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Volumn 220, Issue 1, 2007, Pages 8-21

From death receptor to reactive oxygen species and c-Jun N-terminal protein kinase: The receptor-interacting protein 1 odyssey

Author keywords

Death receptor; JNK; NF B; RIP1; ROS

Indexed keywords

DEATH RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE;

EID: 35748944844     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/j.1600-065X.2007.00560.x     Document Type: Review
Times cited : (89)

References (180)
  • 1
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science 1998 281 : 1305 1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 2
    • 1642617628 scopus 로고    scopus 로고
    • The protein kinase PKR is required for macrophage apoptosis after activation of Toll-like receptor 4
    • Hsu LC, et al. The protein kinase PKR is required for macrophage apoptosis after activation of Toll-like receptor 4. Nature 2004 428 : 341 345.
    • (2004) Nature , vol.428 , pp. 341-345
    • Hsu, L.C.1
  • 3
    • 29644433629 scopus 로고    scopus 로고
    • NF-kappaB protects macrophages from lipopolysaccharide-induced cell death: The role of caspase 8 and receptor-interacting protein
    • Ma Y, Temkin V, Liu H, Pope RM. NF-kappaB protects macrophages from lipopolysaccharide-induced cell death: the role of caspase 8 and receptor-interacting protein. J Biol Chem 2005 280 : 41827 41834.
    • (2005) J Biol Chem , vol.280 , pp. 41827-41834
    • Ma, Y.1    Temkin, V.2    Liu, H.3    Pope, R.M.4
  • 4
    • 24344498989 scopus 로고    scopus 로고
    • Proteinase-activated receptor-1 mediates elastase-induced apoptosis of human lung epithelial cells
    • Suzuki T, et al. Proteinase-activated receptor-1 mediates elastase-induced apoptosis of human lung epithelial cells. Am J Respir Cell Mol Biol 2005 33 : 231 247.
    • (2005) Am J Respir Cell Mol Biol , vol.33 , pp. 231-247
    • Suzuki, T.1
  • 5
    • 34548499520 scopus 로고    scopus 로고
    • The endocannabinoid 2-arachidonoyl glycerol induces death of hepatic stellate cells via mitochondrial reactive oxygen species
    • Siegmund SV, et al. The endocannabinoid 2-arachidonoyl glycerol induces death of hepatic stellate cells via mitochondrial reactive oxygen species. FASEB J 2007 21 : 2798 2806.
    • (2007) FASEB J , vol.21 , pp. 2798-2806
    • Siegmund, S.V.1
  • 6
    • 33845627660 scopus 로고    scopus 로고
    • Cannabinoid receptors as novel targets for the treatment of melanoma
    • Blazquez C, et al. Cannabinoid receptors as novel targets for the treatment of melanoma. FASEB J 2006 20 : 2633 2635.
    • (2006) FASEB J , vol.20 , pp. 2633-2635
    • Blazquez, C.1
  • 7
    • 16444375370 scopus 로고    scopus 로고
    • Cannabinoid receptor as a novel target for the treatment of prostate cancer
    • Sarfaraz S, Afaq F, Adhami VM, Mukhtar H. Cannabinoid receptor as a novel target for the treatment of prostate cancer. Cancer Res 2005 65 : 1635 1641.
    • (2005) Cancer Res , vol.65 , pp. 1635-1641
    • Sarfaraz, S.1    Afaq, F.2    Adhami, V.M.3    Mukhtar, H.4
  • 8
    • 0037253496 scopus 로고    scopus 로고
    • Inhibition of skin tumor growth and angiogenesis in vivo by activation of cannabinoid receptors
    • Casanova ML, et al. Inhibition of skin tumor growth and angiogenesis in vivo by activation of cannabinoid receptors. J Clin Invest 2003 111 : 43 50.
    • (2003) J Clin Invest , vol.111 , pp. 43-50
    • Casanova, M.L.1
  • 10
    • 2342541774 scopus 로고    scopus 로고
    • Adenosine induces apoptosis in the human gastric cancer cells via an intrinsic pathway relevant to activation of AMP-activated protein kinase
    • Saitoh M, Nagai K, Nakagawa K, Yamamura T, Yamamoto S, Nishizaki T. Adenosine induces apoptosis in the human gastric cancer cells via an intrinsic pathway relevant to activation of AMP-activated protein kinase. Biochem Pharmacol 2004 67 : 2005 2011.
    • (2004) Biochem Pharmacol , vol.67 , pp. 2005-2011
    • Saitoh, M.1    Nagai, K.2    Nakagawa, K.3    Yamamura, T.4    Yamamoto, S.5    Nishizaki, T.6
  • 11
    • 0034713235 scopus 로고    scopus 로고
    • Induction of apoptosis in rat cardiocytes by A3 adenosine receptor activation and its suppression by isoproterenol
    • Shneyvays V, et al. Induction of apoptosis in rat cardiocytes by A3 adenosine receptor activation and its suppression by isoproterenol. Exp Cell Res 2000 257 : 111 126.
    • (2000) Exp Cell Res , vol.257 , pp. 111-126
    • Shneyvays, V.1
  • 12
    • 33645957656 scopus 로고    scopus 로고
    • CD72 down-modulates BCR-induced signal transduction and diminishes survival in primary mature B lymphocytes
    • Li DH, et al. CD72 down-modulates BCR-induced signal transduction and diminishes survival in primary mature B lymphocytes. J Immunol 2006 176 : 5321 5328.
    • (2006) J Immunol , vol.176 , pp. 5321-5328
    • Li, D.H.1
  • 13
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • Vercammen D, et al. Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J Exp Med 1998 187 : 1477 1485.
    • (1998) J Exp Med , vol.187 , pp. 1477-1485
    • Vercammen, D.1
  • 14
    • 1642299768 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation
    • Lin Y, et al. Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation. J Biol Chem 2004 279 : 10822 10828.
    • (2004) J Biol Chem , vol.279 , pp. 10822-10828
    • Lin, Y.1
  • 15
    • 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, Karin M. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 2005 120 : 649 661.
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 16
    • 8344260568 scopus 로고    scopus 로고
    • Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species
    • Pham CG, et al. Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species. Cell 2004 119 : 529 542.
    • (2004) Cell , vol.119 , pp. 529-542
    • Pham, C.G.1
  • 17
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 2007 26 : 1749 1760.
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 18
    • 25844520458 scopus 로고    scopus 로고
    • Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism
    • Jezek P, Hlavata L. Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int J Biochem Cell Biol 2005 37 : 2478 2503.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 2478-2503
    • Jezek, P.1    Hlavata, L.2
  • 20
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols
    • Brown GC, Borutaite V. Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols. Biochim Biophys Acta 2004 1658 : 44 49.
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2
  • 21
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ, Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 2001 30 : 1191 1212.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 22
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S, Finkel T. Mitochondria, oxidants, and aging. Cell 2005 120 : 483 495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 23
    • 0023667777 scopus 로고
    • Oxygen free radicals linked to many diseases
    • Marx JL. Oxygen free radicals linked to many diseases. Science 1987 235 : 529 531.
    • (1987) Science , vol.235 , pp. 529-531
    • Marx, J.L.1
  • 24
    • 8644221211 scopus 로고    scopus 로고
    • Mammalian peroxisomes and reactive oxygen species
    • Schrader M, Fahimi HD. Mammalian peroxisomes and reactive oxygen species. Histochem Cell Biol 2004 122 : 383 393.
    • (2004) Histochem Cell Biol , vol.122 , pp. 383-393
    • Schrader, M.1    Fahimi, H.D.2
  • 25
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD, Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 2003 112 : 481 490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 26
    • 11144303507 scopus 로고    scopus 로고
    • Reactive oxygen species and the mitochondrial signaling pathway of cell death
    • Le Bras M, Clement MV, Pervaiz S, Brenner C. Reactive oxygen species and the mitochondrial signaling pathway of cell death. Histol Histopathol 2005 20 : 205 219.
    • (2005) Histol Histopathol , vol.20 , pp. 205-219
    • Le Bras, M.1    Clement, M.V.2    Pervaiz, S.3    Brenner, C.4
  • 27
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death
    • Liu ZG, Hsu H, Goeddel DV, Karin M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell 1996 87 : 565 576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 28
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • Boveris A, Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem J 1973 134 : 707 716.
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 29
    • 0028241374 scopus 로고
    • Generation of superoxide radicals as byproduct of cellular respiration
    • Nohl H. Generation of superoxide radicals as byproduct of cellular respiration. Ann Biol Clin (Paris) 1994 52 : 199 204.
    • (1994) Ann Biol Clin (Paris) , vol.52 , pp. 199-204
    • Nohl, H.1
  • 30
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S, Robinson BH. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem Sci 2000 25 : 502 508.
    • (2000) Trends Biochem Sci , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 31
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol 2003 552 : 335 344.
    • (2003) J Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 32
    • 0032525349 scopus 로고    scopus 로고
    • 2 production of heart mitochondria and aging rate are slower in canaries and parakeets than in mice: Sites of free radical generation and mechanisms involved
    • 2 production of heart mitochondria and aging rate are slower in canaries and parakeets than in mice: sites of free radical generation and mechanisms involved. Mech Ageing Dev 1998 103 : 133 146.
    • (1998) Mech Ageing Dev , vol.103 , pp. 133-146
    • Herrero, A.1    Barja, G.2
  • 33
    • 4544359913 scopus 로고    scopus 로고
    • Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species
    • Starkov AA, et al. Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species. J Neurosci 2004 24 : 7779 7788.
    • (2004) J Neurosci , vol.24 , pp. 7779-7788
    • Starkov, A.A.1
  • 34
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
    • Zhang L, Yu L, Yu CA. Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. J Biol Chem 1998 273 : 33972 33976.
    • (1998) J Biol Chem , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3
  • 35
    • 2942581328 scopus 로고    scopus 로고
    • Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain
    • Ricci JE, et al. Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain. Cell 2004 117 : 773 786.
    • (2004) Cell , vol.117 , pp. 773-786
    • Ricci, J.E.1
  • 36
    • 10644244369 scopus 로고    scopus 로고
    • AIF deficiency compromises oxidative phosphorylation
    • Vahsen N, et al. AIF deficiency compromises oxidative phosphorylation. EMBO J 2004 23 : 4679 4689.
    • (2004) EMBO J , vol.23 , pp. 4679-4689
    • Vahsen, N.1
  • 37
    • 18544371050 scopus 로고    scopus 로고
    • DNA binding is required for the apoptogenic action of apoptosis inducing factor
    • Ye H, et al. DNA binding is required for the apoptogenic action of apoptosis inducing factor. Nat Struct Biol 2002 9 : 680 684.
    • (2002) Nat Struct Biol , vol.9 , pp. 680-684
    • Ye, H.1
  • 38
    • 0035844170 scopus 로고    scopus 로고
    • NADH oxidase activity of mitochondrial apoptosis-inducing factor
    • Miramar MD, et al. NADH oxidase activity of mitochondrial apoptosis-inducing factor. J Biol Chem 2001 276 : 16391 16398.
    • (2001) J Biol Chem , vol.276 , pp. 16391-16398
    • Miramar, M.D.1
  • 39
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E, Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 2000 29 : 222 230.
    • (2000) Free Radic Biol Med , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 40
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov SS, Skulachev VP, Starkov AA. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett 1997 416 : 15 18.
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 41
    • 0032570577 scopus 로고    scopus 로고
    • Cytochrome c in the apoptotic and antioxidant cascades
    • Skulachev VP. Cytochrome c in the apoptotic and antioxidant cascades. FEBS Lett 1998 423 : 275 280.
    • (1998) FEBS Lett , vol.423 , pp. 275-280
    • Skulachev, V.P.1
  • 42
    • 0033667705 scopus 로고    scopus 로고
    • Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production
    • Arsenijevic D, et al. Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nat Genet 2000 26 : 435 439.
    • (2000) Nat Genet , vol.26 , pp. 435-439
    • Arsenijevic, D.1
  • 43
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J, Jones DP. Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J Biol Chem 1998 273 : 11401 11404.
    • (1998) J Biol Chem , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 44
    • 22744447211 scopus 로고    scopus 로고
    • Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis
    • Giorgio M, et al. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 2005 122 : 221 233.
    • (2005) Cell , vol.122 , pp. 221-233
    • Giorgio, M.1
  • 45
    • 0033912405 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress. Physiologic consequences and potential for a role in aging
    • Melov S. Mitochondrial oxidative stress. Physiologic consequences and potential for a role in aging. Ann NY Acad Sci 2000 908 : 219 225.
    • (2000) Ann NY Acad Sci , vol.908 , pp. 219-225
    • Melov, S.1
  • 46
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto A, Fridovich I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J Biol Chem 2001 276 : 38388 38393.
    • (2001) J Biol Chem , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 47
    • 0019073929 scopus 로고
    • The metabolic fate of mitochondrial hydrogen peroxide
    • Nohl H, Jordan W. The metabolic fate of mitochondrial hydrogen peroxide. Eur J Biochem 1980 111 : 203 210.
    • (1980) Eur J Biochem , vol.111 , pp. 203-210
    • Nohl, H.1    Jordan, W.2
  • 48
    • 0031984162 scopus 로고    scopus 로고
    • Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability
    • Rigobello MP, Callegaro MT, Barzon E, Benetti M, Bindoli A. Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability. Free Radic Biol Med 1998 24 : 370 376.
    • (1998) Free Radic Biol Med , vol.24 , pp. 370-376
    • Rigobello, M.P.1    Callegaro, M.T.2    Barzon, E.3    Benetti, M.4    Bindoli, A.5
  • 50
    • 0023645831 scopus 로고
    • The mitochondrial inner membrane anion channel. Regulation by divalent cations and protons
    • Beavis AD, Garlid KD. The mitochondrial inner membrane anion channel. Regulation by divalent cations and protons. J Biol Chem 1987 262 : 15085 15093.
    • (1987) J Biol Chem , vol.262 , pp. 15085-15093
    • Beavis, A.D.1    Garlid, K.D.2
  • 51
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • Han D, Antunes F, Canali R, Rettori D, Cadenas E. Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol. J Biol Chem 2003 278 : 5557 5563.
    • (2003) J Biol Chem , vol.278 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 52
    • 3042732123 scopus 로고    scopus 로고
    • Fatty acids induce chloride permeation in rat liver mitochondria by activation of the inner membrane anion channel (IMAC)
    • Schonfeld P, Sayeed I, Bohnensack R, Siemen D. Fatty acids induce chloride permeation in rat liver mitochondria by activation of the inner membrane anion channel (IMAC). J Bioenerg Biomembr 2004 36 : 241 248.
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 241-248
    • Schonfeld, P.1    Sayeed, I.2    Bohnensack, R.3    Siemen, D.4
  • 53
    • 33845292901 scopus 로고    scopus 로고
    • Peroxisomes and oxidative stress
    • Schrader M, Fahimi HD. Peroxisomes and oxidative stress. Biochim Biophys Acta 2006 1763 : 1755 1766.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 1755-1766
    • Schrader, M.1    Fahimi, H.D.2
  • 54
    • 12344276944 scopus 로고    scopus 로고
    • Superoxide dismutase evolution and life span regulation
    • Landis GN, Tower J. Superoxide dismutase evolution and life span regulation. Mech Ageing Dev 2005 126 : 365 379.
    • (2005) Mech Ageing Dev , vol.126 , pp. 365-379
    • Landis, G.N.1    Tower, J.2
  • 55
    • 33746335977 scopus 로고    scopus 로고
    • Lysosomal ROS formation
    • Nohl H, Gille L. Lysosomal ROS formation. Redox Rep 2005 10 : 199 205.
    • (2005) Redox Rep , vol.10 , pp. 199-205
    • Nohl, H.1    Gille, L.2
  • 56
    • 33749047437 scopus 로고    scopus 로고
    • Localizing NADPH oxidase-derived ROS
    • Ushio-Fukai M. Localizing NADPH oxidase-derived ROS. Sci STKE 2006 2006 : re8.
    • (2006) Sci STKE , vol.2006
    • Ushio-Fukai, M.1
  • 57
    • 29244468563 scopus 로고    scopus 로고
    • The superoxide-producing NAD(P)H oxidase Nox4 in the nucleus of human vascular endothelial cells
    • Kuroda J, et al. The superoxide-producing NAD(P)H oxidase Nox4 in the nucleus of human vascular endothelial cells. Genes Cells 2005 10 : 1139 1151.
    • (2005) Genes Cells , vol.10 , pp. 1139-1151
    • Kuroda, J.1
  • 58
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A, Oshino N, Chance B. The cellular production of hydrogen peroxide. Biochem J 1972 128 : 617 630.
    • (1972) Biochem J , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 59
    • 16944361876 scopus 로고    scopus 로고
    • A mouse model for Zellweger syndrome
    • Baes M, et al. A mouse model for Zellweger syndrome. Nat Genet 1997 17 : 49 57.
    • (1997) Nat Genet , vol.17 , pp. 49-57
    • Baes, M.1
  • 60
    • 33744832661 scopus 로고    scopus 로고
    • Oxidative stress in asthma and COPD: Antioxidants as a therapeutic strategy
    • Kirkham P, Rahman I. Oxidative stress in asthma and COPD: antioxidants as a therapeutic strategy. Pharmacol Ther 2006 111 : 476 494.
    • (2006) Pharmacol Ther , vol.111 , pp. 476-494
    • Kirkham, P.1    Rahman, I.2
  • 61
    • 0842312531 scopus 로고    scopus 로고
    • Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants
    • Nelson DR, Zeldin DC, Hoffman SM, Maltais LJ, Wain HM, Nebert DW. Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 2004 14 : 1 18.
    • (2004) Pharmacogenetics , vol.14 , pp. 1-18
    • Nelson, D.R.1    Zeldin, D.C.2    Hoffman, S.M.3    Maltais, L.J.4    Wain, H.M.5    Nebert, D.W.6
  • 62
    • 4444268690 scopus 로고    scopus 로고
    • Mechanisms that regulate production of reactive oxygen species by cytochrome P450
    • Zangar RC, Davydov DR, Verma S. Mechanisms that regulate production of reactive oxygen species by cytochrome P450. Toxicol Appl Pharmacol 2004 199 : 316 331.
    • (2004) Toxicol Appl Pharmacol , vol.199 , pp. 316-331
    • Zangar, R.C.1    Davydov, D.R.2    Verma, S.3
  • 63
    • 1942424159 scopus 로고    scopus 로고
    • Antioxidant properties of S-adenosyl-l-methionine in Fe(2+)-initiated oxidations
    • Caro AA, Cederbaum AI. Antioxidant properties of S-adenosyl-l-methionine in Fe(2+)-initiated oxidations. Free Radic Biol Med 2004 36 : 1303 1316.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1303-1316
    • Caro, A.A.1    Cederbaum, A.I.2
  • 64
    • 0037478407 scopus 로고    scopus 로고
    • Human extrahepatic cytochromes P450: Function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts
    • Ding X, Kaminsky LS. Human extrahepatic cytochromes P450: function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts. Annu Rev Pharmacol Toxicol 2003 43 : 149 173.
    • (2003) Annu Rev Pharmacol Toxicol , vol.43 , pp. 149-173
    • Ding, X.1    Kaminsky, L.S.2
  • 65
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth JD. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 2004 4 : 181 189.
    • (2004) Nat Rev Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 66
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • Cheng G, Cao Z, Xu X, van Meir EG, Lambeth JD. Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 2001 269 : 131 140.
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    Van Meir, E.G.4    Lambeth, J.D.5
  • 67
    • 31744443116 scopus 로고    scopus 로고
    • Lipid raft clustering and redox signaling platform formation in coronary arterial endothelial cells
    • Zhang AY, Yi F, Zhang G, Gulbins E, Li PL. Lipid raft clustering and redox signaling platform formation in coronary arterial endothelial cells. Hypertension 2006 47 : 74 80.
    • (2006) Hypertension , vol.47 , pp. 74-80
    • Zhang, A.Y.1    Yi, F.2    Zhang, G.3    Gulbins, E.4    Li, P.L.5
  • 68
    • 33744913842 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase gamma signaling through protein kinase Czeta induces NADPH oxidase-mediated oxidant generation and NF-kappaB activation in endothelial cells
    • Frey RS, Gao X, Javaid K, Siddiqui SS, Rahman A, Malik AB. Phosphatidylinositol 3-kinase gamma signaling through protein kinase Czeta induces NADPH oxidase-mediated oxidant generation and NF-kappaB activation in endothelial cells. J Biol Chem 2006 281 : 16128 16138.
    • (2006) J Biol Chem , vol.281 , pp. 16128-16138
    • Frey, R.S.1    Gao, X.2    Javaid, K.3    Siddiqui, S.S.4    Rahman, A.5    Malik, A.B.6
  • 69
    • 0034617071 scopus 로고    scopus 로고
    • A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall
    • Gorlach A, Brandes RP, Nguyen K, Amidi M, Dehghani F, Busse R. A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall. Circ Res 2000 87 : 26 32.
    • (2000) Circ Res , vol.87 , pp. 26-32
    • Gorlach, A.1    Brandes, R.P.2    Nguyen, K.3    Amidi, M.4    Dehghani, F.5    Busse, R.6
  • 71
    • 33644750712 scopus 로고    scopus 로고
    • Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases
    • Ueyama T, Geiszt M, Leto TL. Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases. Mol Cell Biol 2006 26 : 2160 2174.
    • (2006) Mol Cell Biol , vol.26 , pp. 2160-2174
    • Ueyama, T.1    Geiszt, M.2    Leto, T.L.3
  • 72
    • 26244444476 scopus 로고    scopus 로고
    • Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
    • Martyn KD, Frederick LM, von Loehneysen K, Dinauer MC, Knaus UG. Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell Signal 2006 18 : 69 82.
    • (2006) Cell Signal , vol.18 , pp. 69-82
    • Martyn, K.D.1    Frederick, L.M.2    Von Loehneysen, K.3    Dinauer, M.C.4    Knaus, U.G.5
  • 73
    • 2442448436 scopus 로고    scopus 로고
    • 2+ activation of the NADPH oxidase 5 (NOX5)
    • 2+ activation of the NADPH oxidase 5 (NOX5). J Biol Chem 2004 279 : 18583 18591.
    • (2004) J Biol Chem , vol.279 , pp. 18583-18591
    • Banfi, B.1
  • 74
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri KF, Kroemer G. Organelle-specific initiation of cell death pathways. Nat Cell Biol 2001 3 : E255 E263.
    • (2001) Nat Cell Biol , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 75
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med 2000 6 : 513 519.
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 76
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green DR, Kroemer G. The pathophysiology of mitochondrial cell death. Science 2004 305 : 626 629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 77
    • 0035881713 scopus 로고    scopus 로고
    • New EMBO members' review: Viral and bacterial proteins regulating apoptosis at the mitochondrial level
    • Boya P, Roques B, Kroemer G. New EMBO members' review: viral and bacterial proteins regulating apoptosis at the mitochondrial level. EMBO J 2001 20 : 4325 4331.
    • (2001) EMBO J , vol.20 , pp. 4325-4331
    • Boya, P.1    Roques, B.2    Kroemer, G.3
  • 78
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M, Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 1999 399 : 483 487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 81
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • Baines CP, Kaiser RA, Sheiko T, Craigen WJ, Molkentin JD. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat Cell Biol 2007 9 : 550 555.
    • (2007) Nat Cell Biol , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 82
    • 0033582526 scopus 로고    scopus 로고
    • Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis
    • Sun XM, MacFarlane M, Zhuang J, Wolf BB, Green DR, Cohen GM. Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis. J Biol Chem 1999 274 : 5053 5060.
    • (1999) J Biol Chem , vol.274 , pp. 5053-5060
    • Sun, X.M.1    MacFarlane, M.2    Zhuang, J.3    Wolf, B.B.4    Green, D.R.5    Cohen, G.M.6
  • 83
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T, et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 2005 434 : 652 658.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1
  • 84
    • 0345529917 scopus 로고    scopus 로고
    • Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria
    • Petrosillo G, Ruggiero FM, Paradies G. Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria. FASEB J 2003 17 : 2202 2208.
    • (2003) FASEB J , vol.17 , pp. 2202-2208
    • Petrosillo, G.1    Ruggiero, F.M.2    Paradies, G.3
  • 85
    • 33644763298 scopus 로고    scopus 로고
    • Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis
    • Temkin V, Huang Q, Liu H, Osada H, Pope RM. Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis. Mol Cell Biol 2006 26 : 2215 2225.
    • (2006) Mol Cell Biol , vol.26 , pp. 2215-2225
    • Temkin, V.1    Huang, Q.2    Liu, H.3    Osada, H.4    Pope, R.M.5
  • 86
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003 114 : 181 190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 87
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L, Karin M. Mammalian MAP kinase signalling cascades. Nature 2001 410 : 37 40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 88
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover
    • Chang L, et al. The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover. Cell 2006 124 : 601 613.
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1
  • 89
    • 0030970013 scopus 로고    scopus 로고
    • Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
    • Thome M, et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 1997 386 : 517 521.
    • (1997) Nature , vol.386 , pp. 517-521
    • Thome, M.1
  • 91
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kagedal K, Zhao M, Svensson I, Brunk UT. Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem J 2001 359 : 335 343.
    • (2001) Biochem J , vol.359 , pp. 335-343
    • Kagedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 92
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route
    • Stoka V, et al. Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J Biol Chem 2001 276 : 3149 3157.
    • (2001) J Biol Chem , vol.276 , pp. 3149-3157
    • Stoka, V.1
  • 93
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N, Lorenzo HK, Carmona S, et al. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J Biol Chem 2003 278 : 31401 31411.
    • (2003) J Biol Chem , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3
  • 94
    • 22544442744 scopus 로고    scopus 로고
    • The cathepsin B death pathway contributes to TNF plus IFN-gamma-mediated human endothelial injury
    • Li JH, Pober JS. The cathepsin B death pathway contributes to TNF plus IFN-gamma-mediated human endothelial injury. J Immunol 2005 175 : 1858 1866.
    • (2005) J Immunol , vol.175 , pp. 1858-1866
    • Li, J.H.1    Pober, J.S.2
  • 95
    • 0040318886 scopus 로고    scopus 로고
    • CD40 signals apoptosis through FAN-regulated activation of the sphingomyelin-ceramide pathway
    • Segui B, et al. CD40 signals apoptosis through FAN-regulated activation of the sphingomyelin-ceramide pathway. J Biol Chem 1999 274 : 37251 37258.
    • (1999) J Biol Chem , vol.274 , pp. 37251-37258
    • Segui, B.1
  • 97
    • 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 HB, Baichwal V, Goeddel DV. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 1996 4 : 387 396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 98
    • 0033821215 scopus 로고    scopus 로고
    • The death domain kinase RIP is essential for TRAIL (Apo2L)-induced activation of IkappaB kinase and c-Jun N-terminal kinase
    • Lin Y, et al. The death domain kinase RIP is essential for TRAIL (Apo2L)-induced activation of IkappaB kinase and c-Jun N-terminal kinase. Mol Cell Biol 2000 20 : 6638 6645.
    • (2000) Mol Cell Biol , vol.20 , pp. 6638-6645
    • Lin, Y.1
  • 100
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: Crucial integrators of cellular stress
    • Meylan E, Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem Sci 2005 30 : 151 159.
    • (2005) Trends Biochem Sci , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 101
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin Y, Devin A, Rodriguez Y, Liu ZG. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev 1999 13 : 2514 2526.
    • (1999) Genes Dev , vol.13 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 102
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler N, et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol 2000 1 : 489 495.
    • (2000) Nat Immunol , vol.1 , pp. 489-495
    • Holler, N.1
  • 103
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger BZ, Leder P, Lee TH, Kim E, Seed B. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 1995 81 : 513 523.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 104
    • 0042090891 scopus 로고    scopus 로고
    • The role of the death-domain kinase RIP in tumour-necrosis-factor-induced activation of mitogen-activated protein kinases
    • Devin A, Lin Y, Liu ZG. The role of the death-domain kinase RIP in tumour-necrosis-factor-induced activation of mitogen-activated protein kinases. EMBO Rep 2003 4 : 623 627.
    • (2003) EMBO Rep , vol.4 , pp. 623-627
    • Devin, A.1    Lin, Y.2    Liu, Z.G.3
  • 105
    • 0031045588 scopus 로고    scopus 로고
    • CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP
    • Ahmad M, et al. CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. Cancer Res 1997 57 : 615 619.
    • (1997) Cancer Res , vol.57 , pp. 615-619
    • Ahmad, M.1
  • 106
    • 3543097542 scopus 로고    scopus 로고
    • RIP links TLR4 to Akt and is essential for cell survival in response to LPS stimulation
    • Vivarelli MS, McDonald D, Miller M, Cusson N, Kelliher M, Geha RS. RIP links TLR4 to Akt and is essential for cell survival in response to LPS stimulation. J Exp Med 2004 200 : 399 404.
    • (2004) J Exp Med , vol.200 , pp. 399-404
    • Vivarelli, M.S.1    McDonald, D.2    Miller, M.3    Cusson, N.4    Kelliher, M.5    Geha, R.S.6
  • 107
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P, Opitz-Araya X, Lazebnik Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science 2002 297 : 1352 1354.
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 108
    • 9744221185 scopus 로고    scopus 로고
    • Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak
    • Majewski N, et al. Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak. Mol Cell 2004 16 : 819 830.
    • (2004) Mol Cell , vol.16 , pp. 819-830
    • Majewski, N.1
  • 109
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007 87 : 99 163.
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 110
    • 0032006449 scopus 로고    scopus 로고
    • The mitochondrial ADP/ATP carrier: Structural, physiological and pathological aspects
    • Fiore C, et al. The mitochondrial ADP/ATP carrier: structural, physiological and pathological aspects. Biochimie 1998 80 : 137 150.
    • (1998) Biochimie , vol.80 , pp. 137-150
    • Fiore, C.1
  • 111
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines CP, et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 2005 434 : 658 662.
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1
  • 112
    • 1542332908 scopus 로고    scopus 로고
    • Cyclophilin D, a component of the permeability transition-pore, is an apoptosis repressor
    • Schubert A, Grimm S. Cyclophilin D, a component of the permeability transition-pore, is an apoptosis repressor. Cancer Res 2004 64 : 85 93.
    • (2004) Cancer Res , vol.64 , pp. 85-93
    • Schubert, A.1    Grimm, S.2
  • 113
    • 0033215256 scopus 로고    scopus 로고
    • Disturbance of myocardial energy metabolism in experimental virus myocarditis by antibodies against the adenine nucleotide translocator
    • Schulze K, Witzenbichler B, Christmann C, Schultheiss HP. Disturbance of myocardial energy metabolism in experimental virus myocarditis by antibodies against the adenine nucleotide translocator. Cardiovasc Res 1999 44 : 91 100.
    • (1999) Cardiovasc Res , vol.44 , pp. 91-100
    • Schulze, K.1    Witzenbichler, B.2    Christmann, C.3    Schultheiss, H.P.4
  • 114
    • 16344384536 scopus 로고    scopus 로고
    • Adeno-associated virus-mediated gene transfer of the heart/muscle adenine nucleotide translocator (ANT) in mouse
    • Flierl A, Chen Y, Coskun PE, Samulski RJ, Wallace DC. Adeno-associated virus-mediated gene transfer of the heart/muscle adenine nucleotide translocator (ANT) in mouse. Gene Ther 2005 12 : 570 578.
    • (2005) Gene Ther , vol.12 , pp. 570-578
    • Flierl, A.1    Chen, Y.2    Coskun, P.E.3    Samulski, R.J.4    Wallace, D.C.5
  • 115
    • 0038601994 scopus 로고    scopus 로고
    • Evidence that reactive oxygen species do not mediate NF-kappaB activation
    • Hayakawa M, et al. Evidence that reactive oxygen species do not mediate NF-kappaB activation. EMBO J 2003 22 : 3356 3366.
    • (2003) EMBO J , vol.22 , pp. 3356-3366
    • Hayakawa, M.1
  • 116
    • 33645242238 scopus 로고    scopus 로고
    • 2-dependent recruitment of TRAF6 to endosomal interleukin-1 receptor complexes
    • 2-dependent recruitment of TRAF6 to endosomal interleukin-1 receptor complexes. Mol Cell Biol 2006 26 : 140 154.
    • (2006) Mol Cell Biol , vol.26 , pp. 140-154
    • Li, Q.1
  • 117
    • 20644433073 scopus 로고    scopus 로고
    • ROS-dependent activation of the TRAF6-ASK1-p38 pathway is selectively required for TLR4-mediated innate immunity
    • Matsuzawa A, et al. ROS-dependent activation of the TRAF6-ASK1-p38 pathway is selectively required for TLR4-mediated innate immunity. Nat Immunol 2005 6 : 587 592.
    • (2005) Nat Immunol , vol.6 , pp. 587-592
    • Matsuzawa, A.1
  • 118
    • 34248228729 scopus 로고    scopus 로고
    • Hemorrhagic shock induces NAD(P)H oxidase activation in neutrophils: Role of HMGB1-TLR4 signaling
    • Fan J, et al. Hemorrhagic shock induces NAD(P)H oxidase activation in neutrophils: role of HMGB1-TLR4 signaling. J Immunol 2007 178 : 6573 6580.
    • (2007) J Immunol , vol.178 , pp. 6573-6580
    • Fan, J.1
  • 119
    • 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 JY, Abraham E. Involvement of reactive oxygen species in Toll-like receptor 4-dependent activation of NF-kappa B. J Immunol 2004 172 : 2522 2529.
    • (2004) J Immunol , vol.172 , pp. 2522-2529
    • Asehnoune, K.1    Strassheim, D.2    Mitra, S.3    Kim, J.Y.4    Abraham, E.5
  • 120
    • 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 KA, Smith MF Jr., Sanders MK, Ernst PB. Reactive oxygen and nitrogen species differentially regulate Toll-like receptor 4-mediated activation of NF-kappa B and interleukin-8 expression. Infect Immun 2004 72 : 2123 2130.
    • (2004) Infect Immun , vol.72 , pp. 2123-2130
    • Ryan, K.A.1    Smith Jr., M.F.2    Sanders, M.K.3    Ernst, P.B.4
  • 121
    • 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 HS, Jung HY, Park EY, Kim J, Lee WJ, Bae YS. 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 2004 173 : 3589 3593.
    • (2004) J Immunol , vol.173 , pp. 3589-3593
    • Park, H.S.1    Jung, H.Y.2    Park, E.Y.3    Kim, J.4    Lee, W.J.5    Bae, Y.S.6
  • 122
    • 22144457305 scopus 로고    scopus 로고
    • A crucial role for reactive oxygen species in RANKL-induced osteoclast differentiation
    • Lee NK, et al. A crucial role for reactive oxygen species in RANKL-induced osteoclast differentiation. Blood 2005 106 : 852 859.
    • (2005) Blood , vol.106 , pp. 852-859
    • Lee, N.K.1
  • 123
    • 1642602694 scopus 로고    scopus 로고
    • Gadd45 beta mediates the NF-kappa B suppression of JNK signalling by targeting MKK7/JNKK2
    • Papa S, et al. Gadd45 beta mediates the NF-kappa B suppression of JNK signalling by targeting MKK7/JNKK2. Nat Cell Biol 2004 6 : 146 153.
    • (2004) Nat Cell Biol , vol.6 , pp. 146-153
    • Papa, S.1
  • 124
    • 0035889252 scopus 로고    scopus 로고
    • Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling
    • De Smaele E, et al. Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling. Nature 2001 414 : 308 313.
    • (2001) Nature , vol.414 , pp. 308-313
    • De Smaele, E.1
  • 125
    • 0035891320 scopus 로고    scopus 로고
    • Inhibition of JNK activation through NF-kappaB target genes
    • Tang G, et al. Inhibition of JNK activation through NF-kappaB target genes. Nature 2001 414 : 313 317.
    • (2001) Nature , vol.414 , pp. 313-317
    • Tang, G.1
  • 126
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin M, Lin A. NF-kappaB at the crossroads of life and death. Nat Immunol 2002 3 : 221 227.
    • (2002) Nat Immunol , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 127
    • 0344496062 scopus 로고    scopus 로고
    • IKKbeta is required for prevention of apoptosis mediated by cell-bound but not by circulating TNFalpha
    • Maeda S, Chang L, Li ZW, Luo JL, Leffert H, Karin M. IKKbeta is required for prevention of apoptosis mediated by cell-bound but not by circulating TNFalpha. Immunity 2003 19 : 725 737.
    • (2003) Immunity , vol.19 , pp. 725-737
    • Maeda, S.1    Chang, L.2    Li, Z.W.3    Luo, J.L.4    Leffert, H.5    Karin, M.6
  • 128
    • 0141953270 scopus 로고    scopus 로고
    • A JNK-dependent pathway is required for TNFalpha-induced apoptosis
    • Deng Y, Ren X, Yang L, Lin Y, Wu X. A JNK-dependent pathway is required for TNFalpha-induced apoptosis. Cell 2003 115 : 61 70.
    • (2003) Cell , vol.115 , pp. 61-70
    • Deng, Y.1    Ren, X.2    Yang, L.3    Lin, Y.4    Wu, X.5
  • 129
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998 94 : 481 490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 130
    • 33846154622 scopus 로고    scopus 로고
    • Bid-independent mitochondrial activation in tumor necrosis factor alpha-induced apoptosis and liver injury
    • Chen X, et al. Bid-independent mitochondrial activation in tumor necrosis factor alpha-induced apoptosis and liver injury. Mol Cell Biol 2007 27 : 541 553.
    • (2007) Mol Cell Biol , vol.27 , pp. 541-553
    • Chen, X.1
  • 131
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • Yeh WC, et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity 2000 12 : 633 642.
    • (2000) Immunity , vol.12 , pp. 633-642
    • Yeh, W.C.1
  • 132
    • 0035065836 scopus 로고    scopus 로고
    • ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
    • Tobiume K, et al. ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis. EMBO Rep 2001 2 : 222 228.
    • (2001) EMBO Rep , vol.2 , pp. 222-228
    • Tobiume, K.1
  • 134
    • 33751558995 scopus 로고    scopus 로고
    • An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway
    • Nakajima A, et al. An antiapoptotic protein, c-FLIPL, directly binds to MKK7 and inhibits the JNK pathway. EMBO J 2006 25 : 5549 5559.
    • (2006) EMBO J , vol.25 , pp. 5549-5559
    • Nakajima, A.1
  • 135
    • 0037188936 scopus 로고    scopus 로고
    • Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner
    • Liu Y, Min W. Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner. Circ Res 2002 90 : 1259 1266.
    • (2002) Circ Res , vol.90 , pp. 1259-1266
    • Liu, Y.1    Min, W.2
  • 136
    • 10044265209 scopus 로고    scopus 로고
    • JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species
    • Ventura JJ, Cogswell P, Flavell RA, Baldwin AS Jr., Davis RJ. JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species. Genes Dev 2004 18 : 2905 2915.
    • (2004) Genes Dev , vol.18 , pp. 2905-2915
    • Ventura, J.J.1    Cogswell, P.2    Flavell, R.A.3    Baldwin Jr., A.S.4    Davis, R.J.5
  • 137
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • Bonizzi G, Karin M. The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol 2004 25 : 280 288.
    • (2004) Trends Immunol , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 138
    • 0033532386 scopus 로고    scopus 로고
    • The IKKbeta subunit of IkappaB kinase (IKK) is essential for nuclear factor kappaB activation and prevention of apoptosis
    • Li ZW, et al. The IKKbeta subunit of IkappaB kinase (IKK) is essential for nuclear factor kappaB activation and prevention of apoptosis. J Exp Med 1999 189 : 1839 1845.
    • (1999) J Exp Med , vol.189 , pp. 1839-1845
    • Li, Z.W.1
  • 139
    • 0033537739 scopus 로고    scopus 로고
    • Severe liver degeneration in mice lacking the IkappaB kinase 2 gene
    • Li Q, Van Antwerp D, Mercurio F, Lee KF, Verma IM. Severe liver degeneration in mice lacking the IkappaB kinase 2 gene. Science 1999 284 : 321 325.
    • (1999) Science , vol.284 , pp. 321-325
    • Li, Q.1    Van Antwerp, D.2    Mercurio, F.3    Lee, K.F.4    Verma, I.M.5
  • 140
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang CY, Mayo MW, Korneluk RG, Goeddel DV, Baldwin AS Jr. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 1998 281 : 1680 1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin Jr., A.S.5
  • 141
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kappaB in preventing TNF-alpha-induced cell death
    • Beg AA, Baltimore D. An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 1996 274 : 782 784.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 142
    • 0037428382 scopus 로고    scopus 로고
    • Oxidized LDL promotes peroxide-mediated mitochondrial dysfunction and cell death in human macrophages: A caspase-3-independent pathway
    • Asmis R, Begley JG. Oxidized LDL promotes peroxide-mediated mitochondrial dysfunction and cell death in human macrophages: a caspase-3-independent pathway. Circ Res 2003 92 : e20 e29.
    • (2003) Circ Res , vol.92
    • Asmis, R.1    Begley, J.G.2
  • 143
    • 0033634663 scopus 로고    scopus 로고
    • Female mice heterozygous for IKK gamma/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti
    • Makris C, et al. Female mice heterozygous for IKK gamma/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti. Mol Cell 2000 5 : 969 979.
    • (2000) Mol Cell , vol.5 , pp. 969-979
    • Makris, C.1
  • 144
    • 24944554790 scopus 로고    scopus 로고
    • Signaling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-kappaB as key regulators
    • Park JM, et al. Signaling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-kappaB as key regulators. Immunity 2005 23 : 319 329.
    • (2005) Immunity , vol.23 , pp. 319-329
    • Park, J.M.1
  • 145
    • 33646380068 scopus 로고    scopus 로고
    • At the gates of death
    • Green DR. At the gates of death. Cancer Cell 2006 9 : 328 330.
    • (2006) Cancer Cell , vol.9 , pp. 328-330
    • Green, D.R.1
  • 146
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana T, et al. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol Cell 2005 17 : 525 535.
    • (2005) Mol Cell , vol.17 , pp. 525-535
    • Kuwana, T.1
  • 147
    • 33751513394 scopus 로고    scopus 로고
    • Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies
    • Kim H, et al. Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies. Nat Cell Biol 2006 8 : 1348 1358.
    • (2006) Nat Cell Biol , vol.8 , pp. 1348-1358
    • Kim, H.1
  • 148
    • 1642566525 scopus 로고    scopus 로고
    • TNF-alpha-induced apoptosis of macrophages following inhibition of NF-kappaB: A central role for disruption of mitochondria
    • Liu H, et al. TNF-alpha-induced apoptosis of macrophages following inhibition of NF-kappaB: a central role for disruption of mitochondria. J Immunol 2004 172 : 1907 1915.
    • (2004) J Immunol , vol.172 , pp. 1907-1915
    • Liu, H.1
  • 149
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 1995 83 : 1243 1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 150
    • 0037149542 scopus 로고    scopus 로고
    • TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2
    • Li X, Yang Y, Ashwell JD. TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. Nature 2002 416 : 345 347.
    • (2002) Nature , vol.416 , pp. 345-347
    • Li, X.1    Yang, Y.2    Ashwell, J.D.3
  • 151
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • Wertz IE, et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature 2004 430 : 694 699.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 152
    • 0141753121 scopus 로고    scopus 로고
    • NF-kappaB protects from the lysosomal pathway of cell death
    • Liu N, et al. NF-kappaB protects from the lysosomal pathway of cell death. EMBO J 2003 22 : 5313 5322.
    • (2003) EMBO J , vol.22 , pp. 5313-5322
    • Liu, N.1
  • 153
    • 0030692715 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha and interleukin-1beta regulate the murine manganese superoxide dismutase gene through a complex intronic enhancer involving C/EBP-beta and NF-kappaB
    • Jones PL, Ping D, Boss JM. Tumor necrosis factor alpha and interleukin-1beta regulate the murine manganese superoxide dismutase gene through a complex intronic enhancer involving C/EBP-beta and NF-kappaB. Mol Cell Biol 1997 17 : 6970 6981.
    • (1997) Mol Cell Biol , vol.17 , pp. 6970-6981
    • Jones, P.L.1    Ping, D.2    Boss, J.M.3
  • 154
    • 0032588841 scopus 로고    scopus 로고
    • An intronic NF-kappaB element is essential for induction of the human manganese superoxide dismutase gene by tumor necrosis factor-alpha and interleukin-1beta
    • Xu Y, et al. An intronic NF-kappaB element is essential for induction of the human manganese superoxide dismutase gene by tumor necrosis factor-alpha and interleukin-1beta. DNA Cell Biol 1999 18 : 709 722.
    • (1999) DNA Cell Biol , vol.18 , pp. 709-722
    • Xu, Y.1
  • 155
    • 0031940986 scopus 로고    scopus 로고
    • A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase
    • Melov S, et al. A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase. Nat Genet 1998 18 : 159 163.
    • (1998) Nat Genet , vol.18 , pp. 159-163
    • Melov, S.1
  • 156
    • 34247527844 scopus 로고    scopus 로고
    • Mutation of an IKK phosphorylation site within the transactivation domain of REL in two patients with B-cell lymphoma enhances REL's in vitro transforming activity
    • Starczynowski DT, et al. Mutation of an IKK phosphorylation site within the transactivation domain of REL in two patients with B-cell lymphoma enhances REL's in vitro transforming activity. Oncogene 2007 26 : 2685 2694.
    • (2007) Oncogene , vol.26 , pp. 2685-2694
    • Starczynowski, D.T.1
  • 157
    • 0024987513 scopus 로고
    • Effect of butylated hydroxyanisole on electron transport in rat liver mitochondria
    • Ferreira J. Effect of butylated hydroxyanisole on electron transport in rat liver mitochondria. Biochem Pharmacol 1990 40 : 677 684.
    • (1990) Biochem Pharmacol , vol.40 , pp. 677-684
    • Ferreira, J.1
  • 158
    • 0042467735 scopus 로고    scopus 로고
    • Cell signalling: Cell survival and a Gadd45-factor deficiency
    • discussion 742.
    • Amanullah A, et al. Cell signalling: cell survival and a Gadd45-factor deficiency. Nature 2003 424 : 741 discussion 742.
    • (2003) Nature , vol.424 , pp. 741
    • Amanullah, A.1
  • 159
    • 17244365963 scopus 로고    scopus 로고
    • Angiogenesis in rheumatoid arthritis
    • Szekanecz Z, Gaspar L, Koch AE. Angiogenesis in rheumatoid arthritis. Front Biosci 2005 10 : 1739 1753.
    • (2005) Front Biosci , vol.10 , pp. 1739-1753
    • Szekanecz, Z.1    Gaspar, L.2    Koch, A.E.3
  • 160
    • 0032981308 scopus 로고    scopus 로고
    • Pathogenesis of joint damage in rheumatoid arthritis
    • Bresnihan B. Pathogenesis of joint damage in rheumatoid arthritis. J Rheumatol 1999 26 : 717 719.
    • (1999) J Rheumatol , vol.26 , pp. 717-719
    • Bresnihan, B.1
  • 161
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • Babior BM. Phagocytes and oxidative stress. Am J Med 2000 109 : 33 44.
    • (2000) Am J Med , vol.109 , pp. 33-44
    • Babior, B.M.1
  • 163
    • 0344154565 scopus 로고    scopus 로고
    • Antioxidant status in rheumatoid arthritis and role of antioxidant therapy
    • Jaswal S, Mehta HC, Sood AK, Kaur J. Antioxidant status in rheumatoid arthritis and role of antioxidant therapy. Clin Chim Acta 2003 338 : 123 129.
    • (2003) Clin Chim Acta , vol.338 , pp. 123-129
    • Jaswal, S.1    Mehta, H.C.2    Sood, A.K.3    Kaur, J.4
  • 164
    • 0029956657 scopus 로고    scopus 로고
    • Enhanced mitochondrial radical production in patients which rheumatoid arthritis correlates with elevated levels of tumor necrosis factor alpha in plasma
    • Miesel R, Murphy MP, Kroger H. Enhanced mitochondrial radical production in patients which rheumatoid arthritis correlates with elevated levels of tumor necrosis factor alpha in plasma. Free Radic Res 1996 25 : 161 169.
    • (1996) Free Radic Res , vol.25 , pp. 161-169
    • Miesel, R.1    Murphy, M.P.2    Kroger, H.3
  • 165
    • 18244381844 scopus 로고    scopus 로고
    • Thioredoxin as a biomarker for oxidative stress in patients with rheumatoid arthritis
    • Jikimoto T, et al. Thioredoxin as a biomarker for oxidative stress in patients with rheumatoid arthritis. Mol Immunol 2002 38 : 765 772.
    • (2002) Mol Immunol , vol.38 , pp. 765-772
    • Jikimoto, T.1
  • 166
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: Not just for leukocytes anymore!
    • Bokoch GM, Knaus UG. NADPH oxidases: not just for leukocytes anymore! Trends Biochem Sci 2003 28 : 502 508.
    • (2003) Trends Biochem Sci , vol.28 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 167
    • 33745843632 scopus 로고    scopus 로고
    • A specific p47-serine phosphorylated by convergent MAPKs mediates neutrophil NADPH oxidase priming at inflammatory sites
    • Dang PM, et al. A specific p47-serine phosphorylated by convergent MAPKs mediates neutrophil NADPH oxidase priming at inflammatory sites. J Clin Invest 2006 116 : 2033 2043.
    • (2006) J Clin Invest , vol.116 , pp. 2033-2043
    • Dang, P.M.1
  • 168
    • 0037224772 scopus 로고    scopus 로고
    • Positional identification of Ncf1 as a gene that regulates arthritis severity in rats
    • Olofsson P, Holmberg J, Tordsson J, Lu S, Akerstrom B, Holmdahl R. Positional identification of Ncf1 as a gene that regulates arthritis severity in rats. Nat Genet 2003 33 : 25 32.
    • (2003) Nat Genet , vol.33 , pp. 25-32
    • Olofsson, P.1    Holmberg, J.2    Tordsson, J.3    Lu, S.4    Akerstrom, B.5    Holmdahl, R.6
  • 169
    • 4344591766 scopus 로고    scopus 로고
    • Enhanced autoimmunity, arthritis, and encephalomyelitis in mice with a reduced oxidative burst due to a mutation in the Ncf1 gene
    • Hultqvist M, Olofsson P, Holmberg J, Backstrom BT, Tordsson J, Holmdahl R. Enhanced autoimmunity, arthritis, and encephalomyelitis in mice with a reduced oxidative burst due to a mutation in the Ncf1 gene. Proc Natl Acad Sci USA 2004 101 : 12646 12651.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12646-12651
    • Hultqvist, M.1    Olofsson, P.2    Holmberg, J.3    Backstrom, B.T.4    Tordsson, J.5    Holmdahl, R.6
  • 171
    • 0036636094 scopus 로고    scopus 로고
    • Apoptosis as a therapeutic tool in rheumatoid arthritis
    • Pope RM. Apoptosis as a therapeutic tool in rheumatoid arthritis. Nat Rev Immunol 2002 2 : 527 535.
    • (2002) Nat Rev Immunol , vol.2 , pp. 527-535
    • Pope, R.M.1
  • 172
    • 33846928411 scopus 로고    scopus 로고
    • NF-kappaB prevents beta cell death and autoimmune diabetes in NOD mice
    • Kim S, et al. NF-kappaB prevents beta cell death and autoimmune diabetes in NOD mice. Proc Natl Acad Sci USA 2007 104 : 1913 1918.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1913-1918
    • Kim, S.1
  • 173
    • 33644749322 scopus 로고    scopus 로고
    • Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: Many differences, few similarities
    • Cnop M, Welsh N, Jonas JC, Jorns A, Lenzen S, Eizirik DL. Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: many differences, few similarities. Diabetes 2005 54 (Suppl.) : S97 S107.
    • (2005) Diabetes , vol.54
    • Cnop, M.1    Welsh, N.2    Jonas, J.C.3    Jorns, A.4    Lenzen, S.5    Eizirik, D.L.6
  • 174
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001 414 : 813 820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 175
    • 0033526068 scopus 로고    scopus 로고
    • In autoimmune diabetes the transition from benign to pernicious insulitis requires an islet cell response to tumor necrosis factor alpha
    • Pakala SV, Chivetta M, Kelly CB, Katz JD. In autoimmune diabetes the transition from benign to pernicious insulitis requires an islet cell response to tumor necrosis factor alpha. J Exp Med 1999 189 : 1053 1062.
    • (1999) J Exp Med , vol.189 , pp. 1053-1062
    • Pakala, S.V.1    Chivetta, M.2    Kelly, C.B.3    Katz, J.D.4
  • 176
    • 33750823407 scopus 로고    scopus 로고
    • Saturated fatty acids inhibit induction of insulin gene transcription by JNK-mediated phosphorylation of insulin-receptor substrates
    • Solinas G, Naugler W, Galimi F, Lee MS, Karin M. Saturated fatty acids inhibit induction of insulin gene transcription by JNK-mediated phosphorylation of insulin-receptor substrates. Proc Natl Acad Sci USA 2006 103 : 16454 16459.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16454-16459
    • Solinas, G.1    Naugler, W.2    Galimi, F.3    Lee, M.S.4    Karin, M.5
  • 177
    • 0037153158 scopus 로고    scopus 로고
    • A central role for JNK in obesity and insulin resistance
    • Hirosumi J, et al. A central role for JNK in obesity and insulin resistance. Nature 2002 420 : 333 336.
    • (2002) Nature , vol.420 , pp. 333-336
    • Hirosumi, J.1
  • 178
    • 21044453408 scopus 로고    scopus 로고
    • Disruption of the Jnk2 (Mapk9) gene reduces destructive insulitis and diabetes in a mouse model of type I diabetes
    • Jaeschke A, et al. Disruption of the Jnk2 (Mapk9) gene reduces destructive insulitis and diabetes in a mouse model of type I diabetes. Proc Natl Acad Sci USA 2005 102 : 6931 6935.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6931-6935
    • Jaeschke, A.1
  • 179
    • 33645860825 scopus 로고    scopus 로고
    • Reactive oxygen species have a causal role in multiple forms of insulin resistance
    • Houstis N, Rosen ED, Lander ES. Reactive oxygen species have a causal role in multiple forms of insulin resistance. Nature 2006 440 : 944 948.
    • (2006) Nature , vol.440 , pp. 944-948
    • Houstis, N.1    Rosen, E.D.2    Lander, E.S.3
  • 180
    • 33746466098 scopus 로고    scopus 로고
    • Mitochondrial mutations in cancer
    • Brandon M, Baldi P, Wallace DC. Mitochondrial mutations in cancer. Oncogene 2006 25 : 4647 4662.
    • (2006) Oncogene , vol.25 , pp. 4647-4662
    • Brandon, M.1    Baldi, P.2    Wallace, D.C.3


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