메뉴 건너뛰기




Volumn 73, Issue , 2014, Pages 318-327

Glutathione transferase Omega 1 is required for the lipopolysaccharide- stimulated induction of NADPH oxidase 1 and the production of reactive oxygen species in macrophages

Author keywords

Free radicals; Glutathione transferase Omega 1; LPS; NADPH oxidase 1; TLR4

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; CATALASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE OMEGA 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; SHORT HAIRPIN RNA; SYNAPTOTAGMIN I; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG; CARRIER PROTEIN; CYTOSKELETON PROTEIN; FREE RADICAL; GSTO1 PROTEIN, MOUSE; HEAT SHOCK PROTEIN; IL1B PROTEIN, MOUSE; INTERLEUKIN 6; KEAP1 PROTEIN, MOUSE; LIPOPOLYSACCHARIDE; NFE2L2 PROTEIN, MOUSE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; RELA PROTEIN, MOUSE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SMALL INTERFERING RNA; TLR4 PROTEIN, MOUSE; TRANSCRIPTION FACTOR NRF2; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA;

EID: 84903278627     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.05.020     Document Type: Article
Times cited : (61)

References (64)
  • 1
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • DOI 10.1021/tx960072x
    • R.N. Armstrong Structure, catalytic mechanism, and evolution of the glutathione transferases Chem. Res. Toxicol. 10 1997 2 18 (Pubitemid 27044902)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.1 , pp. 2-18
    • Armstrong, R.N.1
  • 2
    • 84875743799 scopus 로고    scopus 로고
    • Glutathione transferases, regulators of cellular metabolism and physiology
    • P.G. Board, and D. Menon Glutathione transferases, regulators of cellular metabolism and physiology Biochim. Biophys 1830 2012 3267 3328
    • (2012) Biochim. Biophys , vol.1830 , pp. 3267-3328
    • Board, P.G.1    Menon, D.2
  • 3
    • 30144439026 scopus 로고    scopus 로고
    • Nomenclature for mammalian soluble glutathione transferases
    • DOI 10.1016/S0076-6879(05)01001-3, PII S0076687905010013, 1, Gluthione Transferases and Gamma-Glutamyl Transpeptidases
    • B. Mannervik, P.G. Board, J.D. Hayes, I. Listowsky, and W.R. Pearson Nomenclature for mammalian soluble glutathione transferases Methods Enzymol. 401 2005 1 8 (Pubitemid 43052383)
    • (2005) Methods in Enzymology , vol.401 , pp. 1-8
    • Mannervik, B.1    Board, P.G.2    Hayes, J.D.3    Listowsky, I.4    Pearson, W.R.5
  • 5
    • 30144438819 scopus 로고    scopus 로고
    • Characterization of the omega class of glutathione transferases
    • DOI 10.1016/S0076-6879(05)01005-0, PII S0076687905010050, 5, Gluthione Transferases and Gamma-Glutamyl Transpeptidases
    • A.K. Whitbread, A. Masoumi, N. Tetlow, E. Schmuck, M. Coggan, and P.G. Board Characterization of the Omega class of glutathione transferases Methods Enzymol. 401 2005 78 99 (Pubitemid 43052387)
    • (2005) Methods in Enzymology , vol.401 , pp. 78-99
    • Whitbread, A.K.1    Masoumi, A.2    Tetlow, N.3    Schmuck, E.4    Coggan, M.5    Board, P.G.6
  • 6
    • 79954570444 scopus 로고    scopus 로고
    • The Omega-class glutathione transferases: Structure, function and genetics
    • P.G. Board The Omega-class glutathione transferases: structure, function and genetics Drug Metab. Rev. 43 2011 226 235
    • (2011) Drug Metab. Rev. , vol.43 , pp. 226-235
    • Board, P.G.1
  • 7
    • 38349182228 scopus 로고    scopus 로고
    • S-(4-nitrophenacyl)glutathione is a specific substrate for glutathione transferase Omega 1-1
    • P.G. Board, M. Coggan, J. Cappello, H. Zhou, A.J. Oakley, and M.W. Anders S-(4-nitrophenacyl)glutathione is a specific substrate for glutathione transferase Omega 1-1 Anal. Biochem. 374 2008 25 30
    • (2008) Anal. Biochem. , vol.374 , pp. 25-30
    • Board, P.G.1    Coggan, M.2    Cappello, J.3    Zhou, H.4    Oakley, A.J.5    Anders, M.W.6
  • 8
    • 33750036726 scopus 로고    scopus 로고
    • Glutathione-S-transferase-omega [MMA(V) reductase] knockout mice: Enzyme and arsenic species concentrations in tissues after arsenate administration
    • DOI 10.1016/j.taap.2006.06.014, PII S0041008X06002316
    • U.K. Chowdhury, R.A. Zakharyan, A. Hernandez, M.D. Avram, M.J. Kopplin, and V. Aposhian Glutathione transferase Omega [MMA(V) reductase] knockout mice: enzyme and arsenic species concentrations in tissues after arsenate administration Toxicol. Appl. Pharmacol. 216 2006 446 457 (Pubitemid 44584319)
    • (2006) Toxicology and Applied Pharmacology , vol.216 , Issue.3 , pp. 446-457
    • Chowdhury, U.K.1    Zakharyan, R.A.2    Hernandez, A.3    Avram, M.D.4    Kopplin, M.J.5    Aposhian, H.V.6
  • 9
    • 22544482100 scopus 로고    scopus 로고
    • Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: Implications for arsenic metabolism and the age-at-onset of Alzheimer's and Parkinson's diseases
    • E.M. Schmuck, P.G. Board, A.K. Whitbread, N. Tetlow, J.A. Cavanaugh, A.C. Blackburn, and A. Masoumi Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimer's and Parkinson's diseases Pharmacogenet. Genomics 15 2005 493 501 (Pubitemid 41017598)
    • (2005) Pharmacogenetics and Genomics , vol.15 , Issue.7 , pp. 493-501
    • Schmuck, E.M.1    Board, P.G.2    Whitbread, A.K.3    Tetlow, N.4    Cavanaugh, J.A.5    Blackburn, A.C.6    Masoumi, A.7
  • 10
    • 84883669771 scopus 로고    scopus 로고
    • A role for glutathione transferase Omega 1 (GSTO1-1) in the glutathionylation cycle
    • D. Menon, and P.G. Board A role for glutathione transferase Omega 1 (GSTO1-1) in the glutathionylation cycle J. Biol. Chem. 288 2013 25769 25779
    • (2013) J. Biol. Chem. , vol.288 , pp. 25769-25779
    • Menon, D.1    Board, P.G.2
  • 11
    • 0037930829 scopus 로고    scopus 로고
    • Glutathione S-transferase omega 1-1 is a target of cytokine release inhibitory drugs and may be responsible for their effect on interleukin-1β posttranslational processing
    • DOI 10.1074/jbc.M211596200
    • R.E. Laliberte, D.G. Peeregaux, L.R. Hoth, P.J. Rosner, C.K. Jordan, K.M. Peese, J.F. Eggler, M.A. Dombroski, K.F. Geoghegan, and C.A. Gabel Glutathione S-transferase Omega 1-1 is a target of cytokine release inhibitory drugs and may be responsible for their effect on interleukin-1beta posttranslational processing J. Biol. Chem. 278 2003 16567 16578 (Pubitemid 36799518)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16567-16578
    • Laliberte, R.E.1    Perregaux, D.G.2    Hoth, L.R.3    Rosner, P.J.4    Jordan, C.K.5    Peese, K.M.6    Eggler, J.F.7    Dombroski, M.A.8    Geoghegan, K.F.9    Gabel, C.A.10
  • 12
    • 84055182560 scopus 로고    scopus 로고
    • The cytokine release inhibitory drug CRID3 targets ASC oligomerisation in the NLRP3 and AIM2 inflammasomes
    • R.C. Coll, and L.A. J. O'Neill The cytokine release inhibitory drug CRID3 targets ASC oligomerisation in the NLRP3 and AIM2 inflammasomes PLoS One 6 2011 e29539
    • (2011) PLoS One , vol.6 , pp. 29539
    • Coll, R.C.1    O'Neill, L.A.J.2
  • 16
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: A caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • L. Franchi, T. Eigenbrod, R. Muñoz-Planillo, and G. Nuñez The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis Nat. Immunol. 10 2009 241 247
    • (2009) Nat. Immunol. , vol.10 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Muñoz-Planillo, R.3    Nuñez, G.4
  • 17
    • 33750924781 scopus 로고    scopus 로고
    • Regulation of the phagocyte NADPH oxidase by Rac GTPase
    • DOI 10.1089/ars.2006.8.1533
    • G.M. Bokoch, and T. Zhao Regulation of the phagocyte NADPH oxidase by Rac GTPase Antioxid. Redox Signaling 8 2006 1533 1548 (Pubitemid 44726329)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.9-10 , pp. 1533-1548
    • Bokoch, G.M.1    Zhao, T.2
  • 18
    • 72149111665 scopus 로고    scopus 로고
    • IRAK-1 contributes to lipopolysaccharide-induced reactive oxygen species generation in macrophages by inducing NOX-1 transcription and Rac1 activation and suppressing the expression of antioxidative enzymes
    • U. Maitra, N. Singh, L. Gan, L. Ringwood, and L. Li IRAK-1 contributes to lipopolysaccharide-induced reactive oxygen species generation in macrophages by inducing NOX-1 transcription and Rac1 activation and suppressing the expression of antioxidative enzymes J. Biol. Chem. 284 2009 35403 35411
    • (2009) J. Biol. Chem. , vol.284 , pp. 35403-35411
    • Maitra, U.1    Singh, N.2    Gan, L.3    Ringwood, L.4    Li, L.5
  • 19
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • DOI 10.1152/physrev.00044.2005
    • K. Bedard, and K.H. Krause The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology Physiol. Rev. 87 2007 245 313 (Pubitemid 46209993)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 245-313
    • Bedard, K.1    Krause, K.-H.2
  • 20
    • 77950338003 scopus 로고    scopus 로고
    • Linking oxidative stress to inflammation: Toll-like receptors
    • R. Gill, A. Tsung, and T. Billiar Linking oxidative stress to inflammation: Toll-like receptors Free Radic. Biol. Med. 48 2010 1121 1132
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 1121-1132
    • Gill, R.1    Tsung, A.2    Billiar, T.3
  • 22
    • 33750537650 scopus 로고    scopus 로고
    • Endotoxin, TLR4 signaling and vascular inflammation: Potential therapeutic targets in cardiovascular disease
    • DOI 10.2174/138161206778743501
    • L.L. Stoll, G.M. Denning, and N.L. Weintraub Endotoxin, TLR4 signaling and vascular inflammation: potential therapeutic targets in cardiovascular disease Curr. Pharm. Des 12 2006 4229 4245 (Pubitemid 44669751)
    • (2006) Current Pharmaceutical Design , vol.12 , Issue.32 , pp. 4229-4245
    • Stoll, L.L.1    Denning, G.M.2    Weintraub, N.L.3
  • 24
    • 0037342498 scopus 로고    scopus 로고
    • Characterization of the human Omega class glutathione transferase genes and associated polymorphisms
    • DOI 10.1097/00008571-200303000-00003
    • A.K. Whitbread, N. Tetlow, H.J. Eyre, G.R. Southerland, and P.G. Board Characterization of the human Omega class glutathione transferase genes and associated polymorphisms Pharmacogenetics 13 2003 131 144 (Pubitemid 36324243)
    • (2003) Pharmacogenetics , vol.13 , Issue.3 , pp. 131-144
    • Whitbread, A.K.1    Tetlow, N.2    Eyre, H.J.3    Sutherland, G.R.4    Board, P.G.5
  • 25
    • 84870653940 scopus 로고    scopus 로고
    • A fluorometric method to quantify protein glutathionylation using glutathione derivatization with 2,3-naphthalenedicarboxaldehyde
    • D. Menon, and P.G. Board A fluorometric method to quantify protein glutathionylation using glutathione derivatization with 2,3- naphthalenedicarboxaldehyde Anal. Biochem. 433 2012 132 136
    • (2012) Anal. Biochem. , vol.433 , pp. 132-136
    • Menon, D.1    Board, P.G.2
  • 26
    • 0015353270 scopus 로고
    • Colorimetric assay of catalase
    • A.K. Sinha Colorimetric assay of catalase Anal. Biochem. 47 1972 389 394
    • (1972) Anal. Biochem. , vol.47 , pp. 389-394
    • Sinha, A.K.1
  • 27
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for Iκb phosphorylation and NF-κB activation
    • DOI 10.1016/S0092-8674(00)80406-7
    • E. Zandi, D.M. Rothwarf, M. Delhase, M. Hayakawa, and M. Karin The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation Cell 91 1997 243 252 (Pubitemid 27456391)
    • (1997) Cell , vol.91 , Issue.2 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 30
    • 0028174061 scopus 로고
    • Function and activation of NF-kappaB in the immune system
    • P.A. Baeuerle, and T. Henkel Function and activation of NF-kappaB in the immune system Annu. Rev. Immunol. 12 1994 141 179
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 31
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • M.S. Hayden, and S. Ghosh Shared principles in NF-κB signaling Cell 132 2008 344 362
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 32
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor IκBα: Evidence for an inducible autoregulatory pathway
    • S.-C. Sun, P.A. Ganchi, D.W. Ballard, and W.C. Greene NF-kappa B controls expression of inhibitor I kappa B alpha: evidence for an inducible autoregulatory pathway Science 259 1993 1912 1915 (Pubitemid 23124465)
    • (1993) Science , vol.259 , Issue.5103 , pp. 1912-1915
    • Sun, S.-C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 33
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for Iκb phosphorylation and NF-κB activation
    • DOI 10.1016/S0092-8674(00)80406-7
    • E. Zandi, D.M. Rothwarf, M. Delhase, M. Hayakawa, and M. Karin The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation Cell 91 1997 243 252 (Pubitemid 27456391)
    • (1997) Cell , vol.91 , Issue.2 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 34
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DOI 10.1038/41493
    • J.A. DiDonato, M. Hayakawa, D.M. Rothwarf, E. Zandi, and M. Karin A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB Nature 388 1997 548 554 (Pubitemid 27339997)
    • (1997) Nature , vol.388 , Issue.6642 , pp. 548-554
    • Didonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 35
    • 0027212534 scopus 로고
    • Lipopolysaccharide induces phosphorylation of MAD3 and activation of c- Rel and related NF-κB proteins in human monocytic THP-1 cells
    • S.R. Cordle, R. Donald, M.A. Read, and J. Hawiger Lipopolysaccharide induces phosphorylation of MAD3 and activation of c-Rel and related NF-kappa B proteins in human monocytic THP-1 cells J. Biol. Chem. 268 1993 11803 11810 (Pubitemid 23168134)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.16 , pp. 11803-11810
    • Cordle, S.R.1    Donald, R.2    Read, M.A.3    Hawiger, J.4
  • 36
    • 0028985248 scopus 로고
    • Proteolytic processing of NF-kappa B/I kappa B in human monocytes: ATP-dependent induction by pro-inflammatory mediators
    • R. Donald, D.W. Ballard, and J. Hawiger Proteolytic processing of NF-kappa B/I kappa B in human monocytes: ATP-dependent induction by pro-inflammatory mediators J. Biol. Chem. 270 1995 9 12
    • (1995) J. Biol. Chem. , vol.270 , pp. 9-12
    • Donald, R.1    Ballard, D.W.2    Hawiger, J.3
  • 37
    • 54949147176 scopus 로고    scopus 로고
    • New regulators of NF-kappaB in inflammation
    • S. Ghosh, and M.S. Hayden New regulators of NF-kappaB in inflammation Nat. Rev. Immunol. 8 2008 837 848
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 837-848
    • Ghosh, S.1    Hayden, M.S.2
  • 39
    • 2442658079 scopus 로고    scopus 로고
    • Transactivation of the PPAR-responsive enhancer module in chemopreventive glutathione S-transferase gene by the peroxisome proliferator-activated receptor-γ and retinoid X receptor heterodimer
    • DOI 10.1158/0008-5472.CAN-03-3924
    • E.Y. Park, I.J. Cho, and S.G. Kim Transactivation of the PPAR-responsive enhancer module in chemopreventive glutathione S-transferase gene by the peroxisome proliferator-activated receptor-γ and retinoid X receptor heterodimer Cancer Res. 64 2004 3701 3713 (Pubitemid 38657951)
    • (2004) Cancer Research , vol.64 , Issue.10 , pp. 3701-3713
    • Park, E.Y.1    Cho, I.J.2    Kim, S.G.3
  • 40
    • 0036908619 scopus 로고    scopus 로고
    • Identification of a functional peroxisome proliferator-activated receptor response element in the rat catalase promoter
    • DOI 10.1210/me.2002-0020
    • G.D. Girnun, F.E. Domann, S.A. Moore, and M.E. Robbins Identification of a functional peroxisome proliferator-activated receptor response element in the rat catalase promoter Mol. Endocrinol. 16 2002 2793 2801 (Pubitemid 36020658)
    • (2002) Molecular Endocrinology , vol.16 , Issue.12 , pp. 2793-2801
    • Girnun, G.D.1    Domann, F.E.2    Moore, S.A.3    Robbins, M.E.C.4
  • 41
    • 0021679964 scopus 로고
    • Sequential alterations in the micro-localization of catalase in mouse liver after treatment with hypolipidemic drugs
    • E. Klucis, D. Crane, and C. Masters Sequential alterations in the micro-localization of catalase in mouse liver after treatment with hypolipidemic drugs Mol. Cell. Biochem. 65 1984 73 82 (Pubitemid 15218498)
    • (1984) Molecular and Cellular Biochemistry , vol.65 , Issue.1 , pp. 73-82
    • Klucis, E.1    Crane, D.2    Masters, C.3
  • 42
    • 53549100479 scopus 로고    scopus 로고
    • Toll like receptor 4 mediates cross talk between peroxisome proliferator activated receptor γ and nuclear factor κb in macrophages
    • B.M. Necela, W. Su, and E.A. Thompson Toll like receptor 4 mediates cross talk between peroxisome proliferator activated receptor γ and nuclear factor κB in macrophages Immunology 125 2008 344 358
    • (2008) Immunology , vol.125 , pp. 344-358
    • Necela, B.M.1    Su, W.2    Thompson, E.A.3
  • 43
    • 38149085905 scopus 로고    scopus 로고
    • Endotoxin downregulates peroxisome proliferator-activated receptor-γ via the increase in TNF-α release
    • M. Zhou, R. Wu, W. Dong, A. Jacob, and P. Wang Endotoxin downregulates peroxisome proliferator-activated receptor-γ via the increase in TNF-α release Am. J. Physiol. Regul. Integr. Comp. Physiol 294 2008 R84 R92
    • (2008) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.294
    • Zhou, M.1    Wu, R.2    Dong, W.3    Jacob, A.4    Wang, P.5
  • 44
    • 34548424587 scopus 로고    scopus 로고
    • Role of NF-κB in transcriptional regulation of the phagocyte NADPH oxidase by tumor necrosis factor-α
    • DOI 10.1189/jlb.1206735
    • K.A. Gauss, L.K. Nelson-Overton, D.W. Siemsen, Y. Gao, F.R. DeLeo, and M.T. Quinn Role of NF-κB in transcriptional regulation of the phagocyte NADPH oxidase by tumor necrosis factor-α J. Leukocyte Biol. 82 2007 729 741 (Pubitemid 47367165)
    • (2007) Journal of Leukocyte Biology , vol.82 , Issue.3 , pp. 729-741
    • Gauss, K.A.1    Nelson-Overton, L.K.2    Siemsen, D.W.3    Gao, Y.4    DeLeo, F.R.5    Quinn, M.T.6
  • 45
    • 84867432702 scopus 로고    scopus 로고
    • TLR-4 signalling accelerates colon cancer cell adhesion via NF-κB mediated transcriptional up-regulation of Nox-1
    • D.P. O'Leary, L. Bhatt, J.F. Woolley, D.R. Gough, J.H. Wang, T.G. Cotter, and H.P. Redmond TLR-4 signalling accelerates colon cancer cell adhesion via NF-κB mediated transcriptional up-regulation of Nox-1 PLoS One 7 2012 e44176
    • (2012) PLoS One , vol.7 , pp. 44176
    • O'Leary, D.P.1    Bhatt, L.2    Woolley, J.F.3    Gough, D.R.4    Wang, J.H.5    Cotter, T.G.6    Redmond, H.P.7
  • 46
    • 0028179929 scopus 로고
    • NF-kappa B regulates IL-1 beta transcription through a consensus NF-kappa B binding site and a nonconsensus CRE-like site
    • J.P. Cogswell, M.M. Godlevski, G. Wisely, W.C. Clay, L.M. Leesnitzer, J.P. Ways, and J.G. Gray NF-kappa B regulates IL-1 beta transcription through a consensus NF-kappa B binding site and a nonconsensus CRE-like site J. Immunol. 153 1994 712 723
    • (1994) J. Immunol. , vol.153 , pp. 712-723
    • Cogswell, J.P.1    Godlevski, M.M.2    Wisely, G.3    Clay, W.C.4    Leesnitzer, L.M.5    Ways, J.P.6    Gray, J.G.7
  • 47
    • 0035164415 scopus 로고    scopus 로고
    • Toll-like receptor-mediated NF-κB activation: A phylogenetically conserved paradigm in innate immunity
    • G. Zhang, and S. Ghosh Toll-like receptor-mediated NF-κB activation: a phylogenetically conserved paradigm in innate immunity J. Clin. Invest. 107 2001 13 19 (Pubitemid 32047406)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.1 , pp. 13-19
    • Zhang, G.1    Ghosh, S.2
  • 48
    • 84880979012 scopus 로고    scopus 로고
    • Distinct mechanisms for induction and tolerance regulate the immediate early genes encoding interleukin 1β and tumor necrosis factor α
    • J. Adamik, K.Z. Wang, S. Unlu, A.-J.A. Su, G.M. Tannahill, D.L. Galson, L.A. O'Neill, and P.E. Auron Distinct mechanisms for induction and tolerance regulate the immediate early genes encoding interleukin 1β and tumor necrosis factor α PLoS One 8 2013 e70622
    • (2013) PLoS One , vol.8 , pp. 70622
    • Adamik, J.1    Wang, K.Z.2    Unlu, S.3    Su, A.-J.A.4    Tannahill, G.M.5    Galson, D.L.6    O'Neill, L.A.7    Auron, P.E.8
  • 49
    • 58149464712 scopus 로고    scopus 로고
    • Glutathione peroxidase 3 mediates the antioxidant effect of peroxisome proliferator-activated receptor γ in human skeletal muscle cells
    • S.S. Chung, M. Kim, B.-S. Youn, N.S. Lee, J.W. Park, I.K. Lee, Y.S. Lee, J.B. Kim, Y.M. Cho, and H.K. Lee Glutathione peroxidase 3 mediates the antioxidant effect of peroxisome proliferator-activated receptor γ in human skeletal muscle cells Mol. Cell. Biol. 29 2009 20 30
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 20-30
    • Chung, S.S.1    Kim, M.2    Youn, B.-S.3    Lee, N.S.4    Park, J.W.5    Lee, I.K.6    Lee, Y.S.7    Kim, J.B.8    Cho, Y.M.9    Lee, H.K.10
  • 50
    • 67649814105 scopus 로고    scopus 로고
    • LPS decreases fatty acid oxidation and nuclear hormone receptors in the kidney
    • K.R. Feingold, Y. Wang, A. Moser, J.K. Shigenaga, and C. Grunfeld LPS decreases fatty acid oxidation and nuclear hormone receptors in the kidney J. Lipid Res. 49 2008 2179 2187
    • (2008) J. Lipid Res. , vol.49 , pp. 2179-2187
    • Feingold, K.R.1    Wang, Y.2    Moser, A.3    Shigenaga, J.K.4    Grunfeld, C.5
  • 53
    • 77957738693 scopus 로고    scopus 로고
    • Antioxidant and anti-inflammatory effects of resveratrol in airway disease
    • L.G. Wood, P.A. Wark, and M.L. Garg Antioxidant and anti-inflammatory effects of resveratrol in airway disease Antioxid. Redox Signaling 13 2010 1535 1548
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 1535-1548
    • Wood, L.G.1    Wark, P.A.2    Garg, M.L.3
  • 54
    • 77951979741 scopus 로고    scopus 로고
    • S-glutathionylation regulates inflammatory activities of S100A9
    • S.Y. Lim, M.J. Raftery, J. Goyette, and C.L. Geczy S-glutathionylation regulates inflammatory activities of S100A9 J. Biol. Chem. 285 2010 14377 14388
    • (2010) J. Biol. Chem. , vol.285 , pp. 14377-14388
    • Lim, S.Y.1    Raftery, M.J.2    Goyette, J.3    Geczy, C.L.4
  • 55
    • 51049091712 scopus 로고    scopus 로고
    • Regulation by reversible S-glutathionylation: Molecular targets implicated in inflammatory diseases
    • M.D. Shelton, and J.J. Mieyal Regulation by reversible S-glutathionylation: molecular targets implicated in inflammatory diseases Mol. Cells 25 2008 332
    • (2008) Mol. Cells , vol.25 , pp. 332
    • Shelton, M.D.1    Mieyal, J.J.2
  • 57
    • 77955631174 scopus 로고    scopus 로고
    • Glutaredoxin 1 regulates cigarette smoke-mediated lung inflammation through differential modulation of IκB kinases in mice: Impact on histone acetylation
    • S. Chung, I.K. Sundar, H. Yao, Y.-S. Ho, and I. Rahman Glutaredoxin 1 regulates cigarette smoke-mediated lung inflammation through differential modulation of IκB kinases in mice: impact on histone acetylation Am. J. Physiol. Lung Cell. Mol. Physiol 299 2010 L192 L203
    • (2010) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.299
    • Chung, S.1    Sundar, I.K.2    Yao, H.3    Ho, Y.-S.4    Rahman, I.5
  • 64
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1979 680 685
    • (1979) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.