메뉴 건너뛰기




Volumn 1840, Issue 2, 2014, Pages 906-912

Peroxiredoxins as biomarkers of oxidative stress

Author keywords

Biomarker; Hydrogen peroxide; Hyperoxidation; Oxidation; Oxidative stress; Peroxiredoxin

Indexed keywords

BIOLOGICAL MARKER; DIMER; HYDROPEROXIDE; PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 2; WATER; ENDOTOXIN; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; MITOGEN ACTIVATED PROTEIN KINASE P38; N ETHYLMALEIMIDE; PEROXIREDOXIN 3; PEROXIREDOXIN 4; PEROXIREDOXIN 6; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFIREDOXIN; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84890116227     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.08.001     Document Type: Review
Times cited : (141)

References (66)
  • 1
    • 79951643450 scopus 로고    scopus 로고
    • Multiple functions of peroxiredoxins: Peroxidases, sensors and regulators of the intracellular messenger H(2)O(2), and protein chaperones
    • S.G. Rhee, and H.A. Woo Multiple functions of peroxiredoxins: peroxidases, sensors and regulators of the intracellular messenger H(2)O(2), and protein chaperones Antioxid. Redox Signal. 15 2011 781 794
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 781-794
    • Rhee, S.G.1    Woo, H.A.2
  • 2
    • 0037222255 scopus 로고    scopus 로고
    • Structure, mechanism and regulation of peroxiredoxins
    • DOI 10.1016/S0968-0004(02)00003-8, PII S0968000402000038
    • Z.A. Wood, E. Schroder, J.R. Harris, and L.B. Poole Structure, mechanism and regulation of peroxiredoxins Trends Biochem. Sci. 28 2003 32 40 (Pubitemid 36051004)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 32-40
    • Wood, Z.A.1    Schroder, E.2    Harris, J.R.3    Poole, L.B.4
  • 3
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • DOI 10.1074/jbc.M206626200
    • K.S. Yang, S.W. Kang, H.A. Woo, S.C. Hwang, H.Z. Chae, K. Kim, and S.G. Rhee Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid J. Biol. Chem. 277 2002 38029 38036 (Pubitemid 35154654)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38029-38036
    • Yang, K.-S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6    Rhee, S.G.7
  • 4
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • DOI 10.1126/science.1080405
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653 (Pubitemid 36520591)
    • (2003) Science , vol.300 , Issue.5619 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 5
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins
    • DOI 10.1021/bi012173m
    • Z.A. Wood, L.B. Poole, R.R. Hantgan, and P.A. Karplus Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins Biochemistry 41 2002 5493 5504 (Pubitemid 34429383)
    • (2002) Biochemistry , vol.41 , Issue.17 , pp. 5493-5504
    • Wood, Z.A.1    Poole, L.B.2    Hantgan, R.R.3    Karplus, P.A.4
  • 6
    • 23244466487 scopus 로고    scopus 로고
    • Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin
    • DOI 10.1021/bi050448i
    • D. Parsonage, D.S. Youngblood, G.N. Sarma, Z.A. Wood, P.A. Karplus, and L.B. Poole Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin Biochemistry 44 2005 10583 10592 (Pubitemid 41098235)
    • (2005) Biochemistry , vol.44 , Issue.31 , pp. 10583-10592
    • Parsonage, D.1    Youngblood, D.S.2    Sarma, G.N.3    Wood, Z.A.4    Karplus, P.A.5    Poole, L.B.6
  • 7
    • 67349155642 scopus 로고    scopus 로고
    • The oligomeric conformation of peroxiredoxins links redox state to function
    • S. Barranco-Medina, J.J. Lazaro, and K.J. Dietz The oligomeric conformation of peroxiredoxins links redox state to function FEBS Lett. 583 2009 1809 1816
    • (2009) FEBS Lett. , vol.583 , pp. 1809-1816
    • Barranco-Medina, S.1    Lazaro, J.J.2    Dietz, K.J.3
  • 9
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • C.C. Winterbourn, and M.B. Hampton Thiol chemistry and specificity in redox signaling Free Radic. Biol. Med. 45 2008 549 561
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 12
    • 2942532835 scopus 로고    scopus 로고
    • Biochemical characterization of 2-cys peroxiredoxins from Schistosoma mansoni
    • DOI 10.1074/jbc.M401748200
    • A.A. Sayed, and D.L. Williams Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni J. Biol. Chem. 279 2004 26159 26166 (Pubitemid 38798761)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 26159-26166
    • Sayed, A.A.1    Williams, D.L.2
  • 13
    • 38749120994 scopus 로고    scopus 로고
    • Kinetics of peroxiredoxins and their role in the decomposition of peroxynitrite
    • M. Trujillo, G. Ferrer-Sueta, L. Thomson, L. Flohe, and R. Radi Kinetics of peroxiredoxins and their role in the decomposition of peroxynitrite Subcell. Biochem. 44 2007 83 113
    • (2007) Subcell. Biochem. , vol.44 , pp. 83-113
    • Trujillo, M.1    Ferrer-Sueta, G.2    Thomson, L.3    Flohe, L.4    Radi, R.5
  • 15
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization
    • DOI 10.1128/JB.183.6.1961-1973.2001
    • L.M. Baker, A. Raudonikiene, P.S. Hoffman, and L.B. Poole Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization J. Bacteriol. 183 2001 1961 1973 (Pubitemid 32225991)
    • (2001) Journal of Bacteriology , vol.183 , Issue.6 , pp. 1961-1973
    • Baker, L.M.S.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 17
    • 33845917628 scopus 로고    scopus 로고
    • Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: Rate constants by competitive kinetics
    • DOI 10.1016/j.freeradbiomed.2006.10.042, PII S0891584906006733
    • R. Ogusucu, D. Rettori, D.C. Munhoz, L.E. Netto, and O. Augusto Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics Free Radic. Biol. Med. 42 2007 326 334 (Pubitemid 46038040)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.3 , pp. 326-334
    • Ogusucu, R.1    Rettori, D.2    Munhoz, D.C.3    Soares Netto, L.E.4    Augusto, O.5
  • 19
    • 77956171017 scopus 로고    scopus 로고
    • Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization
    • A. Hall, D. Parsonage, L.B. Poole, and P.A. Karplus Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization J. Mol. Biol. 402 2010 194 209
    • (2010) J. Mol. Biol. , vol.402 , pp. 194-209
    • Hall, A.1    Parsonage, D.2    Poole, L.B.3    Karplus, P.A.4
  • 21
    • 0343953384 scopus 로고    scopus 로고
    • Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution
    • DOI 10.1016/S0969-2126(00)00147-7
    • E. Schroder, J.A. Littlechild, A.A. Lebedev, N. Errington, A.A. Vagin, and M.N. Isupov Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution Structure 8 2000 605 615 (Pubitemid 30409313)
    • (2000) Structure , vol.8 , Issue.6 , pp. 605-615
    • Schroder, E.1    Littlechild, J.A.2    Lebedev, A.A.3    Errington, N.4    Vagin, A.A.5    Isupov, M.N.6
  • 22
    • 84877886960 scopus 로고    scopus 로고
    • Hyperoxidation of peroxiredoxins 2 and 3: Rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine
    • A.V. Peskin, N. Dickerhof, R.A. Poynton, L.N. Paton, P.E. Pace, M.B. Hampton, and C.C. Winterbourn Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine J. Biol. Chem. 288 2013 14170 14177
    • (2013) J. Biol. Chem. , vol.288 , pp. 14170-14177
    • Peskin, A.V.1    Dickerhof, N.2    Poynton, R.A.3    Paton, L.N.4    Pace, P.E.5    Hampton, M.B.6    Winterbourn, C.C.7
  • 23
    • 0037067763 scopus 로고    scopus 로고
    • Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation
    • DOI 10.1074/jbc.M110432200
    • T.S. Chang, W. Jeong, S.Y. Choi, S. Yu, S.W. Kang, and S.G. Rhee Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation J. Biol. Chem. 277 2002 25370 25376 (Pubitemid 34951848)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25370-25376
    • Chang, T.-S.1    Jeong, W.2    Choi, S.Y.3    Yu, S.4    Kang, S.W.5    Rhee, S.G.6
  • 25
    • 79953871561 scopus 로고    scopus 로고
    • Glutathionylation of peroxiredoxin i induces decamer to dimers dissociation with concomitant loss of chaperone activity
    • J.W. Park, G. Piszczek, S.G. Rhee, and P.B. Chock Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity Biochemistry 50 2011 3204 3210
    • (2011) Biochemistry , vol.50 , pp. 3204-3210
    • Park, J.W.1    Piszczek, G.2    Rhee, S.G.3    Chock, P.B.4
  • 26
    • 84876546405 scopus 로고    scopus 로고
    • Multilevel regulation of 2-Cys peroxiredoxin reaction cycle by S-nitrosylation
    • R. Engelman, P. Weisman-Shomer, T. Ziv, J. Xu, E.S. Arner, and M. Benhar Multilevel regulation of 2-Cys peroxiredoxin reaction cycle by S-nitrosylation J. Biol. Chem. 288 2013 11312 11324
    • (2013) J. Biol. Chem. , vol.288 , pp. 11312-11324
    • Engelman, R.1    Weisman-Shomer, P.2    Ziv, T.3    Xu, J.4    Arner, E.S.5    Benhar, M.6
  • 27
    • 76749102420 scopus 로고    scopus 로고
    • Inactivation of peroxiredoxin i by phosphorylation allows localized H(2)O(2) accumulation for cell signaling
    • H.A. Woo, S.H. Yim, D.H. Shin, D. Kang, D.Y. Yu, and S.G. Rhee Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling Cell 140 2010 517 528
    • (2010) Cell , vol.140 , pp. 517-528
    • Woo, H.A.1    Yim, S.H.2    Shin, D.H.3    Kang, D.4    Yu, D.Y.5    Rhee, S.G.6
  • 28
    • 0346850874 scopus 로고    scopus 로고
    • Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence
    • DOI 10.1074/jbc.C300428200
    • H.A. Woo, S.W. Kang, H.K. Kim, K.S. Yang, H.Z. Chae, and S.G. Rhee Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid - immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence J. Biol. Chem. 278 2003 47361 47364 (Pubitemid 37523174)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , pp. 47361-47364
    • Woo, H.A.1    Kang, S.W.2    Kim, H.K.3    Yang, K.-S.4    Chae, H.Z.5    Rhee, S.G.6
  • 29
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. Cerevisiae sulphiredoxin
    • DOI 10.1038/nature02075
    • B. Biteau, J. Labarre, and M.B. Toledano ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin Nature 425 2003 980 984 (Pubitemid 37376931)
    • (2003) Nature , vol.425 , Issue.6961 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 30
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • DOI 10.1074/jbc.M409482200
    • T.S. Chang, W. Jeong, H.A. Woo, S.M. Lee, S. Park, and S.G. Rhee Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine J. Biol. Chem. 279 2004 50994 51001 (Pubitemid 40017840)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50994-51001
    • Chang, T.-S.1    Jeong, W.2    Hyun, A.W.3    Sun, M.L.4    Park, S.5    Sue, G.R.6
  • 31
    • 84862186506 scopus 로고    scopus 로고
    • Oxidation of 2-cys peroxiredoxins in human endothelial cells by hydrogen peroxide, hypochlorous acid, and chloramines
    • M.M. Stacey, M.C. Vissers, and C.C. Winterbourn Oxidation of 2-cys peroxiredoxins in human endothelial cells by hydrogen peroxide, hypochlorous acid, and chloramines Antioxid. Redox Signal. 17 2012 411 421
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 411-421
    • Stacey, M.M.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 32
    • 84863463209 scopus 로고    scopus 로고
    • Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression
    • W. Jeong, S.H. Bae, M.B. Toledano, and S.G. Rhee Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression Free Radic. Biol. Med. 53 2012 447 456
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 447-456
    • Jeong, W.1    Bae, S.H.2    Toledano, M.B.3    Rhee, S.G.4
  • 33
    • 73849144014 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling
    • A.G. Cox, C.C. Winterbourn, and M.B. Hampton Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling Biochem. J. 425 2010 313 325
    • (2010) Biochem. J. , vol.425 , pp. 313-325
    • Cox, A.G.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 34
    • 20544459926 scopus 로고    scopus 로고
    • Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells
    • DOI 10.1042/BJ20050337
    • J.W. Baty, M.B. Hampton, and C.C. Winterbourn Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells Biochem. J. 389 2005 785 795 (Pubitemid 41117338)
    • (2005) Biochemical Journal , vol.389 , Issue.3 , pp. 785-795
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 35
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • J.W. Baty, M.B. Hampton, and C.C. Winterbourn Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis Proteomics 2 2002 1261 1266
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 37
    • 78650764507 scopus 로고    scopus 로고
    • Measuring the redox state of cellular peroxiredoxins by immunoblotting
    • A.G. Cox, C.C. Winterbourn, and M.B. Hampton Measuring the redox state of cellular peroxiredoxins by immunoblotting Methods Enzymol. 474 2010 51 66
    • (2010) Methods Enzymol. , vol.474 , pp. 51-66
    • Cox, A.G.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 38
    • 61749089821 scopus 로고    scopus 로고
    • Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion
    • V. Kumar, N. Kitaeff, M.B. Hampton, M.B. Cannell, and C.C. Winterbourn Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion FEBS Lett. 583 2009 997 1000
    • (2009) FEBS Lett. , vol.583 , pp. 997-1000
    • Kumar, V.1    Kitaeff, N.2    Hampton, M.B.3    Cannell, M.B.4    Winterbourn, C.C.5
  • 40
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
    • DOI 10.1182/blood-2006-09-048728
    • F.M. Low, M.B. Hampton, A.V. Peskin, and C.C. Winterbourn Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte Blood 109 2007 2611 2617 (Pubitemid 46425910)
    • (2007) Blood , vol.109 , Issue.6 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3    Winterbourn, C.C.4
  • 41
    • 84881158368 scopus 로고    scopus 로고
    • Neutrophil-mediated oxidation of erythrocyte peroxiredoxin 2 as a potential marker of oxidative stress in inflammation
    • S.B. Bayer, G. Maghzal, R. Stocker, M.B. Hampton, and C.C. Winterbourn Neutrophil-mediated oxidation of erythrocyte peroxiredoxin 2 as a potential marker of oxidative stress in inflammation FASEB J. 27 2013 3315 3322
    • (2013) FASEB J. , vol.27 , pp. 3315-3322
    • Bayer, S.B.1    Maghzal, G.2    Stocker, R.3    Hampton, M.B.4    Winterbourn, C.C.5
  • 42
    • 46649084593 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin 3 is rapidly oxidised in cells treated with isothiocyanates
    • K.K. Brown, S.E. Eriksson, E.S.J. Arner, and M.B. Hampton Mitochondrial peroxiredoxin 3 is rapidly oxidised in cells treated with isothiocyanates Free Radic. Biol. Med. 45 2008 494 502
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 494-502
    • Brown, K.K.1    Eriksson, S.E.2    Arner, E.S.J.3    Hampton, M.B.4
  • 43
    • 39949083765 scopus 로고    scopus 로고
    • Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis
    • A.G. Cox, J.M. Pullar, G. Hughes, E.C. Ledgerwood, and M.B. Hampton Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis Free Radic. Biol. Med. 44 2008 1001 1009
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1001-1009
    • Cox, A.G.1    Pullar, J.M.2    Hughes, G.3    Ledgerwood, E.C.4    Hampton, M.B.5
  • 44
    • 53649092133 scopus 로고    scopus 로고
    • The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation
    • A.G. Cox, K.K. Brown, E.S. Arner, and M.B. Hampton The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation Biochem. Pharmacol. 76 2008 1097 1109
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1097-1109
    • Cox, A.G.1    Brown, K.K.2    Arner, E.S.3    Hampton, M.B.4
  • 45
    • 77950370157 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin
    • K.K. Brown, A.G. Cox, and M.B. Hampton Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin FEBS Lett. 584 2010 1257 1262
    • (2010) FEBS Lett. , vol.584 , pp. 1257-1262
    • Brown, K.K.1    Cox, A.G.2    Hampton, M.B.3
  • 46
    • 58649096345 scopus 로고    scopus 로고
    • The effects of acrolein on peroxiredoxins, thioredoxins, and thioredoxin reductase in human bronchial epithelial cells
    • C.R. Myers, and J.M. Myers The effects of acrolein on peroxiredoxins, thioredoxins, and thioredoxin reductase in human bronchial epithelial cells Toxicology 257 2009 95 104
    • (2009) Toxicology , vol.257 , pp. 95-104
    • Myers, C.R.1    Myers, J.M.2
  • 47
    • 79851516124 scopus 로고    scopus 로고
    • The intracellular redox stress caused by hexavalent chromium is selective for proteins that have key roles in cell survival and thiol redox control
    • J.M. Myers, W.E. Antholine, and C.R. Myers The intracellular redox stress caused by hexavalent chromium is selective for proteins that have key roles in cell survival and thiol redox control Toxicology 281 2011 37 47
    • (2011) Toxicology , vol.281 , pp. 37-47
    • Myers, J.M.1    Antholine, W.E.2    Myers, C.R.3
  • 48
    • 70350034011 scopus 로고    scopus 로고
    • The effects of hexavalent chromium on thioredoxin reductase and peroxiredoxins in human bronchial epithelial cells
    • J.M. Myers, and C.R. Myers The effects of hexavalent chromium on thioredoxin reductase and peroxiredoxins in human bronchial epithelial cells Free Radic. Biol. Med. 47 2009 1477 1485
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1477-1485
    • Myers, J.M.1    Myers, C.R.2
  • 49
    • 84875974995 scopus 로고    scopus 로고
    • Redox proteomics of thiol proteins in mouse heart during ischemia/reperfusion using ICAT reagents and mass spectrometry
    • V. Kumar, T. Kleffmann, M.B. Hampton, M.B. Cannell, and C.C. Winterbourn Redox proteomics of thiol proteins in mouse heart during ischemia/reperfusion using ICAT reagents and mass spectrometry Free Radic. Biol. Med. 58 2013 109 117
    • (2013) Free Radic. Biol. Med. , vol.58 , pp. 109-117
    • Kumar, V.1    Kleffmann, T.2    Hampton, M.B.3    Cannell, M.B.4    Winterbourn, C.C.5
  • 50
    • 79958242400 scopus 로고    scopus 로고
    • Assessment of redox changes to hydrogen peroxide-sensitive proteins during EGF signaling
    • S.L. Cuddihy, C.C. Winterbourn, and M.B. Hampton Assessment of redox changes to hydrogen peroxide-sensitive proteins during EGF signaling Antioxid. Redox Signal. 15 2011 167 174
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 167-174
    • Cuddihy, S.L.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 51
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds
    • DOI 10.1074/jbc.273.32.20096
    • S. Gromer, L.D. Arscott, C.H. Williams Jr., R.H. Schirmer, and K. Becker Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds J. Biol. Chem. 273 1998 20096 20101 (Pubitemid 28377564)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 20096-20101
    • Gromer, S.1    Arscott, L.D.2    Williams Jr., C.H.3    Schirmeri, R.H.4    Becker, K.5
  • 52
    • 0034906096 scopus 로고    scopus 로고
    • Oxidized forms of peroxiredoxins and DJ-1 on two-dimensional gels increased in response to sublethal levels of paraquat
    • A. Mitsumoto, Y. Nakagawa, A. Takeuchi, K. Okawa, A. Iwamatsu, and Y. Takanezawa Oxidized forms of peroxiredoxins and DJ-1 on two-dimensional gels increased in response to sublethal levels of paraquat Free Radic. Res. 35 2001 301 310 (Pubitemid 32734231)
    • (2001) Free Radical Research , vol.35 , Issue.3 , pp. 301-310
    • Mitsumoto, A.1    Nakagawa, Y.2    Takeuchi, A.3    Okawa, K.4    Iwamatsu, A.5    Takanezawa, Y.6
  • 54
    • 64549111760 scopus 로고    scopus 로고
    • Induction of sulfiredoxin via an Nrf2-dependent pathway and hyperoxidation of peroxiredoxin III in the lungs of mice exposed to hyperoxia
    • S.H. Bae, H.A. Woo, S.H. Sung, H.E. Lee, S.K. Lee, I.S. Kil, and S.G. Rhee Induction of sulfiredoxin via an Nrf2-dependent pathway and hyperoxidation of peroxiredoxin III in the lungs of mice exposed to hyperoxia Antioxid. Redox Signal. 11 2009 937 948
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 937-948
    • Bae, S.H.1    Woo, H.A.2    Sung, S.H.3    Lee, H.E.4    Lee, S.K.5    Kil, I.S.6    Rhee, S.G.7
  • 57
    • 79952224744 scopus 로고    scopus 로고
    • Concerted action of sulfiredoxin and peroxiredoxin i protects against alcohol-induced oxidative injury in mouse liver
    • S.H. Bae, S.H. Sung, E.J. Cho, S.K. Lee, H.E. Lee, H.A. Woo, D.Y. Yu, I.S. Kil, and S.G. Rhee Concerted action of sulfiredoxin and peroxiredoxin I protects against alcohol-induced oxidative injury in mouse liver Hepatology 53 2011 945 953
    • (2011) Hepatology , vol.53 , pp. 945-953
    • Bae, S.H.1    Sung, S.H.2    Cho, E.J.3    Lee, S.K.4    Lee, H.E.5    Woo, H.A.6    Yu, D.Y.7    Kil, I.S.8    Rhee, S.G.9
  • 58
    • 84862826137 scopus 로고    scopus 로고
    • Hyperoxidized peroxiredoxins in peripheral blood mononuclear cells of asthma patients is associated with asthma severity
    • H.S. Kwon, Y.J. Bae, K.A. Moon, Y.S. Lee, T. Lee, K.Y. Lee, T.B. Kim, C.S. Park, H.B. Moon, and Y.S. Cho Hyperoxidized peroxiredoxins in peripheral blood mononuclear cells of asthma patients is associated with asthma severity Life Sci. 90 2012 502 508
    • (2012) Life Sci. , vol.90 , pp. 502-508
    • Kwon, H.S.1    Bae, Y.J.2    Moon, K.A.3    Lee, Y.S.4    Lee, T.5    Lee, K.Y.6    Kim, T.B.7    Park, C.S.8    Moon, H.B.9    Cho, Y.S.10
  • 60
    • 79251566511 scopus 로고    scopus 로고
    • Circadian clocks in human red blood cells
    • J.S. O'Neill, and A.B. Reddy Circadian clocks in human red blood cells Nature 469 2011 498 503
    • (2011) Nature , vol.469 , pp. 498-503
    • O'Neill, J.S.1    Reddy, A.B.2
  • 61
    • 34447638199 scopus 로고    scopus 로고
    • Hyperoxidized peroxiredoxins and glyceraldehyde-3-phosphate dehydrogenase immunoreactivity and protein levels are changed in the gerbil hippocampal CA1 region after transient forebrain ischemia
    • DOI 10.1007/s11064-007-9345-6
    • I.K. Hwang, K.Y. Yoo, D.W. Kim, J.H. Choi, I.S. Lee, and M.H. Won Hyperoxidized peroxiredoxins and glyceraldehyde-3-phosphate dehydrogenase immunoreactivity and protein levels are changed in the gerbil hippocampal CA1 region after transient forebrain ischemia Neurochem. Res. 32 2007 1530 1538 (Pubitemid 47094414)
    • (2007) Neurochemical Research , vol.32 , Issue.9 , pp. 1530-1538
    • Hwang, I.K.1    Yoo, K.-Y.2    Kim, D.W.3    Choi, J.H.4    Lee, I.S.5    Won, M.H.6
  • 62
    • 67349089861 scopus 로고    scopus 로고
    • Expression and changes of hyperoxidized peroxiredoxins in non-pyramidal and polymorphic cells in the gerbil hippocampus during normal aging
    • K.Y. Yoo, O.K. Park, J. Yu, B. Yan, H. Li, C.H. Lee, J.H. Choi, D.W. Kim, I.K. Hwang, and M.H. Won Expression and changes of hyperoxidized peroxiredoxins in non-pyramidal and polymorphic cells in the gerbil hippocampus during normal aging Cell. Mol. Neurobiol. 29 2009 413 421
    • (2009) Cell. Mol. Neurobiol. , vol.29 , pp. 413-421
    • Yoo, K.Y.1    Park, O.K.2    Yu, J.3    Yan, B.4    Li, H.5    Lee, C.H.6    Choi, J.H.7    Kim, D.W.8    Hwang, I.K.9    Won, M.H.10
  • 63
    • 78650786227 scopus 로고    scopus 로고
    • Maternal undernutrition significantly impacts ovarian follicle number and increases ovarian oxidative stress in adult rat offspring
    • A.B. Bernal, M.H. Vickers, M.B. Hampton, R.A. Poynton, and D.M. Sloboda Maternal undernutrition significantly impacts ovarian follicle number and increases ovarian oxidative stress in adult rat offspring PLoS One 5 2010 e15558
    • (2010) PLoS One , vol.5 , pp. 15558
    • Bernal, A.B.1    Vickers, M.H.2    Hampton, M.B.3    Poynton, R.A.4    Sloboda, D.M.5
  • 64
    • 0042591328 scopus 로고    scopus 로고
    • Reaction mechanism of plant 2-Cys peroxiredoxin: Role of the C terminus and the quaternary structure
    • DOI 10.1074/jbc.M301145200
    • J. Konig, K. Lotte, R. Plessow, A. Brockhinke, M. Baier, and K.J. Dietz Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure J. Biol. Chem. 278 2003 24409 24420 (Pubitemid 37548592)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24409-24420
    • Konig, J.1    Lotte, K.2    Plessow, R.3    Brockhinke, A.4    Baier, M.5    Dietz, K.-J.6
  • 65
    • 35148883298 scopus 로고    scopus 로고
    • Bcl-2 over-expression promotes genomic instability by inhibiting apoptosis of cells exposed to hydrogen peroxide
    • DOI 10.1093/carcin/bgm093
    • A.G. Cox, and M.B. Hampton Bcl-2 over-expression promotes genomic instability by inhibiting apoptosis of cells exposed to hydrogen peroxide Carcinogenesis 28 2007 2166 2171 (Pubitemid 47543378)
    • (2007) Carcinogenesis , vol.28 , Issue.10 , pp. 2166-2171
    • Cox, A.G.1    Hampton, M.B.2
  • 66
    • 84862777700 scopus 로고    scopus 로고
    • Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival
    • A.M. Day, J.D. Brown, S.R. Taylor, J.D. Rand, B.A. Morgan, and E.A. Veal Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival Mol. Cell 45 2012 398 408
    • (2012) Mol. Cell , vol.45 , pp. 398-408
    • Day, A.M.1    Brown, J.D.2    Taylor, S.R.3    Rand, J.D.4    Morgan, B.A.5    Veal, E.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.