842321777 scopus 로고    scopus 로고
    • Involvement of reactive oxygen species in Toll-like receptor 4-dependent activation of NF-kappa B
    • Asehnoune K., Strassheim D., Mitra S., Kim J.Y., and Abraham E. Involvement of reactive oxygen species in Toll-like receptor 4-dependent activation of NF-kappa B. J Immunol 172 4 (2004) 2522-2529
    • (2004) J Immunol , vol.172 , Issue.4 , pp. 2522-2529
    • Asehnoune, K.1    Strassheim, D.2    Mitra, S.3    Kim, J.Y.4    Abraham, E.5
  • 133
    • 1842588614 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species differentially regulate Toll-like receptor 4-mediated activation of NF-kappa B and interleukin-8 expression
    • Ryan K.A., Smith Jr. M.F., Sanders M.K., and Ernst P.B. Reactive oxygen and nitrogen species differentially regulate Toll-like receptor 4-mediated activation of NF-kappa B and interleukin-8 expression. Infect Immun 72 4 (2004) 2123-2130
    • (2004) Infect Immun , vol.72 , Issue.4 , pp. 2123-2130
    • Ryan, K.A.1    Smith Jr., M.F.2    Sanders, M.K.3    Ernst, P.B.4
  • 134
    • 0035839437 scopus 로고    scopus 로고
    • Lipopolysaccharide induces Rac1-dependent reactive oxygen species formation and coordinates tumor necrosis factor-alpha secretion through IKK regulation of NF-kappa B
    • Sanlioglu S., Williams C.M., Samavati L., Butler N.S., Wang G., McCray Jr. P.B., et al. Lipopolysaccharide induces Rac1-dependent reactive oxygen species formation and coordinates tumor necrosis factor-alpha secretion through IKK regulation of NF-kappa B. J Biol Chem 276 32 (2001) 30188-30198
    • (2001) J Biol Chem , vol.276 , Issue.32 , pp. 30188-30198
    • Sanlioglu, S.1    Williams, C.M.2    Samavati, L.3    Butler, N.S.4    Wang, G.5    McCray Jr., P.B.6
  • 135
    • 4644350365 scopus 로고    scopus 로고
    • Cutting edge: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B
    • Park H.S., Jung H.Y., Park E.Y., Kim J., Lee W.J., and Bae Y.S. Cutting edge: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B. J Immunol 173 6 (2004) 3589-3593
    • (2004) J Immunol , vol.173 , Issue.6 , 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
  • 136
    • 20644433073 scopus 로고    scopus 로고
    • ROS-dependent activation of the TRAF6-ASK1-p38 pathway is selectively required for TLR4-mediated innate immunity
    • Matsuzawa A., Saegusa K., Noguchi T., Sadamitsu C., Nishitoh H., Nagai S., et al. ROS-dependent activation of the TRAF6-ASK1-p38 pathway is selectively required for TLR4-mediated innate immunity. Nat Immunol 6 6 (2005) 587-592
    • (2005) Nat Immunol , vol.6 , Issue.6 , pp. 587-592
    • Matsuzawa, A.1    Saegusa, K.2    Noguchi, T.3    Sadamitsu, C.4    Nishitoh, H.5    Nagai, S.6
  • 137
    • 0037430971 scopus 로고    scopus 로고
    • Oxidative stress in cell culture: an under-appreciated problem?
    • Halliwell B. Oxidative stress in cell culture: an under-appreciated problem?. FEBS Lett 540 1-3 (2003) 3-6
    • (2003) FEBS Lett , vol.540 , Issue.1-3 , pp. 3-6
    • Halliwell, B.1


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