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Volumn 14, Issue 5, 2013, Pages 9126-9167

Targeting the redox balance in inflammatory skin conditions

Author keywords

Antioxidant; Inflammation; Oxidative stress; ROS; Skin

Indexed keywords

ACETYLCYSTEINE; ALPHA CAROTENE; ALPHA TOCOPHEROL; ANTIOXIDANT; ASCORBIC ACID; BETA CAROTENE; CHELATING AGENT; COPPER ZINC SUPEROXIDE DISMUTASE; CURCUMIN; EXTRACELLULAR SUPEROXIDE DISMUTASE; FREE RADICAL; HEME OXYGENASE 1; HYDROGEN PEROXIDE; MANGANESE SUPEROXIDE DISMUTASE; POLYPHENOL; REACTIVE OXYGEN METABOLITE; UBIDECARENONE;

EID: 84876896360     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14059126     Document Type: Review
Times cited : (161)

References (371)
  • 1
    • 84863469984 scopus 로고    scopus 로고
    • Interleukin-1, inflammasomes, autoinflammation and the skin
    • doi:10.4414/smw.2012.13590
    • Contassot, E.; Beer, H.D.; French, L.E. Interleukin-1, inflammasomes, autoinflammation and the skin. Swiss Med. Wkly. 2012, 142, doi:10.4414/smw.2012.13590.
    • (2012) Swiss Med. Wkly. , vol.142
    • Contassot, E.1    Beer, H.D.2    French, L.E.3
  • 5
    • 0036245242 scopus 로고    scopus 로고
    • Getting under the skin of epidermal morphogenesis
    • Fuchs, E.; Raghavan, S. Getting under the skin of epidermal morphogenesis. Nat. Rev. Genet. 2002, 3, 199-209.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 199-209
    • Fuchs, E.1    Raghavan, S.2
  • 6
    • 1342305179 scopus 로고    scopus 로고
    • Fibroblast heterogeneity: More than skin deep
    • Sorrell, J.M.; Caplan, A.I. Fibroblast heterogeneity: More than skin deep. J. Cell Sci. 2004, 117, 667-675.
    • (2004) J. Cell Sci. , vol.117 , pp. 667-675
    • Sorrell, J.M.1    Caplan, A.I.2
  • 8
    • 84882285470 scopus 로고    scopus 로고
    • Specific inflammasomes in complex diseases
    • doi:10.1016/j.clim.2012.12.006
    • Masters, S.L. Specific inflammasomes in complex diseases. Clin. Immunol. 2012, doi:10.1016/j.clim.2012.12.006.
    • (2012) Clin. Immunol.
    • Masters, S.L.1
  • 9
    • 77952295021 scopus 로고    scopus 로고
    • Interleukin-1 (IL-1) pathway
    • doi:10.1126/scisignal.3105cm1
    • Weber, A.; Wasiliew, P.; Kracht, M. Interleukin-1 (IL-1) pathway. Sci. Signal. 2010, 3, doi:10.1126/scisignal.3105cm1.
    • (2010) Sci. Signal. , vol.3
    • Weber, A.1    Wasiliew, P.2    Kracht, M.3
  • 11
    • 51349096358 scopus 로고    scopus 로고
    • Molecular regulation of inflammation and cell death
    • Yeretssian, G.; Labbe, K.; Saleh, M. Molecular regulation of inflammation and cell death. Cytokine 2008, 43, 380-390.
    • (2008) Cytokine , vol.43 , pp. 380-390
    • Yeretssian, G.1    Labbe, K.2    Saleh, M.3
  • 13
    • 34250835251 scopus 로고    scopus 로고
    • The inflammasome mediates UVB-induced activation and secretion of interleukin-1beta by keratinocytes
    • Feldmeyer, L.; Keller, M.; Niklaus, G.; Hohl, D.; Werner, S.; Beer, H.D. The inflammasome mediates UVB-induced activation and secretion of interleukin-1beta by keratinocytes. Curr. Biol. 2007, 17, 1140-1145.
    • (2007) Curr. Biol. , vol.17 , pp. 1140-1145
    • Feldmeyer, L.1    Keller, M.2    Niklaus, G.3    Hohl, D.4    Werner, S.5    Beer, H.D.6
  • 15
    • 0023000943 scopus 로고
    • Human keratinocytes contain mRNA indistinguishable from monocyte interleukin 1 alpha and beta mRNA. Keratinocyte epidermal cell-derived thymocyte-activating factor is identical to interleukin 1
    • Kupper, T.S.; Ballard, D.W.; Chua, A.O.; McGuire, J.S.; Flood, P.M.; Horowitz, M.C.; Langdon, R.; Lightfoot, L.; Gubler, U. Human keratinocytes contain mRNA indistinguishable from monocyte interleukin 1 alpha and beta mRNA. Keratinocyte epidermal cell-derived thymocyte-activating factor is identical to interleukin 1. J. Exp. Med. 1986, 164, 2095-2100.
    • (1986) J. Exp. Med. , vol.164 , pp. 2095-2100
    • Kupper, T.S.1    Ballard, D.W.2    Chua, A.O.3    McGuire, J.S.4    Flood, P.M.5    Horowitz, M.C.6    Langdon, R.7    Lightfoot, L.8    Gubler, U.9
  • 16
    • 0028180294 scopus 로고
    • Differential modulation of interleukin-1 alpha (IL-1 alpha) and interleukin-1 beta (IL-1 beta) in human epidermal keratinocytes by UVB
    • Kondo, S.; Sauder, D.N.; Kono, T.; Galley, K.A.; McKenzie, R.C. Differential modulation of interleukin-1 alpha (IL-1 alpha) and interleukin-1 beta (IL-1 beta) in human epidermal keratinocytes by UVB. Exp. Dermatol. 1994, 3, 29-39.
    • (1994) Exp. Dermatol. , vol.3 , pp. 29-39
    • Kondo, S.1    Sauder, D.N.2    Kono, T.3    Galley, K.A.4    McKenzie, R.C.5
  • 18
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein links oxidative stress to inflammasome activation
    • Zhou, R.; Tardivel, A.; Thorens, B.; Choi, I.; Tschopp, J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat. Immunol. 2010, 11, 136-140.
    • (2010) Nat. Immunol. , vol.11 , pp. 136-140
    • Zhou, R.1    Tardivel, A.2    Thorens, B.3    Choi, I.4    Tschopp, J.5
  • 19
    • 77649179433 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production?
    • Tschopp, J.; Schroder, K. NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production? Nat. Rev. Immunol. 2010, 10, 210-215.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 210-215
    • Tschopp, J.1    Schroder, K.2
  • 22
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. Free radicals in the physiological control of cell function. Physiol. Rev. 2002, 82, 47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 23
    • 50949103793 scopus 로고    scopus 로고
    • The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal
    • Forman, H.J.; Fukuto, J.M.; Miller, T.; Zhang, H.; Rinna, A.; Levy, S. The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal. Arch. Biochem. Biophys. 2008, 477, 183-195.
    • (2008) Arch. Biochem. Biophys. , vol.477 , pp. 183-195
    • Forman, H.J.1    Fukuto, J.M.2    Miller, T.3    Zhang, H.4    Rinna, A.5    Levy, S.6
  • 24
    • 67649255876 scopus 로고    scopus 로고
    • A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • Niethammer, P.; Grabher, C.; Look, A.T.; Mitchison, T.J. A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 2009, 459, 996-999.
    • (2009) Nature , vol.459 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 25
    • 0032889677 scopus 로고    scopus 로고
    • Redox regulation of cellular signalling
    • Kamata, H.; Hirata, H. Redox regulation of cellular signalling. Cell. Signal. 1999, 11, 1-14.
    • (1999) Cell. Signal. , vol.11 , pp. 1-14
    • Kamata, H.1    Hirata, H.2
  • 27
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel, T. Signal transduction by reactive oxygen species. J. Cell. Biol. 2011, 194, 7-15.
    • (2011) J. Cell. Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 29
    • 0036829062 scopus 로고    scopus 로고
    • Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors
    • Haddad, J.J. Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors. Cell. Signal. 2002, 14, 879-897.
    • (2002) Cell. Signal. , vol.14 , pp. 879-897
    • Haddad, J.J.1
  • 30
    • 84861182619 scopus 로고    scopus 로고
    • S-Glutathionylation signaling in cell biology: Progress and prospects
    • Pastore, A.; Piemonte, F. S-Glutathionylation signaling in cell biology: Progress and prospects. Eur. J. Pharm. Sci. 2012, 46, 279-292.
    • (2012) Eur. J. Pharm. Sci. , vol.46 , pp. 279-292
    • Pastore, A.1    Piemonte, F.2
  • 31
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • Jones, D.P. Radical-free biology of oxidative stress. Am. J. Physiol. Cell Physiol. 2008, 295, C849-C868.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Jones, D.P.1
  • 32
    • 0242299711 scopus 로고    scopus 로고
    • APE/Ref-1 and the mammalian response to genotoxic stress
    • Fritz, G.; Grosch, S.; Tomicic, M.; Kaina, B. APE/Ref-1 and the mammalian response to genotoxic stress. Toxicology 2003, 193, 67-78.
    • (2003) Toxicology , vol.193 , pp. 67-78
    • Fritz, G.1    Grosch, S.2    Tomicic, M.3    Kaina, B.4
  • 33
    • 4143070452 scopus 로고    scopus 로고
    • Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression
    • Rahman, I.; Marwick, J.; Kirkham, P. Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression. Biochem. Pharm. 2004, 68, 1255-1267.
    • (2004) Biochem. Pharm. , vol.68 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 34
    • 33646853458 scopus 로고    scopus 로고
    • Direct oxidative modifications of signalling proteins in mammalian cells and their effects on apoptosis
    • England, K.; Cotter, T.G. Direct oxidative modifications of signalling proteins in mammalian cells and their effects on apoptosis. Redox Rep. 2005, 10, 237-245.
    • (2005) Redox Rep. , vol.10 , pp. 237-245
    • England, K.1    Cotter, T.G.2
  • 35
    • 0035009582 scopus 로고    scopus 로고
    • The importance of proteins in defense against oxidation
    • Bourdon, E.; Blache, D. The importance of proteins in defense against oxidation. Antioxid. Redox Signal. 2001, 3, 293-311.
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 293-311
    • Bourdon, E.1    Blache, D.2
  • 38
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and selenium: The role of oxidation state in protein structure and function
    • Jacob, C.; Giles, G.I.; Giles, N.M.; Sies, H. Sulfur and selenium: The role of oxidation state in protein structure and function. Angew. Chem. 2003, 42, 4742-4758.
    • (2003) Angew. Chem. , vol.42 , pp. 4742-4758
    • Jacob, C.1    Giles, G.I.2    Giles, N.M.3    Sies, H.4
  • 39
    • 84055213065 scopus 로고    scopus 로고
    • Molecular mechanism of glyceraldehyde-3-phosphate dehydrogenase inactivation by alpha, beta-unsaturated carbonyl derivatives
    • Martyniuk, C.J.; Fang, B.; Koomen, J.M.; Gavin, T.; Zhang, L.; Barber, D.S.; Lopachin, R.M. Molecular mechanism of glyceraldehyde-3-phosphate dehydrogenase inactivation by alpha, beta-unsaturated carbonyl derivatives. Chem. Res. Toxicol. 2011, 24, 2302-2311.
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 2302-2311
    • Martyniuk, C.J.1    Fang, B.2    Koomen, J.M.3    Gavin, T.4    Zhang, L.5    Barber, D.S.6    Lopachin, R.M.7
  • 40
    • 84867176110 scopus 로고    scopus 로고
    • Protein cysteines map to functional networks according to steady-state level of oxidation
    • Go, Y.M.; Duong, D.M.; Peng, J.; Jones, D.P. Protein cysteines map to functional networks according to steady-state level of oxidation. J. Proteomics Bioinform. 2011, 4, 196-209.
    • (2011) J. Proteomics Bioinform. , vol.4 , pp. 196-209
    • Go, Y.M.1    Duong, D.M.2    Peng, J.3    Jones, D.P.4
  • 41
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: Thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman, H.J.; Fukuto, J.M.; Torres, M. Redox signaling: Thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am. J. Physiol. Cell Physiol. 2004, 287, C246-C256.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 42
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn, C.C.; Hampton, M.B. Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 2008, 45, 549-561.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 43
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • Paulsen, C.E.; Carroll, K.S. Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem. Biol. 2010, 5, 47-62.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 44
    • 84872831805 scopus 로고    scopus 로고
    • Cysteine oxidative posttranslational modifications: Emerging regulation in the cardiovascular system
    • Chung, H.S.; Wang, S.B.; Venkatraman, V.; Murray, C.I.; Van Eyk, J.E. Cysteine oxidative posttranslational modifications: Emerging regulation in the cardiovascular system. Circ. Res. 2013, 112, 382-392.
    • (2013) Circ. Res. , vol.112 , pp. 382-392
    • Chung, H.S.1    Wang, S.B.2    Venkatraman, V.3    Murray, C.I.4    van Eyk, J.E.5
  • 45
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu, J.M.; Dixon, J.E. Protein tyrosine phosphatases: Mechanisms of catalysis and regulation. Curr. Opin. Chem. Biol. 1998, 2, 633-641.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 633-641
    • Denu, J.M.1    Dixon, J.E.2
  • 46
    • 80053513183 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatases by reversible oxidation
    • Ostman, A.; Frijhoff, J.; Sandin, A.; Bohmer, F.D. Regulation of protein tyrosine phosphatases by reversible oxidation. J. Biochem. 2011, 150, 345-356.
    • (2011) J. Biochem. , vol.150 , pp. 345-356
    • Ostman, A.1    Frijhoff, J.2    Sandin, A.3    Bohmer, F.D.4
  • 47
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu, B.P.; Weissman, J.S. Oxidative protein folding in eukaryotes: Mechanisms and consequences. J. Cell. Biol. 2004, 164, 341-346.
    • (2004) J. Cell. Biol. , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 48
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand, A.R.; Cuozzo, J.W.; Kaiser, C.A. Pathways for protein disulphide bond formation. Trends Cell. Biol. 2000, 10, 203-210.
    • (2000) Trends Cell. Biol. , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 49
    • 9444243245 scopus 로고    scopus 로고
    • Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control
    • Jones, D.P.; Go, Y.M.; Anderson, C.L.; Ziegler, T.R.; Kinkade, J.M., Jr.; Kirlin, W.G. Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control. FASEB J. 2004, 18, 1246-1248.
    • (2004) FASEB J. , vol.18 , pp. 1246-1248
    • Jones, D.P.1    Go, Y.M.2    Anderson, C.L.3    Ziegler, T.R.4    Kinkade Jr., J.M.5    Kirlin, W.G.6
  • 50
    • 64349117191 scopus 로고    scopus 로고
    • Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines
    • Chen, C.Y.; Willard, D.; Rudolph, J. Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines. Biochemistry 2009, 48, 1399-1409.
    • (2009) Biochemistry , vol.48 , pp. 1399-1409
    • Chen, C.Y.1    Willard, D.2    Rudolph, J.3
  • 51
    • 0032484012 scopus 로고    scopus 로고
    • The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2
    • Caselli, A.; Marzocchini, R.; Camici, G.; Manao, G.; Moneti, G.; Pieraccini, G.; Ramponi, G. The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J. Biol. Chem. 1998, 273, 32554-32560.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32554-32560
    • Caselli, A.1    Marzocchini, R.2    Camici, G.3    Manao, G.4    Moneti, G.5    Pieraccini, G.6    Ramponi, G.7
  • 52
    • 0037036358 scopus 로고    scopus 로고
    • Reversible inactivation of the tumor suppressor PTEN by H2O2
    • Lee, S.R.; Yang, K.S.; Kwon, J.; Lee, C.; Jeong, W.; Rhee, S.G. Reversible inactivation of the tumor suppressor PTEN by H2O2. J. Biol. Chem. 2002, 277, 20336-20342.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20336-20342
    • Lee, S.R.1    Yang, K.S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 53
    • 0041323072 scopus 로고    scopus 로고
    • Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction
    • Sohn, J.; Rudolph, J. Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction. Biochemistry 2003, 42, 10060-10070.
    • (2003) Biochemistry , vol.42 , pp. 10060-10070
    • Sohn, J.1    Rudolph, J.2
  • 54
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks, N.K. Redox redux: Revisiting PTPs and the control of cell signaling. Cell 2005, 121, 667-670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 57
    • 77957032845 scopus 로고    scopus 로고
    • Redox control of protein-DNA interactions: From molecular mechanisms to significance in signal transduction, gene expression, and DNA replication
    • Shlomai, J. Redox control of protein-DNA interactions: From molecular mechanisms to significance in signal transduction, gene expression, and DNA replication. Antioxid. Redox Signal. 2010, 13, 1429-1476.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1429-1476
    • Shlomai, J.1
  • 58
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova, A.T.; Holtzclaw, W.D.; Cole, R.N.; Itoh, K.; Wakabayashi, N.; Katoh, Y.; Yamamoto, M.; Talalay, P. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc. Natl. Acad. Sci. USA 2002, 99, 11908-11913.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 59
    • 51049091712 scopus 로고    scopus 로고
    • Regulation by reversible S-glutathionylation: Molecular targets implicated in inflammatory diseases
    • Shelton, M.D.; Mieyal, J.J. Regulation by reversible S-glutathionylation: Molecular targets implicated in inflammatory diseases. Mol. Cells 2008, 25, 332-346.
    • (2008) Mol. Cells , vol.25 , pp. 332-346
    • Shelton, M.D.1    Mieyal, J.J.2
  • 60
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappaB
    • Qanungo, S.; Starke, D.W.; Pai, H.V.; Mieyal, J.J.; Nieminen, A.L. Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappaB. J. Biol. Chem. 2007, 282, 18427-18436.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18427-18436
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.L.5
  • 61
    • 33750915802 scopus 로고    scopus 로고
    • Regulation of signal transduction through protein cysteine oxidation
    • Cross, J.V.; Templeton, D.J. Regulation of signal transduction through protein cysteine oxidation. Antioxid. Redox Signal. 2006, 8, 1819-1827.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1819-1827
    • Cross, J.V.1    Templeton, D.J.2
  • 62
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-kappaB: Players, pathways, perspectives
    • Gilmore, T.D. Introduction to NF-kappaB: Players, pathways, perspectives. Oncogene 2006, 25, 6680-6684.
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 63
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • Benhar, M.; Forrester, M.T.; Stamler, J.S. Protein denitrosylation: Enzymatic mechanisms and cellular functions. Nat. Rev. Mol. Cell Biol. 2009, 10, 721-732.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 64
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar, M.; Forrester, M.T.; Hess, D.T.; Stamler, J.S. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 2008, 320, 1050-1054.
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 66
    • 84876902031 scopus 로고    scopus 로고
    • S-Nitrosylation: Specificity, occupancy, and interaction with other post-translational modifications
    • doi:10.1089/ars.2012.5056
    • Evangelista, A.M.; Kohr, M.J.; Murphy, E. S-Nitrosylation: Specificity, occupancy, and interaction with other post-translational modifications. Antioxid. Redox Signal. 2013, doi:10.1089/ars.2012.5056.
    • (2013) Antioxid. Redox Signal.
    • Evangelista, A.M.1    Kohr, M.J.2    Murphy, E.3
  • 68
    • 0347624596 scopus 로고    scopus 로고
    • S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway
    • Kim, S.; Wing, S.S.; Ponka, P. S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway. Mol. Cell. Biol. 2004, 24, 330-337.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 330-337
    • Kim, S.1    Wing, S.S.2    Ponka, P.3
  • 69
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417, 1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 74
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • Winterbourn, C.C. Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 2008, 4, 278-286.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 75
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen, A.; Fridovich, I. Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J. Biol. Chem. 1994, 269, 29405-29408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 76
    • 0030806863 scopus 로고    scopus 로고
    • Superoxide anion radical (O2-·), superoxide dismutases, and related matters
    • Fridovich, I. Superoxide anion radical (O2-·), superoxide dismutases, and related matters. J. Biol. Chem. 1997, 272, 18515-18517.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 77
    • 0039174315 scopus 로고    scopus 로고
    • Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation
    • Vasquez-Vivar, J.; Kalyanaraman, B.; Kennedy, M.C. Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation. J. Biol. Chem. 2000, 275, 14064-14069.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14064-14069
    • Vasquez-Vivar, J.1    Kalyanaraman, B.2    Kennedy, M.C.3
  • 79
    • 24344438196 scopus 로고    scopus 로고
    • Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression
    • Kietzmann, T.; Gorlach, A. Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression. Semin. Cell Dev. Biol. 2005, 16, 474-486.
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 474-486
    • Kietzmann, T.1    Gorlach, A.2
  • 80
    • 84866565340 scopus 로고    scopus 로고
    • Modulating mitochondrial intracellular location as a redox signal
    • doi:10.1126/scisignal.2003386
    • Murphy, M.P. Modulating mitochondrial intracellular location as a redox signal. Sci. Signal. 2012, 5, doi:10.1126/scisignal.2003386.
    • (2012) Sci. Signal. , vol.5
    • Murphy, M.P.1
  • 82
    • 77956713136 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 activation in nonhypoxic conditions: The essential role of mitochondrial-derived reactive oxygen species
    • Patten, D.A.; Lafleur, V.N.; Robitaille, G.A.; Chan, D.A.; Giaccia, A.J.; Richard, D.E. Hypoxia-inducible factor-1 activation in nonhypoxic conditions: The essential role of mitochondrial-derived reactive oxygen species. Mol. Biol. Cell 2010, 21, 3247-3257.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3247-3257
    • Patten, D.A.1    Lafleur, V.N.2    Robitaille, G.A.3    Chan, D.A.4    Giaccia, A.J.5    Richard, D.E.6
  • 83
    • 44449125132 scopus 로고    scopus 로고
    • Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy
    • Ushio-Fukai, M.; Nakamura, Y. Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy. Cancer Lett. 2008, 266, 37-52.
    • (2008) Cancer Lett. , vol.266 , pp. 37-52
    • Ushio-Fukai, M.1    Nakamura, Y.2
  • 84
    • 84870941135 scopus 로고    scopus 로고
    • Hypoxia-regulated target genes implicated in tumor metastasis
    • doi:10.1186/1423-0127-19-102
    • Tsai, Y.P.; Wu, K.J. Hypoxia-regulated target genes implicated in tumor metastasis. J. Biomed. Sci. 2012, 19, doi:10.1186/1423-0127-19-102.
    • (2012) J. Biomed. Sci. , vol.19
    • Tsai, Y.P.1    Wu, K.J.2
  • 85
    • 33745201378 scopus 로고    scopus 로고
    • The good, the bad and the ugly in oxygen-sensing: ROS, cytochromes and prolyl-hydroxylases
    • Acker, T.; Fandrey, J.; Acker, H. The good, the bad and the ugly in oxygen-sensing: ROS, cytochromes and prolyl-hydroxylases. Cardiovasc. Res. 2006, 71, 195-207.
    • (2006) Cardiovasc. Res. , vol.71 , pp. 195-207
    • Acker, T.1    Fandrey, J.2    Acker, H.3
  • 88
    • 84866133072 scopus 로고    scopus 로고
    • Reactive oxygen species in health and disease
    • doi:10.1155/2012/936486
    • Alfadda, A.A.; Sallam, R.M. Reactive oxygen species in health and disease. J. Biomed. Biotechnol. 2012, 2012, doi:10.1155/2012/936486.
    • (2012) J. Biomed. Biotechnol. , vol.2012
    • Alfadda, A.A.1    Sallam, R.M.2
  • 89
    • 84865434841 scopus 로고    scopus 로고
    • Mitochondrial proticity and ROS signaling: Lessons from the uncoupling proteins
    • Mailloux, R.J.; Harper, M.E. Mitochondrial proticity and ROS signaling: Lessons from the uncoupling proteins. Trends Endocrinol. Metab. 2012, 23, 451-458.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 451-458
    • Mailloux, R.J.1    Harper, M.E.2
  • 90
    • 84859886931 scopus 로고    scopus 로고
    • Mitochondria and reactive oxygen species. Which role in physiology and pathology?
    • Lenaz, G. Mitochondria and reactive oxygen species. Which role in physiology and pathology? Adv. Exp. Med. Biol. 2012, 942, 93-136.
    • (2012) Adv. Exp. Med. Biol. , vol.942 , pp. 93-136
    • Lenaz, G.1
  • 91
    • 79953183067 scopus 로고    scopus 로고
    • Vitamins D, C, and E in the prevention of type 2 diabetes mellitus: Modulation of inflammation and oxidative stress
    • Garcia-Bailo, B.; El-Sohemy, A.; Haddad, P.S.; Arora, P.; Benzaied, F.; Karmali, M.; Badawi, A. Vitamins D, C, and E in the prevention of type 2 diabetes mellitus: Modulation of inflammation and oxidative stress. Biologics 2011, 5, 7-19.
    • (2011) Biologics , vol.5 , pp. 7-19
    • Garcia-Bailo, B.1    El-Sohemy, A.2    Haddad, P.S.3    Arora, P.4    Benzaied, F.5    Karmali, M.6    Badawi, A.7
  • 92
    • 84865968346 scopus 로고    scopus 로고
    • Inflammasome activation of IL-1 family mediators in response to cutaneous photodamage
    • Nasti, T.H.; Timares, L. Inflammasome activation of IL-1 family mediators in response to cutaneous photodamage. Photochem. Photobiol. 2012, 88, 1111-1125.
    • (2012) Photochem. Photobiol. , vol.88 , pp. 1111-1125
    • Nasti, T.H.1    Timares, L.2
  • 93
    • 77549086995 scopus 로고    scopus 로고
    • The UV response of the skin: A review of the MAPK, NFkappaB and TNFalpha signal transduction pathways
    • Muthusamy, V.; Piva, T.J. The UV response of the skin: A review of the MAPK, NFkappaB and TNFalpha signal transduction pathways. Arch. Dermatol. Res. 2010, 302, 5-17.
    • (2010) Arch. Dermatol. Res. , vol.302 , pp. 5-17
    • Muthusamy, V.1    Piva, T.J.2
  • 94
    • 84874772328 scopus 로고    scopus 로고
    • Sun exposure behavior and protection: Recommendations for travelers
    • Diaz, J.H.; Nesbitt, L.T., Jr. Sun exposure behavior and protection: Recommendations for travelers. J. Travel Med. 2013, 20, 108-118.
    • (2013) J. Travel Med. , vol.20 , pp. 108-118
    • Diaz, J.H.1    Nesbitt Jr., L.T.2
  • 95
    • 84255160826 scopus 로고    scopus 로고
    • Iron, oxidative stress and the example of solar ultraviolet A radiation
    • Aroun, A.; Zhong, J.L.; Tyrrell, R.M.; Pourzand, C. Iron, oxidative stress and the example of solar ultraviolet A radiation. Photochem. Photobiol. Sci. 2012, 11, 118-134.
    • (2012) Photochem. Photobiol. Sci. , vol.11 , pp. 118-134
    • Aroun, A.1    Zhong, J.L.2    Tyrrell, R.M.3    Pourzand, C.4
  • 96
    • 79957851398 scopus 로고    scopus 로고
    • Molecular mechanisms of ultraviolet radiation-induced DNA damage and repair
    • doi:10.4061/2010/592980
    • Rastogi, R.P.; Richa; Kumar, A.; Tyagi, M.B.; Sinha, R.P. Molecular mechanisms of ultraviolet radiation-induced DNA damage and repair. J. Nucleic Acids 2010, 2010, doi:10.4061/2010/592980.
    • (2010) J. Nucleic Acids , vol.2010
    • Rastogi, R.P.1    Richa Kumar, A.2    Tyagi, M.B.3    Sinha, R.P.4
  • 97
    • 32444433202 scopus 로고    scopus 로고
    • Free radicals, metals and antioxidants in oxidative stress-induced cancer
    • Valko, M.; Rhodes, C.J.; Moncol, J.; Izakovic, M.; Mazur, M. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem. Biol. Interact. 2006, 160, 1-40.
    • (2006) Chem. Biol. Interact. , vol.160 , pp. 1-40
    • Valko, M.1    Rhodes, C.J.2    Moncol, J.3    Izakovic, M.4    Mazur, M.5
  • 100
    • 0035182390 scopus 로고    scopus 로고
    • Ultraviolet light induced injury: Immunological and inflammatory effects
    • Clydesdale, G.J.; Dandie, G.W.; Muller, H.K. Ultraviolet light induced injury: Immunological and inflammatory effects. Immunol. Cell Biol. 2001, 79, 547-568.
    • (2001) Immunol. Cell Biol. , vol.79 , pp. 547-568
    • Clydesdale, G.J.1    Dandie, G.W.2    Muller, H.K.3
  • 101
    • 33751112220 scopus 로고    scopus 로고
    • Oxidative stress in the pathogenesis of skin disease
    • Bickers, D.R.; Athar, M. Oxidative stress in the pathogenesis of skin disease. J. Investig. Dermatol. 2006, 126, 2565-2575.
    • (2006) J. Investig. Dermatol. , vol.126 , pp. 2565-2575
    • Bickers, D.R.1    Athar, M.2
  • 102
    • 0028980212 scopus 로고
    • Activation of NF-kappa B in human skin fibroblasts by the oxidative stress generated by UVA radiation
    • Vile, G.F.; Tanew-Ilitschew, A.; Tyrrell, R.M. Activation of NF-kappa B in human skin fibroblasts by the oxidative stress generated by UVA radiation. Photochem. Photobiol. 1995, 62, 463-468.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 463-468
    • Vile, G.F.1    Tanew-Ilitschew, A.2    Tyrrell, R.M.3
  • 103
    • 0028967768 scopus 로고
    • UVA radiation-induced oxidative damage to lipids and proteins in vitro and in human skin fibroblasts is dependent on iron and singlet oxygen
    • Vile, G.F.; Tyrrell, R.M. UVA radiation-induced oxidative damage to lipids and proteins in vitro and in human skin fibroblasts is dependent on iron and singlet oxygen. Free Radic. Biol. Med. 1995, 18, 721-730.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 721-730
    • Vile, G.F.1    Tyrrell, R.M.2
  • 106
    • 0031811520 scopus 로고    scopus 로고
    • Singlet molecular oxygen (1)O2): A possible effector of eukaryotic gene expression
    • Ryter, S.W.; Tyrrell, R.M. Singlet molecular oxygen (1)O2): A possible effector of eukaryotic gene expression. Free Radic. Biol. Med. 1998, 24, 1520-1534.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 1520-1534
    • Ryter, S.W.1    Tyrrell, R.M.2
  • 107
    • 0031963543 scopus 로고    scopus 로고
    • UV-irradiation depletes antioxidants and causes oxidative damage in a model of human skin
    • Podda, M.; Traber, M.G.; Weber, C.; Yan, L.J.; Packer, L. UV-irradiation depletes antioxidants and causes oxidative damage in a model of human skin. Free Radic. Biol. Med. 1998, 24, 55-65.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 55-65
    • Podda, M.1    Traber, M.G.2    Weber, C.3    Yan, L.J.4    Packer, L.5
  • 108
    • 84873447588 scopus 로고    scopus 로고
    • Psoriasis and the risk of diabetes mellitus: A systematic review and meta-analysis
    • Armstrong, A.W.; Harskamp, C.T.; Armstrong, E.J. Psoriasis and the risk of diabetes mellitus: A systematic review and meta-analysis. JAMA Dermatol. 2013, 149, 84-91.
    • (2013) JAMA Dermatol. , vol.149 , pp. 84-91
    • Armstrong, A.W.1    Harskamp, C.T.2    Armstrong, E.J.3
  • 109
    • 84865253902 scopus 로고    scopus 로고
    • Increased risk of diabetes mellitus and likelihood of receiving diabetes mellitus treatment in patients with psoriasis
    • Azfar, R.S.; Seminara, N.M.; Shin, D.B.; Troxel, A.B.; Margolis, D.J.; Gelfand, J.M. Increased risk of diabetes mellitus and likelihood of receiving diabetes mellitus treatment in patients with psoriasis. Arch. Dermatol. 2012, 148, 995-1000.
    • (2012) Arch. Dermatol. , vol.148 , pp. 995-1000
    • Azfar, R.S.1    Seminara, N.M.2    Shin, D.B.3    Troxel, A.B.4    Margolis, D.J.5    Gelfand, J.M.6
  • 110
    • 84857901017 scopus 로고    scopus 로고
    • Psoriasis increased the risk of diabetes: A meta-analysis
    • Cheng, J.; Kuai, D.; Zhang, L.; Yang, X.; Qiu, B. Psoriasis increased the risk of diabetes: A meta-analysis. Arch. Dermatol. Res. 2012, 304, 119-125.
    • (2012) Arch. Dermatol. Res. , vol.304 , pp. 119-125
    • Cheng, J.1    Kuai, D.2    Zhang, L.3    Yang, X.4    Qiu, B.5
  • 112
    • 84872593263 scopus 로고    scopus 로고
    • Psoriasis epidemiology: The interplay of genes and the environment
    • Enamandram, M.; Kimball, A.B. Psoriasis epidemiology: The interplay of genes and the environment. J. Investig. Dermatol. 2013, 133, 287-289.
    • (2013) J. Investig. Dermatol. , vol.133 , pp. 287-289
    • Enamandram, M.1    Kimball, A.B.2
  • 114
    • 33847279025 scopus 로고    scopus 로고
    • Pathogenesis and therapy of psoriasis
    • Lowes, M.A.; Bowcock, A.M.; Krueger, J.G. Pathogenesis and therapy of psoriasis. Nature 2007, 445, 866-873.
    • (2007) Nature , vol.445 , pp. 866-873
    • Lowes, M.A.1    Bowcock, A.M.2    Krueger, J.G.3
  • 116
    • 0242624562 scopus 로고    scopus 로고
    • Antioxidant activity, lipid peroxidation and skin diseases. What's new
    • Briganti, S.; Picardo, M. Antioxidant activity, lipid peroxidation and skin diseases. What's new. J. Eur. Acad. Dermatol. Venereol. 2003, 17, 663-669.
    • (2003) J. Eur. Acad. Dermatol. Venereol. , vol.17 , pp. 663-669
    • Briganti, S.1    Picardo, M.2
  • 117
    • 84860000460 scopus 로고    scopus 로고
    • Molecular pathophysiology of psoriasis and molecular targets of antipsoriatic therapy
    • Racz, E.; Prens, E.P. Molecular pathophysiology of psoriasis and molecular targets of antipsoriatic therapy. Expert Rev. Mol. Med. 2009, 11, e38.
    • (2009) Expert Rev. Mol. Med. , vol.11
    • Racz, E.1    Prens, E.P.2
  • 119
    • 33846694581 scopus 로고    scopus 로고
    • Accumulation of oxidized low-density lipoprotein in psoriatic skin and changes of plasma lipid levels in psoriatic patients
    • Tekin, N.S.; Tekin, I.O.; Barut, F.; Sipahi, E.Y. Accumulation of oxidized low-density lipoprotein in psoriatic skin and changes of plasma lipid levels in psoriatic patients. Mediators Inflamm. 2007, 2007, 78454.
    • (2007) Mediators Inflamm. , vol.2007 , pp. 78454
    • Tekin, N.S.1    Tekin, I.O.2    Barut, F.3    Sipahi, E.Y.4
  • 121
    • 0345425787 scopus 로고    scopus 로고
    • Antioxidants and lipid peroxidation status in the blood of patients with psoriasis
    • Kokcam, I.; Naziroglu, M. Antioxidants and lipid peroxidation status in the blood of patients with psoriasis. Clin. Chim. Acta 1999, 289, 23-31.
    • (1999) Clin. Chim. Acta , vol.289 , pp. 23-31
    • Kokcam, I.1    Naziroglu, M.2
  • 125
    • 0030903157 scopus 로고    scopus 로고
    • The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene
    • Frank, S.; Munz, B.; Werner, S. The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. Oncogene 1997, 14, 915-921.
    • (1997) Oncogene , vol.14 , pp. 915-921
    • Frank, S.1    Munz, B.2    Werner, S.3
  • 126
    • 80053103198 scopus 로고    scopus 로고
    • Proteomic analysis of psoriatic skin tissue for identification of differentially expressed proteins: Up-regulation of GSTP1, SFN and PRDX2 in psoriatic skin
    • Ryu, J.; Park, S.G.; Park, B.C.; Choe, M.; Lee, K.S.; Cho, J.W. Proteomic analysis of psoriatic skin tissue for identification of differentially expressed proteins: Up-regulation of GSTP1, SFN and PRDX2 in psoriatic skin. Int. J. Mol. Med. 2011, 28, 785-792.
    • (2011) Int. J. Mol. Med. , vol.28 , pp. 785-792
    • Ryu, J.1    Park, S.G.2    Park, B.C.3    Choe, M.4    Lee, K.S.5    Cho, J.W.6
  • 127
  • 128
    • 0036876857 scopus 로고    scopus 로고
    • Extracellular regulated kinase and c-Jun N-terminal kinase are activated in psoriatic involved epidermis
    • Takahashi, H.; Ibe, M.; Nakamura, S.; Ishida-Yamamoto, A.; Hashimoto, Y.; Iizuka, H. Extracellular regulated kinase and c-Jun N-terminal kinase are activated in psoriatic involved epidermis. J. Dermatol. Sci. 2002, 30, 94-99.
    • (2002) J. Dermatol. Sci. , vol.30 , pp. 94-99
    • Takahashi, H.1    Ibe, M.2    Nakamura, S.3    Ishida-Yamamoto, A.4    Hashimoto, Y.5    Iizuka, H.6
  • 129
    • 20544461306 scopus 로고    scopus 로고
    • Inverse regulation of the nuclear factor-kappaB binding to the p53 and interleukin-8 kappaB response elements in lesional psoriatic skin
    • Johansen, C.; Flindt, E.; Kragballe, K.; Henningsen, J.; Westergaard, M.; Kristiansen, K.; Iversen, L. Inverse regulation of the nuclear factor-kappaB binding to the p53 and interleukin-8 kappaB response elements in lesional psoriatic skin. J. Investig. Dermatol. 2005, 124, 1284-1292.
    • (2005) J. Investig. Dermatol. , vol.124 , pp. 1284-1292
    • Johansen, C.1    Flindt, E.2    Kragballe, K.3    Henningsen, J.4    Westergaard, M.5    Kristiansen, K.6    Iversen, L.7
  • 130
    • 36148934536 scopus 로고    scopus 로고
    • Expression and localization of the activated mitogen-activated protein kinase in lesional psoriatic skin
    • Yu, X.J.; Li, C.Y.; Dai, H.Y.; Cai, D.X.; Wang, K.Y.; Xu, Y.H.; Chen, L.M.; Zhou, C.L. Expression and localization of the activated mitogen-activated protein kinase in lesional psoriatic skin. Exp. Mol. Pathol. 2007, 83, 413-418.
    • (2007) Exp. Mol. Pathol. , vol.83 , pp. 413-418
    • Yu, X.J.1    Li, C.Y.2    Dai, H.Y.3    Cai, D.X.4    Wang, K.Y.5    Xu, Y.H.6    Chen, L.M.7    Zhou, C.L.8
  • 131
    • 42049085112 scopus 로고    scopus 로고
    • Evaluation of survivin and NF-kappaB in psoriasis, an immunohistochemical study
    • Abdou, A.G.; Hanout, H.M. Evaluation of survivin and NF-kappaB in psoriasis, an immunohistochemical study. J. Cutan. Pathol. 2008, 35, 445-451.
    • (2008) J. Cutan. Pathol. , vol.35 , pp. 445-451
    • Abdou, A.G.1    Hanout, H.M.2
  • 132
    • 20544451475 scopus 로고    scopus 로고
    • Differential expression of phosphorylated NF-kappaB/RelA in normal and psoriatic epidermis and downregulation of NF-kappaB in response to treatment with etanercept
    • Lizzul, P.F.; Aphale, A.; Malaviya, R.; Sun, Y.; Masud, S.; Dombrovskiy, V.; Gottlieb, A.B. Differential expression of phosphorylated NF-kappaB/RelA in normal and psoriatic epidermis and downregulation of NF-kappaB in response to treatment with etanercept. J. Investig. Dermatol. 2005, 124, 1275-1283.
    • (2005) J. Investig. Dermatol. , vol.124 , pp. 1275-1283
    • Lizzul, P.F.1    Aphale, A.2    Malaviya, R.3    Sun, Y.4    Masud, S.5    Dombrovskiy, V.6    Gottlieb, A.B.7
  • 133
    • 77955906264 scopus 로고    scopus 로고
    • The nuclear factor NF-kappaB pathway in inflammation
    • doi:10.1101/cshperspect.a001651
    • Lawrence, T. The nuclear factor NF-kappaB pathway in inflammation. Cold Spring Harb. Perspect. Biol. 2009, 1, doi:10.1101/cshperspect.a001651.
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1
    • Lawrence, T.1
  • 134
    • 0345732760 scopus 로고    scopus 로고
    • Dimethylfumarate is a potent inducer of apoptosis in human T cells
    • Treumer, F.; Zhu, K.; Glaser, R.; Mrowietz, U. Dimethylfumarate is a potent inducer of apoptosis in human T cells. J. Investig. Dermatol. 2003, 121, 1383-1388.
    • (2003) J. Investig. Dermatol. , vol.121 , pp. 1383-1388
    • Treumer, F.1    Zhu, K.2    Glaser, R.3    Mrowietz, U.4
  • 135
    • 34848831226 scopus 로고    scopus 로고
    • Antipsoriatic effects of avarol-3'-thiosalicylate are mediated by inhibition of TNF-alpha generation and NF-kappaB activation in mouse skin
    • Amigo, M.; Paya, M.; De Rosa, S.; Terencio, M.C. Antipsoriatic effects of avarol-3'-thiosalicylate are mediated by inhibition of TNF-alpha generation and NF-kappaB activation in mouse skin. Br. J. Pharmacol. 2007, 152, 353-365.
    • (2007) Br. J. Pharmacol. , vol.152 , pp. 353-365
    • Amigo, M.1    Paya, M.2    de Rosa, S.3    Terencio, M.C.4
  • 136
    • 33751088274 scopus 로고    scopus 로고
    • Identification of avarol derivatives as potential antipsoriatic drugs using an in vitro model for keratinocyte growth and differentiation
    • Amigo, M.; Schalkwijk, J.; Olthuis, D.; De Rosa, S.; Paya, M.; Terencio, M.C.; Lamme, E. Identification of avarol derivatives as potential antipsoriatic drugs using an in vitro model for keratinocyte growth and differentiation. Life Sci. 2006, 79, 2395-2404.
    • (2006) Life Sci. , vol.79 , pp. 2395-2404
    • Amigo, M.1    Schalkwijk, J.2    Olthuis, D.3    de Rosa, S.4    Paya, M.5    Terencio, M.C.6    Lamme, E.7
  • 137
    • 0031691282 scopus 로고    scopus 로고
    • Interleukin-17 and interferon-gamma synergize in the enhancement of proinflammatory cytokine production by human keratinocytes
    • Teunissen, M.B.; Koomen, C.W.; de Waal Malefyt, R.; Wierenga, E.A.; Bos, J.D. Interleukin-17 and interferon-gamma synergize in the enhancement of proinflammatory cytokine production by human keratinocytes. J. Investig. Dermatol. 1998, 111, 645-649.
    • (1998) J. Investig. Dermatol. , vol.111 , pp. 645-649
    • Teunissen, M.B.1    Koomen, C.W.2    de Waal Malefyt, R.3    Wierenga, E.A.4    Bos, J.D.5
  • 138
    • 84865766847 scopus 로고    scopus 로고
    • Impact of reactive oxygen species on keratinocyte signaling pathways
    • Bito, T.; Nishigori, C. Impact of reactive oxygen species on keratinocyte signaling pathways. J. Dermatol. Sci. 2012, 68, 3-8.
    • (2012) J. Dermatol. Sci. , vol.68 , pp. 3-8
    • Bito, T.1    Nishigori, C.2
  • 140
    • 0035371110 scopus 로고    scopus 로고
    • The involvement of free radicals in burn injury: A review
    • Latha, B.; Babu, M. The involvement of free radicals in burn injury: A review. Burns 2001, 27, 309-317.
    • (2001) Burns , vol.27 , pp. 309-317
    • Latha, B.1    Babu, M.2
  • 141
    • 0022549722 scopus 로고
    • The human burn wound as a primary source of interleukin-1 activity
    • Kupper, T.S.; Deitch, E.A.; Baker, C.C.; Wong, W.C. The human burn wound as a primary source of interleukin-1 activity. Surgery 1986, 100, 409-415.
    • (1986) Surgery , vol.100 , pp. 409-415
    • Kupper, T.S.1    Deitch, E.A.2    Baker, C.C.3    Wong, W.C.4
  • 142
    • 0025673833 scopus 로고
    • Pathophysiologic events related to thermal injury of skin
    • Ward, P.A.; Till, G.O. Pathophysiologic events related to thermal injury of skin. J. Trauma 1990, 30, S75-S79.
    • (1990) J. Trauma , vol.30
    • Ward, P.A.1    Till, G.O.2
  • 144
    • 0021833156 scopus 로고
    • Lipid peroxidation and acute lung injury after thermal trauma to skin. Evidence of a role for hydroxyl radical
    • Till, G.O.; Hatherill, J.R.; Tourtellotte, W.W.; Lutz, M.J.; Ward, P.A. Lipid peroxidation and acute lung injury after thermal trauma to skin. Evidence of a role for hydroxyl radical. Am. J. Pathol. 1985, 119, 376-384.
    • (1985) Am. J. Pathol. , vol.119 , pp. 376-384
    • Till, G.O.1    Hatherill, J.R.2    Tourtellotte, W.W.3    Lutz, M.J.4    Ward, P.A.5
  • 145
    • 17044440807 scopus 로고    scopus 로고
    • Oxidative organ damage in a rat model of thermal injury: The effect of cyclosporin A
    • Gurbuz, V.; Corak, A.; Yegen, B.C.; Kurtel, H.; Alican, I. Oxidative organ damage in a rat model of thermal injury: The effect of cyclosporin A. Burns 1997, 23, 37-42.
    • (1997) Burns , vol.23 , pp. 37-42
    • Gurbuz, V.1    Corak, A.2    Yegen, B.C.3    Kurtel, H.4    Alican, I.5
  • 146
    • 3543062692 scopus 로고    scopus 로고
    • The healing-promoting effect of saliva on skin burn is mediated by epidermal growth factor (EGF): Role of the neutrophils
    • Jahovic, N.; Guzel, E.; Arbak, S.; Yegen, B.C. The healing-promoting effect of saliva on skin burn is mediated by epidermal growth factor (EGF): Role of the neutrophils. Burns 2004, 30, 531-538.
    • (2004) Burns , vol.30 , pp. 531-538
    • Jahovic, N.1    Guzel, E.2    Arbak, S.3    Yegen, B.C.4
  • 147
    • 0345040749 scopus 로고    scopus 로고
    • Modulating the functions of neutrophils and lipid peroxidation by FK506 in a rat model of thermal injury
    • Cetinkale, O.; Konukoglu, D.; Senel, O.; Kemerli, G.D.; Yazar, S. Modulating the functions of neutrophils and lipid peroxidation by FK506 in a rat model of thermal injury. Burns 1999, 25, 105-112.
    • (1999) Burns , vol.25 , pp. 105-112
    • Cetinkale, O.1    Konukoglu, D.2    Senel, O.3    Kemerli, G.D.4    Yazar, S.5
  • 148
    • 0031417977 scopus 로고    scopus 로고
    • Oxidative damage to protein and alterations to antioxidant levels in human cutaneous thermal injury
    • Haycock, J.W.; Ralston, D.R.; Morris, B.; Freedlander, E.; MacNeil, S. Oxidative damage to protein and alterations to antioxidant levels in human cutaneous thermal injury. Burns 1997, 23, 533-540.
    • (1997) Burns , vol.23 , pp. 533-540
    • Haycock, J.W.1    Ralston, D.R.2    Morris, B.3    Freedlander, E.4    McNeil, S.5
  • 149
    • 0026506983 scopus 로고
    • The metabolic effects of thermal injury
    • Tredget, E.E.; Yu, Y.M. The metabolic effects of thermal injury. World J. Surg. 1992, 16, 68-79.
    • (1992) World J. Surg. , vol.16 , pp. 68-79
    • Tredget, E.E.1    Yu, Y.M.2
  • 151
    • 0038073062 scopus 로고    scopus 로고
    • Free radicals and lipid peroxidation mediated injury in burn trauma: The role of antioxidant therapy
    • Horton, J.W. Free radicals and lipid peroxidation mediated injury in burn trauma: The role of antioxidant therapy. Toxicology 2003, 189, 75-88.
    • (2003) Toxicology , vol.189 , pp. 75-88
    • Horton, J.W.1
  • 152
    • 0028937859 scopus 로고
    • Increased lipid peroxidation and decreased antioxidant activity correspond with death after smoke exposure in the rat
    • Demling, R.; Ikegami, K.; Lalonde, C. Increased lipid peroxidation and decreased antioxidant activity correspond with death after smoke exposure in the rat. J. Burn Care Rehabil. 1995, 16, 104-110.
    • (1995) J. Burn Care Rehabil. , vol.16 , pp. 104-110
    • Demling, R.1    Ikegami, K.2    Lalonde, C.3
  • 153
    • 1042301039 scopus 로고    scopus 로고
    • The effect of CAPE on lipid peroxidation and nitric oxide levels in the plasma of rats following thermal injury
    • Hosnuter, M.; Gurel, A.; Babuccu, O.; Armutcu, F.; Kargi, E.; Isikdemir, A. The effect of CAPE on lipid peroxidation and nitric oxide levels in the plasma of rats following thermal injury. Burns 2004, 30, 121-125.
    • (2004) Burns , vol.30 , pp. 121-125
    • Hosnuter, M.1    Gurel, A.2    Babuccu, O.3    Armutcu, F.4    Kargi, E.5    Isikdemir, A.6
  • 154
    • 0021361768 scopus 로고
    • Superoxide radical involvement in the pathogenesis of burn shock
    • Saez, J.C.; Ward, P.H.; Gunther, B.; Vivaldi, E. Superoxide radical involvement in the pathogenesis of burn shock. Circ. Shock 1984, 12, 229-239.
    • (1984) Circ. Shock , vol.12 , pp. 229-239
    • Saez, J.C.1    Ward, P.H.2    Gunther, B.3    Vivaldi, E.4
  • 155
    • 0023690735 scopus 로고
    • Activation of complement by hydroxyl radical in thermal injury
    • Oldham, K.T.; Guice, K.S.; Till, G.O.; Ward, P.A. Activation of complement by hydroxyl radical in thermal injury. Surgery 1988, 104, 272-279.
    • (1988) Surgery , vol.104 , pp. 272-279
    • Oldham, K.T.1    Guice, K.S.2    Till, G.O.3    Ward, P.A.4
  • 156
    • 0036024028 scopus 로고    scopus 로고
    • Melatonin improves oxidative organ damage in a rat model of thermal injury
    • Sener, G.; Sehirli, A.O.; Satiroglu, H.; Keyer-Uysal, M.; Yegen, B.C. Melatonin improves oxidative organ damage in a rat model of thermal injury. Burns 2002, 28, 419-425.
    • (2002) Burns , vol.28 , pp. 419-425
    • Sener, G.1    Sehirli, A.O.2    Satiroglu, H.3    Keyer-Uysal, M.4    Yegen, B.C.5
  • 159
    • 0030997845 scopus 로고    scopus 로고
    • Evaluation of lipid peroxidation and total antioxidant status in plasma of rats following thermal injury
    • Cetinkale, O.; Belce, A.; Konukoglu, D.; Senyuva, C.; Gumustas, M.K.; Tas, T. Evaluation of lipid peroxidation and total antioxidant status in plasma of rats following thermal injury. Burns 1997, 23, 114-116.
    • (1997) Burns , vol.23 , pp. 114-116
    • Cetinkale, O.1    Belce, A.2    Konukoglu, D.3    Senyuva, C.4    Gumustas, M.K.5    Tas, T.6
  • 160
    • 0033558780 scopus 로고    scopus 로고
    • Different types of ROS-scavenging enzymes are expressed during cutaneous wound repair
    • Steiling, H.; Munz, B.; Werner, S.; Brauchle, M. Different types of ROS-scavenging enzymes are expressed during cutaneous wound repair. Exp. Cell Res. 1999, 247, 484-494.
    • (1999) Exp. Cell Res. , vol.247 , pp. 484-494
    • Steiling, H.1    Munz, B.2    Werner, S.3    Brauchle, M.4
  • 161
    • 84868007565 scopus 로고    scopus 로고
    • Physiological roles of mitochondrial reactive oxygen species
    • Sena, L.A.; Chandel, N.S. Physiological roles of mitochondrial reactive oxygen species. Mol. Cell 2012, 48, 158-167.
    • (2012) Mol. Cell , vol.48 , pp. 158-167
    • Sena, L.A.1    Chandel, N.S.2
  • 162
    • 80051935440 scopus 로고    scopus 로고
    • Xanthine oxidoreductase: A journey from purine metabolism to cardiovascular excitation-contraction coupling
    • Agarwal, A.; Banerjee, A.; Banerjee, U.C. Xanthine oxidoreductase: A journey from purine metabolism to cardiovascular excitation-contraction coupling. Crit. Rev. Biotechnol. 2011, 31, 264-280.
    • (2011) Crit. Rev. Biotechnol. , vol.31 , pp. 264-280
    • Agarwal, A.1    Banerjee, A.2    Banerjee, U.C.3
  • 163
    • 0037195783 scopus 로고    scopus 로고
    • Myeloperoxidase functions as a major enzymatic catalyst for initiation of lipid peroxidation at sites of inflammation
    • Zhang, R.; Brennan, M.L.; Shen, Z.; MacPherson, J.C.; Schmitt, D.; Molenda, C.E.; Hazen, S.L. Myeloperoxidase functions as a major enzymatic catalyst for initiation of lipid peroxidation at sites of inflammation. J. Biol. Chem. 2002, 277, 46116-46122.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46116-46122
    • Zhang, R.1    Brennan, M.L.2    Shen, Z.3    McPherson, J.C.4    Schmitt, D.5    Molenda, C.E.6    Hazen, S.L.7
  • 164
    • 0035910620 scopus 로고    scopus 로고
    • Endothelium-derived hyperpolarizing factor synthase (Cytochrome P450 2C9) is a functionally significant source of reactive oxygen species in coronary arteries
    • Fleming, I.; Michaelis, U.R.; Bredenkotter, D.; Fisslthaler, B.; Dehghani, F.; Brandes, R.P.; Busse, R. Endothelium-derived hyperpolarizing factor synthase (Cytochrome P450 2C9) is a functionally significant source of reactive oxygen species in coronary arteries. Circ. Res. 2001, 88, 44-51.
    • (2001) Circ. Res. , vol.88 , pp. 44-51
    • Fleming, I.1    Michaelis, U.R.2    Bredenkotter, D.3    Fisslthaler, B.4    Dehghani, F.5    Brandes, R.P.6    Busse, R.7
  • 165
    • 84859644104 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species in pulmonary hypertension
    • Tabima, D.M.; Frizzell, S.; Gladwin, M.T. Reactive oxygen and nitrogen species in pulmonary hypertension. Free Radic. Biol. Med. 2012, 52, 1970-1986.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1970-1986
    • Tabima, D.M.1    Frizzell, S.2    Gladwin, M.T.3
  • 166
    • 0033567065 scopus 로고    scopus 로고
    • Enzymatic function of nitric oxide synthases
    • Andrew, P.J.; Mayer, B. Enzymatic function of nitric oxide synthases. Cardiovasc. Res. 1999, 43, 521-531.
    • (1999) Cardiovasc. Res. , vol.43 , pp. 521-531
    • Andrew, P.J.1    Mayer, B.2
  • 167
    • 0032475865 scopus 로고    scopus 로고
    • Superoxide generation from endothelial nitric-oxide synthase. A Ca2+/calmodulin-dependent and tetrahydrobiopterin regulatory process
    • Xia, Y.; Tsai, A.L.; Berka, V.; Zweier, J.L. Superoxide generation from endothelial nitric-oxide synthase. A Ca2+/calmodulin-dependent and tetrahydrobiopterin regulatory process. J. Biol. Chem. 1998, 273, 25804-25808.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25804-25808
    • Xia, Y.1    Tsai, A.L.2    Berka, V.3    Zweier, J.L.4
  • 168
    • 84864800398 scopus 로고    scopus 로고
    • Nitric oxide synthase uncoupling: A therapeutic target in cardiovascular diseases
    • Roe, N.D.; Ren, J. Nitric oxide synthase uncoupling: A therapeutic target in cardiovascular diseases. Vasc. Pharmacol. 2012, 57, 168-172.
    • (2012) Vasc. Pharmacol. , vol.57 , pp. 168-172
    • Roe, N.D.1    Ren, J.2
  • 172
    • 79952026736 scopus 로고    scopus 로고
    • NADPH oxidase-mediated redox signaling: Roles in cellular stress response, stress tolerance, and tissue repair
    • Jiang, F.; Zhang, Y.; Dusting, G.J. NADPH oxidase-mediated redox signaling: Roles in cellular stress response, stress tolerance, and tissue repair. Pharmacol. Rev. 2011, 63, 218-242.
    • (2011) Pharmacol. Rev. , vol.63 , pp. 218-242
    • Jiang, F.1    Zhang, Y.2    Dusting, G.J.3
  • 173
    • 34250888056 scopus 로고    scopus 로고
    • Regulation of Nox and Duox enzymatic activity and expression
    • Lambeth, J.D.; Kawahara, T.; Diebold, B. Regulation of Nox and Duox enzymatic activity and expression. Free Radic. Biol. Med. 2007, 43, 319-331.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 319-331
    • Lambeth, J.D.1    Kawahara, T.2    Diebold, B.3
  • 174
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K.; Krause, K.H. The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology. Physiol. Rev. 2007, 87, 245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 176
    • 0037031875 scopus 로고    scopus 로고
    • Oxidant-induced vascular endothelial growth factor expression in human keratinocytes and cutaneous wound healing
    • Sen, C.K.; Khanna, S.; Babior, B.M.; Hunt, T.K.; Ellison, E.C.; Roy, S. Oxidant-induced vascular endothelial growth factor expression in human keratinocytes and cutaneous wound healing. J. Biol. Chem. 2002, 277, 33284-33290.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33284-33290
    • Sen, C.K.1    Khanna, S.2    Babior, B.M.3    Hunt, T.K.4    Ellison, E.C.5    Roy, S.6
  • 177
    • 0035461303 scopus 로고    scopus 로고
    • TGF-beta-induced p38 activation is mediated by Rac1-regulated generation of reactive oxygen species in cultured human keratinocytes
    • Chiu, C.; Maddock, D.A.; Zhang, Q.; Souza, K.P.; Townsend, A.R.; Wan, Y. TGF-beta-induced p38 activation is mediated by Rac1-regulated generation of reactive oxygen species in cultured human keratinocytes. Int. J. Mol. Med. 2001, 8, 251-255.
    • (2001) Int. J. Mol. Med. , vol.8 , pp. 251-255
    • Chiu, C.1    Maddock, D.A.2    Zhang, Q.3    Souza, K.P.4    Townsend, A.R.5    Wan, Y.6
  • 178
    • 0141730304 scopus 로고    scopus 로고
    • Association of gp91phox homolog Nox1 with anchorage-independent growth and MAP kinase-activation of transformed human keratinocytes
    • Chamulitrat, W.; Schmidt, R.; Tomakidi, P.; Stremmel, W.; Chunglok, W.; Kawahara, T.; Rokutan, K. Association of gp91phox homolog Nox1 with anchorage-independent growth and MAP kinase-activation of transformed human keratinocytes. Oncogene 2003, 22, 6045-6053.
    • (2003) Oncogene , vol.22 , pp. 6045-6053
    • Chamulitrat, W.1    Schmidt, R.2    Tomakidi, P.3    Stremmel, W.4    Chunglok, W.5    Kawahara, T.6    Rokutan, K.7
  • 179
    • 0027185676 scopus 로고
    • Extracellular production of singlet oxygen by stimulated macrophages quantified using 9,10-diphenylanthracene and perylene in a polystyrene film
    • Steinbeck, M.J.; Khan, A.U.; Karnovsky, M.J. Extracellular production of singlet oxygen by stimulated macrophages quantified using 9,10-diphenylanthracene and perylene in a polystyrene film. J. Biol. Chem. 1993, 268, 15649-15654.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15649-15654
    • Steinbeck, M.J.1    Khan, A.U.2    Karnovsky, M.J.3
  • 180
    • 33744493616 scopus 로고    scopus 로고
    • Heme as key regulator of major mammalian cellular functions: Molecular, cellular, and pharmacological aspects
    • Tsiftsoglou, A.S.; Tsamadou, A.I.; Papadopoulou, L.C. Heme as key regulator of major mammalian cellular functions: Molecular, cellular, and pharmacological aspects. Pharmacol. Ther. 2006, 111, 327-345.
    • (2006) Pharmacol. Ther. , vol.111 , pp. 327-345
    • Tsiftsoglou, A.S.1    Tsamadou, A.I.2    Papadopoulou, L.C.3
  • 182
    • 0033973712 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivity. Heme oxygenase has both pro-and antioxidant properties
    • Ryter, S.W.; Tyrrell, R.M. The heme synthesis and degradation pathways: Role in oxidant sensitivity. Heme oxygenase has both pro-and antioxidant properties. Free Radic. Biol. Med. 2000, 28, 289-309.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 289-309
    • Ryter, S.W.1    Tyrrell, R.M.2
  • 183
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B.; Gutteridge, J.M. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 1984, 219, 1-14.
    • (1984) Biochem. J. , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 184
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • Kumar, S.; Bandyopadhyay, U. Free heme toxicity and its detoxification systems in human. Toxicol. Lett. 2005, 157, 175-188.
    • (2005) Toxicol. Lett. , vol.157 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 185
    • 0036790992 scopus 로고    scopus 로고
    • Protein nitration is mediated by heme and free metals through Fenton-type chemistry: An alternative to the NO/O2-reaction
    • Thomas, D.D.; Espey, M.G.; Vitek, M.P.; Miranda, K.M.; Wink, D.A. Protein nitration is mediated by heme and free metals through Fenton-type chemistry: An alternative to the NO/O2-reaction. Proc. Natl. Acad. Sci. USA 2002, 99, 12691-12696.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12691-12696
    • Thomas, D.D.1    Espey, M.G.2    Vitek, M.P.3    Miranda, K.M.4    Wink, D.A.5
  • 187
    • 0026318447 scopus 로고
    • Hemin: A possible physiological mediator of low density lipoprotein oxidation and endothelial injury
    • Balla, G.; Jacob, H.S.; Eaton, J.W.; Belcher, J.D.; Vercellotti, G.M. Hemin: A possible physiological mediator of low density lipoprotein oxidation and endothelial injury. Arterioscler. Thromb. 1991, 11, 1700-1711.
    • (1991) Arterioscler. Thromb. , vol.11 , pp. 1700-1711
    • Balla, G.1    Jacob, H.S.2    Eaton, J.W.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 188
    • 0027358877 scopus 로고
    • Endothelial-cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidant damage
    • Balla, J.; Jacob, H.S.; Balla, G.; Nath, K.; Eaton, J.W.; Vercellotti, G.M. Endothelial-cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidant damage. Proc. Natl. Acad. Sci. USA 1993, 90, 9285-9289.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellotti, G.M.6
  • 189
    • 0035252322 scopus 로고    scopus 로고
    • Heme-induced cell adhesion in the pathogenesis of sickle-cell disease and inflammation
    • Wagener, F.A.; Abraham, N.G.; van, K.Y.; de, W.T.; Figdor, C.G. Heme-induced cell adhesion in the pathogenesis of sickle-cell disease and inflammation. Trends Pharmacol. Sci. 2001, 22, 52-54.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 52-54
    • Wagener, F.A.1    Abraham, N.G.2    Van, K.Y.3    De, W.T.4    Figdor, C.G.5
  • 190
    • 0032881831 scopus 로고    scopus 로고
    • Differential effects of heme oxygenase isoforms on heme mediation of endothelial intracellular adhesion molecule 1 expression
    • Wagener, F.A.; da Silva, J.L.; Farley, T.; de, W.T.; Kappas, A.; Abraham, N.G. Differential effects of heme oxygenase isoforms on heme mediation of endothelial intracellular adhesion molecule 1 expression. J. Pharmacol. Exp. Ther. 1999, 291, 416-423.
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , pp. 416-423
    • Wagener, F.A.1    da Silva, J.L.2    Farley, T.3    De, W.T.4    Kappas, A.5    Abraham, N.G.6
  • 191
    • 0030734872 scopus 로고    scopus 로고
    • Heme induces the expression of adhesion molecules ICAM-1, VCAM-1, and E selectin in vascular endothelial cells
    • Wagener, F.A.; Feldman, E.; de, W.T.; Abraham, N.G. Heme induces the expression of adhesion molecules ICAM-1, VCAM-1, and E selectin in vascular endothelial cells. Proc. Soc. Exp. Biol. Med. 1997, 216, 456-463.
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.216 , pp. 456-463
    • Wagener, F.A.1    Feldman, E.2    De, W.T.3    Abraham, N.G.4
  • 192
    • 0036893587 scopus 로고    scopus 로고
    • Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis
    • Tolosano, E.; Fagoonee, S.; Hirsch, E.; Berger, F.G.; Baumann, H.; Silengo, L.; Altruda, F. Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis. Blood 2002, 100, 4201-4208.
    • (2002) Blood , vol.100 , pp. 4201-4208
    • Tolosano, E.1    Fagoonee, S.2    Hirsch, E.3    Berger, F.G.4    Baumann, H.5    Silengo, L.6    Altruda, F.7
  • 193
    • 33947492363 scopus 로고    scopus 로고
    • Hemin modulates cytokine expressions in macrophage-derived foam cells via heme oxygenase-1 induction
    • Ma, J.L.; Yang, P.Y.; Rui, Y.C.; Lu, L.; Kang, H.; Zhang, J. Hemin modulates cytokine expressions in macrophage-derived foam cells via heme oxygenase-1 induction. J. Pharmacol. Sci. 2007, 103, 261-266.
    • (2007) J. Pharmacol. Sci. , vol.103 , pp. 261-266
    • Ma, J.L.1    Yang, P.Y.2    Rui, Y.C.3    Lu, L.4    Kang, H.5    Zhang, J.6
  • 194
    • 77953912361 scopus 로고    scopus 로고
    • The IL-12p70/IL-10 interplay is differentially regulated by free heme and hemozoin in murine bone-marrow-derived macrophages
    • Cambos, M.; Bazinet, S.; Abed, E.; Sanchez-Dardon, J.; Bernard, C.; Moreau, R.; Olivier, M.; Scorza, T. The IL-12p70/IL-10 interplay is differentially regulated by free heme and hemozoin in murine bone-marrow-derived macrophages. Int J. Parasitol. 2010, 40, 1003-1012.
    • (2010) Int J. Parasitol. , vol.40 , pp. 1003-1012
    • Cambos, M.1    Bazinet, S.2    Abed, E.3    Sanchez-Dardon, J.4    Bernard, C.5    Moreau, R.6    Olivier, M.7    Scorza, T.8
  • 195
    • 79251569904 scopus 로고    scopus 로고
    • Robust erythrophagocytosis leads to macrophage apoptosis via a hemin-mediated redox imbalance: Role in hemolytic disorders
    • Cambos, M.; Scorza, T. Robust erythrophagocytosis leads to macrophage apoptosis via a hemin-mediated redox imbalance: Role in hemolytic disorders. J. Leukoc. Biol. 2011, 89, 159-171.
    • (2011) J. Leukoc. Biol. , vol.89 , pp. 159-171
    • Cambos, M.1    Scorza, T.2
  • 197
    • 0026634285 scopus 로고
    • Regulation of antioxidant enzymes
    • Harris, E.D. Regulation of antioxidant enzymes. FASEB J. 1992, 6, 2675-2683.
    • (1992) FASEB J. , vol.6 , pp. 2675-2683
    • Harris, E.D.1
  • 198
    • 80051581331 scopus 로고    scopus 로고
    • The O(2) reduction and proton pumping gate mechanism of bovine heart cytochrome c oxidase
    • Yoshikawa, S.; Muramoto, K.; Shinzawa-Itoh, K. The O(2) reduction and proton pumping gate mechanism of bovine heart cytochrome c oxidase. Biochim. Biophys. Acta 2011, 1807, 1279-1286.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1279-1286
    • Yoshikawa, S.1    Muramoto, K.2    Shinzawa-Itoh, K.3
  • 199
    • 84863704376 scopus 로고    scopus 로고
    • Cellular transport and homeostasis of essential and nonessential metals
    • Martinez-Finley, E.J.; Chakraborty, S.; Fretham, S.J.; Aschner, M. Cellular transport and homeostasis of essential and nonessential metals. Metallomics 2012, 4, 593-605.
    • (2012) Metallomics , vol.4 , pp. 593-605
    • Martinez-Finley, E.J.1    Chakraborty, S.2    Fretham, S.J.3    Aschner, M.4
  • 200
    • 79954642381 scopus 로고    scopus 로고
    • Advances in metal-induced oxidative stress and human disease
    • Jomova, K.; Valko, M. Advances in metal-induced oxidative stress and human disease. Toxicology 2011, 283, 65-87.
    • (2011) Toxicology , vol.283 , pp. 65-87
    • Jomova, K.1    Valko, M.2
  • 201
  • 202
    • 0036378944 scopus 로고    scopus 로고
    • Antioxidants and the response of skin to oxidative stress: Vitamin E as a key indicator
    • Packer, L.; Valacchi, G. Antioxidants and the response of skin to oxidative stress: Vitamin E as a key indicator. Skin Pharmacol. Appl. Skin Physiol. 2002, 15, 282-290.
    • (2002) Skin Pharmacol. Appl. Skin Physiol. , vol.15 , pp. 282-290
    • Packer, L.1    Valacchi, G.2
  • 203
    • 0036667555 scopus 로고    scopus 로고
    • Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
    • Zelko, I.N.; Mariani, T.J.; Folz, R.J. Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 2002, 33, 337-349.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 337-349
    • Zelko, I.N.1    Mariani, T.J.2    Folz, R.J.3
  • 204
    • 46449130668 scopus 로고    scopus 로고
    • The peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system
    • Zamocky, M.; Jakopitsch, C.; Furtmuller, P.G.; Dunand, C.; Obinger, C. The peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system. Proteins 2008, 72, 589-605.
    • (2008) Proteins , vol.72 , pp. 589-605
    • Zamocky, M.1    Jakopitsch, C.2    Furtmuller, P.G.3    Dunand, C.4    Obinger, C.5
  • 205
    • 33750629812 scopus 로고    scopus 로고
    • Glutathione peroxidases and redox-regulated transcription factors
    • Brigelius-Flohe, R. Glutathione peroxidases and redox-regulated transcription factors. Biol. Chem. 2006, 387, 1329-1335.
    • (2006) Biol. Chem. , vol.387 , pp. 1329-1335
    • Brigelius-Flohe, R.1
  • 206
    • 0034489653 scopus 로고    scopus 로고
    • The glutathione peroxidases
    • Arthur, J.R. The glutathione peroxidases. Cell. Mol. Life Sci. 2000, 57, 1825-1835.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1825-1835
    • Arthur, J.R.1
  • 207
    • 14444271790 scopus 로고    scopus 로고
    • Mice with a homozygous null mutation for the most abundant glutathione peroxidase, Gpx1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide
    • De Haan, J.B.; Bladier, C.; Griffiths, P.; Kelner, M.; O'Shea, R.D.; Cheung, N.S.; Bronson, R.T.; Silvestro, M.J.; Wild, S.; Zheng, S.S.; et al. Mice with a homozygous null mutation for the most abundant glutathione peroxidase, Gpx1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J. Biol. Chem. 1998, 273, 22528-22536.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22528-22536
    • de Haan, J.B.1    Bladier, C.2    Griffiths, P.3    Kelner, M.4    O'Shea, R.D.5    Cheung, N.S.6    Bronson, R.T.7    Silvestro, M.J.8    Wild, S.9    Zheng, S.S.10
  • 209
    • 0037274133 scopus 로고    scopus 로고
    • An imbalance in antioxidant defense affects cellular function: The pathophysiological consequences of a reduction in antioxidant defense in the glutathione peroxidase-1 (Gpx1) knockout mouse
    • De Haan, J.B.; Crack, P.J.; Flentjar, N.; Iannello, R.C.; Hertzog, P.J.; Kola, I. An imbalance in antioxidant defense affects cellular function: The pathophysiological consequences of a reduction in antioxidant defense in the glutathione peroxidase-1 (Gpx1) knockout mouse. Redox Rep. 2003, 8, 69-79.
    • (2003) Redox Rep. , vol.8 , pp. 69-79
    • de Haan, J.B.1    Crack, P.J.2    Flentjar, N.3    Iannello, R.C.4    Hertzog, P.J.5    Kola, I.6
  • 210
    • 84876917760 scopus 로고    scopus 로고
    • Thioredoxins, glutaredoxins, and peroxiredoxins-molecular mechanisms and health significance: From cofactors to antioxidants to redox signaling
    • doi:10.1089/ars.2012.4599
    • Hanschmann, E.M.; Godoy, J.R.; Berndt, C.; Hudemann, C.; Lillig, C.H. Thioredoxins, glutaredoxins, and peroxiredoxins-molecular mechanisms and health significance: From cofactors to antioxidants to redox signaling. Antioxid. Redox Signal. 2013, doi:10.1089/ars.2012.4599.
    • (2013) Antioxid. Redox Signal.
    • Hanschmann, E.M.1    Godoy, J.R.2    Berndt, C.3    Hudemann, C.4    Lillig, C.H.5
  • 211
    • 0037015001 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage
    • Manevich, Y.; Sweitzer, T.; Pak, J.H.; Feinstein, S.I.; Muzykantov, V.; Fisher, A.B. 1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage. Proc. Natl. Acad. Sci. USA 2002, 99, 11599-11604.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11599-11604
    • Manevich, Y.1    Sweitzer, T.2    Pak, J.H.3    Feinstein, S.I.4    Muzykantov, V.5    Fisher, A.B.6
  • 212
    • 2442671688 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury
    • Wang, Y.; Manevich, Y.; Feinstein, S.I.; Fisher, A.B. Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury. Am. J. Physiol. Lung Cell. Mol. Physiol. 2004, 286, L1188-L1193.
    • (2004) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.286
    • Wang, Y.1    Manevich, Y.2    Feinstein, S.I.3    Fisher, A.B.4
  • 213
    • 33845911313 scopus 로고    scopus 로고
    • Peroxiredoxin 6 is a potent cytoprotective enzyme in the epidermis
    • Kumin, A.; Huber, C.; Rulicke, T.; Wolf, E.; Werner, S. Peroxiredoxin 6 is a potent cytoprotective enzyme in the epidermis. Am. J. Pathol. 2006, 169, 1194-1205.
    • (2006) Am. J. Pathol. , vol.169 , pp. 1194-1205
    • Kumin, A.1    Huber, C.2    Rulicke, T.3    Wolf, E.4    Werner, S.5
  • 214
    • 0037147158 scopus 로고    scopus 로고
    • An antisense oligonucleotide to 1-cys peroxiredoxin causes lipid peroxidation and apoptosis in lung epithelial cells
    • Pak, J.H.; Manevich, Y.; Kim, H.S.; Feinstein, S.I.; Fisher, A.B. An antisense oligonucleotide to 1-cys peroxiredoxin causes lipid peroxidation and apoptosis in lung epithelial cells. J. Biol. Chem. 2002, 277, 49927-49934.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49927-49934
    • Pak, J.H.1    Manevich, Y.2    Kim, H.S.3    Feinstein, S.I.4    Fisher, A.B.5
  • 215
    • 0344009504 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin knock-out mice express mRNA but not protein for a highly related intronless gene
    • Mo, Y.; Feinstein, S.I.; Manevich, Y.; Zhang, Q.; Lu, L.; Ho, Y.S.; Fisher, A.B. 1-Cys peroxiredoxin knock-out mice express mRNA but not protein for a highly related intronless gene. FEBS Lett. 2003, 555, 192-198.
    • (2003) FEBS Lett. , vol.555 , pp. 192-198
    • Mo, Y.1    Feinstein, S.I.2    Manevich, Y.3    Zhang, Q.4    Lu, L.5    Ho, Y.S.6    Fisher, A.B.7
  • 217
    • 37549068090 scopus 로고    scopus 로고
    • NAD+/NADH and NADP+/NADPH in cellular functions and cell death: Regulation and biological consequences
    • Ying, W. NAD+/NADH and NADP+/NADPH in cellular functions and cell death: Regulation and biological consequences. Antioxid. Redox Signal. 2008, 10, 179-206.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 179-206
    • Ying, W.1
  • 218
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • Wu, G.; Fang, Y.Z.; Yang, S.; Lupton, J.R.; Turner, N.D. Glutathione metabolism and its implications for health. J. Nutr. 2004, 134, 489-492.
    • (2004) J. Nutr. , vol.134 , pp. 489-492
    • Wu, G.1    Fang, Y.Z.2    Yang, S.3    Lupton, J.R.4    Turner, N.D.5
  • 219
    • 84859787172 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase, NADPH, and cell survival
    • Stanton, R.C. Glucose-6-phosphate dehydrogenase, NADPH, and cell survival. IUBMB Life 2012, 64, 362-369.
    • (2012) IUBMB Life , vol.64 , pp. 362-369
    • Stanton, R.C.1
  • 220
    • 0028176627 scopus 로고
    • Glucose-6-phosphate dehydrogenase: A "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress
    • Kletzien, R.F.; Harris, P.K.; Foellmi, L.A. Glucose-6-phosphate dehydrogenase: A "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress. FASEB J. 1994, 8, 174-181.
    • (1994) FASEB J. , vol.8 , pp. 174-181
    • Kletzien, R.F.1    Harris, P.K.2    Foellmi, L.A.3
  • 221
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi, P.P.; Sonati, F.; Rivi, R.; Mason, P.; Grosveld, F.; Luzzatto, L. Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 1995, 14, 5209-5215.
    • (1995) EMBO J. , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1    Sonati, F.2    Rivi, R.3    Mason, P.4    Grosveld, F.5    Luzzatto, L.6
  • 222
    • 0016632381 scopus 로고
    • Isolation of mammalian cell mutants deficient in glucose-6-phosphate dehydrogenase activity: Linkage to hypoxanthine phosphoribosyl transferase
    • Rosenstraus, M.; Chasin, L.A. Isolation of mammalian cell mutants deficient in glucose-6-phosphate dehydrogenase activity: Linkage to hypoxanthine phosphoribosyl transferase. Proc. Natl. Acad. Sci. USA 1975, 72, 493-497.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 493-497
    • Rosenstraus, M.1    Chasin, L.A.2
  • 223
    • 67650095384 scopus 로고    scopus 로고
    • Superoxide production by NAD(P)H oxidase and mitochondria is increased in genetically obese and hyperglycemic rat heart and aorta before the development of cardiac dysfunction. The role of glucose-6-phosphate dehydrogenase-derived NADPH
    • Serpillon, S.; Floyd, B.C.; Gupte, R.S.; George, S.; Kozicky, M.; Neito, V.; Recchia, F.; Stanley, W.; Wolin, M.S.; Gupte, S.A. Superoxide production by NAD(P)H oxidase and mitochondria is increased in genetically obese and hyperglycemic rat heart and aorta before the development of cardiac dysfunction. The role of glucose-6-phosphate dehydrogenase-derived NADPH. Am. J. Physiol. Heart. Circ. Physiol. 2009, 297, H153-H162.
    • (2009) Am. J. Physiol. Heart. Circ. Physiol. , vol.297
    • Serpillon, S.1    Floyd, B.C.2    Gupte, R.S.3    George, S.4    Kozicky, M.5    Neito, V.6    Recchia, F.7    Stanley, W.8    Wolin, M.S.9    Gupte, S.A.10
  • 224
    • 84857501489 scopus 로고    scopus 로고
    • Role of haeme oxygenase-1 in resolution of oxidative stress-related pathologies: Focus on cardiovascular, lung, neurological and kidney disorders
    • Haines, D.D.; Lekli, I.; Teissier, P.; Bak, I.; Tosaki, A. Role of haeme oxygenase-1 in resolution of oxidative stress-related pathologies: Focus on cardiovascular, lung, neurological and kidney disorders. Acta Physiol. 2012, 204, 487-501.
    • (2012) Acta Physiol. , vol.204 , pp. 487-501
    • Haines, D.D.1    Lekli, I.2    Teissier, P.3    Bak, I.4    Tosaki, A.5
  • 225
    • 41149177025 scopus 로고    scopus 로고
    • Pharmacological and clinical aspects of heme oxygenase
    • Abraham, N.G.; Kappas, A. Pharmacological and clinical aspects of heme oxygenase. Pharmacol. Rev. 2008, 60, 79-127.
    • (2008) Pharmacol. Rev. , vol.60 , pp. 79-127
    • Abraham, N.G.1    Kappas, A.2
  • 226
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines, M.D. Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J. 1988, 2, 2557-2568.
    • (1988) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 227
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen, R.; Marver, H.S.; Schmid, R. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc. Natl. Acad. Sci. USA 1968, 61, 748-755.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 229
    • 84866051194 scopus 로고    scopus 로고
    • Heme oxygenase, inflammation, and fibrosis: The good, the bad, and the ugly?
    • Lundvig, D.M.; Immenschuh, S.; Wagener, F.A. Heme oxygenase, inflammation, and fibrosis: The good, the bad, and the ugly? Front. Pharmacol. 2012, 3, 81.
    • (2012) Front. Pharmacol. , vol.3 , pp. 81
    • Lundvig, D.M.1    Immenschuh, S.2    Wagener, F.A.3
  • 230
    • 84856380036 scopus 로고    scopus 로고
    • Haem oxygenase-1: Non-canonical roles in physiology and pathology
    • Grochot-Przeczek, A.; Dulak, J.; Jozkowicz, A. Haem oxygenase-1: Non-canonical roles in physiology and pathology. Clin. Sci. 2012, 122, 93-103.
    • (2012) Clin. Sci. , vol.122 , pp. 93-103
    • Grochot-Przeczek, A.1    Dulak, J.2    Jozkowicz, A.3
  • 231
    • 0024516371 scopus 로고
    • Transcriptional activation of the heme oxygenase gene by heme and cadmium in mouse hepatoma cells
    • Alam, J.; Shibahara, S.; Smith, A. Transcriptional activation of the heme oxygenase gene by heme and cadmium in mouse hepatoma cells. J. Biol. Chem. 1989, 264, 6371-6375.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6371-6375
    • Alam, J.1    Shibahara, S.2    Smith, A.3
  • 232
    • 0029257545 scopus 로고
    • Two genes contribute to different extents to the heme oxygenase enzyme activity measured in cultured human skin fibroblasts and keratinocytes: Implications for protection against oxidant stress
    • Applegate, L.A.; Noel, A.; Vile, G.; Frenk, E.; Tyrrell, R.M. Two genes contribute to different extents to the heme oxygenase enzyme activity measured in cultured human skin fibroblasts and keratinocytes: Implications for protection against oxidant stress. Photochem. Photobiol. 1995, 61, 285-291.
    • (1995) Photochem. Photobiol. , vol.61 , pp. 285-291
    • Applegate, L.A.1    Noel, A.2    Vile, G.3    Frenk, E.4    Tyrrell, R.M.5
  • 234
    • 0036010763 scopus 로고    scopus 로고
    • The role of heme oxygenase signaling in various disorders
    • Tosaki, A.; Das, D.K. The role of heme oxygenase signaling in various disorders. Mol. Cell. Biochem. 2002, 232, 149-157.
    • (2002) Mol. Cell. Biochem. , vol.232 , pp. 149-157
    • Tosaki, A.1    Das, D.K.2
  • 235
    • 4544242791 scopus 로고    scopus 로고
    • Solar ultraviolet A radiation: An oxidizing skin carcinogen that activates heme oxygenase-1
    • Tyrrell, R.M. Solar ultraviolet A radiation: An oxidizing skin carcinogen that activates heme oxygenase-1. Antioxid. Redox Signal. 2004, 6, 835-840.
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 835-840
    • Tyrrell, R.M.1
  • 239
    • 0034041022 scopus 로고    scopus 로고
    • Heme oxygenase modulates selectin expression in different regional vascular beds
    • Vachharajani, T.J.; Work, J.; Issekutz, A.C.; Granger, D.N. Heme oxygenase modulates selectin expression in different regional vascular beds. Am. J. Physiol. 2000, 278, H1613-H1617.
    • (2000) Am. J. Physiol. , vol.278
    • Vachharajani, T.J.1    Work, J.2    Issekutz, A.C.3    Granger, D.N.4
  • 243
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker, R.; Yamamoto, Y.; McDonagh, A.F.; Glazer, A.N.; Ames, B.N. Bilirubin is an antioxidant of possible physiological importance. Science 1987, 235, 1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 244
    • 84865967056 scopus 로고    scopus 로고
    • Physiological antioxidative network of the bilirubin system in aging and age-related diseases
    • Kim, S.Y.; Park, S.C. Physiological antioxidative network of the bilirubin system in aging and age-related diseases. Front. Pharmacol. 2012, 3, 45.
    • (2012) Front. Pharmacol. , vol.3 , pp. 45
    • Kim, S.Y.1    Park, S.C.2
  • 245
    • 0033374730 scopus 로고    scopus 로고
    • Neuroprotective action of bilirubin against oxidative stress in primary hippocampal cultures
    • Dore, S.; Snyder, S.H. Neuroprotective action of bilirubin against oxidative stress in primary hippocampal cultures. Ann. N. Y. Acad. Sci. 1999, 890, 167-172.
    • (1999) Ann. N. Y. Acad. Sci. , vol.890 , pp. 167-172
    • Dore, S.1    Snyder, S.H.2
  • 247
    • 27744592135 scopus 로고    scopus 로고
    • Bilirubin decreases nos2 expression via inhibition of NAD(P)H oxidase: Implications for protection against endotoxic shock in rats
    • Lanone, S.; Bloc, S.; Foresti, R.; Almolki, A.; Taille, C.; Callebert, J.; Conti, M.; Goven, D.; Aubier, M.; Dureuil, B.; et al. Bilirubin decreases nos2 expression via inhibition of NAD(P)H oxidase: Implications for protection against endotoxic shock in rats. FASEB J. 2005, 19, 1890-1892.
    • (2005) FASEB J. , vol.19 , pp. 1890-1892
    • Lanone, S.1    Bloc, S.2    Foresti, R.3    Almolki, A.4    Taille, C.5    Callebert, J.6    Conti, M.7    Goven, D.8    Aubier, M.9    Dureuil, B.10
  • 248
    • 33750260791 scopus 로고    scopus 로고
    • NO modulates NADPH oxidase function via heme oxygenase-1 in human endothelial cells
    • Jiang, F.; Roberts, S.J.; Datla, S.; Dusting, G.J. NO modulates NADPH oxidase function via heme oxygenase-1 in human endothelial cells. Hypertension 2006, 48, 950-957.
    • (2006) Hypertension , vol.48 , pp. 950-957
    • Jiang, F.1    Roberts, S.J.2    Datla, S.3    Dusting, G.J.4
  • 249
    • 33750922153 scopus 로고    scopus 로고
    • Carbon monoxide and bilirubin from heme oxygenase-1 suppresses reactive oxygen species generation and plasminogen activator inhibitor-1 induction
    • Matsumoto, H.; Ishikawa, K.; Itabe, H.; Maruyama, Y. Carbon monoxide and bilirubin from heme oxygenase-1 suppresses reactive oxygen species generation and plasminogen activator inhibitor-1 induction. Mol. Cell. Biochem. 2006, 291, 21-28.
    • (2006) Mol. Cell. Biochem. , vol.291 , pp. 21-28
    • Matsumoto, H.1    Ishikawa, K.2    Itabe, H.3    Maruyama, Y.4
  • 250
    • 77955092575 scopus 로고    scopus 로고
    • The biliverdin-bilirubin antioxidant cycle of cellular protection: Missing a wheel?
    • McDonagh, A.F. The biliverdin-bilirubin antioxidant cycle of cellular protection: Missing a wheel? Free Radic. Biol. Med. 2010, 49, 814-820.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 814-820
    • McDonagh, A.F.1
  • 251
    • 80055078417 scopus 로고    scopus 로고
    • Importance of iron chelation in free radical-induced oxidative stress and human disease
    • Jomova, K.; Valko, M. Importance of iron chelation in free radical-induced oxidative stress and human disease. Curr. Pharm. Des. 2011, 17, 3460-3473.
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 3460-3473
    • Jomova, K.1    Valko, M.2
  • 252
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P.M.; Arosio, P. The ferritins: Molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1996, 1275, 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 253
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti, F.M.; Torti, S.V. Regulation of ferritin genes and protein. Blood 2002, 99, 3505-3516.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 254
    • 54449085184 scopus 로고    scopus 로고
    • Molecular, physiological and clinical aspects of the iron storage protein ferritin
    • Orino, K.; Watanabe, K. Molecular, physiological and clinical aspects of the iron storage protein ferritin. Vet. J. 2008, 178, 191-201.
    • (2008) Vet. J. , vol.178 , pp. 191-201
    • Orino, K.1    Watanabe, K.2
  • 255
    • 35448950829 scopus 로고    scopus 로고
    • Regulatory role of vitamins E and C on extracellular matrix components of the vascular system
    • Villacorta, L.; Azzi, A.; Zingg, J.M. Regulatory role of vitamins E and C on extracellular matrix components of the vascular system. Mol. Asp. Med. 2007, 28, 507-537.
    • (2007) Mol. Asp. Med. , vol.28 , pp. 507-537
    • Villacorta, L.1    Azzi, A.2    Zingg, J.M.3
  • 256
    • 0036479117 scopus 로고    scopus 로고
    • Role of neutrophil NADPH oxidase in the mechanism of tumor necrosis factor-alpha-induced NF-kappa B activation and intercellular adhesion molecule-1 expression in endothelial cells
    • Fan, J.; Frey, R.S.; Rahman, A.; Malik, A.B. Role of neutrophil NADPH oxidase in the mechanism of tumor necrosis factor-alpha-induced NF-kappa B activation and intercellular adhesion molecule-1 expression in endothelial cells. J. Biol. Chem. 2002, 277, 3404-3411.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3404-3411
    • Fan, J.1    Frey, R.S.2    Rahman, A.3    Malik, A.B.4
  • 259
    • 0036847602 scopus 로고    scopus 로고
    • In vivo lipid-derived free radical formation by NADPH oxidase in acute lung injury induced by lipopolysaccharide: A model for ARDS
    • Sato, K.; Kadiiska, M.B.; Ghio, A.J.; Corbett, J.; Fann, Y.C.; Holland, S.M.; Thurman, R.G.; Mason, R.P. In vivo lipid-derived free radical formation by NADPH oxidase in acute lung injury induced by lipopolysaccharide: A model for ARDS. FASEB J. 2002, 16, 1713-1720.
    • (2002) FASEB J. , vol.16 , pp. 1713-1720
    • Sato, K.1    Kadiiska, M.B.2    Ghio, A.J.3    Corbett, J.4    Fann, Y.C.5    Holland, S.M.6    Thurman, R.G.7    Mason, R.P.8
  • 260
    • 0031706281 scopus 로고    scopus 로고
    • E-selectin expression in human endothelial cells by TNF-alpha-induced oxidant generation and NF-kappaB activation
    • Rahman, A.; Kefer, J.; Bando, M.; Niles, W.D.; Malik, A.B. E-selectin expression in human endothelial cells by TNF-alpha-induced oxidant generation and NF-kappaB activation. Am. J. Physiol. 1998, 275, L533-L544.
    • (1998) Am. J. Physiol. , vol.275
    • Rahman, A.1    Kefer, J.2    Bando, M.3    Niles, W.D.4    Malik, A.B.5
  • 261
    • 14844349754 scopus 로고    scopus 로고
    • Acute tumor necrosis factor alpha signaling via NADPH oxidase in microvascular endothelial cells: Role of p47phox phosphorylation and binding to TRAF4
    • Li, J.M.; Fan, L.M.; Christie, M.R.; Shah, A.M. Acute tumor necrosis factor alpha signaling via NADPH oxidase in microvascular endothelial cells: Role of p47phox phosphorylation and binding to TRAF4. Mol. Cell. Biol. 2005, 25, 2320-2330.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2320-2330
    • Li, J.M.1    Fan, L.M.2    Christie, M.R.3    Shah, A.M.4
  • 263
  • 264
    • 67651156448 scopus 로고    scopus 로고
    • Small-molecule NOX inhibitors: ROS-generating NADPH oxidases as therapeutic targets
    • Jaquet, V.; Scapozza, L.; Clark, R.A.; Krause, K.H.; Lambeth, J.D. Small-molecule NOX inhibitors: ROS-generating NADPH oxidases as therapeutic targets. Antioxid. Redox Signal. 2009, 11, 2535-2552.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2535-2552
    • Jaquet, V.1    Scapozza, L.2    Clark, R.A.3    Krause, K.H.4    Lambeth, J.D.5
  • 265
    • 60449099432 scopus 로고    scopus 로고
    • Genetic deficiency of NADPH oxidase does not diminish, but rather enhances, LPS-induced acute inflammatory responses in vivo
    • Zhang, W.J.; Wei, H.; Frei, B. Genetic deficiency of NADPH oxidase does not diminish, but rather enhances, LPS-induced acute inflammatory responses in vivo. Free Radic. Biol. Med. 2009, 46, 791-798.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 791-798
    • Zhang, W.J.1    Wei, H.2    Frei, B.3
  • 267
    • 0028177211 scopus 로고
    • The role of O2.-in the production of HO.: In vitro and in vivo
    • Liochev, S.I.; Fridovich, I. The role of O2.-in the production of HO.: In vitro and in vivo. Free Radic. Biol. Med. 1994, 16, 29-33.
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 29-33
    • Liochev, S.I.1    Fridovich, I.2
  • 268
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: Characterization, measurement, and participation in cellular processes(1)
    • Kakhlon, O.; Cabantchik, Z.I. The labile iron pool: Characterization, measurement, and participation in cellular processes(1). Free Radic. Biol. Med. 2002, 33, 1037-1046.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 269
    • 84856292277 scopus 로고    scopus 로고
    • Iron overload in human disease
    • Fleming, R.E.; Ponka, P. Iron overload in human disease. N. Engl. J. Med. 2012, 366, 348-359.
    • (2012) N. Engl. J. Med. , vol.366 , pp. 348-359
    • Fleming, R.E.1    Ponka, P.2
  • 270
    • 84866046917 scopus 로고    scopus 로고
    • Heme cytotoxicity and the pathogenesis of immune-mediated inflammatory diseases
    • Larsen, R.; Gouveia, Z.; Soares, M.P.; Gozzelino, R. Heme cytotoxicity and the pathogenesis of immune-mediated inflammatory diseases. Front. Pharmacol. 2012, 3, 77.
    • (2012) Front. Pharmacol. , vol.3 , pp. 77
    • Larsen, R.1    Gouveia, Z.2    Soares, M.P.3    Gozzelino, R.4
  • 271
    • 78649444888 scopus 로고    scopus 로고
    • Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examples
    • Kell, D.B. Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examples. Arch. Toxicol. 2010, 84, 825-889.
    • (2010) Arch. Toxicol. , vol.84 , pp. 825-889
    • Kell, D.B.1
  • 272
    • 63149091751 scopus 로고    scopus 로고
    • A review of the antioxidant mechanisms of polyphenol compounds related to iron binding
    • Perron, N.R.; Brumaghim, J.L. A review of the antioxidant mechanisms of polyphenol compounds related to iron binding. Cell Biochem. Biophys. 2009, 53, 75-100.
    • (2009) Cell Biochem. Biophys. , vol.53 , pp. 75-100
    • Perron, N.R.1    Brumaghim, J.L.2
  • 273
    • 0032527633 scopus 로고    scopus 로고
    • Quercetin prevents DNA single strand breakage and cytotoxicity caused by tert-butylhydroperoxide: Free radical scavenging versus iron chelating mechanism
    • Sestili, P.; Guidarelli, A.; Dacha, M.; Cantoni, O. Quercetin prevents DNA single strand breakage and cytotoxicity caused by tert-butylhydroperoxide: Free radical scavenging versus iron chelating mechanism. Free Radic. Biol. Med. 1998, 25, 196-200.
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 196-200
    • Sestili, P.1    Guidarelli, A.2    Dacha, M.3    Cantoni, O.4
  • 274
    • 79961193678 scopus 로고    scopus 로고
    • Superoxide dismutases: Role in redox signaling, vascular function, and diseases
    • Fukai, T.; Ushio-Fukai, M. Superoxide dismutases: Role in redox signaling, vascular function, and diseases. Antioxid. Redox Signal. 2011, 15, 1583-1606.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 1583-1606
    • Fukai, T.1    Ushio-Fukai, M.2
  • 275
    • 0021218456 scopus 로고
    • Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species
    • Marklund, S.L. Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species. Biochem. J. 1984, 222, 649-655.
    • (1984) Biochem. J. , vol.222 , pp. 649-655
    • Marklund, S.L.1
  • 276
    • 0027310308 scopus 로고
    • Ultraviolet A-induced lipid peroxidation and antioxidant defense systems in cultured human skin fibroblasts
    • Moysan, A.; Marquis, I.; Gaboriau, F.; Santus, R.; Dubertret, L.; Morliere, P. Ultraviolet A-induced lipid peroxidation and antioxidant defense systems in cultured human skin fibroblasts. J. Investig. Dermatol. 1993, 100, 692-698.
    • (1993) J. Investig. Dermatol. , vol.100 , pp. 692-698
    • Moysan, A.1    Marquis, I.2    Gaboriau, F.3    Santus, R.4    Dubertret, L.5    Morliere, P.6
  • 278
    • 8344262326 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase tissue distribution and the patterns of superoxide dismutase mRNA expression following ultraviolet irradiation on mouse skin
    • Choung, B.Y.; Byun, S.J.; Suh, J.G.; Kim, T.Y. Extracellular superoxide dismutase tissue distribution and the patterns of superoxide dismutase mRNA expression following ultraviolet irradiation on mouse skin. Exp. Dermatol. 2004, 13, 691-699.
    • (2004) Exp. Dermatol. , vol.13 , pp. 691-699
    • Choung, B.Y.1    Byun, S.J.2    Suh, J.G.3    Kim, T.Y.4
  • 279
    • 0028066981 scopus 로고
    • Successful treatment of radiation-induced fibrosis using liposomal Cu/Zn superoxide dismutase: Clinical trial
    • Delanian, S.; Baillet, F.; Huart, J.; Lefaix, J.L.; Maulard, C.; Housset, M. Successful treatment of radiation-induced fibrosis using liposomal Cu/Zn superoxide dismutase: Clinical trial. Radiother. Oncol. 1994, 32, 12-20.
    • (1994) Radiother. Oncol. , vol.32 , pp. 12-20
    • Delanian, S.1    Baillet, F.2    Huart, J.3    Lefaix, J.L.4    Maulard, C.5    Housset, M.6
  • 281
    • 6444226659 scopus 로고    scopus 로고
    • Gene therapy of endothelial nitric oxide synthase and manganese superoxide dismutase restores delayed wound healing in type 1 diabetic mice
    • Luo, J.D.; Wang, Y.Y.; Fu, W.L.; Wu, J.; Chen, A.F. Gene therapy of endothelial nitric oxide synthase and manganese superoxide dismutase restores delayed wound healing in type 1 diabetic mice. Circulation 2004, 110, 2484-2493.
    • (2004) Circulation , vol.110 , pp. 2484-2493
    • Luo, J.D.1    Wang, Y.Y.2    Fu, W.L.3    Wu, J.4    Chen, A.F.5
  • 282
    • 44849131121 scopus 로고    scopus 로고
    • Decreasing intracellular superoxide corrects defective ischemia-induced new vessel formation in diabetic mice
    • Ceradini, D.J.; Yao, D.; Grogan, R.H.; Callaghan, M.J.; Edelstein, D.; Brownlee, M.; Gurtner, G.C. Decreasing intracellular superoxide corrects defective ischemia-induced new vessel formation in diabetic mice. J. Biol. Chem. 2008, 283, 10930-10938.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10930-10938
    • Ceradini, D.J.1    Yao, D.2    Grogan, R.H.3    Callaghan, M.J.4    Edelstein, D.5    Brownlee, M.6    Gurtner, G.C.7
  • 283
    • 33746888210 scopus 로고    scopus 로고
    • Inhibition of the TPA-induced cutaneous inflammation and hyperplasia by EC-SOD
    • Ha, H.Y.; Kim, Y.; Ryoo, Z.Y.; Kim, T.Y. Inhibition of the TPA-induced cutaneous inflammation and hyperplasia by EC-SOD. Biochem. Biophys. Res. Commun. 2006, 348, 450-458.
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 450-458
    • Ha, H.Y.1    Kim, Y.2    Ryoo, Z.Y.3    Kim, T.Y.4
  • 284
    • 80255133209 scopus 로고    scopus 로고
    • Regulation of skin inflammation and angiogenesis by EC-SOD via HIF-1alpha and NF-kappaB pathways
    • Kim, Y.; Kim, B.H.; Lee, H.; Jeon, B.; Lee, Y.S.; Kwon, M.J.; Kim, T.Y. Regulation of skin inflammation and angiogenesis by EC-SOD via HIF-1alpha and NF-kappaB pathways. Free Radic. Biol. Med. 2011, 51, 1985-1995.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1985-1995
    • Kim, Y.1    Kim, B.H.2    Lee, H.3    Jeon, B.4    Lee, Y.S.5    Kwon, M.J.6    Kim, T.Y.7
  • 285
    • 84873736060 scopus 로고    scopus 로고
    • Loss of extracellular superoxide dismutase induces severe IL-23-mediated skin inflammation in mice
    • Lee, Y.S.; Cheon, I.S.; Kim, B.H.; Kwon, M.J.; Lee, H.W.; Kim, T.Y. Loss of extracellular superoxide dismutase induces severe IL-23-mediated skin inflammation in mice. J. Investig. Dermatol. 2013, 133, 732-741.
    • (2013) J. Investig. Dermatol. , vol.133 , pp. 732-741
    • Lee, Y.S.1    Cheon, I.S.2    Kim, B.H.3    Kwon, M.J.4    Lee, H.W.5    Kim, T.Y.6
  • 286
    • 84866285250 scopus 로고    scopus 로고
    • Superoxide dismutase 3 controls adaptive immune responses and contributes to the inhibition of ovalbumin-induced allergic airway inflammation in mice
    • Kwon, M.J.; Jeon, Y.J.; Lee, K.Y.; Kim, T.Y. Superoxide dismutase 3 controls adaptive immune responses and contributes to the inhibition of ovalbumin-induced allergic airway inflammation in mice. Antioxid. Redox Signal. 2012, 17, 1376-1392.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1376-1392
    • Kwon, M.J.1    Jeon, Y.J.2    Lee, K.Y.3    Kim, T.Y.4
  • 288
    • 38049027217 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase (ecSOD) in vascular biology: An update on exogenous gene transfer and endogenous regulators of ecSOD
    • Qin, Z.; Reszka, K.J.; Fukai, T.; Weintraub, N.L. Extracellular superoxide dismutase (ecSOD) in vascular biology: An update on exogenous gene transfer and endogenous regulators of ecSOD. Transl. Res. 2008, 151, 68-78.
    • (2008) Transl. Res. , vol.151 , pp. 68-78
    • Qin, Z.1    Reszka, K.J.2    Fukai, T.3    Weintraub, N.L.4
  • 289
    • 0029992837 scopus 로고    scopus 로고
    • The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid
    • Carlsson, L.M.; Marklund, S.L.; Edlund, T. The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid. Proc. Natl. Acad. Sci. USA 1996, 93, 5219-5222.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5219-5222
    • Carlsson, L.M.1    Marklund, S.L.2    Edlund, T.3
  • 290
    • 7644233498 scopus 로고    scopus 로고
    • Gene transfer of extracellular superoxide dismutase failed to prevent cerebral vasospasm after experimental subarachnoid hemorrhage
    • Yamaguchi, M.; Zhou, C.; Heistad, D.D.; Watanabe, Y.; Zhang, J.H. Gene transfer of extracellular superoxide dismutase failed to prevent cerebral vasospasm after experimental subarachnoid hemorrhage. Stroke 2004, 35, 2512-2517.
    • (2004) Stroke , vol.35 , pp. 2512-2517
    • Yamaguchi, M.1    Zhou, C.2    Heistad, D.D.3    Watanabe, Y.4    Zhang, J.H.5
  • 291
    • 77954735594 scopus 로고    scopus 로고
    • Superoxide dismutase mimics: Chemistry, pharmacology, and therapeutic potential
    • Batinic-Haberle, I.; Reboucas, J.S.; Spasojevic, I. Superoxide dismutase mimics: Chemistry, pharmacology, and therapeutic potential. Antioxid. Redox Signal. 2010, 13, 877-918.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 877-918
    • Batinic-Haberle, I.1    Reboucas, J.S.2    Spasojevic, I.3
  • 292
    • 58249130590 scopus 로고    scopus 로고
    • Catalase and glutathione peroxidase mimics
    • Day, B.J. Catalase and glutathione peroxidase mimics. Biochem. Pharmacol. 2009, 77, 285-296.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 285-296
    • Day, B.J.1
  • 294
    • 2942623947 scopus 로고    scopus 로고
    • Catalytic antioxidants: A radical approach to new therapeutics
    • Day, B.J. Catalytic antioxidants: A radical approach to new therapeutics. Drug Discov. Today 2004, 9, 557-566.
    • (2004) Drug Discov. Today , vol.9 , pp. 557-566
    • Day, B.J.1
  • 295
    • 0033578309 scopus 로고    scopus 로고
    • EUK-134, a synthetic superoxide dismutase and catalase mimetic, prevents oxidative stress and attenuates kainate-induced neuropathology
    • Rong, Y.; Doctrow, S.R.; Tocco, G.; Baudry, M. EUK-134, a synthetic superoxide dismutase and catalase mimetic, prevents oxidative stress and attenuates kainate-induced neuropathology. Proc. Natl. Acad. Sci. USA 1999, 96, 9897-9902.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9897-9902
    • Rong, Y.1    Doctrow, S.R.2    Tocco, G.3    Baudry, M.4
  • 296
    • 0038491473 scopus 로고    scopus 로고
    • Reversal of age-related learning deficits and brain oxidative stress in mice with superoxide dismutase/catalase mimetics
    • Liu, R.; Liu, I.Y.; Bi, X.; Thompson, R.F.; Doctrow, S.R.; Malfroy, B.; Baudry, M. Reversal of age-related learning deficits and brain oxidative stress in mice with superoxide dismutase/catalase mimetics. Proc. Natl. Acad. Sci. USA 2003, 100, 8526-8531.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8526-8531
    • Liu, R.1    Liu, I.Y.2    Bi, X.3    Thompson, R.F.4    Doctrow, S.R.5    Malfroy, B.6    Baudry, M.7
  • 297
    • 9444222523 scopus 로고    scopus 로고
    • Redox modulation of the liver with chronic antioxidant enzyme mimetic treatment prevents age-related oxidative damage associated with environmental stress
    • Zhang, H.J.; Doctrow, S.R.; Xu, L.; Oberley, L.W.; Beecher, B.; Morrison, J.; Oberley, T.D.; Kregel, K.C. Redox modulation of the liver with chronic antioxidant enzyme mimetic treatment prevents age-related oxidative damage associated with environmental stress. FASEB J. 2004, 18, 1547-1549.
    • (2004) FASEB J. , vol.18 , pp. 1547-1549
    • Zhang, H.J.1    Doctrow, S.R.2    Xu, L.3    Oberley, L.W.4    Beecher, B.5    Morrison, J.6    Oberley, T.D.7    Kregel, K.C.8
  • 298
    • 74149083183 scopus 로고    scopus 로고
    • Prevention of cognitive deficits and brain oxidative stress with superoxide dismutase/catalase mimetics in aged mice
    • Clausen, A.; Doctrow, S.; Baudry, M. Prevention of cognitive deficits and brain oxidative stress with superoxide dismutase/catalase mimetics in aged mice. Neurobiol. Aging 2010, 31, 425-433.
    • (2010) Neurobiol. Aging , vol.31 , pp. 425-433
    • Clausen, A.1    Doctrow, S.2    Baudry, M.3
  • 299
    • 80051949650 scopus 로고    scopus 로고
    • Mitochondrial transporter ATP binding cassette mitochondrial erythroid is a novel gene required for cardiac recovery after ischemia/reperfusion
    • Liesa, M.; Luptak, I.; Qin, F.; Hyde, B.B.; Sahin, E.; Siwik, D.A.; Zhu, Z.; Pimentel, D.R.; Xu, X.J.; Ruderman, N.B.; et al. Mitochondrial transporter ATP binding cassette mitochondrial erythroid is a novel gene required for cardiac recovery after ischemia/reperfusion. Circulation 2011, 124, 806-813.
    • (2011) Circulation , vol.124 , pp. 806-813
    • Liesa, M.1    Luptak, I.2    Qin, F.3    Hyde, B.B.4    Sahin, E.5    Siwik, D.A.6    Zhu, Z.7    Pimentel, D.R.8    Xu, X.J.9    Ruderman, N.B.10
  • 302
    • 60649095328 scopus 로고    scopus 로고
    • Heme oxygenase-1: From biology to therapeutic potential
    • Soares, M.P.; Bach, F.H. Heme oxygenase-1: From biology to therapeutic potential. Trends Mol. Med. 2009, 15, 50-58.
    • (2009) Trends Mol. Med. , vol.15 , pp. 50-58
    • Soares, M.P.1    Bach, F.H.2
  • 303
    • 0034243847 scopus 로고    scopus 로고
    • Structural evidence of genomic exon-deletion mediated by Alu-Alu recombination in a human case with heme oxygenase-1 deficiency
    • Saikawa, Y.; Kaneda, H.; Yue, L.; Shimura, S.; Toma, T.; Kasahara, Y.; Yachie, A.; Koizumi, S. Structural evidence of genomic exon-deletion mediated by Alu-Alu recombination in a human case with heme oxygenase-1 deficiency. Hum. Mutat. 2000, 16, 178-179.
    • (2000) Hum. Mutat. , vol.16 , pp. 178-179
    • Saikawa, Y.1    Kaneda, H.2    Yue, L.3    Shimura, S.4    Toma, T.5    Kasahara, Y.6    Yachie, A.7    Koizumi, S.8
  • 305
    • 4644226200 scopus 로고    scopus 로고
    • The role of heme oxygenase-1 promoter polymorphisms in human disease
    • Exner, M.; Minar, E.; Wagner, O.; Schillinger, M. The role of heme oxygenase-1 promoter polymorphisms in human disease. Free Radic. Biol. Med. 2004, 37, 1097-1104.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1097-1104
    • Exner, M.1    Minar, E.2    Wagner, O.3    Schillinger, M.4
  • 306
    • 0021285125 scopus 로고
    • Control of heme and cytochrome P-450 metabolism by inorganic metals, organometals and synthetic metalloporphyrins
    • Kappas, A.; Drummond, G.S. Control of heme and cytochrome P-450 metabolism by inorganic metals, organometals and synthetic metalloporphyrins. Environ. Health Perspect. 1984, 57, 301-306.
    • (1984) Environ. Health Perspect. , vol.57 , pp. 301-306
    • Kappas, A.1    Drummond, G.S.2
  • 307
    • 33746138114 scopus 로고    scopus 로고
    • Heme arginate pretreatment attenuates pulmonary NF-kappaB and AP-1 activation induced by hemorrhagic shock via heme oxygenase-1 induction
    • Sasaki, T.; Takahashi, T.; Maeshima, K.; Shimizu, H.; Toda, Y.; Morimatsu, H.; Takeuchi, M.; Yokoyama, M.; Akagi, R.; Morita, K. Heme arginate pretreatment attenuates pulmonary NF-kappaB and AP-1 activation induced by hemorrhagic shock via heme oxygenase-1 induction. Med. Chem. 2006, 2, 271-274.
    • (2006) Med. Chem. , vol.2 , pp. 271-274
    • Sasaki, T.1    Takahashi, T.2    Maeshima, K.3    Shimizu, H.4    Toda, Y.5    Morimatsu, H.6    Takeuchi, M.7    Yokoyama, M.8    Akagi, R.9    Morita, K.10
  • 308
    • 0031940457 scopus 로고    scopus 로고
    • Acute porphyria: Treatment with heme
    • Tenhunen, R.; Mustajoki, P. Acute porphyria: Treatment with heme. Semin. Liver Dis. 1998, 18, 53-55.
    • (1998) Semin. Liver Dis. , vol.18 , pp. 53-55
    • Tenhunen, R.1    Mustajoki, P.2
  • 310
    • 0034655773 scopus 로고    scopus 로고
    • Curcumin, an antioxidant and anti-inflammatory agent, induces heme oxygenase-1 and protects endothelial cells against oxidative stress
    • Motterlini, R.; Foresti, R.; Bassi, R.; Green, C.J. Curcumin, an antioxidant and anti-inflammatory agent, induces heme oxygenase-1 and protects endothelial cells against oxidative stress. Free Radic. Biol. Med. 2000, 28, 1303-1312.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1303-1312
    • Motterlini, R.1    Foresti, R.2    Bassi, R.3    Green, C.J.4
  • 311
    • 0037569694 scopus 로고    scopus 로고
    • Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element
    • Balogun, E.; Hoque, M.; Gong, P.; Killeen, E.; Green, C.J.; Foresti, R.; Alam, J.; Motterlini, R. Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element. Biochem. J. 2003, 371, 887-895.
    • (2003) Biochem. J. , vol.371 , pp. 887-895
    • Balogun, E.1    Hoque, M.2    Gong, P.3    Killeen, E.4    Green, C.J.5    Foresti, R.6    Alam, J.7    Motterlini, R.8
  • 312
    • 34147165621 scopus 로고    scopus 로고
    • Curcumin induces heme oxygenase 1 through generation of reactive oxygen species, p38 activation and phosphatase inhibition
    • McNally, S.J.; Harrison, E.M.; Ross, J.A.; Garden, O.J.; Wigmore, S.J. Curcumin induces heme oxygenase 1 through generation of reactive oxygen species, p38 activation and phosphatase inhibition. Int. J. Mol. Med. 2007, 19, 165-172.
    • (2007) Int. J. Mol. Med. , vol.19 , pp. 165-172
    • McNally, S.J.1    Harrison, E.M.2    Ross, J.A.3    Garden, O.J.4    Wigmore, S.J.5
  • 313
    • 2342518882 scopus 로고    scopus 로고
    • Mechanism of heme oxygenase-1 gene induction by quercetin in rat aortic smooth muscle cells
    • Lin, H.C.; Cheng, T.H.; Chen, Y.C.; Juan, S.H. Mechanism of heme oxygenase-1 gene induction by quercetin in rat aortic smooth muscle cells. Pharmacology 2004, 71, 107-112.
    • (2004) Pharmacology , vol.71 , pp. 107-112
    • Lin, H.C.1    Cheng, T.H.2    Chen, Y.C.3    Juan, S.H.4
  • 314
    • 34347392509 scopus 로고    scopus 로고
    • Quercetin protects human hepatocytes from ethanol-derived oxidative stress by inducing heme oxygenase-1 via the MAPK/Nrf2 pathways
    • Yao, P.; Nussler, A.; Liu, L.; Hao, L.; Song, F.; Schirmeier, A.; Nussler, N. Quercetin protects human hepatocytes from ethanol-derived oxidative stress by inducing heme oxygenase-1 via the MAPK/Nrf2 pathways. J. Hepatol. 2007, 47, 253-261.
    • (2007) J. Hepatol. , vol.47 , pp. 253-261
    • Yao, P.1    Nussler, A.2    Liu, L.3    Hao, L.4    Song, F.5    Schirmeier, A.6    Nussler, N.7
  • 315
    • 33645635277 scopus 로고    scopus 로고
    • Associations of vitamin C status, fruit and vegetable intakes, and markers of inflammation and hemostasis
    • quiz 726-567
    • Wannamethee, S.G.; Lowe, G.D.; Rumley, A.; Bruckdorfer, K.R.; Whincup, P.H. Associations of vitamin C status, fruit and vegetable intakes, and markers of inflammation and hemostasis. Am. J. Clin. Nutr. 2006, 83, 567-574; quiz 726-567.
    • (2006) Am. J. Clin. Nutr. , vol.83 , pp. 567-574
    • Wannamethee, S.G.1    Lowe, G.D.2    Rumley, A.3    Bruckdorfer, K.R.4    Whincup, P.H.5
  • 320
    • 79958764508 scopus 로고    scopus 로고
    • Signalling pathways from NADPH oxidase-4 to idiopathic pulmonary fibrosis
    • Crestani, B.; Besnard, V.; Boczkowski, J. Signalling pathways from NADPH oxidase-4 to idiopathic pulmonary fibrosis. Int. J. Biochem. Cell Biol. 2011, 43, 1086-1089.
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1086-1089
    • Crestani, B.1    Besnard, V.2    Boczkowski, J.3
  • 322
    • 84861394764 scopus 로고    scopus 로고
    • Prednisone, azathioprine, and N-acetylcysteine for pulmonary fibrosis
    • Idiopathic Pulmonary Fibrosis Clinical Research, N.; Raghu, G.; Anstrom, K.J.; King, T.E., Jr.; Lasky, J.A.; Martinez, F.J. Prednisone, azathioprine, and N-acetylcysteine for pulmonary fibrosis. N. Engl. J. Med. 2012, 366, 1968-1977.
    • (2012) N. Engl. J. Med. , vol.366 , pp. 1968-1977
    • Raghu, G.1    Anstrom, K.J.2    King Jr., T.E.3    Lasky, J.A.4    Martinez, F.J.5
  • 324
    • 12944249329 scopus 로고    scopus 로고
    • Ultraviolet B-induced DNA damage in human epidermis is modified by the antioxidants ascorbic acid and D-alpha-tocopherol
    • Placzek, M.; Gaube, S.; Kerkmann, U.; Gilbertz, K.P.; Herzinger, T.; Haen, E.; Przybilla, B. Ultraviolet B-induced DNA damage in human epidermis is modified by the antioxidants ascorbic acid and D-alpha-tocopherol. J. Investig. Dermatol. 2005, 124, 304-307.
    • (2005) J. Investig. Dermatol. , vol.124 , pp. 304-307
    • Placzek, M.1    Gaube, S.2    Kerkmann, U.3    Gilbertz, K.P.4    Herzinger, T.5    Haen, E.6    Przybilla, B.7
  • 326
    • 34347344721 scopus 로고    scopus 로고
    • Relevance of vitamins C and E in cutaneous photoprotection
    • Eberlein-Konig, B.; Ring, J. Relevance of vitamins C and E in cutaneous photoprotection. J. Cosmet. Dermatol. 2005, 4, 4-9.
    • (2005) J. Cosmet. Dermatol. , vol.4 , pp. 4-9
    • Eberlein-Konig, B.1    Ring, J.2
  • 327
    • 0034003859 scopus 로고    scopus 로고
    • Carotenoids and carotenoids plus vitamin E protect against ultraviolet light-induced erythema in humans
    • Stahl, W.; Heinrich, U.; Jungmann, H.; Sies, H.; Tronnier, H. Carotenoids and carotenoids plus vitamin E protect against ultraviolet light-induced erythema in humans. Am. J. Clin. Nutr. 2000, 71, 795-798.
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 795-798
    • Stahl, W.1    Heinrich, U.2    Jungmann, H.3    Sies, H.4    Tronnier, H.5
  • 328
    • 0034089988 scopus 로고    scopus 로고
    • Carotenoid supplementation reduces erythema in human skin after simulated solar radiation exposure
    • Lee, J.; Jiang, S.; Levine, N.; Watson, R.R. Carotenoid supplementation reduces erythema in human skin after simulated solar radiation exposure. Proc. Soc. Exp. Biol. Med. 2000, 223, 170-174.
    • (2000) Proc. Soc. Exp. Biol. Med. , vol.223 , pp. 170-174
    • Lee, J.1    Jiang, S.2    Levine, N.3    Watson, R.R.4
  • 329
    • 0037224749 scopus 로고    scopus 로고
    • Supplementation with beta-carotene or a similar amount of mixed carotenoids protects humans from UV-induced erythema
    • Heinrich, U.; Gartner, C.; Wiebusch, M.; Eichler, O.; Sies, H.; Tronnier, H.; Stahl, W. Supplementation with beta-carotene or a similar amount of mixed carotenoids protects humans from UV-induced erythema. J. Nutr. 2003, 133, 98-101.
    • (2003) J. Nutr. , vol.133 , pp. 98-101
    • Heinrich, U.1    Gartner, C.2    Wiebusch, M.3    Eichler, O.4    Sies, H.5    Tronnier, H.6    Stahl, W.7
  • 330
    • 0028670506 scopus 로고
    • beta-Carotene quenches singlet oxygen formed by isolated photosystem II reaction centers
    • Telfer, A.; Dhami, S.; Bishop, S.M.; Phillips, D.; Barber, J. beta-Carotene quenches singlet oxygen formed by isolated photosystem II reaction centers. Biochemistry 1994, 33, 14469-14474.
    • (1994) Biochemistry , vol.33 , pp. 14469-14474
    • Telfer, A.1    Dhami, S.2    Bishop, S.M.3    Phillips, D.4    Barber, J.5
  • 331
    • 0028178121 scopus 로고
    • UVA-induced peroxidation of lipid in the dried film state
    • Bose, B.; Chatterjee, S.N. UVA-induced peroxidation of lipid in the dried film state. J. Photochem. Photobiol. B 1994, 23, 119-123.
    • (1994) J. Photochem. Photobiol. B , vol.23 , pp. 119-123
    • Bose, B.1    Chatterjee, S.N.2
  • 334
    • 77449147298 scopus 로고    scopus 로고
    • Skin photoprotection by natural polyphenols: Anti-inflammatory, antioxidant and DNA repair mechanisms
    • Nichols, J.A.; Katiyar, S.K. Skin photoprotection by natural polyphenols: Anti-inflammatory, antioxidant and DNA repair mechanisms. Arch. Dermatol. Res. 2010, 302, 71-83.
    • (2010) Arch. Dermatol. Res. , vol.302 , pp. 71-83
    • Nichols, J.A.1    Katiyar, S.K.2
  • 335
    • 0027692047 scopus 로고
    • Protection against ultraviolet B radiation-induced effects in the skin of SKH-1 hairless mice by a polyphenolic fraction isolated from green tea
    • Agarwal, R.; Katiyar, S.K.; Khan, S.G.; Mukhtar, H. Protection against ultraviolet B radiation-induced effects in the skin of SKH-1 hairless mice by a polyphenolic fraction isolated from green tea. Photochem. Photobiol. 1993, 58, 695-700.
    • (1993) Photochem. Photobiol. , vol.58 , pp. 695-700
    • Agarwal, R.1    Katiyar, S.K.2    Khan, S.G.3    Mukhtar, H.4
  • 336
    • 0029398608 scopus 로고
    • Protection against ultraviolet-B radiation-induced local and systemic suppression of contact hypersensitivity and edema responses in C3H/HeN mice by green tea polyphenols
    • Katiyar, S.K.; Elmets, C.A.; Agarwal, R.; Mukhtar, H. Protection against ultraviolet-B radiation-induced local and systemic suppression of contact hypersensitivity and edema responses in C3H/HeN mice by green tea polyphenols. Photochem. Photobiol. 1995, 62, 855-861.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 855-861
    • Katiyar, S.K.1    Elmets, C.A.2    Agarwal, R.3    Mukhtar, H.4
  • 338
    • 0035374660 scopus 로고    scopus 로고
    • Green tea polyphenolic antioxidants and skin photoprotection (Review)
    • Katiyar, S.K.; Elmets, C.A. Green tea polyphenolic antioxidants and skin photoprotection (Review). Int. J. Oncol. 2001, 18, 1307-1313.
    • (2001) Int. J. Oncol. , vol.18 , pp. 1307-1313
    • Katiyar, S.K.1    Elmets, C.A.2
  • 340
    • 13844297030 scopus 로고    scopus 로고
    • Inhibition of carcinogenesis by polyphenols: Evidence from laboratory investigations
    • Lambert, J.D.; Hong, J.; Yang, G.Y.; Liao, J.; Yang, C.S. Inhibition of carcinogenesis by polyphenols: Evidence from laboratory investigations. Am. J. Clin. Nutr. 2005, 81, 284S-291S.
    • (2005) Am. J. Clin. Nutr. , vol.81
    • Lambert, J.D.1    Hong, J.2    Yang, G.Y.3    Liao, J.4    Yang, C.S.5
  • 341
    • 0028036392 scopus 로고
    • Enzymic and non-enzymic antioxidants in epidermis and dermis of human skin
    • Shindo, Y.; Witt, E.; Han, D.; Epstein, W.; Packer, L. Enzymic and non-enzymic antioxidants in epidermis and dermis of human skin. J. Investig. Dermatol. 1994, 102, 122-124.
    • (1994) J. Investig. Dermatol. , vol.102 , pp. 122-124
    • Shindo, Y.1    Witt, E.2    Han, D.3    Epstein, W.4    Packer, L.5
  • 342
    • 0036710515 scopus 로고    scopus 로고
    • Effects of coenzyme Q(10) administration on its tissue concentrations, mitochondrial oxidant generation, and oxidative stress in the rat
    • Kwong, L.K.; Kamzalov, S.; Rebrin, I.; Bayne, A.C.; Jana, C.K.; Morris, P.; Forster, M.J.; Sohal, R.S. Effects of coenzyme Q(10) administration on its tissue concentrations, mitochondrial oxidant generation, and oxidative stress in the rat. Free Radic. Biol. Med. 2002, 33, 627-638.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 627-638
    • Kwong, L.K.1    Kamzalov, S.2    Rebrin, I.3    Bayne, A.C.4    Jana, C.K.5    Morris, P.6    Forster, M.J.7    Sohal, R.S.8
  • 343
    • 31344439942 scopus 로고    scopus 로고
    • Effect of coenzyme Q10 intake on endogenous coenzyme Q content, mitochondrial electron transport chain, antioxidative defenses, and life span of mice
    • Sohal, R.S.; Kamzalov, S.; Sumien, N.; Ferguson, M.; Rebrin, I.; Heinrich, K.R.; Forster, M.J. Effect of coenzyme Q10 intake on endogenous coenzyme Q content, mitochondrial electron transport chain, antioxidative defenses, and life span of mice. Free Radic. Biol. Med. 2006, 40, 480-487.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 480-487
    • Sohal, R.S.1    Kamzalov, S.2    Sumien, N.3    Ferguson, M.4    Rebrin, I.5    Heinrich, K.R.6    Forster, M.J.7
  • 346
    • 80054867485 scopus 로고    scopus 로고
    • Biochemical rationale and experimental data on the antiaging properties of CoQ(10) at skin level
    • Blatt, T.; Littarru, G.P. Biochemical rationale and experimental data on the antiaging properties of CoQ(10) at skin level. BioFactors 2011, 37, 381-385.
    • (2011) BioFactors , vol.37 , pp. 381-385
    • Blatt, T.1    Littarru, G.P.2
  • 348
    • 84864718454 scopus 로고    scopus 로고
    • Functions, applications and production of 2-O-D-glucopyranosyl-L-ascorbic acid
    • Han, R.; Liu, L.; Li, J.; Du, G.; Chen, J. Functions, applications and production of 2-O-D-glucopyranosyl-L-ascorbic acid. Appl. Microbiol. Biotech. 2012, 95, 313-320.
    • (2012) Appl. Microbiol. Biotech. , vol.95 , pp. 313-320
    • Han, R.1    Liu, L.2    Li, J.3    Du, G.4    Chen, J.5
  • 349
    • 84885945970 scopus 로고    scopus 로고
    • Updates on chemical and biological research on botanical ingredients in dietary supplements
    • doi:10.1007/s00216-012-6691-2
    • Pawar, R.S.; Tamta, H.; Ma, J.; Krynitsky, A.J.; Grundel, E.; Wamer, W.G.; Rader, J.I. Updates on chemical and biological research on botanical ingredients in dietary supplements. Anal. Bioanal. Chem. 2013, doi:10.1007/s00216-012-6691-2.
    • (2013) Anal. Bioanal. Chem.
    • Pawar, R.S.1    Tamta, H.2    Ma, J.3    Krynitsky, A.J.4    Grundel, E.5    Wamer, W.G.6    Rader, J.I.7
  • 351
    • 4344691399 scopus 로고    scopus 로고
    • A review of the epidemiological evidence for the 'antioxidant hypothesis'
    • Stanner, S.A.; Hughes, J.; Kelly, C.N.; Buttriss, J. A review of the epidemiological evidence for the 'antioxidant hypothesis'. Public Health Nutr. 2004, 7, 407-422.
    • (2004) Public Health Nutr. , vol.7 , pp. 407-422
    • Stanner, S.A.1    Hughes, J.2    Kelly, C.N.3    Buttriss, J.4
  • 352
    • 84857825705 scopus 로고    scopus 로고
    • Do dietary supplements have beneficial health effects in industrialized nations: What is the evidence?
    • Marik, P.E.; Flemmer, M. Do dietary supplements have beneficial health effects in industrialized nations: What is the evidence? J. Parenteral Enteral Nutr. 2012, 36, 159-168.
    • (2012) J. Parenteral Enteral Nutr. , vol.36 , pp. 159-168
    • Marik, P.E.1    Flemmer, M.2
  • 353
    • 80054732967 scopus 로고    scopus 로고
    • Dietary supplements and mortality rate in older women: The Iowa Women's Health Study
    • Mursu, J.; Robien, K.; Harnack, L.J.; Park, K.; Jacobs, D.R., Jr. Dietary supplements and mortality rate in older women: The Iowa Women's Health Study. Arch. Intern. Med. 2011, 171, 1625-1633.
    • (2011) Arch. Intern. Med. , vol.171 , pp. 1625-1633
    • Mursu, J.1    Robien, K.2    Harnack, L.J.3    Park, K.4    Jacobs Jr., D.R.5
  • 357
    • 84865165560 scopus 로고    scopus 로고
    • Mitochondrial function and dysfunction: An update
    • Davis, R.E.; Williams, M. Mitochondrial function and dysfunction: An update. J. Pharmacol. Exp. Ther. 2012, 342, 598-607.
    • (2012) J. Pharmacol. Exp. Ther. , vol.342 , pp. 598-607
    • Davis, R.E.1    Williams, M.2
  • 359
    • 3042717908 scopus 로고    scopus 로고
    • Pilot trial of high dosages of coenzyme Q10 in patients with Parkinson's disease
    • Shults, C.W.; Flint Beal, M.; Song, D.; Fontaine, D. Pilot trial of high dosages of coenzyme Q10 in patients with Parkinson's disease. Exp. Neurol. 2004, 188, 491-494.
    • (2004) Exp. Neurol. , vol.188 , pp. 491-494
    • Shults, C.W.1    Flint Beal, M.2    Song, D.3    Fontaine, D.4
  • 360
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Ernster, L.; Dallner, G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim. Biophys. 1995, 1271, 195-204.
    • (1995) Biochim. Biophys. , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 361
    • 0028847947 scopus 로고
    • Uptake of dietary coenzyme Q supplement is limited in rats
    • Zhang, Y.; Aberg, F.; Appelkvist, E.L.; Dallner, G.; Ernster, L. Uptake of dietary coenzyme Q supplement is limited in rats. J. Nutr. 1995, 125, 446-453.
    • (1995) J. Nutr. , vol.125 , pp. 446-453
    • Zhang, Y.1    Aberg, F.2    Appelkvist, E.L.3    Dallner, G.4    Ernster, L.5
  • 362
    • 0032555066 scopus 로고    scopus 로고
    • Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects
    • Matthews, R.T.; Yang, L.; Browne, S.; Baik, M.; Beal, M.F. Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects. Proc. Natl. Acad. Sci. USA 1998, 95, 8892-8897.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8892-8897
    • Matthews, R.T.1    Yang, L.2    Browne, S.3    Baik, M.4    Beal, M.F.5
  • 366
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • Murphy, M.P.; Smith, R.A. Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Ann. Rev. Pharmacol. Toxicol. 2007, 47, 629-656.
    • (2007) Ann. Rev. Pharmacol. Toxicol. , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.2
  • 367
    • 37648998990 scopus 로고    scopus 로고
    • A biochemical approach to the problem of aging: "Megaproject" on membrane-penetrating ions. The first results and prospects
    • Skulachev, V.P. A biochemical approach to the problem of aging: "Megaproject" on membrane-penetrating ions. The first results and prospects. Biochemistry (Mosc.) 2007, 72, 1385-1396.
    • (2007) Biochemistry (Mosc.) , vol.72 , pp. 1385-1396
    • Skulachev, V.P.1
  • 370
    • 84867089289 scopus 로고    scopus 로고
    • Engineering of blended nanoparticle platform for delivery of mitochondria-acting therapeutics
    • Marrache, S.; Dhar, S. Engineering of blended nanoparticle platform for delivery of mitochondria-acting therapeutics. Proc. Natl. Acad. Sci. USA 2012, 109, 16288-16293.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16288-16293
    • Marrache, S.1    Dhar, S.2
  • 371
    • 80655125027 scopus 로고    scopus 로고
    • Translocation of heme oxygenase-1 to mitochondria is a novel cytoprotective mechanism against non-steroidal anti-inflammatory drug-induced mitochondrial oxidative stress, apoptosis, and gastric mucosal injury
    • Bindu, S.; Pal, C.; Dey, S.; Goyal, M.; Alam, A.; Iqbal, M.S.; Dutta, S.; Sarkar, S.; Kumar, R.; Maity, P.; et al. Translocation of heme oxygenase-1 to mitochondria is a novel cytoprotective mechanism against non-steroidal anti-inflammatory drug-induced mitochondrial oxidative stress, apoptosis, and gastric mucosal injury. J. Biol. Chem. 2011, 286, 39387-39402.
    • (2011) J. Biol. Chem. , vol.286 , pp. 39387-39402
    • Bindu, S.1    Pal, C.2    Dey, S.3    Goyal, M.4    Alam, A.5    Iqbal, M.S.6    Dutta, S.7    Sarkar, S.8    Kumar, R.9    Maity, P.10


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