메뉴 건너뛰기




Volumn 65, Issue , 2013, Pages 162-174

Bidirectional regulation of NF-κB by reactive oxygen species: A role of unfolded protein response

Author keywords

Endoplasmic reticulum stress; NF B; Reactive oxygen species; Unfolded protein response

Indexed keywords

HEME OXYGENASE 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 84884556412     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.06.020     Document Type: Review
Times cited : (247)

References (167)
  • 2
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • P.A. Baeuerle, and T. Henkel Function and activation of NF-κB in the immune system Annu. Rev. Immunol. 12 1994 141 179
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 3
    • 0036546501 scopus 로고    scopus 로고
    • NF-κB in cancer: From innocent bystander to major culprit
    • M. Karin, Y. Cao, F.R. Greten, and Z.W. Li NF-κB in cancer: from innocent bystander to major culprit Nat. Rev. Cancer 2 2002 301 310 (Pubitemid 37328783)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.4 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.-W.4
  • 4
    • 0030615201 scopus 로고    scopus 로고
    • Nuclear factor-κB - A pivotal transcription factor in chronic inflammatory diseases
    • DOI 10.1056/NEJM199704103361506
    • P.J. Barnes, and M. Karin Nuclear factor-κB: a pivotal transcription factor in chronic inflammatory diseases N. Engl. J. Med. 336 1997 1066 1071 (Pubitemid 27163860)
    • (1997) New England Journal of Medicine , vol.336 , Issue.15 , pp. 1066-1071
    • Barnes, P.J.1    Karin, M.2
  • 5
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • M.S. Hayden, and S. Ghosh Signaling to NF-κB Genes Dev. 18 2004 2195 2224
    • (2004) Genes Dev. , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 6
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation
    • DOI 10.1016/S0092-8674(00)81466-X
    • S. Yamaoka, G. Courtois, C. Bessia, S.T. Whiteside, R. Weil, F. Agou, H.E. Kirk, R.J. Kay, and A. Israël Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation Cell 93 1998 1231 1240 (Pubitemid 28307427)
    • (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    Kirk, H.E.7    Kay, R.J.8    Israel, A.9
  • 7
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for Iκb phosphorylation and NF-κB activation
    • DOI 10.1016/S0092-8674(00)80406-7
    • E. Zandi, D.M. Rothwarf, M. Delhase, M. Hayakawa, and M. Karin The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation Cell 91 1997 243 252 (Pubitemid 27456391)
    • (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
  • 8
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-κB activation pathways and their role in innate and adaptive immunity
    • DOI 10.1016/j.it.2004.03.008, PII S1471490604001000
    • G. Bonizzi, and M. Karin The two NF-κB activation pathways and their role in innate and adaptive immunity Trends Immunol. 25 2004 280 288 (Pubitemid 38610351)
    • (2004) Trends in Immunology , vol.25 , Issue.6 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 9
    • 0037064536 scopus 로고    scopus 로고
    • Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family
    • DOI 10.1016/S0167-4889(02)00320-8, PII S0167488902003208
    • M.U. Martin, and H. Wesche Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family Biochim. Biophys. Acta 1592 2002 265 280 (Pubitemid 35284883)
    • (2002) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1592 , Issue.3 , pp. 265-280
    • Martin, M.U.1    Wesche, H.2
  • 10
    • 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
    • A. Devin, A. Cook, Y. Lin, Y. Rodriguez, M. Kelliher, and Z. Liu 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 2000 419 429
    • (2000) Immunity , vol.12 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3    Rodriguez, Y.4    Kelliher, M.5    Liu, Z.6
  • 11
    • 30044442866 scopus 로고    scopus 로고
    • How Toll-like receptors signal: What we know and what we don't know
    • DOI 10.1016/j.coi.2005.11.012, PII S0952791505002050, Innate Immunity/Antigen Processing and Recognition
    • L.A. O'Neill How Toll-like receptors signal: what we know and what we don't know Curr. Opin. Immunol. 18 2006 3 9 (Pubitemid 43049641)
    • (2006) Current Opinion in Immunology , vol.18 , Issue.1 , pp. 3-9
    • O'Neill, L.A.J.1
  • 12
    • 18644380147 scopus 로고    scopus 로고
    • The lymphotoxin-β receptor induces different patterns of gene expression via two NF-κB pathways
    • DOI 10.1016/S1074-7613(02)00423-5
    • E. Dejardin, N.M. Droin, M. Delhase, E. Haas, Y. Cao, C. Makris, Z.W. Li, M. Karin, C.F. Ware, and D.R. Green The lymphotoxin-β receptor induces different patterns of gene expression via two NF-κB pathways Immunity 17 2002 525 535 (Pubitemid 35223540)
    • (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    Li, Z.-W.7    Karin, M.8    Ware, C.F.9    Green, D.R.10
  • 13
    • 0036794398 scopus 로고    scopus 로고
    • BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells
    • DOI 10.1038/ni842
    • E. Claudio, K. Brown, S. Park, H. Wang, and U. Siebenlist BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells Nat. Immunol. 3 2002 958 965 (Pubitemid 35154010)
    • (2002) Nature Immunology , vol.3 , Issue.10 , pp. 958-965
    • Claudio, E.1    Brown, K.2    Park, S.3    Wang, H.4    Siebenlist, U.5
  • 15
    • 0034745420 scopus 로고    scopus 로고
    • NF-κB-inducing kinase regulates the processing of NF-κB2 p100
    • DOI 10.1016/S1097-2765(01)00187-3
    • G. Xiao, E.W. Harhaj, and S.C. Sun NF-κB-inducing kinase regulates the processing of NF-κB2 p100 Mol. Cell 7 2001 401 409 (Pubitemid 32206507)
    • (2001) Molecular Cell , vol.7 , Issue.2 , pp. 401-409
    • Xiao, G.1    Harhaj, E.W.2    Sun, S.-C.3
  • 17
    • 0025820624 scopus 로고
    • A role for oxygen radicals as second messengers
    • R. Schreck, and P.A. Baeuerle A role for oxygen radicals as second messengers Trends Cell Biol. 1 1991 39 42 (Pubitemid 121002486)
    • (1991) Trends in Cell Biology , vol.1 , Issue.2-3 , pp. 39-42
    • Schreck, R.1    Baeuerle, P.A.2
  • 18
    • 0030612264 scopus 로고    scopus 로고
    • Selective inhibition of IκBα phosphorylation and HIV-1 LTR-directed gene expression by novel antioxidant compounds
    • DOI 10.1006/viro.1997.8642
    • R. Lee, P. Beauparlant, H. Elford, P. Ponka, and J. Hiscott Selective inhibition of lκBα phosphorylation and HIV-1 LTR-directed gene expression by novel antioxidant compounds Virology 234 1997 277 290 (Pubitemid 27360119)
    • (1997) Virology , vol.234 , Issue.2 , pp. 277-290
    • Lee, R.1    Beauparlant, P.2    Elford, H.3    Ponka, P.4    Hiscott, J.5
  • 19
    • 0030425975 scopus 로고    scopus 로고
    • Interleukin-1β induces nuclear factor κB in epithelial cells independently of the production of reactive oxygen intermediates
    • G. Bonizzi, E. Dejardin, B. Piret, J. Piette, M.P. Merville, and V. Bours Interleukin-1β induces nuclear factor-κB in epithelial cells independently of the production of reactive oxygen intermediates Eur. J. Biochem. 242 1996 544 549 (Pubitemid 27121135)
    • (1996) European Journal of Biochemistry , vol.242 , Issue.3 , pp. 544-549
    • Bonizzl, G.1    Dejardin, E.2    Piret, B.3    Piette, J.4    Merville, M.-P.5    Bours, V.6
  • 20
    • 0031575774 scopus 로고    scopus 로고
    • Redox regulation of lipopolysaccharide(LPS)-induced interleukin-8 (IL-8) gene expression mediated by NFκB and AP-1 in human astrocytoma U373 cells
    • DOI 10.1006/bbrc.1997.6264
    • C. Tanaka, H. Kamata, H. Takeshita, H. Yagisawa, and H. Hirata Redox regulation of lipopolysaccharide (LPS)-induced interleukin-8 (IL-8) gene expression mediated by NF-κB and AP-1 in human astrocytoma U373 cells Biochem. Biophys. Res. Commun. 232 1997 568 573 (Pubitemid 27216262)
    • (1997) Biochemical and Biophysical Research Communications , vol.232 , Issue.2 , pp. 568-573
    • Tanaka, C.1    Kamata, H.2    Takeshita, H.3    Yagisawa, H.4    Hirata, H.5
  • 21
    • 0032889677 scopus 로고    scopus 로고
    • Redox regulation of cellular signalling
    • DOI 10.1016/S0898-6568(98)00037-0, PII S0898656898000370
    • H. Kamata, and H. Hirata Redox regulation of cellular signalling Cell. Signal. 11 1999 1 14 (Pubitemid 28546635)
    • (1999) Cellular Signalling , vol.11 , Issue.1 , pp. 1-14
    • Kamata, H.1    Hirata, H.2
  • 22
    • 0036829062 scopus 로고    scopus 로고
    • Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors
    • DOI 10.1016/S0898-6568(02)00053-0, PII S0898656802000530
    • J.J. Haddad Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors Cell. Signal. 14 2002 879 897 (Pubitemid 35247561)
    • (2002) Cellular Signalling , vol.14 , Issue.11 , pp. 879-897
    • Haddad, J.J.1
  • 23
    • 0033815334 scopus 로고    scopus 로고
    • Nitrosation and oxidation in the regulation of gene expression
    • H.E. Marshall, K. Merchant, and J.S. Stamler Nitrosation and oxidation in the regulation of gene expression FASEB J. 14 2000 1889 1900
    • (2000) FASEB J. , vol.14 , pp. 1889-1900
    • Marshall, H.E.1    Merchant, K.2    Stamler, J.S.3
  • 25
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • V. Adler, Z. Yin, K.D. Tew, and Z. Ronai Role of redox potential and reactive oxygen species in stress signaling Oncogene 18 1999 6104 6111
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 26
    • 78650894319 scopus 로고    scopus 로고
    • Crosstalk of reactive oxygen species and NF-κB signaling
    • M.J. Morgan, and Z.G. Liu Crosstalk of reactive oxygen species and NF-κB signaling Cell Res. 21 2011 103 115
    • (2011) Cell Res. , vol.21 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.G.2
  • 27
    • 33750523632 scopus 로고    scopus 로고
    • NF-κB activation by reactive oxygen species: Fifteen years later
    • DOI 10.1016/j.bcp.2006.04.011, PII S0006295206002255, Cell Signalling, Transcription and Translation as Therapeutic Tergets
    • G. Gloire, S. Legrand-Poels, and J. Piette NF-κB activation by reactive oxygen species: fifteen years later Biochem. Pharmacol. 72 2006 1493 1505 (Pubitemid 44666727)
    • (2006) Biochemical Pharmacology , vol.72 , Issue.11 , pp. 1493-1505
    • Gloire, G.1    Legrand-Poels, S.2    Piette, J.3
  • 28
    • 0037413711 scopus 로고    scopus 로고
    • Protein kinase D mediates a stress-induced NF-κB activation and survival pathway
    • DOI 10.1093/emboj/cdg009
    • P. Storz, and A. Toker Protein kinase D mediates a stress-induced NF-κB activation and survival pathway EMBO J. 22 2003 109 120 (Pubitemid 36091274)
    • (2003) EMBO Journal , vol.22 , Issue.1 , pp. 109-120
    • Storz, P.1    Toker, A.2
  • 29
    • 1642379541 scopus 로고    scopus 로고
    • Protein Kinase Cδ Selectively Regulates Protein Kinase D-Dependent Activation of NF-κB in Oxidative Stress Signaling
    • DOI 10.1128/MCB.24.7.2614-2626.2004
    • P. Storz, H. Döppler, and A. Toker Protein kinase Cδ selectively regulates protein kinase D-dependent activation of NF-κB in oxidative stress signaling Mol. Cell. Biol. 24 2004 2614 2626 (Pubitemid 38381256)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.7 , pp. 2614-2626
    • Storz, P.1    Doppler, H.2    Toker, A.3
  • 30
    • 33644990327 scopus 로고    scopus 로고
    • 2-mediated activation of NF-κB-inducing kinase
    • 2-mediated activation of NF-κB-inducing kinase J. Biol. Chem. 281 2006 1495 1505
    • (2006) J. Biol. Chem. , vol.281 , pp. 1495-1505
    • Li, Q.1    Engelhardt, J.F.2
  • 31
    • 0037449777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of IκBα activates NFκB through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation
    • DOI 10.1074/jbc.M206718200
    • C. Fan, Q. Li, D. Ross, and J.F. Engelhardt Tyrosine phosphorylation of IκBα activates NFκB through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation J. Biol. Chem. 278 2003 2072 2080 (Pubitemid 36801452)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.3 , pp. 2072-2080
    • Fan, C.1    Li, Q.2    Ross, D.3    Engelhardt, J.F.4
  • 32
    • 33748433789 scopus 로고    scopus 로고
    • Restoration of SHIP-1 activity in human leukemic cells modifies NF-κB activation pathway and cellular survival upon oxidative stress
    • DOI 10.1038/sj.onc.1209542, PII 1209542
    • G. Gloire, E. Charlier, S. Rahmouni, C. Volanti, A. Chariot, C. Erneux, and J. Piette Restoration of SHIP-1 activity in human leukemic cells modifies NF-κB activation pathway and cellular survival upon oxidative stress Oncogene 25 2006 5485 5494 (Pubitemid 44344099)
    • (2006) Oncogene , vol.25 , Issue.40 , pp. 5485-5494
    • Gloire, G.1    Charlier, E.2    Rahmouni, S.3    Volanti, C.4    Chariot, A.5    Erneux, C.6    Piette, J.7
  • 33
    • 0034655179 scopus 로고    scopus 로고
    • Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl- terminal PEST domain of IκBα in NF-κB activation by an oxidative stress
    • S. Schoonbroodt, V. Ferreira, M. Best-Belpomme, J.R. Boelaert, S. Legrand-Poels, M. Korner, and J. Piette Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress J. Immunol. 164 2000 4292 4300 (Pubitemid 30215091)
    • (2000) Journal of Immunology , 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    Piette, J.7
  • 34
    • 0037591401 scopus 로고    scopus 로고
    • Hydrogen peroxide activates NF-κB through tyrosine phosphorylation of IκBα and serine phosphorylation of p65. Evidence for the involvement of IκBα kinase and Syk protein-tyrosine kinase
    • DOI 10.1074/jbc.M212389200
    • Y. Takada, A. Mukhopadhyay, G.C. Kundu, G.H. Mahabeleshwar, S. Singh, and B.B. Aggarwal Hydrogen peroxide activates NF-κB through tyrosine phosphorylation of IκBα and serine phosphorylation of p65: evidence for the involvement of IκBα kinase and Syk protein-tyrosine kinase J. Biol. Chem. 278 2003 24233 24241 (Pubitemid 36830260)
    • (2003) Journal of Biological Chemistry , 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
  • 36
    • 0035082793 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent activation of NF-κB: Requirement for p56 LCK and ZAP-70 protein tyrosine kinases
    • DOI 10.1046/j.1432-1327.2001.02028.x
    • A. Livolsi, V. Busuttil, V. Imbert, R.T. Abraham, and J.F. Peyron Tyrosine phosphorylation-dependent activation of NF-κB. Requirement for p56 LCK and ZAP-70 protein tyrosine kinases Eur. J. Biochem. 268 2001 1508 1515 (Pubitemid 32231906)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.5 , pp. 1508-1515
    • Livolsi, A.1    Busuttil, V.2    Imbert, V.3    Abraham, R.T.4    Peyron, J.-F.5
  • 38
    • 34047244896 scopus 로고    scopus 로고
    • 2+-dependent necrotic cell death through calpain-triggered mitochondrial depolarization and reactive oxygen species-mediated inhibition of nuclear factor-κB activity. Chem
    • 2+-dependent necrotic cell death through calpain-triggered mitochondrial depolarization and reactive oxygen species-mediated inhibition of nuclear factor-κB activity. Chem Res. Toxicol. 20 2007 406 415
    • (2007) Res. Toxicol. , vol.20 , pp. 406-415
    • Yang, P.M.1    Chen, H.C.2    Tsai, J.S.3    Lin, L.Y.4
  • 39
    • 33645810796 scopus 로고    scopus 로고
    • Cadmium-induced apoptosis in rat kidney epithelial cells involves decrease in nuclear factor-κB activity
    • J. Xie, and Z.A. Shaikh Cadmium-induced apoptosis in rat kidney epithelial cells involves decrease in nuclear factor-κB activity Toxicol. Sci. 91 2006 299 308
    • (2006) Toxicol. Sci. , vol.91 , pp. 299-308
    • Xie, J.1    Shaikh, Z.A.2
  • 40
    • 0034668171 scopus 로고    scopus 로고
    • Oxidative stress interference with the nuclear factor-κB activation pathways
    • S. Schoonbroodt, and J. Piette Oxidative stress interference with the nuclear factor-κB activation pathways Biochem. Pharmacol. 60 2000 1075 1083
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1075-1083
    • Schoonbroodt, S.1    Piette, J.2
  • 41
    • 0030907987 scopus 로고    scopus 로고
    • PI3K: Downstream AKTion blocks apoptosis
    • DOI 10.1016/S0092-8674(00)81883-8
    • T.F. Franke, D.R. Kaplan, and L.C. Cantley PI3K: downstream AKTion blocks apoptosis Cell 88 1997 435 437 (Pubitemid 27154408)
    • (1997) Cell , vol.88 , Issue.4 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 43
    • 0034839145 scopus 로고    scopus 로고
    • Effect of the Alzheimer amyloid fragment Aβ(25-35) on Akt/PKB kinase and survival of PC12 cells
    • DOI 10.1046/j.1471-4159.2001.00472.x
    • D. Martín, M. Salinas, R. López-Valdaliso, E. Serrano, M. Recuero, and A. Cuadrado Effect of the Alzheimer amyloid fragment Aβ(25-35) on Akt/PKB kinase and survival of PC12 cells J. Neurochem. 78 2001 1000 1008 (Pubitemid 32823149)
    • (2001) Journal of Neurochemistry , vol.78 , Issue.5 , pp. 1000-1008
    • Martin, D.1    Salinas, M.2    Lopez-Valdaliso, R.3    Serrano, E.4    Recuero, M.5    Cuadrado, A.6
  • 45
    • 0030785701 scopus 로고    scopus 로고
    • Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27
    • DOI 10.1016/S0014-5793(97)00541-3, PII S0014579397005413
    • H. Konishi, H. Matsuzaki, M. Tanaka, Y. Takemura, S. Kuroda, Y. Ono, and U. Kikkawa Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27 FEBS Lett. 410 1997 493 498 (Pubitemid 27304124)
    • (1997) FEBS Letters , vol.410 , Issue.2-3 , pp. 493-498
    • Konishi, H.1    Matsuzaki, H.2    Tanaka, M.3    Takemura, Y.4    Kuroda, S.5    Ono, Y.6    Kikkawa, U.7
  • 46
    • 0032533546 scopus 로고    scopus 로고
    • 2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2
    • 2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2 Biochem. J. 336 1998 241 246 (Pubitemid 28532583)
    • (1998) Biochemical Journal , vol.336 , Issue.1 , pp. 241-246
    • Shaw, M.1    Cohen, P.2    Alessi, D.R.3
  • 47
    • 0034640524 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-dependent Akt activation by oxidative stress enhances cell survival
    • DOI 10.1074/jbc.275.19.14624
    • X. Wang, K.D. McCullough, T.F. Franke, and N.J. Holbrook Epidermal growth factor receptor-dependent Akt activation by oxidative stress enhances cell survival J. Biol. Chem. 275 2000 14624 14631 (Pubitemid 30339753)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14624-14631
    • Wang, X.1    McCullough, K.D.2    Franke, T.F.3    Holbrook, N.J.4
  • 49
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin Exerts an Antiapoptotic Effect by Regulating the Redox State of Akt
    • DOI 10.1074/jbc.M310171200
    • H. Murata, Y. Ihara, H. Nakamura, J. Yodoi, K. Sumikawa, and T. Kondo Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt J. Biol. Chem. 278 2003 50226 50233 (Pubitemid 37548863)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 50
    • 0028948497 scopus 로고
    • Activation of the transcription factor NF-κB in human tracheobronchial epithelial cells by inflammatory stimuli
    • B. Jany, R. Betz, and R. Schreck Activation of the transcription factor NF-κB in human tracheobronchial epithelial cells by inflammatory stimuli Eur. Respir. J. 8 1995 387 391
    • (1995) Eur. Respir. J. , vol.8 , pp. 387-391
    • Jany, B.1    Betz, R.2    Schreck, R.3
  • 51
    • 0037157177 scopus 로고    scopus 로고
    • Hydrogen peroxide activates IκB kinases through phosphorylation of serine residues in the activation loops
    • DOI 10.1016/S0014-5793(02)02712-6, PII S0014579302027126
    • H. Kamata, T. Manabe, S. Oka, K. Kamata, and H. Hirata Hydrogen peroxide activates IκB kinases through phosphorylation of serine residues in the activation loops FEBS Lett. 519 2002 231 237 (Pubitemid 34522025)
    • (2002) FEBS Letters , vol.519 , Issue.1-3 , pp. 231-237
    • Kamata, H.1    Manabe, T.2    Oka, S.-I.3    Kamata, K.4    Hirata, H.5
  • 54
    • 0029170274 scopus 로고
    • The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB
    • K.N. Schmidt, P. Amstad, P. Cerutti, and P.A. Baeuerle The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB Chem. Biol. 2 1995 13 22
    • (1995) Chem. Biol. , vol.2 , pp. 13-22
    • Schmidt, K.N.1    Amstad, P.2    Cerutti, P.3    Baeuerle, P.A.4
  • 56
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation
    • DOI 10.1016/S0006-291X(02)00268-1
    • R.K. Rao, and L.W. Clayton Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation Biochem. Biophys. Res. Commun. 293 2002 610 616 (Pubitemid 34694253)
    • (2002) Biochemical and Biophysical Research Communications , vol.293 , Issue.1 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 57
    • 0141703513 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-induced IKK phosphorylation of NF-κB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway
    • DOI 10.1074/jbc.M301598200
    • H. Sakurai, S. Suzuki, N. Kawasaki, H. Nakano, T. Okazaki, A. Chino, T. Doi, and I. Saiki Tumor necrosis factor-α-induced IKK phosphorylation of NF-κB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway J. Biol. Chem. 278 2003 36916 36923 (Pubitemid 37140026)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36916-36923
    • Sakurai, H.1    Suzuki, S.2    Kawasaki, N.3    Nakano, H.4    Okazaki, T.5    Chino, A.6    Doi, T.7    Saiki, I.8
  • 58
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • DOI 10.1128/MCB.21.20.7065-7077.2001
    • B.P. Ashburner, S.D. Westerheide, and A.S. Baldwin Jr. The p65 (RelA) subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression Mol. Cell. Biol. 21 2001 7065 7077 (Pubitemid 32916079)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.20 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin Jr., A.S.3
  • 59
    • 4143070452 scopus 로고    scopus 로고
    • Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-κB and pro-inflammatory gene expression
    • DOI 10.1016/j.bcp.2004.05.042, PII S0006295204003843
    • I. Rahman, J. Marwick, and P. Kirkham Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-κB and pro-inflammatory gene expression Biochem. Pharmacol. 68 2004 1255 1267 (Pubitemid 39094292)
    • (2004) Biochemical Pharmacology , vol.68 , Issue.6 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 60
    • 0842308109 scopus 로고    scopus 로고
    • Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: Role of tyrosine nitration
    • DOI 10.1016/j.bbrc.2004.01.046
    • K. Ito, T. Hanazawa, K. Tomita, P.J. Barnes, and I.M. Adcock Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: role of tyrosine nitration Biochem. Biophys. Res. Commun. 315 2004 240 245 (Pubitemid 38175212)
    • (2004) Biochemical and Biophysical Research Communications , vol.315 , Issue.1 , pp. 240-245
    • Ito, K.1    Hanazawa, T.2    Tomita, K.3    Barnes, P.J.4    Adcock, I.M.5
  • 61
    • 34249289745 scopus 로고    scopus 로고
    • 276 phosphorylation and enhanceosome formation is mediated by an ROS-dependent PKAc pathway
    • DOI 10.1016/j.cellsig.2007.01.020, PII S0898656807000344
    • M. Jamaluddin, S. Wang, I. Boldogh, B. Tian, and A.R. Brasier TNF-α-induced NF-κB/RelA Ser276 phosphorylation and enhanceosome formation is mediated by an ROS-dependent PKAc pathway Cell. Signal. 19 2007 1419 1433 (Pubitemid 46818908)
    • (2007) Cellular Signalling , vol.19 , Issue.7 , pp. 1419-1433
    • Jamaluddin, M.1    Wang, S.2    Boldogh, I.3    Tian, B.4    Brasier, A.R.5
  • 63
    • 0035929670 scopus 로고    scopus 로고
    • Cytokine-induced activation of nuclear factor-κB is inhibited by hydrogen peroxide through oxidative inactivation of IκB kinase
    • S.H. Korn, E.F. Wouters, N. Vos, and Y.M. Janssen-Heininger Cytokine-induced activation of nuclear factor-κB is inhibited by hydrogen peroxide through oxidative inactivation of IκB kinase J. Biol. Chem. 276 2001 35693 35700
    • (2001) J. Biol. Chem. , vol.276 , pp. 35693-35700
    • Korn, S.H.1    Wouters, E.F.2    Vos, N.3    Janssen-Heininger, Y.M.4
  • 64
    • 27144547642 scopus 로고    scopus 로고
    • Peroxynitrite is a potent inhibitor of NF-κB activation triggered by inflammatory stimuli in cardiac and endothelial cell lines
    • DOI 10.1074/jbc.M501977200
    • S. Levrand, B. Pesse, F. Feihl, B. Waeber, P. Pacher, J. Rolli, M.D. Schaller, and L. Liaudet Peroxynitrite is a potent inhibitor of NF-κB activation triggered by inflammatory stimuli in cardiac and endothelial cell lines J. Biol. Chem. 280 2005 34878 34887 (Pubitemid 41504622)
    • (2005) Journal of Biological Chemistry , 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    Schaller, M.-D.7    Liaudet, L.8
  • 65
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • DOI 10.1016/j.coph.2007.06.003, PII S1471489207001038, Cancer/Immunomodulation
    • M.M. Gallogly, and J.J. Mieyal Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress Curr. Opin. Pharmacol. 7 2007 381 391 (Pubitemid 47304000)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.4 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 66
    • 51049091712 scopus 로고    scopus 로고
    • Regulation by reversible S-glutathionylation: Molecular targets implicated in inflammatory diseases
    • M.D. Shelton, and J.J. Mieyal Regulation by reversible S-glutathionylation: molecular targets implicated in inflammatory diseases Mol. Cells 25 2008 332 346
    • (2008) Mol. Cells , vol.25 , pp. 332-346
    • Shelton, M.D.1    Mieyal, J.J.2
  • 69
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFκB
    • DOI 10.1074/jbc.M610934200
    • S. Qanungo, D.W. Starke, H.V. Pai, J.J. Mieyal, and A.L. Nieminen Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NF-κB J. Biol. Chem. 282 2007 18427 18436 (Pubitemid 47100260)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18427-18436
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.-L.5
  • 70
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-κB by reduction of a disulphide bond involving cysteine 62
    • J.R. Matthews, N. Wakasugi, J.L. Virelizier, J. Yodoi, and R.T. Hay Thioredoxin regulates the DNA binding activity of NF-κB by reduction of a disulphide bond involving cysteine 62 Nucleic Acids Res. 20 1992 3821 3830
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3    Yodoi, J.4    Hay, R.T.5
  • 71
    • 0034745011 scopus 로고    scopus 로고
    • Control of IκBα proteolysis by the ubiquitin-proteasome pathway
    • K. Tanaka, T. Kawakami, K. Tateishi, H. Yashiroda, and T. Chiba Control of IκBα proteolysis by the ubiquitin-proteasome pathway Biochimie 83 2001 351 356
    • (2001) Biochimie , vol.83 , pp. 351-356
    • Tanaka, K.1    Kawakami, T.2    Tateishi, K.3    Yashiroda, H.4    Chiba, T.5
  • 73
    • 0031893232 scopus 로고    scopus 로고
    • Redox regulation of ubiquitin-conjugating enzymes: Mechanistic insights using the thiol-specific oxidant diamide
    • M. Obin, F. Shang, X. Gong, G. Handelman, J. Blumberg, and A. Taylor Redox regulation of ubiquitin-conjugating enzymes: mechanistic insights using the thiol-specific oxidant diamide FASEB J. 12 1998 561 569 (Pubitemid 28183515)
    • (1998) FASEB Journal , vol.12 , Issue.7 , pp. 561-569
    • Obin, M.1    Shang, F.2    Gong, X.3    Handelman, G.4    Blumberg, J.5    Taylor, A.6
  • 74
    • 0037414784 scopus 로고    scopus 로고
    • 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • DOI 10.1074/jbc.M209282200
    • M. Demasi, G.M. Silva, and L.E. Netto 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated J. Biol. Chem. 278 2003 679 685 (Pubitemid 36043622)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.S.3
  • 75
    • 57449104348 scopus 로고    scopus 로고
    • Sustained oxidative stress inhibits NF-κB activation partially via inactivating the proteasome
    • M. Wu, Q. Bian, Y. Liu, A.F. Fernandes, A. Taylor, P. Pereira, and F. Shang Sustained oxidative stress inhibits NF-κB activation partially via inactivating the proteasome Free Radic. Biol. Med. 46 2009 62 69
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 62-69
    • Wu, M.1    Bian, Q.2    Liu, Y.3    Fernandes, A.F.4    Taylor, A.5    Pereira, P.6    Shang, F.7
  • 76
    • 35648973301 scopus 로고    scopus 로고
    • Commensal bacteria modulate cullin-dependent signaling via generation of reactive oxygen species
    • DOI 10.1038/sj.emboj.7601867, PII 7601867
    • A. Kumar, H. Wu, L.S. Collier-Hyams, J.M. Hansen, T. Li, K. Yamoah, Z.Q. Pan, D.P. Jones, and A.S. Neish Commensal bacteria modulate cullin-dependent signaling via generation of reactive oxygen species EMBO J. 26 2007 4457 4466 (Pubitemid 350036625)
    • (2007) EMBO Journal , vol.26 , Issue.21 , pp. 4457-4466
    • Kumar, A.1    Wu, H.2    Collier-Hyams, L.S.3    Hansen, J.M.4    Li, T.5    Yamoah, K.6    Pan, Z.-Q.7    Jones, D.P.8    Neish, A.S.9
  • 77
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in NF-κB activation
    • K. Iwai Diverse ubiquitin signaling in NF-κB activation Trends Cell Biol. 22 2012 355 364
    • (2012) Trends Cell Biol. , vol.22 , pp. 355-364
    • Iwai, K.1
  • 78
    • 84867905831 scopus 로고    scopus 로고
    • Linear ubiquitination: A novel NF-κB regulatory mechanism for inflammatory and immune responses by the LUBAC ubiquitin ligase complex
    • F. Tokunaga, and K. Iwai Linear ubiquitination: a novel NF-κB regulatory mechanism for inflammatory and immune responses by the LUBAC ubiquitin ligase complex Endocr. J. 59 2012 641 652
    • (2012) Endocr. J. , vol.59 , pp. 641-652
    • Tokunaga, F.1    Iwai, K.2
  • 79
    • 0043268709 scopus 로고    scopus 로고
    • Heme oxygenase-1: Unleashing the protective properties of heme
    • DOI 10.1016/S1471-4906(03)00181-9
    • L.E. Otterbein, M.P. Soares, K. Yamashita, and F.H. Bach Heme oxygenase-1: unleashing the protective properties of heme Trends Immunol. 24 2003 449 455 (Pubitemid 36928103)
    • (2003) Trends in Immunology , vol.24 , Issue.8 , pp. 449-455
    • Otterbein, L.E.1    Soares, M.P.2    Yamashita, K.3    Bach, F.H.4
  • 80
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • DOI 10.1073/pnas.86.1.99
    • S.M. Keyse, and R.M. Tyrrell Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite Proc. Natl. Acad. Sci. USA 86 1989 99 103 (Pubitemid 19036341)
    • (1989) Proceedings of the National Academy of Sciences of the United States of America , vol.86 , Issue.1 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 81
    • 10344228211 scopus 로고    scopus 로고
    • Phosphorylation and hypoxia-induced heme oxygenase-1 gene expression in cardiomyocytes
    • G. Wu, J. Marín-García, T.B. Rogers, E.G. Lakatta, and X. Long Phosphorylation and hypoxia-induced heme oxygenase-1 gene expression in cardiomyocytes J. Card. Fail. 10 2004 519 526
    • (2004) J. Card. Fail. , vol.10 , pp. 519-526
    • Wu, G.1    Marín-García, J.2    Rogers, T.B.3    Lakatta, E.G.4    Long, X.5
  • 82
    • 84863548057 scopus 로고    scopus 로고
    • PI3K/Akt signaling pathway-induced heme oxygenase-1 upregulation mediates the adaptive cytoprotection of hydrogen peroxide preconditioning against oxidative injury in PC12 cells
    • L. Mo, C. Yang, M. Gu, D. Zheng, L. Lin, X. Wang, A. Lan, F. Hu, and J. Feng PI3K/Akt signaling pathway-induced heme oxygenase-1 upregulation mediates the adaptive cytoprotection of hydrogen peroxide preconditioning against oxidative injury in PC12 cells Int. J. Mol. Med. 30 2012 314 320
    • (2012) Int. J. Mol. Med. , vol.30 , pp. 314-320
    • Mo, L.1    Yang, C.2    Gu, M.3    Zheng, D.4    Lin, L.5    Wang, X.6    Lan, A.7    Hu, F.8    Feng, J.9
  • 83
    • 0036127426 scopus 로고    scopus 로고
    • Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice
    • T.S. Lee, and L.Y. Chau Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice Nat. Med. 8 2002 240 246
    • (2002) Nat. Med. , vol.8 , pp. 240-246
    • Lee, T.S.1    Chau, L.Y.2
  • 84
    • 33745115862 scopus 로고    scopus 로고
    • Hydrogen sulfide inhibits nitric oxide production and nuclear factor-κB via heme oxygenase-1 expression in RAW264.7 macrophages stimulated with lipopolysaccharide
    • DOI 10.1016/j.freeradbiomed.2006.03.021, PII S0891584906002152
    • G.S. Oh, H.O. Pae, B.S. Lee, B.N. Kim, J.M. Kim, H.R. Kim, S.B. Jeon, W.K. Jeon, H.J. Chae, and H.T. Chung Hydrogen sulfide inhibits nitric oxide production and nuclear factor-κB via heme oxygenase-1 expression in RAW264.7 macrophages stimulated with lipopolysaccharide Free Radic. Biol. Med. 41 2006 106 119 (Pubitemid 43884782)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.1 , pp. 106-119
    • Oh, G.-S.1    Pae, H.-O.2    Lee, B.-S.3    Kim, B.-N.4    Kim, J.-M.5    Kim, H.-R.6    Jeon, S.B.7    Jeon, W.K.8    Chae, H.-J.9    Chung, H.-T.10
  • 85
    • 38849203158 scopus 로고    scopus 로고
    • Heme oxygenase-1 inhibits the expression of adhesion molecules associated with endothelial cell activation via inhibition of NF-κB RelA phosphorylation at serine 276
    • M.P. Seldon, G. Silva, N. Pejanovic, R. Larsen, I.P. Gregoire, J. Filipe, J. Anrather, and M.P. Soares Heme oxygenase-1 inhibits the expression of adhesion molecules associated with endothelial cell activation via inhibition of NF-κB RelA phosphorylation at serine 276 J. Immunol. 179 2007 7840 7851
    • (2007) J. Immunol. , vol.179 , pp. 7840-7851
    • Seldon, M.P.1    Silva, G.2    Pejanovic, N.3    Larsen, R.4    Gregoire, I.P.5    Filipe, J.6    Anrather, J.7    Soares, M.P.8
  • 86
    • 84869081486 scopus 로고    scopus 로고
    • Inhibition of NF-κB nuclear translocation via HO-1 activation underlies α-tocopheryl succinate toxicity
    • I. Bellezza, A. Tucci, F. Galli, S. Grottelli, A.L. Mierla, F. Pilolli, and A. Minelli Inhibition of NF-κB nuclear translocation via HO-1 activation underlies α-tocopheryl succinate toxicity J. Nutr. Biochem. 23 2012 1583 1591
    • (2012) J. Nutr. Biochem. , vol.23 , pp. 1583-1591
    • Bellezza, I.1    Tucci, A.2    Galli, F.3    Grottelli, S.4    Mierla, A.L.5    Pilolli, F.6    Minelli, A.7
  • 87
    • 84870445676 scopus 로고    scopus 로고
    • Docosahexaenoic acid inhibition of inflammation is partially via cross-talk between Nrf2/heme oxygenase 1 and IKK/NF-κB pathways
    • Y.C. Yang, C.K. Lii, Y.L. Wei, C.C. Li, C. Lu, K.L. Liu, and H.W. Chen Docosahexaenoic acid inhibition of inflammation is partially via cross-talk between Nrf2/heme oxygenase 1 and IKK/NF-κB pathways J. Nutr. Biochem. 24 2013 204 212
    • (2013) J. Nutr. Biochem. , vol.24 , pp. 204-212
    • Yang, Y.C.1    Lii, C.K.2    Wei, Y.L.3    Li, C.C.4    Lu, C.5    Liu, K.L.6    Chen, H.W.7
  • 88
    • 68149139538 scopus 로고    scopus 로고
    • The ubiquitin-editing enzyme A20 (TNFAIP3) is a central regulator of immunopathology
    • L. Vereecke, R. Beyaert, and G. van Loo The ubiquitin-editing enzyme A20 (TNFAIP3) is a central regulator of immunopathology Trends Immunol. 30 2009 383 391
    • (2009) Trends Immunol. , vol.30 , pp. 383-391
    • Vereecke, L.1    Beyaert, R.2    Van Loo, G.3
  • 89
    • 67649778720 scopus 로고    scopus 로고
    • A20: Central gatekeeper in inflammation and immunity
    • B. Coornaert, I. Carpentier, and R. Beyaert A20: central gatekeeper in inflammation and immunity J. Biol. Chem. 284 2009 8217 8221
    • (2009) J. Biol. Chem. , vol.284 , pp. 8217-8221
    • Coornaert, B.1    Carpentier, I.2    Beyaert, R.3
  • 90
    • 77649225756 scopus 로고    scopus 로고
    • Inhibition of NF-κB signaling by A20 through disruption of ubiquitin enzyme complexes
    • N. Shembade, A. Ma, and E.W. Harhaj Inhibition of NF-κB signaling by A20 through disruption of ubiquitin enzyme complexes Science 327 2010 1135 1139
    • (2010) Science , vol.327 , pp. 1135-1139
    • Shembade, N.1    Ma, A.2    Harhaj, E.W.3
  • 93
    • 78349305572 scopus 로고    scopus 로고
    • The oxidative stress-endoplasmic reticulum stress axis in cadmium toxicity
    • M. Kitamura, and N. Hiramatsu The oxidative stress-endoplasmic reticulum stress axis in cadmium toxicity Biometals 23 2010 941 950
    • (2010) Biometals , vol.23 , pp. 941-950
    • Kitamura, M.1    Hiramatsu, N.2
  • 94
    • 60549085835 scopus 로고    scopus 로고
    • Acquisition of anergy to proinflammatory cytokines in nonimmune cells through endoplasmic reticulum stress response: A mechanism for subsidence of inflammation
    • K. Hayakawa, N. Hiramatsu, M. Okamura, H. Yamazaki, S. Nakajima, J. Yao, A.W. Paton, J.C. Paton, and M. Kitamura Acquisition of anergy to proinflammatory cytokines in nonimmune cells through endoplasmic reticulum stress response: a mechanism for subsidence of inflammation J. Immunol. 182 2009 1182 1191
    • (2009) J. Immunol. , vol.182 , pp. 1182-1191
    • Hayakawa, K.1    Hiramatsu, N.2    Okamura, M.3    Yamazaki, H.4    Nakajima, S.5    Yao, J.6    Paton, A.W.7    Paton, J.C.8    Kitamura, M.9
  • 97
    • 79958723123 scopus 로고    scopus 로고
    • Effects of 810-nm laser on murine bone-marrow-derived dendritic cells
    • A.C. Chen, Y.Y. Huang, S.K. Sharma, and M.R. Hamblin Effects of 810-nm laser on murine bone-marrow-derived dendritic cells Photomed. Laser Surg. 29 2011 383 389
    • (2011) Photomed. Laser Surg. , vol.29 , pp. 383-389
    • Chen, A.C.1    Huang, Y.Y.2    Sharma, S.K.3    Hamblin, M.R.4
  • 98
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • DOI 10.1016/j.tcb.2003.11.001
    • D.T. Rutkowski, and R.J. Kaufman A trip to the ER: coping with stress Trends Cell Biol. 14 2004 20 28 (Pubitemid 38076857)
    • (2004) Trends in Cell Biology , vol.14 , Issue.1 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 99
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • DOI 10.1089/ars.2007.1782
    • J.D. Malhotra, and R.J. Kaufman Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxid. Redox Signal. 9 2007 2277 2293 (Pubitemid 350059010)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.12 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 101
    • 45049083557 scopus 로고    scopus 로고
    • Induction of apoptosis by cigarette smoke via ROS-dependent endoplasmic reticulum stress and CCAAT/enhancer-binding protein-homologous protein (CHOP)
    • Y. Tagawa, N. Hiramatsu, A. Kasai, K. Hayakawa, M. Okamura, J. Yao, and M. Kitamura Induction of apoptosis by cigarette smoke via ROS-dependent endoplasmic reticulum stress and CCAAT/enhancer-binding protein-homologous protein (CHOP) Free Radic. Biol. Med. 45 2008 50 59
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 50-59
    • Tagawa, Y.1    Hiramatsu, N.2    Kasai, A.3    Hayakawa, K.4    Okamura, M.5    Yao, J.6    Kitamura, M.7
  • 106
    • 0033984036 scopus 로고    scopus 로고
    • Modulation of endoplasmic reticulum-bound cholesterol regulatory enzymes by iron/ascorbate-mediated lipid peroxidation
    • DOI 10.1016/S0891-5849(99)00197-5, PII S0891584999001975
    • S. Brunet, L. Thibault, G. Lepage, E.G. Seidman, N. Dube, and E. Levy Modulation of endoplasmic reticulum-bound cholesterol regulatory enzymes by iron/ascorbate-mediated lipid peroxidation Free Radic. Biol. Med. 28 2000 46 54 (Pubitemid 30045572)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.1 , pp. 46-54
    • Brunet, S.1    Thibault, L.2    Lepage, G.3    Seidman, E.G.4    Dube, N.5    Levy, E.6
  • 107
    • 0029001576 scopus 로고
    • A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-κB
    • H.L. Pahl, and P.A. Baeuerle A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-κB EMBO J. 14 1995 2580 2588
    • (1995) EMBO J. , vol.14 , pp. 2580-2588
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 108
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • G.S. Hotamisligil Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Cell 140 2010 900 917
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 109
    • 8644282751 scopus 로고    scopus 로고
    • Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2
    • DOI 10.1128/MCB.24.23.10161-10168.2004
    • J. Deng, P.D. Lu, Y. Zhang, D. Scheuner, R.J. Kaufman, N. Sonenberg, H.P. Harding, and D. Ron Translational repression mediates activation of nuclear factor-κB by phosphorylated translation initiation factor 2 Mol. Cell. Biol. 24 2004 10161 10168 (Pubitemid 39507856)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.23 , pp. 10161-10168
    • Deng, J.1    Lu, P.D.2    Zhang, Y.3    Scheuner, D.4    Kaufman, R.J.5    Sonenberg, N.6    Harding, H.P.7    Ron, D.8
  • 110
    • 33645815074 scopus 로고    scopus 로고
    • Autocrine tumor necrosis factor α links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and down-regulation of TRAF2 expression
    • P. Hu, Z. Han, A.D. Couvillon, R.J. Kaufman, and J.H. Exton Autocrine tumor necrosis factor α links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and down-regulation of TRAF2 expression Mol. Cell. Biol. 26 2006 3071 3084
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3071-3084
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3    Kaufman, R.J.4    Exton, J.H.5
  • 111
  • 112
    • 48749112866 scopus 로고    scopus 로고
    • Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways
    • J.J. Wolfson, K.L. May, C.M. Thorpe, D.M. Jandhyala, J.C. Paton, and A.W. Paton Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signalling pathways Cell. Microbiol. 10 2008 1775 1786
    • (2008) Cell. Microbiol. , vol.10 , pp. 1775-1786
    • Wolfson, J.J.1    May, K.L.2    Thorpe, C.M.3    Jandhyala, D.M.4    Paton, J.C.5    Paton, A.W.6
  • 114
    • 68949214606 scopus 로고    scopus 로고
    • Biphasic, bidirectional regulation of NF-κB by endoplasmic reticulum stress
    • M. Kitamura Biphasic, bidirectional regulation of NF-κB by endoplasmic reticulum stress Antioxid. Redox Signal. 11 2009 2353 2364
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2353-2364
    • Kitamura, M.1
  • 117
    • 79953146630 scopus 로고    scopus 로고
    • Selective abrogation of BiP/GRP78 blunts activation of NF-κB through the ATF6 branch of the UPR: Involvement of C/EBPβ and mTOR-dependent dephosphorylation of Akt
    • S. Nakajima, N. Hiramatsu, K. Hayakawa, Y. Saito, H. Kato, T. Huang, J. Yao, A.W. Paton, J.C. Paton, and M. Kitamura Selective abrogation of BiP/GRP78 blunts activation of NF-κB through the ATF6 branch of the UPR: involvement of C/EBPβ and mTOR-dependent dephosphorylation of Akt Mol. Cell. Biol. 31 2011 1710 1718
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1710-1718
    • Nakajima, S.1    Hiramatsu, N.2    Hayakawa, K.3    Saito, Y.4    Kato, H.5    Huang, T.6    Yao, J.7    Paton, A.W.8    Paton, J.C.9    Kitamura, M.10
  • 118
    • 58749100827 scopus 로고    scopus 로고
    • The zinc finger protein A20 targets TRAF2 to the lysosomes for degradation
    • L. Li, N. Soetandyo, Q. Wang, and Y. Ye The zinc finger protein A20 targets TRAF2 to the lysosomes for degradation Biochim. Biophys. Acta 1793 2009 346 353
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 346-353
    • Li, L.1    Soetandyo, N.2    Wang, Q.3    Ye, Y.4
  • 119
    • 0037205442 scopus 로고    scopus 로고
    • Regulation of TRAF2 signaling by self-induced degradation
    • DOI 10.1074/jbc.M111522200
    • K.D. Brown, B.S. Hostager, and G.A. Bishop Regulation of TRAF2 signaling by self-induced degradation J. Biol. Chem. 277 2002 19433 19438 (Pubitemid 34967452)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 19433-19438
    • Brown, K.D.1    Hostager, B.S.2    Bishop, G.A.3
  • 120
    • 3142545837 scopus 로고    scopus 로고
    • Human CCAAT/enhancer-binding protein β gene expression is activated by endoplasmic reticulum stress through an unfolded protein response element downstream of the protein coding sequence
    • DOI 10.1074/jbc.M313920200
    • C. Chen, E.E. Dudenhausen, Y.X. Pan, C. Zhong, and M.S. Kilberg Human CCAAT/enhancer-binding protein β gene expression is activated by endoplasmic reticulum stress through an unfolded protein response element downstream of the protein coding sequence J. Biol. Chem. 279 2004 27948 27956 (Pubitemid 38900063)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 27948-27956
    • Chen, C.1    Dudenhausen, E.E.2    Pan, Y.-X.3    Zhong, C.4    Kilberg, M.S.5
  • 121
    • 0027316201 scopus 로고
    • Functional and physical associations between NF-κB and C/EBP family members: A rel domain-bZIP interaction
    • B. Stein, P.C. Cogswell, and A.S. Baldwin Jr. Functional and physical associations between NF-κB and C/EBP family members: a Rel domain-bZIP interaction Mol. Cell. Biol. 13 1993 3964 3974 (Pubitemid 23187624)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.7 , pp. 3964-3974
    • Stein, B.1    Cogswell, P.C.2    Baldwin Jr., A.S.3
  • 122
    • 79953001199 scopus 로고    scopus 로고
    • Preconditioning with endoplasmic reticulum stress mitigates retinal endothelial inflammation via activation of X-box binding protein 1
    • J. Li, J.J. Wang, and S.X. Zhang Preconditioning with endoplasmic reticulum stress mitigates retinal endothelial inflammation via activation of X-box binding protein 1 J. Biol. Chem. 286 2011 4912 4921
    • (2011) J. Biol. Chem. , vol.286 , pp. 4912-4921
    • Li, J.1    Wang, J.J.2    Zhang, S.X.3
  • 123
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • J. Alam, D. Stewart, C. Touchard, S. Boinapally, A.M. Choi, and J.L. Cook Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene J. Biol. Chem. 274 1999 26071 26078
    • (1999) J. Biol. Chem. , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 124
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • K. Itoh, N. Wakabayashi, Y. Katoh, T. Ishii, K. Igarashi, J.D. Engel, and M. Yamamoto Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain Genes Dev. 13 1999 76 86 (Pubitemid 29045117)
    • (1999) Genes and Development , vol.13 , Issue.1 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 127
    • 0035798578 scopus 로고    scopus 로고
    • CCAAT/enhancer-binding proteins α and β negatively influence the capacity of tumor necrosis factor α to up-regulate the human cytomegalovirus IE1/2 enhancer/promoter by nuclear factor κb during monocyte differentiation
    • S. Prösch, A.K. Heine, H.D. Volk, and D.H. Krüger CCAAT/enhancer-binding proteins α and β negatively influence the capacity of tumor necrosis factor α to up-regulate the human cytomegalovirus IE1/2 enhancer/promoter by nuclear factor κB during monocyte differentiation J. Biol. Chem. 276 2001 40712 40720
    • (2001) J. Biol. Chem. , vol.276 , pp. 40712-40720
    • Prösch, S.1    Heine, A.K.2    Volk, H.D.3    Krüger, D.H.4
  • 129
    • 63049095364 scopus 로고    scopus 로고
    • Activating transcription factor 4 and CCAAT/enhancer-binding protein-β negatively regulate the mammalian target of rapamycin via Redd1 expression in response to oxidative and endoplasmic reticulum stress
    • H.O. Jin, S.K. Seo, S.H. Woo, E.S. Kim, H.C. Lee, D.H. Yoo, S. An, T.B. Choe, S.J. Lee, S.I. Hong, C.H. Rhee, J.I. Kim, and I.C. Park Activating transcription factor 4 and CCAAT/enhancer-binding protein-β negatively regulate the mammalian target of rapamycin via Redd1 expression in response to oxidative and endoplasmic reticulum stress Free Radic. Biol. Med. 46 2009 1158 1167
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1158-1167
    • Jin, H.O.1    Seo, S.K.2    Woo, S.H.3    Kim, E.S.4    Lee, H.C.5    Yoo, D.H.6    An, S.7    Choe, T.B.8    Lee, S.J.9    Hong, S.I.10    Rhee, C.H.11    Kim, J.I.12    Park, I.C.13
  • 130
    • 84879122483 scopus 로고    scopus 로고
    • Pleiotropic potential of dehydroxymethylepoxyquinomicin for NF-κB suppression via reactive oxygen species and unfolded protein response
    • Nakajima, S.; Kato, H.; Gu, L.; Takahashi, S.; Johno, H.; Umezawa, K.; Kitamura, M. Pleiotropic potential of dehydroxymethylepoxyquinomicin for NF-κB suppression via reactive oxygen species and unfolded protein response. J. Immunol. 190:6559-6569; 2013.
    • (2013) J. Immunol. , vol.190 , pp. 6559-6569
    • Nakajima, S.1    Kato, H.2    Gu, L.3    Takahashi, S.4    Johno, H.5    Umezawa, K.6    Kitamura, M.7
  • 132
  • 134
    • 0029077772 scopus 로고
    • Hypoxia, oxidative stress and rheumatoid arthritis
    • P.I. Mapp, M.C. Grootveld, and D.R. Blake Hypoxia, oxidative stress and rheumatoid arthritis Br. Med. Bull. 51 1995 419 436
    • (1995) Br. Med. Bull. , vol.51 , pp. 419-436
    • Mapp, P.I.1    Grootveld, M.C.2    Blake, D.R.3
  • 137
    • 0005282746 scopus 로고    scopus 로고
    • Cancer and oxidative stress
    • N. Noda, and H. Wakasugi Cancer and oxidative stress J. Jpn Med. Assoc. 44 2001 535 539
    • (2001) J. Jpn Med. Assoc. , vol.44 , pp. 535-539
    • Noda, N.1    Wakasugi, H.2
  • 138
    • 0035137882 scopus 로고    scopus 로고
    • Control of oncogenesis and cancer therapy resistance by the transcription factor NF-κB
    • A.S. Baldwin Control of oncogenesis and cancer therapy resistance by the transcription factor NF-κB. J Clin. Invest. 107 2001 241 246 (Pubitemid 32157954)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.3 , pp. 241-246
    • Baldwin, A.S.1
  • 139
    • 0033866278 scopus 로고    scopus 로고
    • Antioxidants and cancers of the esophagus and gastric cardia
    • DOI 10.1002/1097-0215(200009 01)87:5<750::AID-I JC19>3.0.CO;2-6
    • P. Terry, J. Lagergren, W. Ye, O. Nyrén, and A. Wolk Antioxidants and cancers of the esophagus and gastric cardia Int. J. Cancer 87 2000 750 754 (Pubitemid 30620420)
    • (2000) International Journal of Cancer , vol.87 , Issue.5 , pp. 750-754
    • Terry, P.1    Lagergren, J.2    Ye, W.3    Nyren, O.4    Wolk, A.5
  • 140
    • 0031734034 scopus 로고    scopus 로고
    • Effects of BX661A, a new therapeutic agent for ulcerative colitis, on reactive oxygen species in comparison with salazosulfapyridine and its metabolite sulfapyridine
    • I. Kimura, T. Kumamoto, A. Matsuda, M. Kataoka, and Y. Kokuba Effects of BX661A, a new therapeutic agent for ulcerative colitis, on reactive oxygen species in comparison with salazosulfapyridine and its metabolite sulfapyridine Arzneimittelforschung 48 1998 1007 1011 (Pubitemid 28496760)
    • (1998) Arzneimittel-Forschung/Drug Research , vol.48 , Issue.10 , pp. 1007-1011
    • Kimura, I.1    Kumamoto, T.2    Matsuda, A.3    Kataoka, M.4    Kokuba, Y.5
  • 142
    • 84864701748 scopus 로고    scopus 로고
    • Pathological neoangiogenesis depends on oxidative stress regulation by ATM
    • Okuno, Y.; Nakamura-Ishizu, A.; Otsu, K.; Suda, T.; Kubota, Y. Pathological neoangiogenesis depends on oxidative stress regulation by ATM. Nat. Med. 18:1208-1216; 2012.
    • (2012) Nat. Med. , vol.18 , pp. 1208-1216
    • Okuno, Y.1    Nakamura-Ishizu, A.2    Otsu, K.3    Suda, T.4    Kubota, Y.5
  • 143
    • 79960390177 scopus 로고    scopus 로고
    • Possible role of peritoneal NF-κB in peripheral inflammation and cancer: Lessons from the inhibitor DHMEQ
    • K. Umezawa Possible role of peritoneal NF-κB in peripheral inflammation and cancer: lessons from the inhibitor DHMEQ Biomed. Pharmacother. 65 2011 252 259
    • (2011) Biomed. Pharmacother. , vol.65 , pp. 252-259
    • Umezawa, K.1
  • 144
    • 67650812043 scopus 로고    scopus 로고
    • Antitumor effects of dehydroxymethylepoxyquinomicin, a novel nuclear factor-κB inhibitor, in human liver cancer cells are mediated through a reactive oxygen species-dependent mechanism
    • N. Lampiasi, A. Azzolina, N. D'Alessandro, K. Umezawa, J.A. McCubrey, G. Montalto, and M. Cervello Antitumor effects of dehydroxymethylepoxyquinomicin, a novel nuclear factor-κB inhibitor, in human liver cancer cells are mediated through a reactive oxygen species-dependent mechanism Mol. Pharmacol. 76 2009 290 300
    • (2009) Mol. Pharmacol. , vol.76 , pp. 290-300
    • Lampiasi, N.1    Azzolina, A.2    D'Alessandro, N.3    Umezawa, K.4    McCubrey, J.A.5    Montalto, G.6    Cervello, M.7
  • 145
    • 34547197625 scopus 로고    scopus 로고
    • Impact of antioxidant supplementation on chemotherapeutic efficacy: A systematic review of the evidence from randomized controlled trials
    • DOI 10.1016/j.ctrv.2007.01.005, PII S0305737207000278
    • K.I. Block, A.C. Koch, M.N. Mead, P.K. Tothy, R.A. Newman, and C. Gyllenhaal Impact of antioxidant supplementation on chemotherapeutic toxicity: a systematic review of the evidence from randomized controlled trials Cancer Treat. Rev. 33 2007 407 418 (Pubitemid 47324224)
    • (2007) Cancer Treatment Reviews , vol.33 , Issue.5 , pp. 407-418
    • Block, K.I.1    Koch, A.C.2    Mead, M.N.3    Tothy, P.K.4    Newman, R.A.5    Gyllenhaal, C.6
  • 146
    • 0032077879 scopus 로고    scopus 로고
    • Nuclear factor kappa B dependent induction of gamma glutamylcysteine synthetase by ionizing radiation in T98G human glioblastoma cells
    • DOI 10.1016/S0891-5849(97)00443-7, PII S0891584997004437
    • M. Iwanaga, K. Mori, T. Iida, Y. Urata, T. Matsuo, A. Yasunaga, S. Shibata, and T. Kondo NF-κB dependent induction of γ glutamylcysteine synthetase by ionizing radiation in T98G human glioblastoma cells Free Radic. Biol. Med. 24 1998 1256 1268 (Pubitemid 28246741)
    • (1998) Free Radical Biology and Medicine , vol.24 , Issue.7-8 , pp. 1256-1268
    • Iwanaga, M.1    Mori, K.2    Iida, T.3    Urata, Y.4    Matsuo, T.5    Yasunaga, A.6    Shibata, S.7    Kondo, T.8
  • 147
    • 0028222788 scopus 로고
    • UVB light induces nuclear factor κB (NFκB) activity independently from chromosomal DNA damage in Cell-Free cytosolic extracts
    • M.M. Simon, Y. Aragane, A. Schwarz, T.A. Luger, and T. Schwarz UVB light induces nuclear factor κB (NF-κB) activity independently from chromosomal DNA damage in cell-free cytosolic extracts J. Invest. Dermatol. 102 1994 422 427 (Pubitemid 24117179)
    • (1994) Journal of Investigative Dermatology , vol.102 , Issue.4 , pp. 422-427
    • Simon, M.M.1    Aragane, Y.2    Schwarz, A.3    Luger, T.A.4    Schwarz, T.5
  • 148
    • 0029789253 scopus 로고    scopus 로고
    • Cholinergic stimulation of AP-1 and NFκB transcription factors is differentially sensitive to oxidative stress in SH-SY5Y neuroblastoma: Relationship to phosphoinositide hydrolysis
    • X. Li, L. Song, and R.S. Jope Cholinergic stimulation of AP-1 and NF-κB transcription factors is differentially sensitive to oxidative stress in SH-SY5Y neuroblastoma: relationship to phosphoinositide hydrolysis J. Neurosci. 16 1996 5914 5922 (Pubitemid 26313967)
    • (1996) Journal of Neuroscience , vol.16 , Issue.19 , pp. 5914-5922
    • Li, X.1    Song, L.2    Jope, R.S.3
  • 149
    • 0032550211 scopus 로고    scopus 로고
    • Induction of cytokine-induced neutrophil chemoattractant in response to various stresses in rat C6 glioma cells
    • DOI 10.1016/S0006-8993(98)00080-8, PII S0006899398000808
    • T. Uehara, I. Baba, and Y. Nomura Induction of cytokine-induced neutrophil chemoattractant in response to various stresses in rat C6 glioma cells Brain Res. 790 1998 284 292 (Pubitemid 28234514)
    • (1998) Brain Research , vol.790 , Issue.1-2 , pp. 284-292
    • Uehara, T.1    Baba, I.2    Nomura, Y.3
  • 150
    • 0028268629 scopus 로고
    • Hypoxia causes the activation of nuclear factor κB through the phosphorylation of IκBα on tyrosine residues
    • A.C. Koong, E.Y. Chen, and A.J. Giaccia Hypoxia causes the activation of nuclear factor κ B through the phosphorylation of IκB on tyrosine residues Cancer Res. 54 1994 1425 1430 (Pubitemid 24106401)
    • (1994) Cancer Research , vol.54 , Issue.6 , pp. 1425-1430
    • Koong, A.C.1    Chen, E.Y.2    Giaccia, A.J.3
  • 151
    • 0031050027 scopus 로고    scopus 로고
    • Activation of the NF-κB transcription factor in a T-lymphocytic cell line by hypochlorous acid
    • S. Schoonbroodt, S. Legrand-Poels, M. Best-Belpomme, and J. Piette Activation of the NF-κB transcription factor in a T-lymphocytic cell line by hypochlorous acid Biochem. J. 321 1997 777 785 (Pubitemid 27084888)
    • (1997) Biochemical Journal , vol.321 , Issue.3 , pp. 777-785
    • Schoonbroodt, S.1    Legrand-Poels, S.2    Best-Belpomme, M.3    Piette, J.4
  • 152
    • 0035629777 scopus 로고    scopus 로고
    • Importance of post-transcriptional regulation of chemokine genes by oxidative stress
    • DOI 10.1042/0264-6021:3600321
    • C. Josse, J.R. Boelaert, M. Best-Belpomme, and J. Piette Importance of post-transcriptional regulation of chemokine genes by oxidative stress Biochem. J. 360 2001 321 333 (Pubitemid 33151327)
    • (2001) Biochemical Journal , vol.360 , Issue.2 , pp. 321-333
    • Josse, C.1    Boelaert, J.R.2    Best-Belpomme, M.3    Piette, J.4
  • 153
    • 0142231354 scopus 로고    scopus 로고
    • Selenium-containing compounds attenuate peroxynitrite-mediated NF-κB and AP-1 activation and interleukin-8 gene and protein expression in human leukocytes
    • DOI 10.1016/S0891-5849(03)00439-8
    • L. József, and J.G. Filep Selenium-containing compounds attenuate peroxynitrite-mediated NF-κB and AP-1 activation and interleukin-8 gene and protein expression in human leukocytes Free Radic. Biol. Med. 35 2003 1018 1027 (Pubitemid 37315695)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.9 , pp. 1018-1027
    • Jozsef, L.1    Filep, J.G.2
  • 154
    • 0029982802 scopus 로고    scopus 로고
    • Lipopolysaccharide activates transcription of the heme oxygenase gene in mouse M1 cells through oxidative activation of nuclear factor κB
    • S. Kurata, M. Matsumoto, Y. Tsuji, and H. Nakajima Lipopolysaccharide activates transcription of the heme oxygenase gene in mouse M1 cells through oxidative activation of NF-κB Eur. J. Biochem. 239 1996 566 571 (Pubitemid 26253072)
    • (1996) European Journal of Biochemistry , vol.239 , Issue.3 , pp. 566-571
    • Kurata, S.-I.1    Matsumoto, M.2    Tsuji, Y.3    Nakajima, H.4
  • 155
    • 0031825098 scopus 로고    scopus 로고
    • Role of protein kinase C in basal and hydrogen peroxide-stimulated NF- κB activation in the murine macrophage J774A.1 cell line
    • DOI 10.1006/abbi.1997.0487
    • N. Kaul, R. Gopalakrishna, U. Gundimeda, J. Choi, and H.J. Forman Role of protein kinase C in basal and hydrogen peroxide-stimulated NF-κB activation in the murine macrophage J774A.1 cell line Arch. Biochem. Biophys. 350 1998 79 86 (Pubitemid 28371171)
    • (1998) Archives of Biochemistry and Biophysics , vol.350 , Issue.1 , pp. 79-86
    • Kaul, N.1    Gopalakrishna, R.2    Gundimeda, U.3    Choi, J.4    Forman, H.J.5
  • 156
    • 0034695660 scopus 로고    scopus 로고
    • Up-regulation of multidrug resistance P-glycoprotein via nuclear factor- κB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis
    • DOI 10.1074/jbc.275.3.1887
    • F. Thévenod, J.M. Friedmann, A.D. Katsen, and I.A. Hauser Up-regulation of multidrug resistance P-glycoprotein via nuclear factor-κB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis J. Biol. Chem. 275 2000 1887 1896 (Pubitemid 30060813)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1887-1896
    • Thevenod, F.1    Friedmann, J.M.2    Katsen, A.D.3    Hauser, I.A.4
  • 157
    • 0030014964 scopus 로고    scopus 로고
    • Involvement of the transcription factor NF-κB in tubular morphogenesis of human microvascular endothelial cells by oxidative stress
    • T. Shono, M. Ono, H. Izumi, S.I. Jimi, K. Matsushima, T. Okamoto, K. Kohno, and M. Kuwano Involvement of the transcription factor NF-κB in tubular morphogenesis of human microvascular endothelial cells by oxidative stress Mol. Cell. Biol. 16 1996 4231 4239 (Pubitemid 26251224)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.8 , pp. 4231-4239
    • Shono, T.1    Ono, M.2    Izumi, H.3    Jimi, S.-I.4    Matsushima, K.5    Okamoto, T.6    Kohno, K.7    Kuwano, M.8
  • 159
    • 0032533372 scopus 로고    scopus 로고
    • 2 in rat heart endothelial cells
    • DOI 10.1016/S0891-5849(98)00115-4, PII S0891584998001154
    • C.C. Chua, R.C. Hamdy, and B.H. Chua Upregulation of vascular endothelial growth factor by H2O2 in rat heart endothelial cells Free Radic. Biol. Med. 25 1998 891 897 (Pubitemid 28538554)
    • (1998) Free Radical Biology and Medicine , vol.25 , Issue.8 , pp. 891-897
    • Chua, C.C.1    Hamdy, R.C.2    Chua, B.H.L.3
  • 160
    • 0036080603 scopus 로고    scopus 로고
    • Peroxynitrite increases iNOS through NF-κB and decreases prostacyclin synthase in endothelial cells
    • C.L. Cooke, and S.T. Davidge Peroxynitrite increases iNOS through NF-κB and decreases prostacyclin synthase in endothelial cells Am. J. Physiol. Cell Physiol. 282 2002 C395 C402
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Cooke, C.L.1    Davidge, S.T.2
  • 161
    • 2942562451 scopus 로고    scopus 로고
    • Ultraviolet A radiation-induced immediate iron release is a key modulator of the activation of NF-κB in human skin fibroblasts
    • DOI 10.1111/j.0022-202X.2004.22620.x
    • O. Reelfs, R.M. Tyrrell, and C. Pourzand Ultraviolet a radiation-induced immediate iron release is a key modulator of the activation of NF-κB in human skin fibroblasts J. Invest. Dermatol. 122 2004 1440 1447 (Pubitemid 38757226)
    • (2004) Journal of Investigative Dermatology , vol.122 , Issue.6 , pp. 1440-1447
    • Reelfs, O.1    Tyrrell, R.M.2    Pourzand, C.3
  • 162
    • 0027959628 scopus 로고
    • Inhibition by N-acetyl-L-cysteine of interleukin-6 mRNA induction and activation of NF-κB by tumor necrosis factor-α in a mouse fibroblastic cell line, Balb/3T3
    • M. Shibanuma, T. Kuroki, and K. Nose Inhibition by N-acetyl-L-cysteine of interleukin-6 mRNA induction and activation of NF-κB by tumor necrosis factor-α in a mouse fibroblastic cell line, Balb/3T3 FEBS Lett. 353 1994 62 66
    • (1994) FEBS Lett. , vol.353 , pp. 62-66
    • Shibanuma, M.1    Kuroki, T.2    Nose, K.3
  • 163
    • 0031561483 scopus 로고    scopus 로고
    • Regulation of NF-κB and HIV-1 LTR activity in mouse L cells by ultraviolet radiation: LTR trans-activation in a nonirradiated genome in heterokaryons
    • DOI 10.1006/excr.1996.3397
    • S.C. Miller, A. Taylor, K. Watanabe, K. Mok, and F.M. Torti Regulation of NF-κB and HIV-1 LTR activity in mouse L cells by ultraviolet radiation: LTR trans-activation in a nonirradiated genome in heterokaryons Exp. Cell Res. 230 1997 9 21 (Pubitemid 27187534)
    • (1997) Experimental Cell Research , vol.230 , Issue.1 , pp. 9-21
    • Miller, S.C.1    Taylor, A.2    Watanabe, K.3    Mok, K.4    Torti, F.M.5
  • 164
    • 0030911732 scopus 로고    scopus 로고
    • Activation of transcription factor NF-κB and p38 mitogen-activated protein kinase is mediated by distinct and separate stress effector pathways
    • DOI 10.1074/jbc.272.19.12422
    • S. Wesselborg, M.K. Bauer, M. Vogt, M.L. Schmitz, and K. Schulze-Osthoff Activation of transcription factor NF-κB and p38 mitogen-activated protein kinase is mediated by distinct and separate stress effector pathways J. Biol. Chem. 272 1997 12422 12429 (Pubitemid 27203330)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.19 , pp. 12422-12429
    • Wesselborg, S.1    Bauer, M.K.A.2    Vogt, M.3    Schmitz, M.L.4    Schulze-Osthoff, K.5
  • 165
    • 0033044551 scopus 로고    scopus 로고
    • Nuclear translocation of green fluorescent protein-nuclear factor κB with a distinct lag time in living cells
    • DOI 10.1016/S0014-5793(99)00002-2, PII S0014579399000022
    • K. Tenjinbaru, T. Furuno, N. Hirashima, and M. Nakanishi Nuclear translocation of green fluorescent protein- NF-κB with a distinct lag time in living cells FEBS Lett. 444 1999 1 4 (Pubitemid 29094628)
    • (1999) FEBS Letters , vol.444 , Issue.1 , pp. 1-4
    • Tenjinbaru, K.1    Furuno, T.2    Hirashima, N.3    Nakanishi, M.4
  • 166
    • 33846543956 scopus 로고    scopus 로고
    • High concentration of antioxidants N-acetylcysteine and mitoquinone-Q induces intercellular adhesion molecule 1 and oxidative stress by increasing intracellular glutathione
    • T.K. Mukherjee, A.K. Mishra, S. Mukhopadhyay, and J.R. Hoidal High concentration of antioxidants N-acetylcysteine and mitoquinone-Q induces intercellular adhesion molecule 1 and oxidative stress by increasing intracellular glutathione J. Immunol. 178 2007 1835 1844 (Pubitemid 46154656)
    • (2007) Journal of Immunology , vol.178 , Issue.3 , pp. 1835-1844
    • Mukherjee, T.K.1    Mishra, A.K.2    Mukhopadhyay, S.3    Hoidal, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.