메뉴 건너뛰기




Volumn 53, Issue 3, 2012, Pages 447-456

Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression

Author keywords

AP 1; Cysteine hyperoxidation; Free radicals; Lipopolysaccharide; Nrf2; Peroxiredoxin; Sulfiredoxin; Toll like receptor 4

Indexed keywords

CIGARETTE SMOKE; CYCLIC AMP; GLUTATHIONE DERIVATIVE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPOPOLYSACCHARIDE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; N METHYL DEXTRO ASPARTIC ACID; PEROXIREDOXIN; PROTEASOME; PROTEIN C JUN; SULFINIC ACID DERIVATIVE; TOLL LIKE RECEPTOR 4; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR NRF2; TRANSCRIPTION FACTOR YAP1; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UBIQUITIN;

EID: 84863463209     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.05.020     Document Type: Review
Times cited : (109)

References (115)
  • 1
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • DOI 10.1038/nature02075
    • B. Biteau, J. Labarre, and M.B. Toledano ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin Nature 425 2003 980 984 (Pubitemid 37376931)
    • (2003) Nature , vol.425 , Issue.6961 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 2
    • 0037424262 scopus 로고    scopus 로고
    • Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway: Identification of novel gene clusters for cell survival
    • DOI 10.1074/jbc.M211898200
    • M.K. Kwak, N. Wakabayashi, K. Itoh, H. Motohashi, M. Yamamoto, and T.W. Kensler Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway: identification of novel gene clusters for cell survival J. Biol. Chem. 278 2003 8135 8145 (Pubitemid 36800555)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8135-8145
    • Kwak, M.-K.1    Wakabayashi, N.2    Itoh, K.3    Motohashi, H.4    Yamamoto, M.5    Kensler, T.W.6
  • 3
    • 60749125535 scopus 로고    scopus 로고
    • Sestrin 2 is not a reductase for cysteine sulfinic acid of peroxiredoxins
    • H.A. Woo, S.H. Bae, S. Park, and S.G. Rhee Sestrin 2 is not a reductase for cysteine sulfinic acid of peroxiredoxins Antioxid. Redox Signaling 11 2009 739 745
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 739-745
    • Woo, H.A.1    Bae, S.H.2    Park, S.3    Rhee, S.G.4
  • 4
    • 33746111275 scopus 로고    scopus 로고
    • A novel role for human sulfiredoxin in the reversal of glutathionylation
    • DOI 10.1158/0008-5472.CAN-06-0484
    • V.J. Findlay, D.M. Townsend, T.E. Morris, J.P. Fraser, L. He, and K.D. Tew A novel role for human sulfiredoxin in the reversal of glutathionylation Cancer Res. 66 2006 6800 6806 (Pubitemid 44085640)
    • (2006) Cancer Research , vol.66 , Issue.13 , pp. 6800-6806
    • Findlay, V.J.1    Townsend, D.M.2    Morris, T.E.3    Fraser, J.P.4    He, L.5    Tew, K.D.6
  • 5
    • 78049372675 scopus 로고    scopus 로고
    • Overoxidation of 2-Cys peroxiredoxin in prokaryotes: Cyanobacterial 2-Cys peroxiredoxins sensitive to oxidative stress
    • M.B. Pascual, A. Mata-Cabana, F.J. Florencio, M. Lindahl, and F.J. Cejudo Overoxidation of 2-Cys peroxiredoxin in prokaryotes: cyanobacterial 2-Cys peroxiredoxins sensitive to oxidative stress J. Biol. Chem. 285 2010 34485 34492
    • (2010) J. Biol. Chem. , vol.285 , pp. 34485-34492
    • Pascual, M.B.1    Mata-Cabana, A.2    Florencio, F.J.3    Lindahl, M.4    Cejudo, F.J.5
  • 6
    • 25444480015 scopus 로고    scopus 로고
    • Evolution of eukaryotic cysteine sulfinic acid reductase, sulfiredoxin (Srx), from bacterial chromosome partitioning protein ParB
    • M.K. Basu, and E.V. Koonin Evolution of eukaryotic cysteine sulfinic acid reductase, sulfiredoxin (Srx), from bacterial chromosome partitioning protein ParB Cell Cycle 4 2005 947 952 (Pubitemid 41359762)
    • (2005) Cell Cycle , vol.4 , Issue.7 , pp. 947-952
    • Basu, M.K.1    Koonin, E.V.2
  • 8
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • DOI 10.1016/j.freeradbiomed.2005.02.026, PII S0891584905000985
    • S.G. Rhee, H.Z. Chae, and K. Kim Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling Free Radic. Biol. Med. 38 2005 1543 1552 (Pubitemid 40726061)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.12 , pp. 1543-1552
    • Sue, G.R.1    Ho, Z.C.2    Kim, K.3
  • 9
    • 79951643450 scopus 로고    scopus 로고
    • Multiple functions of peroxiredoxins: Peroxidases, sensors and regulators of the intracellular messenger HO, and protein chaperones
    • S.G. Rhee, and H.A. Woo Multiple functions of peroxiredoxins: peroxidases, sensors and regulators of the intracellular messenger HO, and protein chaperones Antioxid. Redox Signaling 15 2011 781 794
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 781-794
    • Rhee, S.G.1    Woo, H.A.2
  • 10
    • 79958059617 scopus 로고    scopus 로고
    • Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins
    • A. Hall, K. Nelson, L.B. Poole, and P.A. Karplus Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins Antioxid. Redox Signaling 15 2011 795 815
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 795-815
    • Hall, A.1    Nelson, K.2    Poole, L.B.3    Karplus, P.A.4
  • 12
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • H.Z. Chae, S.J. Chung, and S.G. Rhee Thioredoxin-dependent peroxide reductase from yeast J. Biol. Chem. 269 1994 27670 27678 (Pubitemid 24346604)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.44 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 13
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • DOI 10.1073/pnas.91.15.7017
    • H.Z. Chae, K. Robison, L.B. Poole, G. Church, G. Storz, and S.G. Rhee Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes Proc. Natl. Acad. Sci. USA 91 1994 7017 7021 (Pubitemid 24226793)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.15 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 14
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • R. Bryk, P. Griffin, and C. Nathan Peroxynitrite reductase activity of bacterial peroxiredoxins Nature 407 2000 211 215
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 15
    • 0037222255 scopus 로고    scopus 로고
    • Structure, mechanism and regulation of peroxiredoxins
    • DOI 10.1016/S0968-0004(02)00003-8, PII S0968000402000038
    • Z.A. Wood, E. Schroder, J. Robin Harris, and L.B. Poole Structure, mechanism and regulation of peroxiredoxins Trends Biochem. Sci. 28 2003 32 40 (Pubitemid 36051004)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 32-40
    • Wood, Z.A.1    Schroder, E.2    Harris, J.R.3    Poole, L.B.4
  • 16
    • 84856940017 scopus 로고    scopus 로고
    • Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
    • S.G. Rhee, H.A. Woo, I.S. Kil, and S.H. Bae Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides J. Biol. Chem. 287 2012 4403 4410
    • (2012) J. Biol. Chem. , vol.287 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 17
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • DOI 10.1126/science.1080405
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653 (Pubitemid 36520591)
    • (2003) Science , vol.300 , Issue.5619 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 18
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • DOI 10.1074/jbc.M106585200
    • T. Rabilloud, M. Heller, F. Gasnier, S. Luche, C. Rey, R. Aebersold, M. Benahmed, P. Louisot, and J. Lunardi Proteomics analysis of cellular response to oxidative stress: evidence for in vivo overoxidation of peroxiredoxins at their active site J. Biol. Chem. 277 2002 19396 19401 (Pubitemid 34967447)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.L.9
  • 19
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • DOI 10.1126/science.1080273
    • H.A. Woo, H.Z. Chae, S.C. Hwang, K.S. Yang, S.W. Kang, K. Kim, and S.G. Rhee Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation Science 300 2003 653 656 (Pubitemid 36520592)
    • (2003) Science , vol.300 , Issue.5619 , pp. 653-656
    • Woo, H.A.1    Chae, H.Z.2    Hwang, S.C.3    Yang, K.-S.4    Kang, S.W.5    Kim, K.6    Rhee, S.G.7
  • 20
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • DOI 10.1074/jbc.M001943200
    • M.S. Seo, S.W. Kang, K. Kim, I.C. Baines, T.H. Lee, and S.G. Rhee Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate J. Biol. Chem. 275 2000 20346 20354 (Pubitemid 30457609)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.27 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 21
    • 79960017554 scopus 로고    scopus 로고
    • Peroxiredoxin 5: Structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin
    • B. Knoops, J. Goemaere, V. Van der Eecken, and J.P. Declercq Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin Antioxid. Redox Signaling 15 2011 817 829
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 817-829
    • Knoops, B.1    Goemaere, J.2    Van Der Eecken, V.3    Declercq, J.P.4
  • 22
    • 79953249112 scopus 로고    scopus 로고
    • Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A activities
    • A.B. Fisher Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A activities Antioxid. Redox Signaling 15 2011 831 844
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 831-844
    • Fisher, A.B.1
  • 23
    • 0346850874 scopus 로고    scopus 로고
    • Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence
    • DOI 10.1074/jbc.C300428200
    • H.A. Woo, S.W. Kang, H.K. Kim, K.S. Yang, H.Z. Chae, and S.G. Rhee Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid: immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence J. Biol. Chem. 278 2003 47361 47364 (Pubitemid 37523174)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , pp. 47361-47364
    • Woo, H.A.1    Kang, S.W.2    Kim, H.K.3    Yang, K.-S.4    Chae, H.Z.5    Rhee, S.G.6
  • 24
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • DOI 10.1074/jbc.M409482200
    • T.S. Chang, W. Jeong, H.A. Woo, S.M. Lee, S. Park, and S.G. Rhee Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine J. Biol. Chem. 279 2004 50994 51001 (Pubitemid 40017840)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50994-51001
    • Chang, T.-S.1    Jeong, W.2    Hyun, A.W.3    Sun, M.L.4    Park, S.5    Sue, G.R.6
  • 25
    • 34547441421 scopus 로고    scopus 로고
    • Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: Its discovery, mechanism of action, and biological significance
    • S.G. Rhee, W. Jeong, T.S. Chang, and H.A. Woo Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significance Kidney Int. Suppl. 106 2007 S3 S8
    • (2007) Kidney Int. Suppl. , vol.106
    • Rhee, S.G.1    Jeong, W.2    Chang, T.S.3    Woo, H.A.4
  • 27
    • 33744919853 scopus 로고    scopus 로고
    • Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin
    • DOI 10.1074/jbc.M511082200
    • W. Jeong, S.J. Park, T.S. Chang, D.Y. Lee, and S.G. Rhee Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin J. Biol. Chem. 281 2006 14400 14407 (Pubitemid 43848370)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14400-14407
    • Jeong, W.1    Sung, J.P.2    Chang, T.-S.3    Lee, D.-Y.4    Sue, G.R.5
  • 28
    • 53049083629 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate
    • T.J. Jonsson, M.S. Murray, L.C. Johnson, and W.T. Lowther Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate J. Biol. Chem. 283 2008 23846 23851
    • (2008) J. Biol. Chem. , vol.283 , pp. 23846-23851
    • Jonsson, T.J.1    Murray, M.S.2    Johnson, L.C.3    Lowther, W.T.4
  • 29
    • 53149092498 scopus 로고    scopus 로고
    • Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin
    • T.J. Jonsson, A.W. Tsang, W.T. Lowther, and C.M. Furdui Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin J. Biol. Chem. 283 2008 22890 22894
    • (2008) J. Biol. Chem. , vol.283 , pp. 22890-22894
    • Jonsson, T.J.1    Tsang, A.W.2    Lowther, W.T.3    Furdui, C.M.4
  • 31
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • DOI 10.1126/science.1130481
    • 2, a necessary evil for cell signaling Science 312 2006 1882 1883 (Pubitemid 43993698)
    • (2006) Science , vol.312 , Issue.5782 , pp. 1882-1883
    • Rhee, S.G.1
  • 32
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • DOI 10.1038/nchembio.85, PII NCHEMBIO85
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286 (Pubitemid 351550893)
    • (2008) Nature Chemical Biology , vol.4 , Issue.5 , pp. 278-286
    • Winterbourn, C.C.1
  • 33
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • DOI 10.1016/S0168-8227(99)00037-6, PII S0168822799000376
    • H.Z. Chae, H.J. Kim, S.W. Kang, and S.G. Rhee Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin Diabetes Res. Clin. Pract. 45 1999 101 112 (Pubitemid 29457756)
    • (1999) Diabetes Research and Clinical Practice , vol.45 , Issue.2-3 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 36
    • 0034714319 scopus 로고    scopus 로고
    • Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis
    • C.A. Chrestensen, D.W. Starke, and J.J. Mieyal Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis J. Biol. Chem. 275 2000 26556 26565
    • (2000) J. Biol. Chem. , vol.275 , pp. 26556-26565
    • Chrestensen, C.A.1    Starke, D.W.2    Mieyal, J.J.3
  • 37
    • 0042665896 scopus 로고    scopus 로고
    • Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells
    • DOI 10.1002/pmic.200300436
    • M. Fratelli, H. Demol, M. Puype, S. Casagrande, P. Villa, I. Eberini, J. Vandekerckhove, E. Gianazza, and P. Ghezzi Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells Proteomics 3 2003 1154 1161 (Pubitemid 36929537)
    • (2003) Proteomics , vol.3 , Issue.7 , pp. 1154-1161
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Villa, P.5    Eberini, I.6    Vandekerckhove, J.7    Gianazza, E.8    Ghezzi, P.9
  • 38
    • 69949115433 scopus 로고    scopus 로고
    • Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin
    • J.W. Park, J.J. Mieyal, S.G. Rhee, and P.B. Chock Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin J. Biol. Chem. 284 2009 23364 23374
    • (2009) J. Biol. Chem. , vol.284 , pp. 23364-23374
    • Park, J.W.1    Mieyal, J.J.2    Rhee, S.G.3    Chock, P.B.4
  • 39
    • 38049177629 scopus 로고    scopus 로고
    • Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: Disulfide formation at dimer-dimer interfaces is not essential for decamerization
    • T. Matsumura, K. Okamoto, S. Iwahara, H. Hori, Y. Takahashi, T. Nishino, and Y. Abe Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerization J. Biol. Chem. 283 2008 284 293
    • (2008) J. Biol. Chem. , vol.283 , pp. 284-293
    • Matsumura, T.1    Okamoto, K.2    Iwahara, S.3    Hori, H.4    Takahashi, Y.5    Nishino, T.6    Abe, Y.7
  • 40
    • 80053614220 scopus 로고    scopus 로고
    • Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis
    • A. Morinaka, Y. Funato, K. Uesugi, and H. Miki Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis Oncogene 30 2011 4208 4218
    • (2011) Oncogene , vol.30 , pp. 4208-4218
    • Morinaka, A.1    Funato, Y.2    Uesugi, K.3    Miki, H.4
  • 41
    • 58149393166 scopus 로고    scopus 로고
    • Sulfiredoxin is an AP-1 target gene that is required for transformation and shows elevated expression in human skin malignancies
    • Q. Wei, H. Jiang, C.P. Matthews, and N.H. Colburn Sulfiredoxin is an AP-1 target gene that is required for transformation and shows elevated expression in human skin malignancies Proc. Natl. Acad. Sci. USA 105 2008 19738 19743
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19738-19743
    • Wei, Q.1    Jiang, H.2    Matthews, C.P.3    Colburn, N.H.4
  • 42
    • 78049361879 scopus 로고    scopus 로고
    • Redox regulation of lipopolysaccharide-mediated sulfiredoxin induction, which depends on both AP-1 and Nrf2
    • H. Kim, Y. Jung, B.S. Shin, H. Song, S.H. Bae, S.G. Rhee, and W. Jeong Redox regulation of lipopolysaccharide-mediated sulfiredoxin induction, which depends on both AP-1 and Nrf2 J. Biol. Chem. 285 2010 34419 34428
    • (2010) J. Biol. Chem. , vol.285 , pp. 34419-34428
    • Kim, H.1    Jung, Y.2    Shin, B.S.3    Song, H.4    Bae, S.H.5    Rhee, S.G.6    Jeong, W.7
  • 43
    • 77953703114 scopus 로고
    • Induction of peroxiredoxin i gene expression by LPS involves the Src/PI3K/JNK signalling pathway
    • A. Bast, K. Fischer, S.F. Erttmann, and R. Walther Induction of peroxiredoxin I gene expression by LPS involves the Src/PI3K/JNK signalling pathway Biochim. Biophys. Acta 402-410 1799 2010
    • (1799) Biochim. Biophys. Acta , vol.402-410 , pp. 2010
    • Bast, A.1    Fischer, K.2    Erttmann, S.F.3    Walther, R.4
  • 44
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • E. Shaulian, and M. Karin AP-1 as a regulator of cell life and death Nat. Cell Biol. 4 2002 E131 E136
    • (2002) Nat. Cell Biol. , vol.4
    • Shaulian, E.1    Karin, M.2
  • 45
    • 34547761232 scopus 로고    scopus 로고
    • Transcriptional response of pancreatic beta cells to metabolic stimulation: Large scale identification of immediate-early and secondary response genes
    • D.A. Glauser, T. Brun, B.R. Gauthier, and W. Schlegel Transcriptional response of pancreatic beta cells to metabolic stimulation: large scale identification of immediate-early and secondary response genes BMC Mol. Biol. 8 2007 54
    • (2007) BMC Mol. Biol. , vol.8 , pp. 54
    • Glauser, D.A.1    Brun, T.2    Gauthier, B.R.3    Schlegel, W.4
  • 47
    • 80053202792 scopus 로고    scopus 로고
    • CRMP5-associated GTPase (CRAG) protein protects neuronal cells against cytotoxicity of expanded polyglutamine protein partially via c-Fos-dependent activator protein-1 activation
    • S. Nagashima, T. Fukuda, Y. Kubota, A. Sugiura, M. Nakao, and R. Inatome Yanagi, S. CRMP5-associated GTPase (CRAG) protein protects neuronal cells against cytotoxicity of expanded polyglutamine protein partially via c-Fos-dependent activator protein-1 activation J. Biol. Chem. 286 2011 33879 33889
    • (2011) J. Biol. Chem. , vol.286 , pp. 33879-33889
    • Nagashima, S.1    Fukuda, T.2    Kubota, Y.3    Sugiura, A.4    Nakao, M.5    Inatome, R.6    Yanagi, S.7
  • 48
    • 34047264014 scopus 로고    scopus 로고
    • Dominant-negative activator protein 1 (TAM67) targets cyclooxygenase-2 and osteopontin under conditions in which it specifically inhibits tumorigenesis
    • DOI 10.1158/0008-5472.CAN-06-0522
    • C.P. Matthews, A.M. Birkholz, A.R. Baker, C.M. Perella, G.R. Beck Jr, M.R. Young, and N.H. Colburn Dominant-negative activator protein 1 (TAM67) targets cyclooxygenase-2 and osteopontin under conditions in which it specifically inhibits tumorigenesis Cancer Res. 67 2007 2430 2438 (Pubitemid 46548927)
    • (2007) Cancer Research , vol.67 , Issue.6 , pp. 2430-2438
    • Matthews, C.P.1    Birkholz, A.M.2    Baker, A.R.3    Perella, C.M.4    Beck Jr., G.R.5    Young, M.R.6    Colburn, N.H.7
  • 50
    • 79955565940 scopus 로고    scopus 로고
    • Sulfiredoxin-peroxiredoxin IV axis promotes human lung cancer progression through modulation of specific phosphokinase signaling
    • Q. Wei, H. Jiang, Z. Xiao, A. Baker, M.R. Young, T.D. Veenstra, and N.H. Colburn Sulfiredoxin-peroxiredoxin IV axis promotes human lung cancer progression through modulation of specific phosphokinase signaling Proc. Natl. Acad. Sci. USA 108 2011 7004 7009
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7004-7009
    • Wei, Q.1    Jiang, H.2    Xiao, Z.3    Baker, A.4    Young, M.R.5    Veenstra, T.D.6    Colburn, N.H.7
  • 51
    • 66449102444 scopus 로고    scopus 로고
    • Role of histone acetylation in the activity-dependent regulation of sulfiredoxin and sestrin 2
    • F.X. Soriano, S. Papadia, K.F. Bell, and G.E. Hardingham Role of histone acetylation in the activity-dependent regulation of sulfiredoxin and sestrin 2 Epigenetics 4 2009 152 158
    • (2009) Epigenetics , vol.4 , pp. 152-158
    • Soriano, F.X.1    Papadia, S.2    Bell, K.F.3    Hardingham, G.E.4
  • 52
    • 32644433693 scopus 로고    scopus 로고
    • A novel GTPase, CRAG, mediates promyelocytic leukemia protein-associated nuclear body formation and degradation of expanded polyglutamine protein
    • DOI 10.1083/jcb.200505079
    • Q. Qin, R. Inatome, A. Hotta, M. Kojima, H. Yamamura, H. Hirai, T. Yoshizawa, H. Tanaka, K. Fukami, and S. Yanagi A novel GTPase, CRAG, mediates promyelocytic leukemia protein-associated nuclear body formation and degradation of expanded polyglutamine protein J. Cell Biol. 172 2006 497 504 (Pubitemid 43243871)
    • (2006) Journal of Cell Biology , vol.172 , Issue.4 , pp. 497-504
    • Qin, Q.1    Inatome, R.2    Hotta, A.3    Kojima, M.4    Yamamura, H.5    Hirai, H.6    Yoshizawa, T.7    Tanaka, H.8    Fukami, K.9    Yanagi, S.10
  • 53
    • 84855499458 scopus 로고    scopus 로고
    • Huntington's disease: Molecular basis of neurodegeneration
    • D.C. Rubinsztein, and J. Carmichael Huntington's disease: molecular basis of neurodegeneration Expert Rev. Mol. Med. 5 2003 1 21
    • (2003) Expert Rev. Mol. Med. , vol.5 , pp. 1-21
    • Rubinsztein, D.C.1    Carmichael, J.2
  • 54
    • 74049120454 scopus 로고    scopus 로고
    • Nrf2: Friend or foe for chemoprevention?
    • T.W. Kensler, and N. Wakabayashi Nrf2: friend or foe for chemoprevention? Carcinogenesis 31 2010 90 99
    • (2010) Carcinogenesis , vol.31 , pp. 90-99
    • Kensler, T.W.1    Wakabayashi, N.2
  • 55
    • 77958125017 scopus 로고    scopus 로고
    • Discovery of the negative regulator of Nrf2, Keap1: A historical overview
    • K. Itoh, J. Mimura, and M. Yamamoto Discovery of the negative regulator of Nrf2, Keap1: a historical overview Antioxid. Redox Signaling 13 2010 1665 1678
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 1665-1678
    • Itoh, K.1    Mimura, J.2    Yamamoto, M.3
  • 56
    • 77958140054 scopus 로고    scopus 로고
    • The Nrf2-Keap1-ARE signaling pathway: The regulation and dual function of Nrf2 in cancer
    • D.D. Zhang The Nrf2-Keap1-ARE signaling pathway: the regulation and dual function of Nrf2 in cancer Antioxid. Redox Signaling 13 2010 1623 1626
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 1623-1626
    • Zhang, D.D.1
  • 57
    • 67649402187 scopus 로고    scopus 로고
    • The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
    • T. Nguyen, P. Nioi, and C.B. Pickett The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress J. Biol. Chem. 284 2009 13291 13295
    • (2009) J. Biol. Chem. , vol.284 , pp. 13291-13295
    • Nguyen, T.1    Nioi, P.2    Pickett, C.B.3
  • 59
    • 53149110452 scopus 로고    scopus 로고
    • Induction of sulfiredoxin expression and reduction of peroxiredoxin hyperoxidation by the neuroprotective Nrf2 activator 3H-1,2-dithiole-3-thione
    • F.X. Soriano, F. Leveille, S. Papadia, L.G. Higgins, J. Varley, P. Baxter, J.D. Hayes, and G.E. Hardingham Induction of sulfiredoxin expression and reduction of peroxiredoxin hyperoxidation by the neuroprotective Nrf2 activator 3H-1,2-dithiole-3-thione J. Neurochem. 107 2008 533 543
    • (2008) J. Neurochem. , vol.107 , pp. 533-543
    • Soriano, F.X.1    Leveille, F.2    Papadia, S.3    Higgins, L.G.4    Varley, J.5    Baxter, P.6    Hayes, J.D.7    Hardingham, G.E.8
  • 61
    • 58049100595 scopus 로고    scopus 로고
    • The cinnamon-derived Michael acceptor cinnamic aldehyde impairs melanoma cell proliferation, invasiveness, and tumor growth
    • C.M. Cabello, W.B. Bair 3rd, S.D. Lamore, S. Ley, A.S. Bause, S. Azimian, and G.T. Wondrak The cinnamon-derived Michael acceptor cinnamic aldehyde impairs melanoma cell proliferation, invasiveness, and tumor growth Free Radic. Biol. Med. 46 2009 220 231
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 220-231
    • Cabello, C.M.1    Bair III, W.B.2    Lamore, S.D.3    Ley, S.4    Bause, A.S.5    Azimian, S.6    Wondrak, G.T.7
  • 63
    • 0042330074 scopus 로고    scopus 로고
    • Identification of a novel NRF2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: Reassessment of the ARE consensus sequence
    • DOI 10.1042/BJ20030754
    • P. Nioi, M. McMahon, K. Itoh, M. Yamamoto, and J.D. Hayes Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence Biochem. J 374 2003 337 348 (Pubitemid 37094093)
    • (2003) Biochemical Journal , vol.374 , Issue.2 , pp. 337-348
    • Nioi, P.1    McMahon, M.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 64
    • 79952224744 scopus 로고    scopus 로고
    • Concerted action of sulfiredoxin and peroxiredoxin i protects against alcohol-induced oxidative injury in mouse liver
    • S.H. Bae, S.H. Sung, E.J. Cho, S.K. Lee, H.E. Lee, H.A. Woo, D.Y. Yu, I.S. Kil, and S.G. Rhee Concerted action of sulfiredoxin and peroxiredoxin I protects against alcohol-induced oxidative injury in mouse liver Hepatology 53 2011 945 953
    • (2011) Hepatology , vol.53 , pp. 945-953
    • Bae, S.H.1    Sung, S.H.2    Cho, E.J.3    Lee, S.K.4    Lee, H.E.5    Woo, H.A.6    Yu, D.Y.7    Kil, I.S.8    Rhee, S.G.9
  • 65
    • 64549111760 scopus 로고    scopus 로고
    • Induction of sulfiredoxin via an Nrf2-dependent pathway and hyperoxidation of peroxiredoxin III in the lungs of mice exposed to hyperoxia
    • S.H. Bae, H.A. Woo, S.H. Sung, H.E. Lee, S.K. Lee, I.S. Kil, and S.G. Rhee Induction of sulfiredoxin via an Nrf2-dependent pathway and hyperoxidation of peroxiredoxin III in the lungs of mice exposed to hyperoxia Antioxid. Redox Signaling 11 2009 937 948
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 937-948
    • Bae, S.H.1    Woo, H.A.2    Sung, S.H.3    Lee, H.E.4    Lee, S.K.5    Kil, I.S.6    Rhee, S.G.7
  • 66
    • 0141494281 scopus 로고    scopus 로고
    • CYP2E1: Biochemistry, toxicology, regulation and function in ethanol-induced liver injury
    • DOI 10.2174/1566524033479609
    • I. Kessova, and A.I. Cederbaum CYP2E1: biochemistry, toxicology, regulation and function in ethanol-induced liver injury Curr. Mol. Med. 3 2003 509 518 (Pubitemid 37168595)
    • (2003) Current Molecular Medicine , vol.3 , Issue.6 , pp. 509-518
    • Kessova, I.1    Cederbaum, A.I.2
  • 67
    • 0028965644 scopus 로고
    • Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin
    • R.J. Ulevitch, and P.S. Tobias Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin Annu. Rev. Immunol. 13 1995 437 457
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 437-457
    • Ulevitch, R.J.1    Tobias, P.S.2
  • 68
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • DOI 10.1016/j.cell.2006.02.015, PII S0092867406001905
    • S. Akira, S. Uematsu, and O. Takeuchi Pathogen recognition and innate immunity Cell 124 2006 783 801 (Pubitemid 43261452)
    • (2006) Cell , vol.124 , Issue.4 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 71
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • DOI 10.1038/35085597
    • C. Wang, L. Deng, M. Hong, G.R. Akkaraju, J. Inoue, and Z.J. Chen TAK1 is a ubiquitin-dependent kinase of MKK and IKK Nature 412 2001 346 351 (Pubitemid 32694385)
    • (2001) Nature , vol.412 , Issue.6844 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.-I.5    Chen, Z.J.6
  • 72
    • 0346496017 scopus 로고    scopus 로고
    • Differential regulation of interleukin 1 receptor and toll-like receptor signaling by MEKK3
    • DOI 10.1038/ni1014
    • Q. Huang, J. Yang, Y. Lin, C. Walker, J. Cheng, Z.G. Liu, and B. Su Differential regulation of interleukin 1 receptor and Toll-like receptor signaling by MEKK3 Nat. Immunol. 5 2004 98 103 (Pubitemid 38081474)
    • (2004) Nature Immunology , vol.5 , Issue.1 , pp. 98-103
    • Huang, Q.1    Yang, J.2    Lin, Y.3    Walker, C.4    Cheng, J.5    Liu, Z.-G.6    Su, B.7
  • 74
    • 0027939931 scopus 로고
    • Role of transcription factor NF-κB/Rel in induction of nitric oxide synthase
    • Q.W. Xie, Y. Kashiwabara, and C. Nathan Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase J. Biol. Chem. 269 1994 4705 4708 (Pubitemid 24239438)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.7 , pp. 4705-4708
    • Xie, Q.-W.1    Kashiwabara, Y.2    Nathan, C.3
  • 75
    • 33845666522 scopus 로고    scopus 로고
    • TGF-β activated kinase-1: New insights into the diverse roles of TAK1 in development and immunity
    • J.R. Delaney, and M. Mlodzik TGF-beta activated kinase-1: new insights into the diverse roles of TAK1 in development and immunity Cell Cycle 5 2006 2852 2855 (Pubitemid 44953934)
    • (2006) Cell Cycle , vol.5 , Issue.24 , pp. 2852-2855
    • Delaney, J.R.1    Mlodzik, M.2
  • 76
    • 0027255749 scopus 로고
    • Promoter of the mouse gene encoding calcium-independent nitric oxide synthase confers inducibility by interferon γ and bacterial lipopolysaccharide
    • Q.W. Xie, R. Whisnant, and C. Nathan Promoter of the mouse gene encoding calcium-independent nitric oxide synthase confers inducibility by interferon gamma and bacterial lipopolysaccharide J. Exp. Med 177 1993 1779 1784 (Pubitemid 23146145)
    • (1993) Journal of Experimental Medicine , vol.177 , Issue.6 , pp. 1779-1784
    • Xie, Q.-W.1    Whisnant, R.2    Nathan, C.3
  • 77
    • 0037332589 scopus 로고    scopus 로고
    • Role of the NF-κB signaling pathway and κB cis-regulatory elements on the IRF-1 and iNOS promoter regions in mycobacterial lipoarabinomannan induction of nitric oxide
    • DOI 10.1128/IAI.71.3.1442-1452.2003
    • K.R. Morris, R.D. Lutz, H.S. Choi, T. Kamitani, K. Chmura, and E.D. Chan Role of the NF-kappaB signaling pathway and kappaB cis-regulatory elements on the IRF-1 and iNOS promoter regions in mycobacterial lipoarabinomannan induction of nitric oxide Infect. Immun. 71 2003 1442 1452 (Pubitemid 36254331)
    • (2003) Infection and Immunity , vol.71 , Issue.3 , pp. 1442-1452
    • Morris, K.R.1    Lutz, R.D.2    Choi, H.-S.3    Kamitani, T.4    Chmura, K.5    Chan, E.D.6
  • 78
    • 0026729267 scopus 로고
    • Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme
    • C.J. Lowenstein, C.S. Glatt, D.S. Bredt, and S.H. Snyder Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme Proc. Natl. Acad. Sci. USA 89 1992 6711 6715
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6711-6715
    • Lowenstein, C.J.1    Glatt, C.S.2    Bredt, D.S.3    Snyder, S.H.4
  • 82
    • 2442535969 scopus 로고    scopus 로고
    • Nitric Oxide-induced Transcriptional Up-regulation of Protective Genes by Nrf2 via the Antioxidant Response Element Counteracts Apoptosis of Neuroblastoma Cells
    • DOI 10.1074/jbc.M312492200
    • S. Dhakshinamoorthy, and A.G. Porter Nitric oxide-induced transcriptional up-regulation of protective genes by Nrf2 via the antioxidant response element counteracts apoptosis of neuroblastoma cells J. Biol. Chem 279 2004 20096 20107 (Pubitemid 38623454)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 20096-20107
    • Dhakshinamoorthy, S.1    Porter, A.G.2
  • 84
    • 0030937832 scopus 로고    scopus 로고
    • Nitric oxide and macrophage function
    • DOI 10.1146/annurev.immunol.15.1.323
    • J. MacMicking, Q.W. Xie, and C. Nathan Nitric oxide and macrophage function Annu. Rev. Immunol. 15 1997 323 350 (Pubitemid 27169284)
    • (1997) Annual Review of Immunology , vol.15 , pp. 323-350
    • MacMicking, J.1    Xie, Q.-W.2    Nathan, C.3
  • 86
    • 0036395928 scopus 로고    scopus 로고
    • Macrophage signaling and respiratory burst
    • K.E. Iles, and H.J. Forman Macrophage signaling and respiratory burst Immunol. Res. 26 2002 95 105 (Pubitemid 35177488)
    • (2002) Immunologic Research , vol.26 , Issue.1-3 , pp. 95-105
    • Iles, K.E.1    Forman, H.J.2
  • 87
    • 0026034432 scopus 로고
    • Role of nitric oxide synthesis in macrophage antimicrobial activity
    • C.F. Nathan, and J.B. Hibbs Jr. Role of nitric oxide synthesis in macrophage antimicrobial activity Curr. Opin. Immunol. 3 1991 65 70
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 65-70
    • Nathan, C.F.1    Hibbs, Jr.J.B.2
  • 89
    • 21944452087 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-κB and AP-1
    • DOI 10.1128/MCB.25.14.5933-5946.2005
    • H. Yang, N. Magilnick, C. Lee, D. Kalmaz, X. Ou, J.Y. Chan, and S.C. Lu Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-kappaB and AP-1 Mol. Cell. Biol. 25 2005 5933 5946 (Pubitemid 40949988)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.14 , pp. 5933-5946
    • Yang, H.1    Magilnick, N.2    Lee, C.3    Kalmaz, D.4    Ou, X.5    Chan, J.Y.6    Lu, S.C.7
  • 90
    • 0036708902 scopus 로고    scopus 로고
    • Antioxidants and oxidants regulated signal transduction pathways
    • DOI 10.1016/S0006-2952(02)01137-1, PII S0006295202011371
    • E.D. Owuor, and A.N. Kong Antioxidants and oxidants regulated signal transduction pathways Biochem. Pharmacol. 64 2002 765 770 (Pubitemid 35238028)
    • (2002) Biochemical Pharmacology , vol.64 , Issue.5-6 , pp. 765-770
    • Owuor, E.D.1    Kong, A.-N.T.2
  • 92
    • 22144457305 scopus 로고    scopus 로고
    • A crucial role for reactive oxygen species in RANKL-induced osteoclast differentiation
    • DOI 10.1182/blood-2004-09-3662
    • N.K. Lee, Y.G. Choi, J.Y. Baik, S.Y. Han, D.W. Jeong, Y.S. Bae, N. Kim, and S.Y. Lee A crucial role for reactive oxygen species in RANKL-induced osteoclast differentiation Blood 106 2005 852 859 (Pubitemid 41076424)
    • (2005) Blood , vol.106 , Issue.3 , pp. 852-859
    • Lee, N.K.1    Choi, Y.G.2    Baik, J.Y.3    Han, S.Y.4    Jeong, D.-W.5    Bae, Y.S.6    Kim, N.7    Lee, S.Y.8
  • 93
    • 70349218996 scopus 로고    scopus 로고
    • Impaired priming and activation of the neutrophil NADPH oxidase in patients with IRAK4 or NEMO deficiency
    • A. Singh, K.A. Zarember, D.B. Kuhns, and J.I. Gallin Impaired priming and activation of the neutrophil NADPH oxidase in patients with IRAK4 or NEMO deficiency J. Immunol. 182 2009 6410 6417
    • (2009) J. Immunol. , vol.182 , pp. 6410-6417
    • Singh, A.1    Zarember, K.A.2    Kuhns, D.B.3    Gallin, J.I.4
  • 94
    • 59849086158 scopus 로고    scopus 로고
    • Macrophages generate reactive oxygen species in response to minimally oxidized low-density lipoprotein: Toll-like receptor 4- and spleen tyrosine kinase-dependent activation of NADPH oxidase 2
    • Y.S. Bae, J.H. Lee, S.H. Choi, S. Kim, F. Almazan, J.L. Witztum, and Y.I. Miller Macrophages generate reactive oxygen species in response to minimally oxidized low-density lipoprotein: toll-like receptor 4- and spleen tyrosine kinase-dependent activation of NADPH oxidase 2 Circ. Res. 104 2009 210 218
    • (2009) Circ. Res. , vol.104 , pp. 210-218
    • Bae, Y.S.1    Lee, J.H.2    Choi, S.H.3    Kim, S.4    Almazan, F.5    Witztum, J.L.6    Miller, Y.I.7
  • 97
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • C. Abate, L. Patel, F.J. Rauscher, and T. Curran Redox regulation of fos and jun DNA-binding activity in vitro Science 249 1990 1157 1161
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher, F.J.3    Curran, T.4
  • 98
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • S. Xanthoudakis, and T. Curran Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity EMBO J 11 1992 653 665
    • (1992) EMBO J , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 99
    • 0035971410 scopus 로고    scopus 로고
    • Redox control of AP-1-like factors in yeast and beyond
    • DOI 10.1038/sj.onc.1204384
    • W.M. Toone, B.A. Morgan, and N. Jones Redox control of AP-1-like factors in yeast and beyond Oncogene 20 2001 2336 2346 (Pubitemid 32531293)
    • (2001) Oncogene , vol.20 , Issue.19 REV. ISS. 2 , pp. 2336-2346
    • Toone, W.M.1    Morgan, B.A.2    Jones, N.3
  • 100
    • 27844595309 scopus 로고    scopus 로고
    • Activation of AP-1 through reactive oxygen species by angiotensin II in rat cardiomyocytes
    • DOI 10.1016/j.freeradbiomed.2005.08.006, PII S089158490500448X
    • S. Wu, J. Gao, C. Ohlemeyer, D. Roos, H. Niessen, E. Kottgen, and R. Gessner Activation of AP-1 through reactive oxygen species by angiotensin II in rat cardiomyocytes Free Radic. Biol. Med. 39 2005 1601 1610 (Pubitemid 41642591)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.12 , pp. 1601-1610
    • Wu, S.1    Gao, J.2    Ohlemeyer, C.3    Roos, D.4    Niessen, H.5    Kottgen, E.6    Gessner, R.7
  • 101
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • DOI 10.1074/jbc.273.25.15366
    • S.R. Lee, K.S. Kwon, S.R. Kim, and S.G. Rhee Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor J. Biol. Chem. 273 1998 15366 15372 (Pubitemid 28298140)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15366-15372
    • Lee, S.-R.1    Kwont, K.-S.2    Kim, S.-R.3    Rhee, S.G.4
  • 102
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • DOI 10.1016/j.cell.2004.12.041
    • H. Kamata, S. Honda, S. Maeda, L. Chang, H. Hirata, and M. Karin Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases Cell 120 2005 649 661 (Pubitemid 40343077)
    • (2005) Cell , vol.120 , Issue.5 , pp. 649-661
    • Kamata, H.1    Honda, S.-I.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 104
    • 0036193169 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating Kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer
    • DOI 10.1002/jcp.10080
    • K. Tobiume, M. Saitoh, and H. Ichijo Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer J. Cell. Physiol 191 2002 95 104 (Pubitemid 34195221)
    • (2002) Journal of Cellular Physiology , vol.191 , Issue.1 , pp. 95-104
    • Tobiume, K.1    Saitoh, M.2    Ichijo, H.3
  • 106
    • 70350131071 scopus 로고    scopus 로고
    • Copper activation of NF-kappaB signaling in HepG2 cells
    • M.K. McElwee, M.O. Song, and J.H. Freedman Copper activation of NF-kappaB signaling in HepG2 cells J. Mol. Biol. 393 2009 1013 1021
    • (2009) J. Mol. Biol. , vol.393 , pp. 1013-1021
    • McElwee, M.K.1    Song, M.O.2    Freedman, J.H.3
  • 109
    • 0028805253 scopus 로고
    • A yeast transcription factor bypassing the requirement for SBF and DSC1/MBF in budding yeast has homology to bacterial signal transduction proteins
    • B.A. Morgan, N. Bouquin, G.F. Merrill, and L.H. Johnston A yeast transcription factor bypassing the requirement for SBF and DSC1/MBF in budding yeast has homology to bacterial signal transduction proteins EMBO J 14 1995 5679 5689
    • (1995) EMBO J , vol.14 , pp. 5679-5689
    • Morgan, B.A.1    Bouquin, N.2    Merrill, G.F.3    Johnston, L.H.4
  • 112
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • R.S. Sohal, and R. Weindruch Oxidative stress, caloric restriction, and aging Science 273 1996 59 63 (Pubitemid 26255420)
    • (1996) Science , vol.273 , Issue.5271 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 113
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • DOI 10.1016/S0891-5849(02)00765-7, PII S0891584902007657
    • R.L. Levine Carbonyl modified proteins in cellular regulation, aging, and disease Free Radic. Biol. Med. 32 2002 790 796 (Pubitemid 34439249)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 790-796
    • Levine, R.L.1
  • 115
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • DOI 10.1146/annurev.micro.59.031805.133833
    • A.G. Hinnebusch Translational regulation of GCN4 and the general amino acid control of yeast Annu. Rev. Microbiol 59 2005 407 450 (Pubitemid 41507438)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.