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Volumn 442, Issue 3, 2012, Pages 453-464

Cell signalling by reactive lipid species: New concepts and molecular mechanisms

Author keywords

Electrophile responsive proteome; Kelch like ECH associated protein 1 (Keap1); Lipid peroxidation; Nuclear factor erythroid 2 related factor (Nrf2); Protein modification; Reactive lipid species (RLS)

Indexed keywords

GLUTATHIONE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; OXIDIZING AGENT; REACTIVE LIPID SPECIES; THIOL; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG;

EID: 84857833776     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111752     Document Type: Review
Times cited : (252)

References (196)
  • 2
    • 0035181940 scopus 로고    scopus 로고
    • Mechanisms for oxidizing low-density lipoprotein: Insights from patterns of oxidation products in the artery wall and from mouse models of atherosclerosis
    • DOI 10.1016/S1050-1738(01)00101-3
    • Gaut, J. P. and Heinecke, J. W. (2001) Mechanisms for oxidizing low-density lipoprotein. Insights from patterns of oxidation products in the artery wall and from mouse models of atherosclerosis. Trends Cardiovasc. Med. 11, 103-112 (Pubitemid 33070332)
    • (2001) Trends in Cardiovascular Medicine , vol.11 , Issue.3-4 , pp. 103-112
    • Gaut, J.P.1    Heinecke, J.W.2
  • 3
    • 33645569222 scopus 로고    scopus 로고
    • F2-isoprostanes as markers of oxidative stress in vivo: An overview
    • Milne, G. L., Musiek, E. S. and Morrow, J. D. (2005) F2-isoprostanes as markers of oxidative stress in vivo: an overview. Biomarkers 10, S10-S23
    • (2005) Biomarkers , vol.10
    • Milne, G.L.1    Musiek, E.S.2    Morrow, J.D.3
  • 4
    • 0036154239 scopus 로고    scopus 로고
    • Reduced vitamin E antioxidant capacity in sickle cell disease is related to transfusion status but not to sickle crisis
    • DOI 10.1002/ajh.10033
    • Marwah, S. S., Blann, A. D., Rea, C., Phillips, J. D., Wright, J. and Bareford, D. (2002) Reduced vitamin E antioxidant capacity in sickle cell disease is related to transfusion status but not to sickle crisis. Am. J. Hematol. 69, 144-146 (Pubitemid 34111170)
    • (2002) American Journal of Hematology , vol.69 , Issue.2 , pp. 144-146
    • Marwah, S.S.1    Blann, A.D.2    Rea, C.3    Phillips, J.D.4    Wright, J.5    Bareford, D.6
  • 5
    • 13244274902 scopus 로고    scopus 로고
    • New insights regarding the autoxidation of polyunsaturated fatty acids
    • DOI 10.1089/ars.2005.7.170
    • Yin, H. and Porter, N. A. (2005) New insights regarding the autoxidation of polyunsaturated fatty acids. Antioxid. Redox Signaling 7, 170-184 (Pubitemid 40187935)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.1-2 , pp. 170-184
    • Yin, H.1    Porter, N.A.2
  • 7
    • 13244279737 scopus 로고    scopus 로고
    • Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans
    • Morrow, J. D. (2005) Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans. Arterioscler. Thromb. Vasc. Biol. 25, 279-286
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 279-286
    • Morrow, J.D.1
  • 9
    • 33646549564 scopus 로고    scopus 로고
    • Cyclopentenone isoprostanes are novel bioactive products of lipid oxidation which enhance neurodegeneration
    • DOI 10.1111/j.1471-4159.2006.03797.x
    • Musiek, E. S., Breeding, R. S., Milne, G. L., Zanoni, G., Morrow, J. D. and McLaughlin, B. (2006) Cyclopentenone isoprostanes are novel bioactive products of lipid oxidation which enhance neurodegeneration. J. Neurochem. 97, 1301-1313 (Pubitemid 43725570)
    • (2006) Journal of Neurochemistry , vol.97 , Issue.5 , pp. 1301-1313
    • Musiek, E.S.1    Breeding, R.S.2    Milne, G.L.3    Zanoni, G.4    Morrow, J.D.5    McLaughlin, B.6
  • 10
    • 37249076004 scopus 로고    scopus 로고
    • Seizure-induced formation of isofurans: Novel products of lipid peroxidation whose formation is positively modulated by oxygen tension
    • DOI 10.1111/j.1471-4159.2007.04974.x
    • Patel, M., Liang, L. P., Hou, H., Williams, B. B., Kmiec, M., Swartz, H. M., Fessel, J. P. and Roberts, II, L. J. (2008) Seizure-induced formation of isofurans: novel products of lipid peroxidation whose formation is positively modulated by oxygen tension. J. Neurochem. 104, 264-270 (Pubitemid 350265056)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.1 , pp. 264-270
    • Patel, M.1    Liang, L.-P.2    Hou, H.3    Williams, B.B.4    Kmiec, M.5    Swartz, H.M.6    Fessel, J.P.7    Roberts II, L.J.8
  • 11
    • 0035196175 scopus 로고    scopus 로고
    • Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart
    • DOI 10.1006/jmcc.2001.1454
    • Chen, J., Henderson, G. I. and Freeman, G. L. (2001) Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart. J. Mol. Cell. Cardiol. 33, 1919-1927 (Pubitemid 33097271)
    • (2001) Journal of Molecular and Cellular Cardiology , vol.33 , Issue.11 , pp. 1919-1927
    • Chen, J.1    Henderson, G.I.2    Freeman, G.L.3
  • 12
    • 34147150684 scopus 로고    scopus 로고
    • Modification of lipids by reactive oxygen and nitrogen species: The oxy-nitroxy-lipidome and its role in redox cell signaling
    • Landar, A., Giles, N. M., Zmijewski, J. W., Watanabe, N., Oh, J. Y. and Darley-Usmar, V. M. (2006) Modification of lipids by reactive oxygen and nitrogen species: the oxy-nitroxy-lipidome and its role in redox cell signaling. Future Lipidol. 1, 203-211
    • (2006) Future Lipidol. , vol.1 , pp. 203-211
    • Landar, A.1    Giles, N.M.2    Zmijewski, J.W.3    Watanabe, N.4    Oh, J.Y.5    Darley-Usmar, V.M.6
  • 15
    • 73349102177 scopus 로고    scopus 로고
    • Transduction of redox signaling by electrophile-protein reactions
    • Rudolph, T. K. and Freeman, B. A. (2009) Transduction of redox signaling by electrophile-protein reactions. Sci. Signaling 2, re7
    • (2009) Sci. Signaling , vol.2
    • Rudolph, T.K.1    Freeman, B.A.2
  • 16
    • 0036803249 scopus 로고    scopus 로고
    • Nanotransducers in cellular redox signaling: Modification of thiols by reactive oxygen and nitrogen species
    • DOI 10.1016/S0968-0004(02)02191-6, PII S0968000402021916
    • Cooper, C. E., Patel, R. P., Brookes, P. S. and Darley-Usmar, V. M. (2002) Nanotransducers in cellular redox signaling: modification of thiols by reactive oxygen and nitrogen species. Trends Biochem. Sci. 27, 489-492 (Pubitemid 35279586)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 489-492
    • Cooper, C.E.1    Patel, R.P.2    Brookes, P.S.3    Darley-Usmar, V.M.4
  • 17
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • Jones, D. P. (2008) Radical-free biology of oxidative stress. Am. J. Physiol. Cell Physiol. 295, C849-C868
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Jones, D.P.1
  • 19
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A. and Shelton, M. D. (2008) Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signaling 10, 1941-1988
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 20
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee, S. G., Chae, H. Z. and Kim, K. (2005) Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radical Biol. Med. 38, 1543-1552
    • (2005) Free Radical Biol. Med. , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 22
    • 84889339053 scopus 로고    scopus 로고
    • The covalent advantage: A new paradigm for cell signaling by thiol reactive lipid oxidation products
    • (Dalle-Donne, I. Scalone, A. and Butterfield, D. A., eds), John Wiley &Sons, Indianapolis
    • Dickinson, D. A., Darley-Usmar, V. M. and Landar, A. (2006) The covalent advantage: a new paradigm for cell signaling by thiol reactive lipid oxidation products. In Redox Proteomics: from Protein Modifications to Cellular Dysfunction and Diseases (Dalle-Donne, I. Scalone, A. and Butterfield, D. A., eds), pp. 345-367, John Wiley &Sons, Indianapolis
    • (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases , pp. 345-367
    • Dickinson, D.A.1    Darley-Usmar, V.M.2    Landar, A.3
  • 23
    • 33947576648 scopus 로고    scopus 로고
    • Prostanoids with cyclopentenone structure as tools for the characterization of electrophilic lipid-protein interactomes
    • DOI 10.1196/annals.1378.096, Signal Transduction Pathways, Part B: Stress Signalling and Transcriptional Control
    • Stamatakis, K. and Perez-Sala, D. (2006) Prostanoids with cyclopentenone structure as tools for the characterization of electrophilic lipid-protein interactomes. Ann. N.Y. Acad. Sci. 1091, 548-570 (Pubitemid 47092266)
    • (2006) Annals of the New York Academy of Sciences , vol.1091 , pp. 548-570
    • Stamatakis, K.1    Perez-Sala, D.2
  • 24
    • 24744453945 scopus 로고    scopus 로고
    • Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation
    • DOI 10.1074/jbc.M503346200
    • Hong, F., Sekhar, K. R., Freeman, M. L. and Liebler, D. C. (2005) Specific patterns of electrophile adduction trigger Keap1 ubiquitination and Nrf2 activation. J. Biol. Chem. 280, 31768-31775 (Pubitemid 41291926)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31768-31775
    • Hong, F.1    Sekhar, K.E.2    Freeman, M.L.3    Liebler, D.C.4
  • 25
    • 41849146057 scopus 로고    scopus 로고
    • Covalent modification at Cys151 dissociates the electrophile sensor Keap1 from the ubiquitin ligase CUL3
    • DOI 10.1021/tx700302s
    • Rachakonda, G., Xiong, Y., Sekhar, K. R., Stamer, S. L., Liebler, D. C. and Freeman, M. L. (2008) Covalent modification at Cys151 dissociates the electrophile sensor Keap1 from the ubiquitin ligase CUL3. Chem. Res. Toxicol. 21, 705-710 (Pubitemid 351498046)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.3 , pp. 705-710
    • Rachakonda, G.1    Xiong, Y.2    Sekhar, K.R.3    Stamer, S.L.4    Liebler, D.C.5    Freeman, M.L.6
  • 26
  • 28
    • 0031889986 scopus 로고    scopus 로고
    • Eicosanoids and isoeicosanoids: Indices of cellular function and oxidant stress
    • Reilly, M. P., Lawson, J. A. and FitzGerald, G. A. (1998) Eicosanoids and isoeicosanoids: indices of cellular function and oxidant stress. J. Nutr. 128, 434S-438S (Pubitemid 28090398)
    • (1998) Journal of Nutrition , vol.128 , Issue.2 SUPPL.
    • Reilly, M.P.1    Lawson, J.A.2    Fitzgerald, G.A.3
  • 30
    • 33846003462 scopus 로고    scopus 로고
    • Direct evidence for the covalent modification of glutathione-S- transferase P1-1 by electrophilic prostaglandins: Implications for enzyme inactivation and cell survival
    • DOI 10.1016/j.abb.2006.10.032, PII S0003986106004188
    • Sanchez-Gomez, F. J., Gayarre, J., Avellano, M. I. and Perez-Sala, D. (2007) Direct evidence for the covalent modification of glutathione-S- transferase P1-1 by electrophilic prostaglandins: implications for enzyme inactivation and cell survival. Arch. Biochem. Biophys. 457, 150-159 (Pubitemid 46048697)
    • (2007) Archives of Biochemistry and Biophysics , vol.457 , Issue.2 , pp. 150-159
    • Sanchez-Gomez, F.J.1    Gayarre, J.2    Avellano, M.I.3    Perez-Sala, D.4
  • 32
    • 0347093658 scopus 로고    scopus 로고
    • The proteasome system and proteasome inhibitors in stroke: Controlling the inflammatory response
    • Di Napoli, M. and Papa, F. (2003) The proteasome system and proteasome inhibitors in stroke: controlling the inflammatory response. Curr. Opin. Invest. Drugs 4, 1333-1342 (Pubitemid 38100579)
    • (2003) Current Opinion in Investigational Drugs , vol.4 , Issue.11 , pp. 1333-1342
    • Di, N.M.1    Papa, F.2
  • 33
    • 42449119839 scopus 로고    scopus 로고
    • 2 adduct formation with Keap1 over time: Effects on potency for intracellular antioxidant defence induction
    • DOI 10.1042/BJ20071189
    • Oh, J. Y., Giles, N., Landar, A. and Darley-Usmar, V. (2008) Accumulation of 15-deoxy-Δ(12,14)-prostaglandin J2 adduct formation with Keap1 over time: effects on potency for intracellular antioxidant defence induction. Biochem. J. 411, 297-306 (Pubitemid 351580182)
    • (2008) Biochemical Journal , vol.411 , Issue.2 , pp. 297-306
    • Oh, J.Y.1    Giles, N.2    Landar, A.3    Darley-Usmar, V.4
  • 34
    • 33644918429 scopus 로고
    • The inhibition of hematin-catalyzed oxidations by α-tocopherol
    • Tappel, A. L. (1953) The inhibition of hematin-catalyzed oxidations by α-tocopherol. Arch. Biochem. Biophys. 47, 223-225
    • (1953) Arch. Biochem. Biophys. , vol.47 , pp. 223-225
    • Tappel, A.L.1
  • 35
    • 27544492751 scopus 로고    scopus 로고
    • Lipid peroxidation: Mechanisms, inhibition, and biological effects
    • DOI 10.1016/j.bbrc.2005.08.072, PII S0006291X05017766
    • Niki, E., Yoshida, Y., Saito, Y. and Noguchi, N. (2005) Lipid peroxidation: mechanisms, inhibition, and biological effects. Biochem. Biophys. Res. Commun. 338, 668-676 (Pubitemid 41540614)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 668-676
    • Niki, E.1    Yoshida, Y.2    Saito, Y.3    Noguchi, N.4
  • 36
    • 59849119874 scopus 로고    scopus 로고
    • Eicosanoids: Generation and detection in mammalian cells
    • O'Donnell, V. B., Maskrey, B. and Taylor, G. W. (2009) Eicosanoids: generation and detection in mammalian cells. Methods Mol. Biol. 462, 5-23
    • (2009) Methods Mol. Biol. , vol.462 , pp. 5-23
    • O'Donnell, V.B.1    Maskrey, B.2    Taylor, G.W.3
  • 37
    • 0842281593 scopus 로고    scopus 로고
    • 2-isoprostane pathway
    • DOI 10.1016/j.chemphyslip.2003.10.007
    • Davies, S. S., Amarnath, V. and Roberts, II, L. J. (2004) Isoketals: highly reactive γ-ketoaldehydes formed from the H2-isoprostane pathway. Chem. Phys. Lipids 128, 85-99 (Pubitemid 38167379)
    • (2004) Chemistry and Physics of Lipids , vol.128 , Issue.1-2 , pp. 85-99
    • Davies, S.S.1    Amarnath, V.2    Roberts II, L.J.3
  • 38
    • 0035910611 scopus 로고    scopus 로고
    • Interactions between nitric oxide and lipid oxidation pathways: Implications for vascular disease
    • O'Donnell, V. B. and Freeman, B. A. (2001) Interactions between nitric oxide and lipid oxidation pathways: implications for vascular disease. Circ. Res. 88, 12-21 (Pubitemid 32064077)
    • (2001) Circulation Research , vol.88 , Issue.1 , pp. 12-21
    • O'Donnell, V.B.1    Freeman, B.A.2
  • 40
    • 11444261543 scopus 로고    scopus 로고
    • 15d-PGJ2: The anti-inflammatory prostaglandin?
    • Scher, J. U. and Pillinger, M. H. (2005) 15d-PGJ2: the anti-inflammatory prostaglandin? Clin. Immunol. 114, 100-109
    • (2005) Clin. Immunol. , vol.114 , pp. 100-109
    • Scher, J.U.1    Pillinger, M.H.2
  • 42
    • 77952650680 scopus 로고    scopus 로고
    • Systems analysis of protein modification and cellular responses induced by electrophile stress
    • Jacobs, A. T. and Marnett, L. J. (2010) Systems analysis of protein modification and cellular responses induced by electrophile stress. Acc. Chem. Res. 43, 673-683
    • (2010) Acc. Chem. Res. , vol.43 , pp. 673-683
    • Jacobs, A.T.1    Marnett, L.J.2
  • 43
    • 41649118986 scopus 로고    scopus 로고
    • Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives
    • Vila, A., Tallman, K. A., Jacobs, A. T., Liebler, D. C., Porter, N. A. and Marnett, L. J. (2008) Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives. Chem. Res. Toxicol. 21, 432-444
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 432-444
    • Vila, A.1    Tallman, K.A.2    Jacobs, A.T.3    Liebler, D.C.4    Porter, N.A.5    Marnett, L.J.6
  • 44
    • 4444314070 scopus 로고    scopus 로고
    • Reactions of 4-hydroxynonenal with proteins and cellular targets
    • DOI 10.1016/j.freeradbiomed.2004.06.012, PII S0891584904004666
    • Petersen, D. R. and Doorn, J. A. (2004) Reactions of 4-hydroxynonenal with proteins and cellular targets. Free Radical Biol. Med. 37, 937-945 (Pubitemid 39164576)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.7 , pp. 937-945
    • Petersen, D.R.1    Doorn, J.A.2
  • 45
    • 33645459848 scopus 로고    scopus 로고
    • Identification of novel protein targets for modification by 15-deoxy-Δ12,14-prostaglandin J2 in mesangial cells reveals multiple interactions with the cytoskeleton
    • Stamatakis, K., Sanchez-Gomez, F. J. and Perez-Sala, D. (2006) Identification of novel protein targets for modification by 15-deoxy-Δ12, 14-prostaglandin J2 in mesangial cells reveals multiple interactions with the cytoskeleton. J. Am. Soc. Nephrol. 17, 89-98
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 89-98
    • Stamatakis, K.1    Sanchez-Gomez, F.J.2    Perez-Sala, D.3
  • 46
    • 0028959042 scopus 로고
    • Mechanisms of free radical oxidation of unsaturated lipids
    • Porter, N. A., Caldwell, S. E. and Mills, K. A. (1995) Mechanisms of free radical oxidation of unsaturated lipids. Lipids 30, 277-290
    • (1995) Lipids , vol.30 , pp. 277-290
    • Porter, N.A.1    Caldwell, S.E.2    Mills, K.A.3
  • 47
    • 78449272101 scopus 로고    scopus 로고
    • Reduction of protein radicals by GSH and ascorbate: Potential biological significance
    • Gebicki, J. M., Nauser, T., Domazou, A., Steinmann, D., Bounds, P. L. and Koppenol, W. H. (2010) Reduction of protein radicals by GSH and ascorbate: potential biological significance. Amino Acids 39, 1131-1137
    • (2010) Amino Acids , vol.39 , pp. 1131-1137
    • Gebicki, J.M.1    Nauser, T.2    Domazou, A.3    Steinmann, D.4    Bounds, P.L.5    Koppenol, W.H.6
  • 48
    • 80052998418 scopus 로고    scopus 로고
    • Exploring the biology of lipid peroxidation-derived protein carbonylation
    • Fritz, K. S. and Petersen, D. R. (2011) Exploring the biology of lipid peroxidation-derived protein carbonylation. Chem. Res. Toxicol. 24, 1411-1419
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1411-1419
    • Fritz, K.S.1    Petersen, D.R.2
  • 49
    • 0030700237 scopus 로고    scopus 로고
    • Nitric oxide inhibition of lipid peroxidation: Kinetics of reaction with lipid peroxyl radicals and comparison with α-tocopherol
    • DOI 10.1021/bi971891z
    • O'Donnell, V. B., Chumley, P. H., Hogg, N., Bloodsworth, A., Darley-Usmar, V. M. and Freeman, B. A. (1997) Nitric oxide inhibition of lipid peroxidation: kinetics of reaction with lipid peroxyl radicals and comparison with α-tocopherol. Biochemistry 36, 15216-15223 (Pubitemid 27527986)
    • (1997) Biochemistry , vol.36 , Issue.49 , pp. 15216-15223
    • O'Donnell, V.B.1    Chumley, P.H.2    Hogg, N.3    Bloodsworth, A.4    Darley-Usmar, V.M.5    Freeman, B.A.6
  • 50
    • 0037369677 scopus 로고    scopus 로고
    • Fatty acid oxidation products in human atherosclerotic plaque: An analysis of clinical and histopathological correlates
    • DOI 10.1016/S0021-9150(02)00391-X, PII S002191500200391X
    • Waddington, E. I., Croft, K. D., Sienuarine, K., Latham, B. and Puddey, I. B. (2003) Fatty acid oxidation products in human atherosclerotic plaque: an analysis of clinical and histopathological correlates. Atherosclerosis 167, 111-120 (Pubitemid 36255642)
    • (2003) Atherosclerosis , vol.167 , Issue.1 , pp. 111-120
    • Waddington, E.I.1    Croft, K.D.2    Sienuarine, K.3    Latham, B.4    Puddey, I.B.5
  • 52
    • 26244432069 scopus 로고    scopus 로고
    • COX-2 and prostaglandins in atherosclerosis
    • Cipollone, F. (2005) COX-2 and prostaglandins in atherosclerosis. Lupus 14, 756-759
    • (2005) Lupus , vol.14 , pp. 756-759
    • Cipollone, F.1
  • 53
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • DOI 10.1152/physrev.00047.2003
    • Stocker, R. and Keaney, Jr, J. F. (2004) Role of oxidative modifications in atherosclerosis. Physiol. Rev. 84, 1381-1478 (Pubitemid 39302636)
    • (2004) Physiological Reviews , vol.84 , Issue.4 , pp. 1381-1478
    • Stocker, R.1    Keaney Jr., J.F.2
  • 54
    • 7244243910 scopus 로고    scopus 로고
    • The radical and redox chemistry of myoglobin and hemoglobin: From in vitro studies to human pathology
    • DOI 10.1089/ars.2004.6.954
    • Reeder, B. J., Svistunenko, D. A., Cooper, C. E. and Wilson, M. T. (2004) The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology. Antioxid. Redox Signaling 6, 954-966 (Pubitemid 39434932)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.6 , pp. 954-966
    • Reeder, B.J.1    Svistunenko, D.A.2    Cooper, C.E.3    Wilson, M.T.4
  • 55
    • 33751241425 scopus 로고    scopus 로고
    • Mechanisms of heme protein-mediated lipid oxidation using hemoglobin and myoglobin variants in raw and heated washed muscle
    • DOI 10.1021/jf061231d
    • Grunwald, E. W. and Richards, M. P. (2006) Mechanisms of heme protein-mediated lipid oxidation using hemoglobin and myoglobin variants in raw and heated washed muscle. J. Agric. Food Chem. 54, 8271-8280 (Pubitemid 44785414)
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.21 , pp. 8271-8280
    • Grunwald, E.W.1    Richards, M.P.2
  • 57
    • 0022391349 scopus 로고
    • 2 activated metmyoglobin
    • 2 activated metmyoglobin. Lipids 20, 625-628
    • (1985) Lipids , vol.20 , pp. 625-628
    • Kanner, J.1    Harel, S.2
  • 58
    • 0022001719 scopus 로고
    • Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin
    • DOI 10.1016/0003-9861(85)90282-6
    • Kanner, J. and Harel, S. (1985) Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Arch. Biochem. Biophys. 237, 314-321 (Pubitemid 15144885)
    • (1985) Archives of Biochemistry and Biophysics , vol.237 , Issue.2 , pp. 314-321
    • Kanner, J.1    Harel, S.2
  • 60
    • 0025874048 scopus 로고
    • Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide
    • Radi, R., Beckman, J. S., Bush, K. M. and Freeman, B. A. (1991) Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch. Biochem. Biophys. 288, 481-487
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 481-487
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 61
    • 0026676388 scopus 로고
    • The simultaneous generation of superoxide and nitric oxide can initiate lipid peroxidation in human low density lipoprotein
    • Darley-Usmar, V. M., Hogg, N., O'Leary, V. J., Wilson, M. T. and Moncada, S. (1992) The simultaneous generation of superoxide and nitric oxide can initiate lipid peroxidation in human low density lipoprotein. Free Radical Res. Commun. 17, 9-20
    • (1992) Free Radical Res. Commun. , vol.17 , pp. 9-20
    • Darley-Usmar, V.M.1    Hogg, N.2    O'Leary, V.J.3    Wilson, M.T.4    Moncada, S.5
  • 62
    • 30444439216 scopus 로고    scopus 로고
    • The discovery of nitric oxide and its role in vascular biology
    • DOI 10.1038/sj.bjp.0706458, PII 0706458
    • Moncada, S. and Higgs, E. A. (2006) The discovery of nitric oxide and its role in vascular biology. Br. J. Pharmacol. 147, S193-S201 (Pubitemid 43077277)
    • (2006) British Journal of Pharmacology , vol.147 , Issue.SUPPL. 1
    • Moncada, S.1    Higgs, E.A.2
  • 64
    • 0030454202 scopus 로고    scopus 로고
    • Formation of oxysterols during oxidation of low density lipoprotein by peroxynitrite, myoglobin, and copper
    • Patel, R. P., Diczfalusy, U., Dzeletovic, S., Wilson, M. T. and Darley-Usmar, V. M. (1996) Formation of oxysterols during oxidation of low density lipoprotein by peroxynitrite, myoglobin, and copper. J. Lipid Res. 37, 2361-2371 (Pubitemid 26427450)
    • (1996) Journal of Lipid Research , vol.37 , Issue.11 , pp. 2361-2371
    • Patel, R.P.1    Diczfalusy, U.2    Dzeletovic, S.3    Wilson, M.T.4    Darley-Usmar, V.M.5
  • 65
    • 0028990886 scopus 로고
    • Formation of F2-isoprostanes during oxidation of human low-density lipoprotein and plasma by peroxynitrite
    • Moore, K. P., Darley-Usmar, V., Morrow, J. and Roberts, II, L. J. (1995) Formation of F2-isoprostanes during oxidation of human low-density lipoprotein and plasma by peroxynitrite. Circ. Res. 77, 335-341
    • (1995) Circ. Res. , vol.77 , pp. 335-341
    • Moore, K.P.1    Darley-Usmar, V.2    Morrow, J.3    Roberts II, L.J.4
  • 68
    • 78650695097 scopus 로고    scopus 로고
    • Old and new generation lipid mediators in acute inflammation and resolution
    • Stables, M. J. and Gilroy, D. W. (2011) Old and new generation lipid mediators in acute inflammation and resolution. Prog. Lipid Res. 50, 35-51
    • (2011) Prog. Lipid Res. , vol.50 , pp. 35-51
    • Stables, M.J.1    Gilroy, D.W.2
  • 69
    • 0035860823 scopus 로고    scopus 로고
    • Coupling between cyclooxygenase, terminal prostanoid synthase, and phospholipase A2
    • Ueno, N., Murakami, M., Tanioka, T., Fujimori, K., Tanabe, T., Urade, Y. and Kudo, I. (2001) Coupling between cyclooxygenase, terminal prostanoid synthase, and phospholipase A2. J. Biol. Chem. 276, 34918-34927
    • (2001) J. Biol. Chem. , vol.276 , pp. 34918-34927
    • Ueno, N.1    Murakami, M.2    Tanioka, T.3    Fujimori, K.4    Tanabe, T.5    Urade, Y.6    Kudo, I.7
  • 72
    • 0036156424 scopus 로고    scopus 로고
    • Cyclooxygenase-2: 10 years later
    • Hinz, B. and Brune, K. (2002) Cyclooxygenase-2: 10 years later. J. Pharmacol. Exp. Ther. 300, 367-375
    • (2002) J. Pharmacol. Exp. Ther. , vol.300 , pp. 367-375
    • Hinz, B.1    Brune, K.2
  • 73
    • 33746551585 scopus 로고    scopus 로고
    • CREB-dependent cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression is mediated by protein kinase C and calcium
    • DOI 10.1002/jcb.20899
    • Pham, H., Shafer, L. M. and Slice, L. W. (2006) CREB-dependent cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression is mediated by protein kinase C and calcium. J. Cell. Biochem. 98, 1653-1666 (Pubitemid 44141867)
    • (2006) Journal of Cellular Biochemistry , vol.98 , Issue.6 , pp. 1653-1666
    • Pham, H.1    Shafer, L.M.2    Slice, L.W.3
  • 74
    • 0031886336 scopus 로고    scopus 로고
    • Posttranslational regulation of cyclooxygenase by tyrosine phosphorylation in cerebral endothelial cells
    • Parfenova, H., Balabanova, L. and Leffler, C. W. (1998) Posttranslational regulation of cyclooxygenase by tyrosine phosphorylation in cerebral endothelial cells. Am. J. Physiol. 274, C72-C81
    • (1998) Am. J. Physiol. , vol.274
    • Parfenova, H.1    Balabanova, L.2    Leffler, C.W.3
  • 75
    • 0033592251 scopus 로고    scopus 로고
    • Regulation of prostaglandin H2 synthase activity by nitrogen oxides
    • Upmacis, R. K., Deeb, R. S. and Hajjar, D. P. (1999) Regulation of prostaglandin H2 synthase activity by nitrogen oxides. Biochemistry 38, 12505-12513
    • (1999) Biochemistry , vol.38 , pp. 12505-12513
    • Upmacis, R.K.1    Deeb, R.S.2    Hajjar, D.P.3
  • 76
    • 33745934653 scopus 로고    scopus 로고
    • Oxidative alterations of cyclooxygenase during atherogenesis
    • DOI 10.1016/j.prostaglandins.2006.05.009, PII S1098882306000669
    • Upmacis, R. K., Deeb, R. S. and Hajjar, D. P. (2006) Oxidative alterations of cyclooxygenase during atherogenesis. Prostaglandins Other Lipid Mediators 80, 1-14 (Pubitemid 44056286)
    • (2006) Prostaglandins and Other Lipid Mediators , vol.80 , Issue.1-2 , pp. 1-14
    • Upmacis, R.K.1    Deeb, R.S.2    Hajjar, D.P.3
  • 77
    • 21744445761 scopus 로고    scopus 로고
    • Peroxynitrite provides the peroxide tone for PGHS-2-dependent prostacyclin synthesis in vascular smooth muscle cells
    • DOI 10.1096/fj.04-3465fje
    • Schildknecht, S., Bachschmid, M. and Ullrich, V. (2005) Peroxynitrite provides the peroxide tone for PGHS-2-dependent prostacyclin synthesis in vascular smooth muscle cells. FASEB J. 19, 1169-1171 (Pubitemid 40946454)
    • (2005) FASEB Journal , vol.19 , Issue.9 , pp. 1169-1171
    • Schildknecht, S.1    Bachschmid, M.2    Ullrich, V.3
  • 78
    • 18044367744 scopus 로고    scopus 로고
    • Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2)
    • DOI 10.1016/j.jmb.2005.03.035
    • Yamada, T., Komoto, J., Watanabe, K., Ohmiya, Y. and Takusagawa, F. (2005) Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2). J. Mol. Biol. 348, 1163-1176 (Pubitemid 40602374)
    • (2005) Journal of Molecular Biology , vol.348 , Issue.5 , pp. 1163-1176
    • Yamada, T.1    Komoto, J.2    Watanabe, K.3    Ohmiya, Y.4    Takusagawa, F.5
  • 80
    • 0031550246 scopus 로고    scopus 로고
    • 2 in lipopolysaccharide- stimulated rat peritoneal macrophages
    • DOI 10.1006/bbrc.1996.5894
    • Matsumoto, H., Naraba, H., Murakami, M., Kudo, I., Yamaki, K., Ueno, A. and Oh-ishi, S. (1997) Concordant induction of prostaglandin E2 synthase with cyclooxygenase-2 leads to preferred production of prostaglandin E2 over thromboxane and prostaglandin D2 in lipopolysaccharide-stimulated rat peritoneal macrophages. Biochem. Biophys. Res. Commun. 230, 110-114 (Pubitemid 27210253)
    • (1997) Biochemical and Biophysical Research Communications , vol.230 , Issue.1 , pp. 110-114
    • Matsumoto, H.1    Naraba, H.2    Murakami, M.3    Kudo, I.4    Yamaki, K.5    Ueno, A.6    Oh-Ishi, S.7
  • 82
    • 0034692689 scopus 로고    scopus 로고
    • Regulation of prostaglandin E2 biosynthesis by inducible membrane-associated prostaglandin E2 synthase that acts in concert with cyclooxygenase-2
    • Murakami, M., Naraba, H., Tanioka, T., Semmyo, N., Nakatani, Y., Kojima, F., Ikeda, T., Fueki, M., Ueno, A., Oh, S. and Kudo, I. (2000) Regulation of prostaglandin E2 biosynthesis by inducible membrane-associated prostaglandin E2 synthase that acts in concert with cyclooxygenase-2. J. Biol. Chem. 275, 32783-32792
    • (2000) J. Biol. Chem. , vol.275 , pp. 32783-32792
    • Murakami, M.1    Naraba, H.2    Tanioka, T.3    Semmyo, N.4    Nakatani, Y.5    Kojima, F.6    Ikeda, T.7    Fueki, M.8    Ueno, A.9    Oh, S.10    Kudo, I.11
  • 83
    • 0034661453 scopus 로고    scopus 로고
    • 2 synthase: Identification by molecular modeling-guided site-specific antibodies
    • DOI 10.1006/abbi.2000.1892
    • Lin, Y. Z., Deng, H. and Ruan, K. H. (2000) Topology of catalytic portion of prostaglandin I2 synthase: identification by molecular modeling-guided site-specific antibodies. Arch. Biochem. Biophys. 379, 188-197 (Pubitemid 30637453)
    • (2000) Archives of Biochemistry and Biophysics , vol.379 , Issue.2 , pp. 188-197
    • Lin, Y.-Z.1    Deng, H.2    Ruan, K.-H.3
  • 85
    • 50649103946 scopus 로고    scopus 로고
    • Electrophilic cyclopentenone neuroprostanes are anti-inflammatory mediators formed from the peroxidation of the omega-3 polyunsaturated fatty acid docosahexaenoic acid
    • Musiek, E. S., Brooks, J. D., Joo, M., Brunoldi, E., Porta, A., Zanoni, G., Vidari, G., Blackwell, T. S., Montine, T. J., Milne, G. L. et al. (2008) Electrophilic cyclopentenone neuroprostanes are anti-inflammatory mediators formed from the peroxidation of the omega-3 polyunsaturated fatty acid docosahexaenoic acid. J. Biol. Chem. 283, 19927-19935
    • (2008) J. Biol. Chem. , vol.283 , pp. 19927-19935
    • Musiek, E.S.1    Brooks, J.D.2    Joo, M.3    Brunoldi, E.4    Porta, A.5    Zanoni, G.6    Vidari, G.7    Blackwell, T.S.8    Montine, T.J.9    Milne, G.L.10
  • 86
    • 0035127254 scopus 로고    scopus 로고
    • Regulation of leukotrienes in the management of asthma: Biology and clinical therapy
    • Leff, A. R. (2001) Regulation of leukotrienes in the management of asthma: biology and clinical therapy. Annu. Rev. Med. 52, 1-14
    • (2001) Annu. Rev. Med. , vol.52 , pp. 1-14
    • Leff, A.R.1
  • 87
    • 0345008359 scopus 로고
    • On the nature of the 5-lipoxygenase reaction in human leukocytes: Enzyme purification and requirement for multiple stimulatory factors
    • DOI 10.1073/pnas.82.18.6040
    • Rouzer, C. A. and Samuelsson, B. (1985) On the nature of the 5-lipoxygenase reaction in human leukocytes: enzyme purification and requirement for multiple stimulatory factors. Proc. Natl. Acad. Sci. U.S.A. 82, 6040-6044 (Pubitemid 16223894)
    • (1985) Proceedings of the National Academy of Sciences of the United States of America , vol.82 , Issue.18 , pp. 6040-6044
    • Rouzer, C.A.1    Samuelsson, B.2
  • 88
    • 0026100805 scopus 로고
    • 'Enzymatic' lipid peroxidation: Reactions of mammalian lipoxygenases
    • Yamamoto, S. (1991) 'Enzymatic' lipid peroxidation: reactions of mammalian lipoxygenases. Free Radical Biol. Med. 10, 149-159
    • (1991) Free Radical Biol. Med. , vol.10 , pp. 149-159
    • Yamamoto, S.1
  • 89
    • 0027958244 scopus 로고
    • Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase
    • DOI 10.1016/0005-2760(94)90234-8
    • Suzuki, H., Kishimoto, K., Yoshimoto, T., Yamamoto, S., Kanai, F., Ebina, Y., Miyatake, A. and Tanabe, T. (1994) Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase. Biochim. Biophys. Acta 1210, 308-316 (Pubitemid 24048874)
    • (1994) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.1210 , Issue.3 , pp. 308-316
    • Suzuki, H.1    Kishimoto, K.2    Yoshimoto, T.3    Yamamoto, S.4    Kanai, F.5    Ebina, Y.6    Miyatake, A.7    Tanabe, T.8
  • 90
    • 0025917177 scopus 로고
    • Reduction of the active-site iron by potent inhibitors of lipoxygenases
    • Nelson, M. J., Batt, D. G., Thompson, J. S. and Wright, S. W. (1991) Reduction of the active-site iron by potent inhibitors of lipoxygenases. J. Biol. Chem. 266, 8225-8229 (Pubitemid 21906500)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.13 , pp. 8225-8229
    • Nelson, M.J.1    Batt, D.G.2    Thompson, J.S.3    Wright, S.W.4
  • 91
    • 0027419580 scopus 로고
    • Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone
    • Weitzel, F. and Wendel, A. (1993) Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone. J. Biol. Chem. 268, 6288-6292 (Pubitemid 23099321)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.9 , pp. 6288-6292
    • Weitzel, F.1    Wendel, A.2
  • 94
    • 0035862064 scopus 로고    scopus 로고
    • Leukotriene B4: Metabolism and signal transduction
    • Yokomizo, T., Izumi, T. and Shimizu, T. (2001) Leukotriene B4: metabolism and signal transduction. Arch. Biochem. Biophys. 385, 231-241
    • (2001) Arch. Biochem. Biophys. , vol.385 , pp. 231-241
    • Yokomizo, T.1    Izumi, T.2    Shimizu, T.3
  • 97
    • 0026496304 scopus 로고
    • Mechanism-based inactivation of leukotriene A4 hydrolase/aminopeptidase by leukotriene A4. Mass spectrometric and kinetic characterization
    • Orning, L., Gierse, J., Duffin, K., Bild, G., Krivi, G. and Fitzpatrick, F. A. (1992) Mechanism-based inactivation of leukotriene A4 hydrolase/ aminopeptidase by leukotriene A4. Mass spectrometric and kinetic characterization. J. Biol. Chem. 267, 22733-22739
    • (1992) J. Biol. Chem. , vol.267 , pp. 22733-22739
    • Orning, L.1    Gierse, J.2    Duffin, K.3    Bild, G.4    Krivi, G.5    Fitzpatrick, F.A.6
  • 98
    • 0028049483 scopus 로고
    • Irreversible inactivation of 5-lipoxygenase by leukotriene A4. Characterization of product inactivation with purified enzyme and intact leukocytes
    • Lepley, R. A. and Fitzpatrick, F. A. (1994) Irreversible inactivation of 5-lipoxygenase by leukotriene A4. Characterization of product inactivation with purified enzyme and intact leukocytes. J. Biol. Chem. 269, 2627-2631
    • (1994) J. Biol. Chem. , vol.269 , pp. 2627-2631
    • Lepley, R.A.1    Fitzpatrick, F.A.2
  • 99
    • 0029086681 scopus 로고
    • Specificity of expression and effects of eicosanoid mediators in normal physiology and human diseases
    • Goetzl, E. J., An, S. and Smith, W. L. (1995) Specificity of expression and effects of eicosanoid mediators in normal physiology and human diseases. FASEB J. 9, 1051-1058
    • (1995) FASEB J. , vol.9 , pp. 1051-1058
    • Goetzl, E.J.1    An, S.2    Smith, W.L.3
  • 100
    • 4444262310 scopus 로고    scopus 로고
    • Pharmacology and signaling of prostaglandin receptors: Multiple roles in inflammation and immune modulation
    • DOI 10.1016/j.pharmthera.2004.06.003, PII S0163725804000968
    • Hata, A. N. and Breyer, R. M. (2004) Pharmacology and signaling of prostaglandin receptors: multiple roles in inflammation and immune modulation. Pharm. Ther. 103, 147-166 (Pubitemid 39209041)
    • (2004) Pharmacology and Therapeutics , vol.103 , Issue.2 , pp. 147-166
    • Hata, A.N.1    Breyer, R.M.2
  • 102
    • 0036323604 scopus 로고    scopus 로고
    • Leukotriene receptors: Classification, gene expression, and signal transduction
    • Izumi, T., Yokomizo, T., Obinata, H., Ogasawara, H. and Shimizu, T. (2002) Leukotriene receptors: classification, gene expression, and signal transduction. J. Biochem. (Tokyo) 132, 1-6 (Pubitemid 34832263)
    • (2002) Journal of Biochemistry , vol.132 , Issue.1 , pp. 1-6
    • Izumi, T.1    Yokomizo, T.2    Obinata, H.3    Ogasawara, H.4    Shimizut, T.5
  • 103
    • 79151478743 scopus 로고    scopus 로고
    • Commonly used leukotriene B4 receptor antagonists possess intrinsic activity as agonists in human endothelial cells: Effects on calcium transients, adhesive events and mediator release
    • Johansson, A. S., Haeggstrom, J. Z. and Palmblad, J. (2011) Commonly used leukotriene B4 receptor antagonists possess intrinsic activity as agonists in human endothelial cells: effects on calcium transients, adhesive events and mediator release. Prostaglandins Leukotrienes Essent. Fatty Acids 84, 109-112
    • (2011) Prostaglandins Leukotrienes Essent. Fatty Acids , vol.84 , pp. 109-112
    • Johansson, A.S.1    Haeggstrom, J.Z.2    Palmblad, J.3
  • 104
    • 0037166335 scopus 로고    scopus 로고
    • 2: Differential pharmacological properties and tissue distribution
    • DOI 10.1074/jbc.M109447200
    • Ogasawara, H., Ishii, S., Yokomizo, T., Kakinuma, T., Komine, M., Tamaki, K., Shimizu, T. and Izumi, T. (2002) Characterization of mouse cysteinyl leukotriene receptors mCysLT1 and mCysLT2: differential pharmacological properties and tissue distribution. J. Biol. Chem. 277, 18763-18768 (Pubitemid 34952434)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18763-18768
    • Ogasawara, H.1    Ishii, S.2    Yokomizo, T.3    Kakinuma, T.4    Komine, M.5    Tamaki, K.6    Shimizu, T.7    Izumi, T.8
  • 109
    • 44649151707 scopus 로고    scopus 로고
    • The PPAR trio: Regulators of myocardial energy metabolism in health and disease
    • Madrazo, J. A. and Kelly, D. P. (2008) The PPAR trio: regulators of myocardial energy metabolism in health and disease. J. Mol. Cell. Cardiol. 44, 968-975
    • (2008) J. Mol. Cell. Cardiol. , vol.44 , pp. 968-975
    • Madrazo, J.A.1    Kelly, D.P.2
  • 110
    • 80054072517 scopus 로고    scopus 로고
    • Formation and signaling actions of electrophilic lipids
    • Schopfer, F. J., Cipollina, C. and Freeman, B. A. (2011) Formation and signaling actions of electrophilic lipids. Chem. Rev. 111, 5997-6021
    • (2011) Chem. Rev. , vol.111 , pp. 5997-6021
    • Schopfer, F.J.1    Cipollina, C.2    Freeman, B.A.3
  • 112
    • 0142195899 scopus 로고    scopus 로고
    • Activation of nuclear receptors by prostaglandins
    • DOI 10.1016/S0049-3848(03)00418-3
    • Ide, T., Egan, K., Bell-Parikh, L. C. and FitzGerald, G. A. (2003) Activation of nuclear receptors by prostaglandins. Thromb. Res. 110, 311-315 (Pubitemid 37329831)
    • (2003) Thrombosis Research , vol.110 , Issue.5-6 , pp. 311-315
    • Ide, T.1    Egan, K.2    Bell-Parikh, L.C.3    FitzGerald, G.A.4
  • 113
    • 85047690989 scopus 로고    scopus 로고
    • 15-Deoxy-Δ12,14-PGJ2: Endogenous PPARγ ligand or minor eicosanoid degradation product?
    • Powell, W. S. (2003) 15-Deoxy-Δ12,14-PGJ2: endogenous PPARγ ligand or minor eicosanoid degradation product? J. Clin. Invest. 112, 828-830
    • (2003) J. Clin. Invest. , vol.112 , pp. 828-830
    • Powell, W.S.1
  • 114
    • 77951242122 scopus 로고    scopus 로고
    • Covalent peroxisome proliferator-activated receptor γ adduction by nitro-fatty acids: Selective ligand activity and anti-diabetic signaling actions
    • Schopfer, F. J., Cole, M. P., Groeger, A. L., Chen, C. S., Khoo, N. K., Woodcock, S. R., Golin-Bisello, F., Motanya, U. N., Li, Y., Zhang, J. et al. (2010) Covalent peroxisome proliferator-activated receptor γ adduction by nitro-fatty acids: selective ligand activity and anti-diabetic signaling actions. J. Biol. Chem. 285, 12321-12333
    • (2010) J. Biol. Chem. , vol.285 , pp. 12321-12333
    • Schopfer, F.J.1    Cole, M.P.2    Groeger, A.L.3    Chen, C.S.4    Khoo, N.K.5    Woodcock, S.R.6    Golin-Bisello, F.7    Motanya, U.N.8    Li, Y.9    Zhang, J.10
  • 116
    • 31344467471 scopus 로고    scopus 로고
    • A sensitive method for the quantitative measurement of protein thiol modification in response to oxidative stress
    • DOI 10.1016/j.freeradbiomed.2005.08.046, PII S0891584905005009
    • Landar, A., Oh, J. Y., Giles, N. M., Isom, A., Kirk, M., Barnes, S. and Darley-Usmar, V. (2006) A sensitive method for the quantitative measurement of protein thiol modification in response to oxidative stress. Free Radical Biol. Med. 40, 459-468 (Pubitemid 43139681)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.3 , pp. 459-468
    • Landar, A.1    Oh, J.-Y.2    Giles, N.M.3    Isom, A.4    Kirk, M.5    Barnes, S.6    Darley-Usmar, V.M.7
  • 117
    • 0043172509 scopus 로고    scopus 로고
    • Basic aspects of the biochemical reactivity of 4-hydroxynonenal
    • Schaur, R. J. (2003) Basic aspects of the biochemical reactivity of 4-hydroxynonenal. Mol. Aspects Med. 24, 149-159
    • (2003) Mol. Aspects Med. , vol.24 , pp. 149-159
    • Schaur, R.J.1
  • 118
    • 84857868182 scopus 로고    scopus 로고
    • Application of the hard and soft, acids and bases (HSAB) theory to toxicant-target interactions
    • doi:10.1021/tx2003257
    • Lopachin, R. M., Gavin, T., Decaprio, A. and Barber, D. S. (2011) Application of the hard and soft, acids and bases (HSAB) theory to toxicant-target interactions. Chem. Res. Toxicol., doi:10.1021/tx2003257
    • (2011) Chem. Res. Toxicol.
    • Lopachin, R.M.1    Gavin, T.2    Decaprio, A.3    Barber, D.S.4
  • 119
    • 0025106197 scopus 로고
    • Assessment of the propensity for covalent binding of electrophiles to biological substrates
    • Carlson, R. M. (1990) Assessment of the propensity for covalent binding of electrophiles to biological substrates. Environ. Health Perspect. 87, 227-232
    • (1990) Environ. Health Perspect. , vol.87 , pp. 227-232
    • Carlson, R.M.1
  • 121
    • 0029852202 scopus 로고    scopus 로고
    • Kinetics of the reaction of a potential chemopreventive agent, 2,6- dithiopurine, and its major metabolite, 2,6-dithiouric acid, with multiple classes of electrophilic toxicants
    • DOI 10.1021/tx960088n
    • Qing, W. G., Powell, K. L. and MacLeod, M. C. (1996) Kinetics of the reaction of a potential chemopreventive agent, 2,6-dithiopurine, and its major metabolite, 2,6-dithiouric acid, with multiple classes of electrophilic toxicants. Chem. Res. Toxicol. 9, 1298-1304 (Pubitemid 26403835)
    • (1996) Chemical Research in Toxicology , vol.9 , Issue.8 , pp. 1298-1304
    • Qing, W.-G.1    Powell, K.L.2    MacLeod, M.C.3
  • 122
    • 1642289985 scopus 로고    scopus 로고
    • Trends in structure-toxicity relationships for carbonyl-containing α,β-unsaturated compounds
    • DOI 10.1080/10629360410001665839
    • Schultz, T. W. and Yarbrough, J. W. (2004) Trends in structure-toxicity relationships for carbonyl-containing α,β-unsaturated compounds. SAR QSAR Environ. Res. 15, 139-146 (Pubitemid 38390852)
    • (2004) SAR and QSAR in Environmental Research , vol.15 , Issue.2 , pp. 139-146
    • Schultz, T.W.1    Yarbrough, J.W.2
  • 123
    • 6944250291 scopus 로고    scopus 로고
    • 2 addition in mesangial cells: Role in the inhibition of pro-inflammatory genes
    • DOI 10.1124/mol.104.002824
    • Sanchez-Gomez, F. J., Cernuda-Morollon, E., Stamatakis, K. and Perez-Sala, D. (2004) Protein thiol modification by 15-deoxy-Δ12,14- prostaglandin J2 addition in mesangial cells: role in the inhibition of pro-inflammatory genes. Mol. Pharmacol. 66, 1349-1358 (Pubitemid 39411076)
    • (2004) Molecular Pharmacology , vol.66 , Issue.5 , pp. 1349-1358
    • Sanchez-Gomez, F.J.1    Cernuda-Morollon, E.2    Stamatakis, K.3    Perez-Sala, D.4
  • 124
    • 34249893910 scopus 로고    scopus 로고
    • Modification and activation of Ras proteins by electrophilic prostanoids with different structure are site-selective
    • DOI 10.1021/bi602389p
    • Renedo, M., Gayarre, J., Garcia-Dominguez, C. A., Perez-Rodriguez, A., Prieto, A., Canada, F. J., Rojas, J. M. and Perez-Sala, D. (2007) Modification and activation of Ras proteins by electrophilic prostanoids with different structure are site-selective. Biochemistry 46, 6607-6616 (Pubitemid 46870126)
    • (2007) Biochemistry , vol.46 , Issue.22 , pp. 6607-6616
    • Renedo, M.1    Gayarre, J.2    Garcia-Dominguez, C.A.3    Perez-Rodriguez, A.4    Prieto, A.5    Javier, C.F.6    Rojas, J.M.7    Perez-Sala, D.8
  • 125
    • 64249099733 scopus 로고    scopus 로고
    • The permissive role of mitochondria in the induction of haem oxygenase-1 in endothelial cells
    • Ricart, K. C., Bolisetty, S., Johnson, M. S., Perez, J., Agarwal, A., Murphy, M. P. and Landar, A. (2009) The permissive role of mitochondria in the induction of haem oxygenase-1 in endothelial cells. Biochem. J. 419, 427-436
    • (2009) Biochem. J. , vol.419 , pp. 427-436
    • Ricart, K.C.1    Bolisetty, S.2    Johnson, M.S.3    Perez, J.4    Agarwal, A.5    Murphy, M.P.6    Landar, A.7
  • 126
    • 0026517333 scopus 로고
    • Structure-activity relationships for inhibition of papain by peptide Michael acceptors
    • Liu, S. and Hanzlik, R. P. (1992) Structure-activity relationships for inhibition of papain by peptide Michael acceptors. J. Med. Chem. 35, 1067-1075
    • (1992) J. Med. Chem. , vol.35 , pp. 1067-1075
    • Liu, S.1    Hanzlik, R.P.2
  • 127
    • 4344676781 scopus 로고    scopus 로고
    • Inactivation of protein disulfide isomerase by alkylators including α,β-unsaturated aldehydes at low physiological pHs
    • Liu, X. W. and Sok, D. E. (2004) Inactivation of protein disulfide isomerase by alkylators including α,β-unsaturated aldehydes at low physiological pHs. Biol. Chem. 385, 633-637
    • (2004) Biol. Chem. , vol.385 , pp. 633-637
    • Liu, X.W.1    Sok, D.E.2
  • 128
    • 34548507495 scopus 로고    scopus 로고
    • Thiol oxidation in signaling and response to stress: Detection and quantification of physiological and pathophysiological thiol modifications
    • DOI 10.1016/j.freeradbiomed.2007.07.014, PII S0891584907004959
    • Ying, J., Clavreul, N., Sethuraman, M., Adachi, T. and Cohen, R. A. (2007) Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications. Free Radical Biol. Med. 43, 1099-1108 (Pubitemid 47374443)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.8 , pp. 1099-1108
    • Ying, J.1    Clavreul, N.2    Sethuraman, M.3    Adachi, T.4    Cohen, R.A.5
  • 129
    • 0035310359 scopus 로고    scopus 로고
    • Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines
    • DOI 10.1042/0264-6021:3550145
    • Mallis, R. J., Buss, J. E. and Thomas, J. A. (2001) Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines. Biochem. J. 355, 145-153 (Pubitemid 32304245)
    • (2001) Biochemical Journal , vol.355 , Issue.1 , pp. 145-153
    • Mallis, R.J.1    Buss, J.E.2    Thomas, J.A.3
  • 130
    • 1042267391 scopus 로고    scopus 로고
    • Detection and proteomic identification of S-nitrosylated proteins in endothelial cells
    • DOI 10.1016/j.abb.2003.12.006
    • Martinez-Ruiz, A. and Lamas, S. (2004) Detection and proteomic identification of S-nitrosylated proteins in endothelial cells. Arch. Biochem. Biophys. 423, 192-199 (Pubitemid 38198228)
    • (2004) Archives of Biochemistry and Biophysics , vol.423 , Issue.1 , pp. 192-199
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 132
    • 31044455445 scopus 로고    scopus 로고
    • Redox modifications of protein-thiols: Emerging roles in cell signaling
    • DOI 10.1016/j.bcp.2005.10.044, PII S0006295205007173
    • Biswas, S., Chida, A. S. and Rahman, I. (2006) Redox modifications of protein-thiols: emerging roles in cell signaling. Biochem. Pharmacol. 71, 551-564 (Pubitemid 43121989)
    • (2006) Biochemical Pharmacology , vol.71 , Issue.5 , pp. 551-564
    • Biswas, S.1    Chida, A.S.2    Rahman, I.3
  • 134
    • 33845606362 scopus 로고    scopus 로고
    • Structure-toxicity analysis of Type-2 Alkenes: In vitro neurotoxicity
    • DOI 10.1093/toxsci/kfl127
    • Lopachin, R. M., Barber, D. S., Geohagen, B. C., Gavin, T., He, D. and Das, S. (2007) Structure-toxicity analysis of type-2 alkenes: in vitro neurotoxicity. Toxicol. Sci. 95, 136-146 (Pubitemid 44942784)
    • (2007) Toxicological Sciences , vol.95 , Issue.1 , pp. 136-146
    • LoPachin, R.M.1    Barber, D.S.2    Geohagen, B.C.3    Gavin, T.4    He, D.5    Das, S.6
  • 135
    • 55549146493 scopus 로고    scopus 로고
    • Application of structure-activity relationships to investigate the molecular mechanisms of hepatocyte toxicity and electrophilic reactivity of α,β-unsaturated aldehydes
    • Chan, K., Poon, R. and O'Brien, P. J. (2008) Application of structure-activity relationships to investigate the molecular mechanisms of hepatocyte toxicity and electrophilic reactivity of α,β-unsaturated aldehydes. J. Appl. Toxicol. 28, 1027-1039
    • (2008) J. Appl. Toxicol. , vol.28 , pp. 1027-1039
    • Chan, K.1    Poon, R.2    O'Brien, P.J.3
  • 136
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • DOI 10.1042/BJ20031049
    • Levonen, A. L., Landar, A., Ramachandran, A., Ceaser, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D. and Darley-Usmar, V. M. (2004) Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem. J. 378, 373-382 (Pubitemid 38367228)
    • (2004) Biochemical Journal , vol.378 , Issue.2 , pp. 373-382
    • Levonen, A.-L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 137
    • 29644443964 scopus 로고    scopus 로고
    • Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane
    • DOI 10.1021/tx0502138
    • Hong, F., Freeman, M. L. and Liebler, D. C. (2005) Identification of sensor cysteines in human Keap1 modified by the cancer chemopreventive agent sulforaphane. Chem. Res. Toxicol. 18, 1917-1926 (Pubitemid 43023050)
    • (2005) Chemical Research in Toxicology , vol.18 , Issue.12 , pp. 1917-1926
    • Hong, F.1    Freeman, M.L.2    Liebler, D.C.3
  • 139
    • 71049139267 scopus 로고    scopus 로고
    • An azido-biotin reagent for use in the isolation of protein adducts of lipid-derived electrophiles by streptavidin catch and photorelease
    • Kim, H. Y., Tallman, K. A., Liebler, D. C. and Porter, N. A. (2009) An azido-biotin reagent for use in the isolation of protein adducts of lipid-derived electrophiles by streptavidin catch and photorelease. Mol. Cell. Proteomics 8, 2080-2089
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2080-2089
    • Kim, H.Y.1    Tallman, K.A.2    Liebler, D.C.3    Porter, N.A.4
  • 140
    • 32944457661 scopus 로고    scopus 로고
    • 2 in mitochondria
    • DOI 10.1042/BJ20051259
    • Landar, A., Shiva, S., Levonen, A. L., Oh, J. Y., Zaragoza, C., Johnson, M. S. and Darley-Usmar, V. M. (2006) Induction of the permeability transition and cytochrome c release by 15-deoxy-Δ12,14-prostaglandin J2 in mitochondria. Biochem. J. 394, 185-195 (Pubitemid 43259668)
    • (2006) Biochemical Journal , vol.394 , Issue.1 , pp. 185-195
    • Landar, A.1    Shiva, S.2    Levonen, A.-L.3    Oh, J.-Y.4    Zaragoza, C.5    Johnson, M.S.6
  • 141
    • 0842346366 scopus 로고    scopus 로고
    • The biochemistry of the isoprostane, neuroprostane, and isofuran pathways of lipid peroxidation
    • DOI 10.1016/j.chemphyslip.2003.09.016
    • Roberts, II, L. J. and Fessel, J. P. (2004) The biochemistry of the isoprostane, neuroprostane, and isofuran pathways of lipid peroxidation. Chem. Phys. Lipids 128, 173-186 (Pubitemid 38167386)
    • (2004) Chemistry and Physics of Lipids , vol.128 , Issue.1-2 , pp. 173-186
    • Roberts II, L.J.1    Fessel, J.P.2
  • 143
    • 33845648094 scopus 로고    scopus 로고
    • Redox regulation of neuronal survival mediated by electrophilic compounds
    • DOI 10.1016/j.tins.2006.11.004, PII S0166223606002670
    • Satoh, T. and Lipton, S. A. (2007) Redox regulation of neuronal survival mediated by electrophilic compounds. Trends Neurosci. 30, 37-45 (Pubitemid 44960491)
    • (2007) Trends in Neurosciences , vol.30 , Issue.1 , pp. 37-45
    • Satoh, T.1    Lipton, S.A.2
  • 144
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne, A., Yeh, J. I., Mallett, T. C., Luba, J., Crane, III, E. J., Charrier, V. and Parsonage, D. (1999) Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38, 15407-15416
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, T.C.3    Luba, J.4    Crane III, E.J.5    Charrier, V.6    Parsonage, D.7
  • 145
    • 78650509515 scopus 로고    scopus 로고
    • Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals
    • McMahon, M., Lamont, D. J., Beattie, K. A. and Hayes, J. D. (2010) Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals. Proc. Natl. Acad. Sci. U.S.A. 107, 18838-18843
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 18838-18843
    • McMahon, M.1    Lamont, D.J.2    Beattie, K.A.3    Hayes, J.D.4
  • 146
    • 84856729192 scopus 로고    scopus 로고
    • Mitochondrial thiols in antioxidant protection and redox signalling: Distinct roles for glutathionylation and other thiol modifications
    • doi:10.1089/ars.2011.4289
    • Murphy, M. P. (2011) Mitochondrial thiols in antioxidant protection and redox signalling: distinct roles for glutathionylation and other thiol modifications. Antioxid. Redox Signaling, doi:10.1089/ars.2011.4289
    • (2011) Antioxid. Redox Signaling
    • Murphy, M.P.1
  • 147
    • 43149121589 scopus 로고    scopus 로고
    • Mitochondrial protein targets of thiol-reactive electrophiles
    • DOI 10.1021/tx700433m
    • Wong, H. L. and Liebler, D. C. (2008) Mitochondrial protein targets of thiol-reactive electrophiles. Chem. Res. Toxicol. 21, 796-804 (Pubitemid 351644557)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.4 , pp. 796-804
    • Wong, H.L.1    Liebler, D.C.2
  • 148
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • DOI 10.1016/S1097-2765(02)00445-8
    • Meng, T. C., Fukada, T. and Tonks, N. K. (2002) Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9, 387-399 (Pubitemid 34195563)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 387-399
    • Meng, T.-C.1    Fukada, T.2    Tonks, N.K.3
  • 151
    • 77749316875 scopus 로고    scopus 로고
    • Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage
    • Requejo, R., Hurd, T. R., Costa, N. J. and Murphy, M. P. (2010) Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage. FEBS J. 277, 1465-1480
    • (2010) FEBS J. , vol.277 , pp. 1465-1480
    • Requejo, R.1    Hurd, T.R.2    Costa, N.J.3    Murphy, M.P.4
  • 152
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • DOI 10.1042/0264-6021:3600001
    • Sheehan, D., Meade, G., Foley, V. M. and Dowd, C. A. (2001) Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360, 1-16 (Pubitemid 33081943)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 153
    • 84455192645 scopus 로고    scopus 로고
    • Inhibitor of Nrf2 (INrf2 or Keap1) degrades Bcl-xL via phosphoglycerate mutase 5 and controls cellular apoptosis
    • Niture, S. K. and Jaiswal, A. K. (2011) Inhibitor of Nrf2 (INrf2 or Keap1) degrades Bcl-xL via phosphoglycerate mutase 5 and controls cellular apoptosis. J. Biol. Chem. 286, 44542-44556
    • (2011) J. Biol. Chem. , vol.286 , pp. 44542-44556
    • Niture, S.K.1    Jaiswal, A.K.2
  • 156
    • 76549096602 scopus 로고    scopus 로고
    • Mitochondrial targeting of the electrophilic lipid 15-deoxy-Δ12,14- prostaglandin J2 increases apoptotic efficacy via redox cell signalling mechanisms
    • Diers, A. R., Higdon, A. N., Ricart, K. C., Johnson, M. S., Agarwal, A., Kalyanaraman, B., Landar, A. and Darley-Usmar, V. M. (2010) Mitochondrial targeting of the electrophilic lipid 15-deoxy-Δ12,14-prostaglandin J2 increases apoptotic efficacy via redox cell signalling mechanisms. Biochem. J. 426, 31-41
    • (2010) Biochem. J. , vol.426 , pp. 31-41
    • Diers, A.R.1    Higdon, A.N.2    Ricart, K.C.3    Johnson, M.S.4    Agarwal, A.5    Kalyanaraman, B.6    Landar, A.7    Darley-Usmar, V.M.8
  • 159
    • 27744488160 scopus 로고    scopus 로고
    • Upregulation of endogenous antioxidants and phase 2 enzymes by the red wine polyphenol, resveratrol in cultured aortic smooth muscle cells leads to cytoprotection against oxidative and electrophilic stress
    • DOI 10.1016/j.phrs.2005.08.002, PII S1043661805001520
    • Li, Y., Cao, Z. and Zhu, H. (2006) Upregulation of endogenous antioxidants and phase 2 enzymes by the red wine polyphenol, resveratrol in cultured aortic smooth muscle cells leads to cytoprotection against oxidative and electrophilic stress. Pharmacol. Res. 53, 6-15 (Pubitemid 41619373)
    • (2006) Pharmacological Research , vol.53 , Issue.1 , pp. 6-15
    • Li, Y.1    Cao, Z.2    Zhu, H.3
  • 160
    • 70450246970 scopus 로고    scopus 로고
    • Nrf2-dependent and -independent responses to nitro-fatty acids in human endothelial cells: Identification of heat shock response as the major pathway activated by nitro-oleic acid
    • Kansanen, E., Jyrkkanen, H. K., Volger, O. L., Leinonen, H., Kivela, A. M., Hakkinen, S. K., Woodcock, S. R., Schopfer, F. J., Horrevoets, A. J., Yla-Herttuala, S. et al. (2009) Nrf2-dependent and -independent responses to nitro-fatty acids in human endothelial cells: identification of heat shock response as the major pathway activated by nitro-oleic acid. J. Biol. Chem. 284, 33233-33241
    • (2009) J. Biol. Chem. , vol.284 , pp. 33233-33241
    • Kansanen, E.1    Jyrkkanen, H.K.2    Volger, O.L.3    Leinonen, H.4    Kivela, A.M.5    Hakkinen, S.K.6    Woodcock, S.R.7    Schopfer, F.J.8    Horrevoets, A.J.9    Yla-Herttuala, S.10
  • 161
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • DOI 10.1016/j.febslet.2007.05.040, PII S0014579307005686, Cellular Stress
    • Powers, M. V. and Workman, P. (2007) Inhibitors of the heat shock response: biology and pharmacology. FEBS Lett. 581, 3758-3769 (Pubitemid 47081010)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 162
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells
    • Mosser, D. D., Theodorakis, N. G. and Morimoto, R. I. (1988) Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells. Mol. Cell. Biol. 8, 4736-4744 (Pubitemid 18261551)
    • (1988) Molecular and Cellular Biology , vol.8 , Issue.11 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 163
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi, Y., Mosser, D. D. and Morimoto, R. I. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12, 654-666 (Pubitemid 28134298)
    • (1998) Genes and Development , vol.12 , Issue.5 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 164
    • 77957252262 scopus 로고    scopus 로고
    • The heat shock factor family and adaptation to proteotoxic stress
    • Fujimoto, M. and Nakai, A. (2010) The heat shock factor family and adaptation to proteotoxic stress. FEBS J. 277, 4112-4125
    • (2010) FEBS J. , vol.277 , pp. 4112-4125
    • Fujimoto, M.1    Nakai, A.2
  • 165
    • 36249026428 scopus 로고    scopus 로고
    • Ozonation of human blood induces a remarkable upregulation of heme oxygenase-1 and heat stress protein-70
    • Bocci, V., Aldinucci, C., Mosci, F., Carraro, F. and Valacchi, G. (2007) Ozonation of human blood induces a remarkable upregulation of heme oxygenase-1 and heat stress protein-70. Mediators Inflammation 2007, 26785
    • (2007) Mediators Inflammation , vol.2007 , pp. 26785
    • Bocci, V.1    Aldinucci, C.2    Mosci, F.3    Carraro, F.4    Valacchi, G.5
  • 166
    • 33646589046 scopus 로고    scopus 로고
    • Metal ions induced heat shock protein response by elevating superoxide anion level in HeLa cells transformed by HSE-SEAP reporter gene
    • DOI 10.1016/j.tox.2006.02.021, PII S0300483X06001363
    • Yu, Z., Yang, X. and Wang, K. (2006) Metal ions induced heat shock protein response by elevating superoxide anion level in HeLa cells transformed by HSE-SEAP reporter gene. Toxicology 223, 1-8 (Pubitemid 43728623)
    • (2006) Toxicology , vol.223 , Issue.1-2 , pp. 1-8
    • Yu, Z.1    Yang, X.2    Wang, K.3
  • 168
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • Murry, C. E., Jennings, R. B. and Reimer, K. A. (1986) Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 74, 1124-1136 (Pubitemid 17174962)
    • (1986) Circulation , vol.74 , Issue.5 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 169
    • 0025687768 scopus 로고
    • Cardiac adaptation to ischemia. Ischemic preconditioning increases myocardial tolerance to subsequent ischemic episodes
    • Reimer, K. A., Murry, C. E. and Jennings, R. B. (1990) Cardiac adaptation to ischemia. Ischemic preconditioning increases myocardial tolerance to subsequent ischemic episodes. Circulation 82, 2266-2268
    • (1990) Circulation , vol.82 , pp. 2266-2268
    • Reimer, K.A.1    Murry, C.E.2    Jennings, R.B.3
  • 170
    • 0031888412 scopus 로고    scopus 로고
    • Lipid peroxidation, arachidonic acid and products of the lipoxygenase pathway in ischaemic preconditioning of rat heart
    • DOI 10.1016/S0008-6363(97)00240-X, PII S000863639700240X
    • Starkopf, J., Andreasen, T. V., Bugge, E. and Ytrehus, K. (1998) Lipid peroxidation, arachidonic acid and products of the lipoxygenase pathway in ischaemic preconditioning of rat heart. Cardiovasc. Res. 37, 66-75 (Pubitemid 28122617)
    • (1998) Cardiovascular Research , vol.37 , Issue.1 , pp. 66-75
    • Starkopf, J.1    Andreasen, T.V.2    Bugge, E.3    Ytrehus, K.4
  • 171
    • 0035082680 scopus 로고    scopus 로고
    • Role of oxidants in the signaling pathway of preconditioning
    • Tritto, I. and Ambrosio, G. (2001) Role of oxidants in the signaling pathway of preconditioning. Antiox. Redox Signaling 3, 3-10 (Pubitemid 32240625)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.1 , pp. 3-10
    • Tritto, I.1    Ambrosio, G.2
  • 172
    • 79952489004 scopus 로고    scopus 로고
    • Ischemic postconditioning attenuates lung reperfusion injury and reduces systemic proinflammatory cytokine release via heme oxygenase 1
    • Xu, B., Gao, X., Xu, J., Lei, S., Xia, Z. Y., Xu, Y. and Xia, Z. (2011) Ischemic postconditioning attenuates lung reperfusion injury and reduces systemic proinflammatory cytokine release via heme oxygenase 1. J. Surg. Res. 166, e157-e164
    • (2011) J. Surg. Res. , vol.166
    • Xu, B.1    Gao, X.2    Xu, J.3    Lei, S.4    Xia, Z.Y.5    Xu, Y.6    Xia, Z.7
  • 176
    • 0027500938 scopus 로고
    • Temporal profile of heat shock protein 70 synthesis in ischemic tolerance induced by preconditioning ischemia in rat hippocampus
    • DOI 10.1016/0306-4522(93)90138-6
    • Liu, Y., Kato, H., Nakata, N. and Kogure, K. (1993) Temporal profile of heat shock protein 70 synthesis in ischemic tolerance induced by preconditioning ischemia in rat hippocampus. Neuroscience 56, 921-927 (Pubitemid 23308647)
    • (1993) Neuroscience , vol.56 , Issue.4 , pp. 921-927
    • Liu, Y.1    Kato, H.2    Nakata, N.3    Kogure, K.4
  • 179
    • 51449090118 scopus 로고    scopus 로고
    • Induction of heat shock protein 70 and preconditioning by sevoflurane: A potent protective interaction against myocardial ischemia-reperfusion injury
    • Pagel, P. S. (2008) Induction of heat shock protein 70 and preconditioning by sevoflurane: a potent protective interaction against myocardial ischemia-reperfusion injury. Anesth. Analg. 107, 742-745
    • (2008) Anesth. Analg. , vol.107 , pp. 742-745
    • Pagel, P.S.1
  • 180
    • 0035053973 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins: New insights on biological activities and cellular targets
    • DOI 10.1002/med.1006
    • Straus, D. S. and Glass, C. K. (2001) Cyclopentenone prostaglandins: new insights on biological activities and cellular targets. Med. Res. Rev. 21, 185-210 (Pubitemid 32303994)
    • (2001) Medicinal Research Reviews , vol.21 , Issue.3 , pp. 185-210
    • Straus, D.S.1    Glass, C.K.2
  • 181
    • 33646508129 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases by lysophosphatidylcholine-induced mitochondrial reactive oxygen species generation in endothelial cells
    • Watanabe, N., Zmijewski, J. W., Takabe, W., Umezu-Goto, M., Le Goffe, C., Sekine, A., Landar, A., Watanabe, A., Aoki, J., Arai, H. et al. (2006) Activation of mitogen-activated protein kinases by lysophosphatidylcholine- induced mitochondrial reactive oxygen species generation in endothelial cells. Am. J. Pathol. 168, 1737-1748
    • (2006) Am. J. Pathol. , vol.168 , pp. 1737-1748
    • Watanabe, N.1    Zmijewski, J.W.2    Takabe, W.3    Umezu-Goto, M.4    Le Goffe, C.5    Sekine, A.6    Landar, A.7    Watanabe, A.8    Aoki, J.9    Arai, H.10
  • 182
    • 41149116150 scopus 로고    scopus 로고
    • Unsaturated lipid peroxidation-derived aldehydes activate autophagy in vascular smooth-muscle cells
    • DOI 10.1042/BJ20071063
    • Hill, B. G., Haberzettl, P., Ahmed, Y., Srivastava, S. and Bhatnagar, A. (2008) Unsaturated lipid peroxidation-derived aldehydes activate autophagy in vascular smooth-muscle cells. Biochem. J. 410, 525-534 (Pubitemid 351429023)
    • (2008) Biochemical Journal , vol.410 , Issue.3 , pp. 525-534
    • Hill, B.G.1    Haberzettl, P.2    Ahmed, Y.3    Srivastava, S.4    Bhatnagar, A.5
  • 183
    • 0035929592 scopus 로고    scopus 로고
    • 15-Deoxy-Δ12,14-prostaglandin J2 inhibition of NF-κB-DNA binding through covalent modification of the p50 subunit
    • Cernuda-Morollon, E., Pineda-Molina, E., Canada, F. J. and Perez-Sala, D. (2001) 15-Deoxy-Δ12,14-prostaglandin J2 inhibition of NF-κB-DNA binding through covalent modification of the p50 subunit. J. Biol. Chem. 276, 35530-35536
    • (2001) J. Biol. Chem. , vol.276 , pp. 35530-35536
    • Cernuda-Morollon, E.1    Pineda-Molina, E.2    Canada, F.J.3    Perez-Sala, D.4
  • 186
    • 33845357331 scopus 로고    scopus 로고
    • Thioredoxin reductase is required for the inactivation of tumor suppressor p53 and for apoptosis induced by endogenous electrophiles
    • DOI 10.1093/carcin/bgl111
    • Cassidy, P. B., Edes, K., Nelson, C. C., Parsawar, K., Fitzpatrick, F. A. and Moos, P. J. (2006) Thioredoxin reductase is required for the inactivation of tumor suppressor p53 and for apoptosis induced by endogenous electrophiles. Carcinogenesis 27, 2538-2549 (Pubitemid 44884113)
    • (2006) Carcinogenesis , vol.27 , Issue.12 , pp. 2538-2549
    • Cassidy, P.B.1    Edes, K.2    Nelson, C.C.3    Parsawar, K.4    Fitzpatrick, F.A.5    Moos, P.J.6
  • 189
    • 23244458797 scopus 로고    scopus 로고
    • Covalent modification of actin by 4-hydroxy-trans-2-nonenal (HNE): LC-ESI-MS/MS evidence for Cys374 Michael adduction
    • DOI 10.1002/jms.872
    • Aldini, G., Dalle-Donne, I., Vistoli, G., Maffei Facino, R. and Carini, M. (2005) Covalent modification of actin by 4-hydroxy-trans-2-nonenal (HNE): LC-ESI-MS/MS evidence for Cys374 Michael adduction. J. Mass Spectrom. 40, 946-954 (Pubitemid 41098081)
    • (2005) Journal of Mass Spectrometry , vol.40 , Issue.7 , pp. 946-954
    • Aldini, G.1    Dalle-Donne, I.2    Vistoli, G.3    Facino, R.M.4    Carini, M.5
  • 190
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidation-sensitive subunit in 26 S proteasome
    • DOI 10.1021/bi051336u
    • Ishii, T., Sakurai, T., Usami, H. and Uchida, K. (2005) Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome. Biochemistry 44, 13893-13901 (Pubitemid 41507469)
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 191
    • 57849098033 scopus 로고    scopus 로고
    • Structural insight into PPARγ activation through covalent modification with endogenous fatty acids
    • Waku, T., Shiraki, T., Oyama, T., Fujimoto, Y., Maebara, K., Kamiya, N., Jingami, H. and Morikawa, K. (2009) Structural insight into PPARγ activation through covalent modification with endogenous fatty acids. J. Mol. Biol. 385, 188-199
    • (2009) J. Mol. Biol. , vol.385 , pp. 188-199
    • Waku, T.1    Shiraki, T.2    Oyama, T.3    Fujimoto, Y.4    Maebara, K.5    Kamiya, N.6    Jingami, H.7    Morikawa, K.8
  • 193
    • 15444370200 scopus 로고    scopus 로고
    • Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria
    • DOI 10.1016/j.bbrc.2005.02.135
    • Yarian, C. S., Rebrin, I. and Sohal, R. S. (2005) Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria. Biochem. Biophys. Res. Commun. 330, 151-156 (Pubitemid 40394947)
    • (2005) Biochemical and Biophysical Research Communications , vol.330 , Issue.1 , pp. 151-156
    • Yarian, C.S.1    Rebrin, I.2    Sohal, R.S.3
  • 194
    • 35948941541 scopus 로고    scopus 로고
    • Oxidative modifications of cardiac mitochondria and inhibition of cytochrome c oxidase activity by 4-hydroxynonenal
    • DOI 10.1179/135100007X200308
    • Kaplan, P., Tatarkova, Z., Racay, P., Lehotsky, J., Pavlikova, M. and Dobrota, D. (2007) Oxidative modifications of cardiac mitochondria and inhibition of cytochrome c oxidase activity by 4-hydroxynonenal. Redox Rep. 12, 211-218 (Pubitemid 350065108)
    • (2007) Redox Report , vol.12 , Issue.5 , pp. 211-218
    • Kaplan, P.1    Tatarkova, Z.2    Racay, P.3    Lehotsky, J.4    Pavlikova, M.5    Dobrota, D.6
  • 195
    • 0032996250 scopus 로고    scopus 로고
    • Formation of 4-hydroxynonenal adducts with cytochrome c oxidase in rats following short-term ethanol intake
    • DOI 10.1002/hep.510290611
    • Chen, J., Robinson, N. C., Schenker, S., Frosto, T. A. and Henderson, G. I. (1999) Formation of 4-hydroxynonenal adducts with cytochrome c oxidase in rats following short-term ethanol intake. Hepatology 29, 1792-1798 (Pubitemid 29247053)
    • (1999) Hepatology , vol.29 , Issue.6 , pp. 1792-1798
    • Chen, J.1    Robinson, N.C.2    Schenker, S.3    Frosto, T.A.4    Henderson, G.I.5
  • 196
    • 0032496339 scopus 로고    scopus 로고
    • Inhibition of cytochrome c oxidase activity by 4-hydroxynonenal (HNE). Role of HNE adduct formation with the enzyme subunits
    • DOI 10.1016/S0304-4165(98)00002-6, PII S0304416598000026
    • Chen, J., Schenker, S., Frosto, T. A. and Henderson, G. I. (1998) Inhibition of cytochrome c oxidase activity by 4-hydroxynonenal (HNE). Role of HNE adduct formation with the enzyme subunits. Biochim. Biophys. Acta 1380, 336-344 (Pubitemid 28210348)
    • (1998) Biochimica et Biophysica Acta - General Subjects , vol.1380 , Issue.3 , pp. 336-344
    • Chen, J.1    Schenker, S.2    Frosto, T.A.3    Henderson, G.I.4


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