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Volumn 8, Issue 9-10, 2006, Pages 1819-1827

Regulation of signal transduction through protein cysteine oxidation

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CYSTEINE; PHOSPHATASE; PROTEIN KINASE; REACTIVE OXYGEN METABOLITE; THIOL GROUP; TRANSCRIPTION FACTOR;

EID: 33750915802     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.1819     Document Type: Review
Times cited : (148)

References (78)
  • 1
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi T, Pimentel DR, Heibeck T, Hou X, Lee YJ, Jiang B, Ido Y, and Cohen RA. S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem 279: 29857-2986, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 29857-32986
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 3
    • 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, and Abraham E. Involvement of reactive oxygen species in Toll-like receptor 4-dependent activation of NF-kappa B. J Immunol 172: 2522-2529, 2004.
    • (2004) J Immunol , vol.172 , pp. 2522-2529
    • Asehnoune, K.1    Strassheim, D.2    Mitra, S.3    Kim, J.Y.4    Abraham, E.5
  • 4
    • 0037219109 scopus 로고    scopus 로고
    • Improvement of the mitochondrial antioxidant defense status prevents cytokine-induced nuclear factor-kappaB activation in insulin-producing cells
    • Azevedo-Martins AK, Lortz S, Lenzen S, Curi R, Eizirik DL, and Tiedge M. Improvement of the mitochondrial antioxidant defense status prevents cytokine-induced nuclear factor-kappaB activation in insulin-producing cells. Diabetes 52: 93-101, 2003.
    • (2003) Diabetes , vol.52 , pp. 93-101
    • Azevedo-Martins, A.K.1    Lortz, S.2    Lenzen, S.3    Curi, R.4    Eizirik, D.L.5    Tiedge, M.6
  • 6
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch GM and Diebold BA. Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood 100: 2692-2696, 2002.
    • (2002) Blood , vol.100 , pp. 2692-2696
    • Bokoch, G.M.1    Diebold, B.A.2
  • 7
    • 0032484012 scopus 로고    scopus 로고
    • The inactivation mechanism of low molecular weight phosphotyrosine- protein phosphatase by H2O2
    • Caselli A, Marzocchini R, Camici G, Manao G, Moneti G, Pieraccini G, and Ramponi G. The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J Biol Chem 273: 32554-32560, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 32554-32560
    • Caselli, A.1    Marzocchini, R.2    Camici, G.3    Manao, G.4    Moneti, G.5    Pieraccini, G.6    Ramponi, G.7
  • 8
    • 0034903753 scopus 로고    scopus 로고
    • Potent inactivation of representative members of each PKC isozyme subfamily and PKD via 5-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine
    • Chu F, Ward NE, and O'Brian CA Potent inactivation of representative members of each PKC isozyme subfamily and PKD via 5-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine. Carcinogenesis 22: 1221-1229, 2001.
    • (2001) Carcinogenesis , vol.22 , pp. 1221-1229
    • Chu, F.1    Ward, N.E.2    O'Brian, C.A.3
  • 9
    • 0037325938 scopus 로고    scopus 로고
    • PKC isozyme S-cysteinylation by cystine stimulates the pro-apoptotic isozyme PKC delta and inactivates the oncogenic isozyme PKC epsilon
    • Chu F, Ward NE, and O'Brian CA. PKC isozyme S-cysteinylation by cystine stimulates the pro-apoptotic isozyme PKC delta and inactivates the oncogenic isozyme PKC epsilon. Carcinogenesis 24: 317-325, 2003.
    • (2003) Carcinogenesis , vol.24 , pp. 317-325
    • Chu, F.1    Ward, N.E.2    O'Brian, C.A.3
  • 10
    • 4344686072 scopus 로고    scopus 로고
    • Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP binding domain
    • Cross JV and Templeton DJ. Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP binding domain. Biochem J 381: 675-683, 2004.
    • (2004) Biochem J , vol.381 , pp. 675-683
    • Cross, J.V.1    Templeton, D.J.2
  • 11
    • 16644387391 scopus 로고    scopus 로고
    • Thiol oxidation of cell signaling proteins: Controlling an apoptotic equilibrium
    • Cross JV and Templeton DJ. Thiol oxidation of cell signaling proteins: Controlling an apoptotic equilibrium. J Cell Biochem 93: 104-111, 2004.
    • (2004) J Cell Biochem , vol.93 , pp. 104-111
    • Cross, J.V.1    Templeton, D.J.2
  • 12
    • 1042298162 scopus 로고    scopus 로고
    • Reactive nitrogen species in the chemical biology of inflammation
    • Dedon PC and Tannenbaum SR. Reactive nitrogen species in the chemical biology of inflammation. Arch Biochem Biophys 423: 12-22, 2004.
    • (2004) Arch Biochem Biophys , vol.423 , pp. 12-22
    • Dedon, P.C.1    Tannenbaum, S.R.2
  • 13
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu JM and Tanner KG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37: 5633-5642, 1998.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 14
    • 0037033433 scopus 로고    scopus 로고
    • Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: Selective regulation of mitogen-activated protein kinase activation and fas ligand expression
    • Devadas S, Zaritskaya L, Rhee SG, Oberley L, and Williams MS. Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression. J Exp Med 195: 59-70, 2002.
    • (2002) J Exp Med , vol.195 , pp. 59-70
    • Devadas, S.1    Zaritskaya, L.2    Rhee, S.G.3    Oberley, L.4    Williams, M.S.5
  • 15
    • 0037163046 scopus 로고    scopus 로고
    • Activation of the p38 signaling pathway by heat shock involves the dissociation of glutathione S-transferase Mu from Ask1
    • Dorion S, Lambert H, and Landry J. Activation of the p38 signaling pathway by heat shock involves the dissociation of glutathione S-transferase Mu from Ask1. J Biol Chem 277: 30792-30797, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 30792-30797
    • Dorion, S.1    Lambert, H.2    Landry, J.3
  • 16
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins 5-thiolated during ischemia and reperfusion
    • Eaton P, Byers HL, Leeds N, Ward MA, and Shattock MJ. Detection, quantitation, purification, and identification of cardiac proteins 5-thiolated during ischemia and reperfusion. J Biol Chem 277: 9806-9811, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 17
    • 0036139524 scopus 로고    scopus 로고
    • Reactive oxygen species and signal transduction
    • Finkel T. Reactive oxygen species and signal transduction. IUBMB Life 52: 3-6, 2001.
    • (2001) IUBMB Life , vol.52 , pp. 3-6
    • Finkel, T.1
  • 18
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
    • Forman HJ and Torres M. Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am J Respir Crit Care Med 166: S4-8, 2002.
    • (2002) Am J Respir Crit Care Med , vol.166
    • Forman, H.J.1    Torres, M.2
  • 19
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: Thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman HJ, Fukuto JM, and Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 287: C246-256, 2004.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 20
    • 0034092777 scopus 로고    scopus 로고
    • Ras regulation and function in lymphocytes
    • Genot E and Cantrell DA. Ras regulation and function in lymphocytes. Curr Opin Immunol 12: 289-294, 2000.
    • (2000) Curr Opin Immunol , vol.12 , pp. 289-294
    • Genot, E.1    Cantrell, D.A.2
  • 21
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • Ghezzi P. Regulation of protein function by glutathionylation. Free Radic Res 39: 573-580, 2005.
    • (2005) Free Radic Res , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 22
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, and Kopp EB. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16: 225-260, 1998.
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 23
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • Ghosh S and Karin M. Missing pieces in the NF-kappaB puzzle. Cell 109 Suppl: S81-96, 2002.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Ghosh, S.1    Karin, M.2
  • 24
    • 0347994954 scopus 로고    scopus 로고
    • Role of TNF receptor-associated factor 3 in the CD40 signaling by production of reactive oxygen species through association with p40phox, a cytosolic subunit of nicotinamide adenine dinucleotide phosphate oxidase
    • Ha YJ and Lee JR. Role of TNF receptor-associated factor 3 in the CD40 signaling by production of reactive oxygen species through association with p40phox, a cytosolic subunit of nicotinamide adenine dinucleotide phosphate oxidase. J Immunol 172: 231-239, 2004.
    • (2004) J Immunol , vol.172 , pp. 231-239
    • Ha, Y.J.1    Lee, J.R.2
  • 25
    • 0027473778 scopus 로고
    • Tumour necrosis factor-alpha induces superoxide anion generation in mitochondria of L929 cells
    • Hennet T, Richter C, and Peterhans E. Tumour necrosis factor-alpha induces superoxide anion generation in mitochondria of L929 cells. Biochem J 289: 587-592, 1993.
    • (1993) Biochem J , vol.289 , pp. 587-592
    • Hennet, T.1    Richter, C.2    Peterhans, E.3
  • 27
    • 0030997261 scopus 로고    scopus 로고
    • Activation of CPP32-like protease in tumor necrosis factor-induced apoptosis is dependent on mitochondrial function
    • Higuchi M, Aggarwal BB, and Yeh ET. Activation of CPP32-like protease in tumor necrosis factor-induced apoptosis is dependent on mitochondrial function. J Clin Invest 99: 1751-1758, 1997.
    • (1997) J Clin Invest , vol.99 , pp. 1751-1758
    • Higuchi, M.1    Aggarwal, B.B.2    Yeh, E.T.3
  • 28
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 3: 239-243, 1995.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 29
    • 22144432216 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate the temporal activation of nuclear factor kappaB to modulate tumour necrosis factor-induced apoptosis: Evidence from mitochondria-targeted antioxidants
    • Hughes G, Murphy MP, and Ledgerwood EC. Mitochondrial reactive oxygen species regulate the temporal activation of nuclear factor kappaB to modulate tumour necrosis factor-induced apoptosis: evidence from mitochondria-targeted antioxidants. Biochem J 389: 83-89, 2005.
    • (2005) Biochem J , vol.389 , pp. 83-89
    • Hughes, G.1    Murphy, M.P.2    Ledgerwood, E.C.3
  • 30
    • 0037044782 scopus 로고    scopus 로고
    • Regulation of cAMP-dependent protein kinase activity by glutathionylation
    • Humphries KM, Juliano C, and Taylor SS. Regulation of cAMP-dependent protein kinase activity by glutathionylation. J Biol Chem 277: 43505-43511, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 43505-43511
    • Humphries, K.M.1    Juliano, C.2    Taylor, S.S.3
  • 31
    • 13244283230 scopus 로고    scopus 로고
    • Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification
    • Humphries KM, Deal MS, and Taylor SS. Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification. J Biol Chem 280: 2750-2758, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 2750-2758
    • Humphries, K.M.1    Deal, M.S.2    Taylor, S.S.3
  • 33
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis GB and Holmgren A. Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J Biol Chem 255: 10261-10265, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 10261-10265
    • Kallis, G.B.1    Holmgren, A.2
  • 35
    • 0035929670 scopus 로고    scopus 로고
    • Cytokine-induced activation of nuclear factor-kappa B is inhibited by hydrogen peroxide through oxidative inactivation of IkappaB kinase
    • Korn SH, Wouters EF, Vos N, and Janssen-Heininger YM. Cytokine-induced activation of nuclear factor-kappa B is inhibited by hydrogen peroxide through oxidative inactivation of IkappaB kinase. J Biol Chem 276: 35693-35700, 2001.
    • (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
  • 36
    • 0033230805 scopus 로고    scopus 로고
    • Implication of reactive oxygen species in the antibacterial activity against Salmonella typhimurium of hepatocyte cell lines
    • Lajarin F, Rubio G, Lorenzo N, Gamiz P, Hernandez-Caselles T, and Garcia-Penarrubia P. Implication of reactive oxygen species in the antibacterial activity against Salmonella typhimurium of hepatocyte cell lines. Free Radic Biol Med 27: 1008-1018, 1999.
    • (1999) Free Radic Biol Med , vol.27 , pp. 1008-1018
    • Lajarin, F.1    Rubio, G.2    Lorenzo, N.3    Gamiz, P.4    Hernandez-Caselles, T.5    Garcia-Penarrubia, P.6
  • 37
    • 0141839828 scopus 로고    scopus 로고
    • Reactive oxygen species play roles on B cell surface receptor CD40-mediated proximal and distal signaling events: Effects of an antioxidant, N-acetyl-L-cysteine treatment
    • Lee JR. Reactive oxygen species play roles on B cell surface receptor CD40-mediated proximal and distal signaling events: effects of an antioxidant, N-acetyl-L-cysteine treatment. Mol Cell Biochem 252: 1-7, 2003.
    • (2003) Mol Cell Biochem , vol.252 , pp. 1-7
    • Lee, J.R.1
  • 38
    • 0032561366 scopus 로고    scopus 로고
    • Paclitaxel (Taxol)-induced gene expression and cell death are both mediated by the activation of c-Jun NH2-terminal kinase (JNK/SAPK)
    • Lee LF, Li G, Templeton DJ, and Ting JP. Paclitaxel (Taxol)-induced gene expression and cell death are both mediated by the activation of c-Jun NH2-terminal kinase (JNK/SAPK). J Biol Chem 273: 28253-28260, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 28253-28260
    • Lee, L.F.1    Li, G.2    Templeton, D.J.3    Ting, J.P.4
  • 39
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee SR, Kwon KS, Kim SR, and Rhee SG. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273: 15366-15372, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 40
    • 0037036358 scopus 로고    scopus 로고
    • Reversible inactivation of the tumor suppressor PTEN by H2O2
    • Lee SR, Yang KS, Kwon J, Lee C, Jeong W, and Rhee SG. Reversible inactivation of the tumor suppressor PTEN by H2O2. J Biol Chem 277: 20336-20342, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 20336-20342
    • Lee, S.R.1    Yang, K.S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 41
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H, Nishitoh H, Ichijo H, and Kyriakis JM. Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol Cell Biol 20: 2198-2208, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 42
    • 0035310359 scopus 로고    scopus 로고
    • Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines
    • Mallis RJ, Buss JE, and Thomas JA. Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines. Biochem J 355: 145-153, 2001.
    • (2001) Biochem J , vol.355 , pp. 145-153
    • Mallis, R.J.1    Buss, J.E.2    Thomas, J.A.3
  • 43
    • 1542328892 scopus 로고    scopus 로고
    • S-nitrosylation: A potential new paradigm in signal transduction
    • Martinez-Ruiz A and Lamas S. S-nitrosylation: a potential new paradigm in signal transduction. Cardiovasc Res 62: 43-52, 2004.
    • (2004) Cardiovasc Res , vol.62 , pp. 43-52
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 45
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62
    • Matthews JR, Wakasugi N, Virelizier JL, Yodoi J, and Hay RT. Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res 20: 3821-3830, 1992.
    • (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
  • 46
    • 0024425516 scopus 로고
    • Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-alpha
    • Meier B, Radeke HH, Selle S, Younes M, Sies H, Resch K, and Habermehl GG. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-alpha. Biochem J263: 539-545, 1989.
    • (1989) Biochem J , vol.263 , pp. 539-545
    • Meier, B.1    Radeke, H.H.2    Selle, S.3    Younes, M.4    Sies, H.5    Resch, K.6    Habermehl, G.G.7
  • 47
    • 0029959753 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate inhibits the production of interleukin-6, interleukin-8, and granulocyte-macrophage colony-stimulating factor by human endothelial cells in response to inflammatory mediators: Modulation of NF-kappa B and AP-1 transcription factors activity
    • Munoz C, Pascual-Salcedo D, Castellanos MC, Alfranca A, Aragones J, Vara A, Redondo MJ, and de Landazuri MO. Pyrrolidine dithiocarbamate inhibits the production of interleukin-6, interleukin-8, and granulocyte-macrophage colony-stimulating factor by human endothelial cells in response to inflammatory mediators: modulation of NF-kappa B and AP-1 transcription factors activity. Blood 88: 3482-3490, 1996.
    • (1996) Blood , vol.88 , pp. 3482-3490
    • Munoz, C.1    Pascual-Salcedo, D.2    Castellanos, M.C.3    Alfranca, A.4    Aragones, J.5    Vara, A.6    Redondo, M.J.7    De Landazuri, M.O.8
  • 48
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • Murata H, Ihara Y, Nakamura H, Yodoi J, Sumikawa K, and Kondo T. Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J Biol Chem 278: 50226-50233, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 49
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J and Arner ES. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31: 1287-1312, 2001.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 50
    • 19044381583 scopus 로고    scopus 로고
    • Post-translational disulfide modifications in cell signaling-role of inter-protein, intraprotein, S-glutathionyl, and S-cysteaminyl disulfide modifications in signal transmission
    • O'Brian CA and Chu F. Post-translational disulfide modifications in cell signaling-role of inter-protein, intraprotein, S-glutathionyl, and S-cysteaminyl disulfide modifications in signal transmission. Free Radic Res 39: 471-480, 2005.
    • (2005) Free Radic Res , vol.39 , pp. 471-480
    • O'Brian, C.A.1    Chu, F.2
  • 51
    • 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, and 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 173: 3589-3593, 2004.
    • (2004) J Immunol , vol.173 , pp. 3589-3593
    • Park, H.S.1    Jung, H.Y.2    Park, E.Y.3    Kim, J.4    Lee, W.J.5    Bae, Y.S.6
  • 52
    • 0032489461 scopus 로고    scopus 로고
    • Deletion of the Saccharomyces cerevisiae TRR1 gene encoding thioredoxin reductase inhibits p53-dependent reporter gene expression
    • Pearson GD and Merrill GF. Deletion of the Saccharomyces cerevisiae TRR1 gene encoding thioredoxin reductase inhibits p53-dependent reporter gene expression. J Biol Chem 273: 5431-5434, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 5431-5434
    • Pearson, G.D.1    Merrill, G.F.2
  • 54
    • 8644227615 scopus 로고    scopus 로고
    • Regulation of the NADPH-oxidase complex of phagocytic leukocytes. Recent insights from structural biology, molecular genetics, and microscopy
    • Robinson JM, Ohira T, and Badwey JA. Regulation of the NADPH-oxidase complex of phagocytic leukocytes. Recent insights from structural biology, molecular genetics, and microscopy. Histochem Cell Biol 122: 293-304, 2004.
    • (2004) Histochem Cell Biol , vol.122 , pp. 293-304
    • Robinson, J.M.1    Ohira, T.2    Badwey, J.A.3
  • 55
    • 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, and 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 72: 2123-2130, 2004.
    • (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
  • 57
    • 0025440085 scopus 로고
    • Modulation of human peripheral blood monocyte superoxide release by interferon-gamma and lipopolysaccharide
    • Salisbury SM and Calhoun WJ. Modulation of human peripheral blood monocyte superoxide release by interferon-gamma and lipopolysaccharide. Wis Med J 89: 271-274, 1990.
    • (1990) Wis Med J , vol.89 , pp. 271-274
    • Salisbury, S.M.1    Calhoun, W.J.2
  • 58
  • 59
    • 0027301258 scopus 로고
    • Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-alpha and immunoglobulin G. Evidence for involvement of reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent oxidase
    • Satriano JA, Shuldiner M, Hora K, Xing Y, Shan Z, and Schlondorff D. Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-alpha and immunoglobulin G. Evidence for involvement of reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent oxidase. J Clin Invest 92: 1564-1571, 1993.
    • (1993) J Clin Invest , vol.92 , pp. 1564-1571
    • Satriano, J.A.1    Shuldiner, M.2    Hora, K.3    Xing, Y.4    Shan, Z.5    Schlondorff, D.6
  • 60
    • 0037036460 scopus 로고    scopus 로고
    • Redox regulation of Cdc25C
    • Savitsky PA and Finkel T. Redox regulation of Cdc25C. J Biol Chem 277: 20535-20540, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 20535-20540
    • Savitsky, P.A.1    Finkel, T.2
  • 61
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ and Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30: 1191-1212, 2001.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 62
    • 0028344541 scopus 로고
    • Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa B and AP-1
    • Schenk H, Klein M, Erdbrugger W, Droge W, and Schulze-Osthoff K. Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa B and AP-1. Proc Natl Acad Sci USA 91: 1672-1676, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1672-1676
    • Schenk, H.1    Klein, M.2    Erdbrugger, W.3    Droge, W.4    Schulze-Osthoff, K.5
  • 63
    • 0037834629 scopus 로고    scopus 로고
    • Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily
    • Schroder E and Ponting CP. Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily. Protein Sci 7: 2465-2468, 1998.
    • (1998) Protein Sci , vol.7 , pp. 2465-2468
    • Schroder, E.1    Ponting, C.P.2
  • 64
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation
    • Schulze-Osthoff K, Bakker AC, Vanhaesebroeck B, Beyaert R, Jacob WA, and Fiers W. Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J Biol Chem 267: 5317-5323, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jacob, W.A.5    Fiers, W.6
  • 65
    • 0027328056 scopus 로고
    • Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF
    • Schulze-Osthoff K, Beyaert R, Vandevoorde V, Haegeman G, and Fiers W. Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF. EMBO J 12: 3095-3104, 1993.
    • (1993) EMBO J , vol.12 , pp. 3095-3104
    • Schulze-Osthoff, K.1    Beyaert, R.2    Vandevoorde, V.3    Haegeman, G.4    Fiers, W.5
  • 66
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton MD, Chock PB, and Mieyal JJ. Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid Redox Signal 1: 348-366, 2005.
    • (2005) Antioxid Redox Signal , vol.1 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 67
    • 0033140337 scopus 로고    scopus 로고
    • Antioxidants differentially regulate activation of nuclear factor-kappa B, activator protein-1, c-jun amino-terminal kinases, and apoptosis induced by tumor necrosis factor: Evidence that JNK and NF-kappa B activation are not linked to apoptosis
    • Shrivastava A and Aggarwal BB. Antioxidants differentially regulate activation of nuclear factor-kappa B, activator protein-1, c-jun amino-terminal kinases, and apoptosis induced by tumor necrosis factor: evidence that JNK and NF-kappa B activation are not linked to apoptosis. Antioxid Redox Signal 1: 181-191, 1999.
    • (1999) Antioxid Redox Signal , vol.1 , pp. 181-191
    • Shrivastava, A.1    Aggarwal, B.B.2
  • 69
    • 2242445273 scopus 로고    scopus 로고
    • Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2
    • Song JJ, Rhee JG, Suntharalingam M, Walsh SA, Spitz DR, and Lee YJ. Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2. J Biol Chem 277: 46566-46575, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 46566-46575
    • Song, J.J.1    Rhee, J.G.2    Suntharalingam, M.3    Walsh, S.A.4    Spitz, D.R.5    Lee, Y.J.6
  • 71
    • 0033829852 scopus 로고    scopus 로고
    • Mitogen-activated kinase kinase kinase 1 regulates T cell receptor- and CD28-mediated signaling events which lead to NF-kappaB activation
    • Tuosto L, Costanzo A, Guido F, Marinari B, Vossio S, Moretti F, Levrero M, and Piccolella E. Mitogen-activated kinase kinase kinase 1 regulates T cell receptor- and CD28-mediated signaling events which lead to NF-kappaB activation. Eur J Immunol 30: 2445-2454, 2000.
    • (2000) Eur J Immunol , vol.30 , pp. 2445-2454
    • Tuosto, L.1    Costanzo, A.2    Guido, F.3    Marinari, B.4    Vossio, S.5    Moretti, F.6    Levrero, M.7    Piccolella, E.8
  • 72
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort RL, Congreve M, Tisi D, Carr R, and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423: 773-777, 2003.
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 73
    • 0030587124 scopus 로고    scopus 로고
    • Role of reactive oxygen intermediates in TCR-induced death of T cell blasts and hybridomas
    • Williams MS and Henkart PA. Role of reactive oxygen intermediates in TCR-induced death of T cell blasts and hybridomas. J Immunol 157: 2395-2402, 1996.
    • (1996) J Immunol , vol.157 , pp. 2395-2402
    • Williams, M.S.1    Henkart, P.A.2
  • 74
    • 0028986629 scopus 로고
    • Tumor necrosis factor alpha rapidly activates the mitogen-activated protein kinase (MAPK) cascade in a MAPK kinase kinase-dependent, c-Raf-1-independent fashion in mouse macrophages
    • Winston BW, Lange-Carter CA, Gardner AM, Johnson GL, and Riches DW. Tumor necrosis factor alpha rapidly activates the mitogen-activated protein kinase (MAPK) cascade in a MAPK kinase kinase-dependent, c-Raf-1-independent fashion in mouse macrophages. Proc Natl Acad Sci USA 92: 1614-1618, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1614-1618
    • Winston, B.W.1    Lange-Carter, C.A.2    Gardner, A.M.3    Johnson, G.L.4    Riches, D.W.5
  • 75
  • 77
    • 0029009630 scopus 로고
    • Stimulation and priming of human neutrophils by IL-1 alpha and IL-1 beta: Complete inhibition by IL-1 receptor antagonist and no interaction with other cytokines
    • Yagisawa M, Yuo A, Kitagawa S, Yazaki Y, Togawa A, and Takaku F. Stimulation and priming of human neutrophils by IL-1 alpha and IL-1 beta: complete inhibition by IL-1 receptor antagonist and no interaction with other cytokines. Exp Hematol 23: 603-608, 1995.
    • (1995) Exp Hematol , vol.23 , pp. 603-608
    • Yagisawa, M.1    Yuo, A.2    Kitagawa, S.3    Yazaki, Y.4    Togawa, A.5    Takaku, F.6
  • 78
    • 0033617405 scopus 로고    scopus 로고
    • MEK kinase 1 (MEKK1) transduces c-Jun NH2-terminal kinase activation in response to changes in the microtubule cytoskeleton
    • Yujiri T, Fanger GR, Garrington TP, Schlesinger TK, Gibson S, and Johnson GL. MEK kinase 1 (MEKK1) transduces c-Jun NH2-terminal kinase activation in response to changes in the microtubule cytoskeleton. J Biol Chem 274: 12605-12610, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 12605-12610
    • Yujiri, T.1    Fanger, G.R.2    Garrington, T.P.3    Schlesinger, T.K.4    Gibson, S.5    Johnson, G.L.6


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