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Volumn 74, Issue , 2014, Pages 35-49

Hydrogen peroxide metabolism and sensing in human erythrocytes: A validated kinetic model and reappraisal of the role of peroxiredoxin II

Author keywords

Free radicals; Peroxiredoxin sulfinylation; Quantitative redox biology; Redox signaling; Systems biology; Thioredoxin

Indexed keywords

CATALASE; DITHIOL DERIVATIVE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; MONOMER; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PEROXIDASE; PEROXIREDOXIN 2; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN; THIOREDOXIN REDUCTASE; PEROXIREDOXIN; PRDX2 PROTEIN, HUMAN;

EID: 84904329372     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.06.007     Document Type: Article
Times cited : (62)

References (79)
  • 2
    • 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
  • 3
    • 74149084415 scopus 로고    scopus 로고
    • The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism
    • R.M. Johnson, Y.-S. Ho, D.-Y. Yu, F.A. Kuypers, Y. Ravindranath, and G.W. Goyette The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism Free Radic. Biol. Med. 48 2010 519 525
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 519-525
    • Johnson, R.M.1    Ho, Y.-S.2    Yu, D.-Y.3    Kuypers, F.A.4    Ravindranath, Y.5    Goyette, G.W.6
  • 6
    • 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
  • 7
    • 0028991435 scopus 로고
    • PHGPx and phospholipase A2/GPx: Comparative importance on the reduction of hydroperoxides in rat liver mitochondria
    • F. Antunes, A. Salvador, and R.E. Pinto PHGPx and phospholipase A2/GPx: comparative importance on the reduction of hydroperoxides in rat liver mitochondria Free Radic. Biol. Med. 19 1995 669 677
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 669-677
    • Antunes, F.1    Salvador, A.2    Pinto, R.E.3
  • 8
    • 0029355440 scopus 로고
    • Kinetic modelling of in vitro lipid peroxidation experiments - Low level validation of a model of in vivo lipid peroxidation
    • A. Salvador, F. Antunes, and R.E. Pinto Kinetic modelling of in vitro lipid peroxidation experiments - low level validation of a model of in vivo lipid peroxidation Free Radic. Res. 23 1995 151 172
    • (1995) Free Radic. Res. , vol.23 , pp. 151-172
    • Salvador, A.1    Antunes, F.2    Pinto, R.E.3
  • 9
    • 0029908304 scopus 로고    scopus 로고
    • Lipid peroxidation in mitochondrial inner membranes. I. An integrative kinetic model
    • DOI 10.1016/S0891-5849(96)00185-2
    • F. Antunes, A. Salvador, H.S. Marinho, R. Alves, and R.E. Pinto Lipid peroxidation in mitochondrial inner membranes. I. An integrative kinetic model Free Radic. Biol. Med. 21 1996 917 943 (Pubitemid 26365948)
    • (1996) Free Radical Biology and Medicine , vol.21 , Issue.7 , pp. 917-943
    • Antunes, F.1    Salvador, A.2    Marinho, H.S.3    Alves, R.4    Pinto, R.E.5
  • 10
    • 0035890104 scopus 로고    scopus 로고
    • Hydroperoxyl, superoxide and pH gradients in the mitochondrial matrix: A theoretical assessment
    • DOI 10.1016/S0891-5849(01)00707-9, PII S0891584901007079
    • A. Salvador, J. Sousa, and R.E. Pinto Hydroperoxyl, superoxide and pH gradients in the mitochondrial matrix: a theoretical assessment Free Radic. Biol. Med. 31 2001 1208 1215 (Pubitemid 33052496)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.10 , pp. 1208-1215
    • Salvador, A.1    Sousa, J.2    Pinto, R.E.3
  • 11
    • 0037096203 scopus 로고    scopus 로고
    • Why does SOD overexpression sometimes enhance, sometimes decrease, hydrogen peroxide production? A minimalist explanation
    • DOI 10.1016/S0891-5849(02)00861-4, PII S0891584902008614
    • R. Gardner, A. Salvador, and P. Moradas-Ferreira Why does SOD overexpression sometimes enhance, sometimes decrease, hydrogen peroxide production? A minimalist explanation Free Radic. Biol. Med. 32 2002 1351 1357 (Pubitemid 34607639)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.12 , pp. 1351-1357
    • Gardner, R.1    Salvador, A.2    Moradas-Ferreira, P.3
  • 14
    • 33747879504 scopus 로고    scopus 로고
    • Why does superoxide dismutase overexpression often increase hydrogen peroxide concentrations? An alternative explanation
    • DOI 10.1016/j.jtbi.2006.04.007, PII S0022519306001615
    • R. Gardner, P. Moradas-Ferreira, and A. Salvador Why does superoxide dismutase overexpression often increase hydrogen peroxide concentrations? An alternative explanation J. Theor. Biol. 242 2006 798 800 (Pubitemid 44291694)
    • (2006) Journal of Theoretical Biology , vol.242 , Issue.3 , pp. 798-800
    • Gardner, R.1    Moradas-Ferreira, P.2    Salvador, A.3
  • 16
    • 63549119474 scopus 로고    scopus 로고
    • Quantifying global tolerance of biochemical systems: Design implications for moiety-transfer cycles
    • P.M. B.M. Coelho, A. Salvador, and M.A. Savageau Quantifying global tolerance of biochemical systems: design implications for moiety-transfer cycles PLoS Comput. Biol. 5 2009 e1000319
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000319
    • Coelho, P.M.B.M.1    Salvador, A.2    Savageau, M.A.3
  • 17
    • 77954935933 scopus 로고    scopus 로고
    • A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses
    • N.J. Adimora, D.P. Jones, and M.L. Kemp A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses Antioxid. Redox Signaling 13 2010 731 743
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 731-743
    • Adimora, N.J.1    Jones, D.P.2    Kemp, M.L.3
  • 18
    • 77958545833 scopus 로고    scopus 로고
    • Relating mutant genotype to phenotype via quantitative behavior of the NADPH redox cycle in human erythrocytes
    • P.M. B.M. Coelho, A. Salvador, and M.A. Savageau Relating mutant genotype to phenotype via quantitative behavior of the NADPH redox cycle in human erythrocytes PLoS One 5 2010 e13031
    • (2010) PLoS One , vol.5 , pp. 13031
    • Coelho, P.M.B.M.1    Salvador, A.2    Savageau, M.A.3
  • 19
    • 78951478981 scopus 로고    scopus 로고
    • The logic of kinetic regulation in the thioredoxin system
    • C.S. Pillay, J.-H.S. Hofmeyr, and J.M. Rohwer The logic of kinetic regulation in the thioredoxin system BMC Syst. Biol. 5 2011 15
    • (2011) BMC Syst. Biol. , vol.5 , pp. 15
    • Pillay, C.S.1    Hofmeyr, J.-H.S.2    Rohwer, J.M.3
  • 21
    • 33745075591 scopus 로고    scopus 로고
    • Tools for kinetic modeling of biochemical networks
    • DOI 10.1038/nbt0606-667, PII N0606667
    • R. Alves, F. Antunes, and A. Salvador Tools for kinetic modeling of biochemical networks Nat. Biotechnol. 24 2006 667 672 (Pubitemid 43884436)
    • (2006) Nature Biotechnology , vol.24 , Issue.6 , pp. 667-672
    • Alves, R.1    Antunes, F.2    Salvador, A.3
  • 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
  • 25
    • 0031575851 scopus 로고    scopus 로고
    • Protein 7.2b of human erythrocyte membranes binds to calpromotin
    • DOI 10.1006/bbrc.1997.6278
    • R.B. Moore, and S.K. Shriver Protein 7.2b of human erythrocyte membranes binds to calpromotin Biochem. Biophys. Res. Commun. 232 1997 294 297 (Pubitemid 27216205)
    • (1997) Biochemical and Biophysical Research Communications , vol.232 , Issue.2 , pp. 294-297
    • Moore, R.B.1    Shriver, S.K.2
  • 26
    • 79953853832 scopus 로고    scopus 로고
    • Oxidative stress-dependent oligomeric status of erythrocyte peroxiredoxin II (PrxII) during storage under standard blood banking conditions
    • S. Rinalducci, G.M. DAmici, B. Blasi, and L. Zolla Oxidative stress-dependent oligomeric status of erythrocyte peroxiredoxin II (PrxII) during storage under standard blood banking conditions Biochimie 93 2011 845 853
    • (2011) Biochimie , vol.93 , pp. 845-853
    • Rinalducci, S.1    Damici, G.M.2    Blasi, B.3    Zolla, L.4
  • 30
    • 0015893027 scopus 로고
    • A branching reaction mechanism of glutathione reductase
    • B. Mannervik A branching reaction mechanism of glutathione reductase Biochem. Biophys. Res. Commun. 53 1973 1151 1158
    • (1973) Biochem. Biophys. Res. Commun. , vol.53 , pp. 1151-1158
    • Mannervik, B.1
  • 31
    • 0022376486 scopus 로고
    • Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress. A study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation
    • DOI 10.1111/j.1432-1033.1985.tb09030.x
    • D.R. Thorburn, and P.W. Kuchel Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress: a study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation Eur. J. Biochem. 150 1985 371 386 (Pubitemid 16237179)
    • (1985) European Journal of Biochemistry , vol.150 , Issue.2 , pp. 371-386
    • Thorburn, D.R.1    Kuchel, P.W.2
  • 32
    • 0017165455 scopus 로고
    • Glutathione reductase from human erythrocytes: Catalytic properties and aggregation
    • D.J. Worthington, and M.A. Rosemeyer Glutathione reductase from human erythrocytes: catalytic properties and aggregation Eur. J. Biochem. 67 1976 231 238
    • (1976) Eur. J. Biochem. , vol.67 , pp. 231-238
    • Worthington, D.J.1    Rosemeyer, M.A.2
  • 34
    • 0011235078 scopus 로고
    • The formation and catalytic role of catalase peroxide compound II
    • P. Nicholls The formation and catalytic role of catalase peroxide compound II Biochim. Biophys. Acta 81 1964 479 495
    • (1964) Biochim. Biophys. Acta , vol.81 , pp. 479-495
    • Nicholls, P.1
  • 35
    • 0033553562 scopus 로고    scopus 로고
    • Mechanisms of protection of catalase by NADPH: Kinetics and stoichiometry
    • H.N. Kirkman, M. Rolfo, A.M. Ferraris, and G.F. Gaetani Mechanisms of protection of catalase by NADPH: kinetics and stoichiometry J. Biol. Chem. 274 1999 13908 13914
    • (1999) J. Biol. Chem. , vol.274 , pp. 13908-13914
    • Kirkman, H.N.1    Rolfo, M.2    Ferraris, A.M.3    Gaetani, G.F.4
  • 36
    • 33745128348 scopus 로고    scopus 로고
    • Truncated mutants of human thioredoxin reductase 1 do not exhibit glutathione reductase activity
    • DOI 10.1016/j.febslet.2006.05.038, PII S0014579306006387
    • S. Urig, J. Lieske, K. Fritz-Wolf, A. Irmler, and K. Becker Truncated mutants of human thioredoxin reductase 1 do not exhibit glutathione reductase activity FEBS Lett. 580 2006 3595 3600 (Pubitemid 43902793)
    • (2006) FEBS Letters , vol.580 , Issue.15 , pp. 3595-3600
    • Urig, S.1    Lieske, J.2    Fritz-Wolf, K.3    Irmler, A.4    Becker, K.5
  • 37
    • 33747369873 scopus 로고    scopus 로고
    • Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase
    • A.A. Turanov, D. Su, and V.N. Gladyshev Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase J. Biol. Chem. 281 2006 22953 22963
    • (2006) J. Biol. Chem. , vol.281 , pp. 22953-22963
    • Turanov, A.A.1    Su, D.2    Gladyshev, V.N.3
  • 38
    • 25844448658 scopus 로고    scopus 로고
    • Glutathione peroxidase, thioredoxin, and membrane protein changes in erythrocytes predict ribavirin-induced anemia
    • DOI 10.1016/j.clpt.2005.07.002, PII S0009923605003048
    • I. Grattagliano, S. Russmann, V.O. Palmieri, P. Portincasa, G. Palasciano, and B.H. Lauterburg Glutathione peroxidase, thioredoxin, and membrane protein changes in erythrocytes predict ribavirin-induced anemia Clin. Pharmacol. Ther. 78 2005 422 432 (Pubitemid 41393677)
    • (2005) Clinical Pharmacology and Therapeutics , vol.78 , Issue.4 , pp. 422-432
    • Grattagliano, I.1    Russmann, S.2    Palmieri, V.O.3    Portincasa, P.4    Palasciano, G.5    Lauterburg, B.H.6
  • 39
    • 0028081399 scopus 로고
    • Single extraction method for the spectrophotometric quantification of oxidized and reduced pyridine nucleotides in erythrocytes
    • DOI 10.1006/abio.1994.1511
    • T.C. Wagner, and M.D. Scott Single extraction method for the spectrophotometric quantification of oxidized and reduced pyridine nucleotides in erythrocytes Anal. Biochem. 222 1994 417 426 (Pubitemid 24338863)
    • (1994) Analytical Biochemistry , vol.222 , Issue.2 , pp. 417-426
    • Wagner, T.C.1    Scott, M.D.2
  • 40
    • 84877589196 scopus 로고    scopus 로고
    • Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease
    • A. George, S. Pushkaran, D.G. Konstantinidis, S. Koochaki, P. Malik, N. Mohandas, Y. Zheng, C.H. Joiner, and T.A. Kalfa Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease Blood 121 2013 2099 2107
    • (2013) Blood , vol.121 , pp. 2099-2107
    • George, A.1    Pushkaran, S.2    Konstantinidis, D.G.3    Koochaki, S.4    Malik, P.5    Mohandas, N.6    Zheng, Y.7    Joiner, C.H.8    Kalfa, T.A.9
  • 41
    • 8644270506 scopus 로고    scopus 로고
    • Interference of plasmatic reduced glutathione and hemolysis on glutathione disulfide levels in human blood
    • DOI 10.1080/10715760400008854
    • D. Giustarini, I. Dalle-Donne, R. Colombo, A. Milzani, and R. Rossi Interference of plasmatic reduced glutathione and hemolysis on glutathione disulfide levels in human blood Free Radic. Res. 38 2004 1101 1106 (Pubitemid 39504345)
    • (2004) Free Radical Research , vol.38 , Issue.10 , pp. 1101-1106
    • Giustarini, D.1    Dalle-Donne, I.2    Colombo, R.3    Milzani, A.4    Rossi, R.5
  • 42
    • 0015219567 scopus 로고
    • The influence of pH and methylene blue on the pathways of glucose utilization and lactate formation in erythrocytes of man
    • V. Albrecht, H. Roigas, M. Schultze, G. Jacobasch, and S. Rapoport The influence of pH and methylene blue on the pathways of glucose utilization and lactate formation in erythrocytes of man Eur. J. Biochem. 20 1971 44 50
    • (1971) Eur. J. Biochem. , vol.20 , pp. 44-50
    • Albrecht, V.1    Roigas, H.2    Schultze, M.3    Jacobasch, G.4    Rapoport, S.5
  • 43
    • 0032189723 scopus 로고    scopus 로고
    • Role of xanthine oxidase in hydrogen peroxide production
    • DOI 10.1016/S0891-5849(98)00154-3, PII S0891584998001543
    • F. Lacy, D.A. Gough, and S. Schmid Role of xanthine oxidase in hydrogen peroxide production Free Radic. Biol. Med. 25 1998 720 727 (Pubitemid 28464939)
    • (1998) Free Radical Biology and Medicine , vol.25 , Issue.6 , pp. 720-727
    • Lacy, F.1    Gough, D.A.2    Schmid-Schonbein, G.W.3
  • 44
    • 0035478537 scopus 로고    scopus 로고
    • A real-time electrochemical technique for measurement of cellular hydrogen peroxide generation and consumption: Evaluation in human polymorphonuclear leukocytes
    • DOI 10.1016/S0891-5849(01)00665-7, PII S0891584901006657
    • X.P. Liu, and J.L. Zweier A real-time electrochemical technique for measurement of cellular hydrogen peroxide generation and consumption: evaluation in human polymorphonuclear leukocytes Free Radic. Biol. Med. 31 2001 894 901 (Pubitemid 32925087)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.7 , pp. 894-901
    • Liu, X.1    Zweier, J.L.2
  • 45
    • 0035341719 scopus 로고    scopus 로고
    • 2 induce apoptosis through fenton chemistry independent of the cellular thiol state
    • DOI 10.1016/S0891-5849(01)00493-2, PII S0891584901004932
    • 2 induce apoptosis through Fenton chemistry independent of the cellular thiol state Free Radic. Biol. Med. 30 2001 1008 1018 (Pubitemid 32333031)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.9 , pp. 1008-1018
    • Antunes, F.1    Cadenas, E.2
  • 46
    • 67649255876 scopus 로고    scopus 로고
    • A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • P. Niethammer, C. Grabher, A.T. Look, and T.J. Mitchison A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish Nature 459 2009 996 999
    • (2009) Nature , vol.459 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 49
    • 49749213167 scopus 로고
    • Studies on the rapidity of complete blood circulation in man
    • G.C. Sutton, J. Karnell, and G. Nylin Studies on the rapidity of complete blood circulation in man Am. Heart J. 39 1950 741 748
    • (1950) Am. Heart J. , vol.39 , pp. 741-748
    • Sutton, G.C.1    Karnell, J.2    Nylin, G.3
  • 50
    • 0031441273 scopus 로고    scopus 로고
    • 2-removing enzyme in human erythrocytes
    • 2-removing enzyme in human erythrocytes Blood 90 1997 4973 4978 (Pubitemid 28007213)
    • (1997) Blood , vol.90 , Issue.12 , pp. 4973-4978
    • Mueller, S.1    Riedel, H.-D.2    Stremmel, W.3
  • 51
    • 0014108436 scopus 로고
    • Studies on quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • D.E. Paglia, and W.N. Valentine Studies on quantitative and qualitative characterization of erythrocyte glutathione peroxidase J. Lab. Clin. Med. 70 1967 158 169
    • (1967) J. Lab. Clin. Med. , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 52
    • 0037174884 scopus 로고    scopus 로고
    • A comparative study on the hydroperoxide and thiol specificity of the glutathione peroxidase family and selenoprotein P
    • DOI 10.1074/jbc.M202773200
    • G. Takebe, J. Yarimizu, Y. Saito, T. Hayashi, H. Nakamura, J. Yodoi, S. Nagasawa, and K. Takahashi A comparative study on the hydroperoxide and thiol specificity of the glutathione peroxidase family and selenoprotein P J. Biol. Chem. 277 2002 41254 41258 (Pubitemid 35215717)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41254-41258
    • Takebe, G.1    Yarimizu, J.2    Saito, Y.3    Hayashi, T.4    Nakamura, H.5    Yodoi, J.6    Nagasawa, S.7    Takahashi, K.8
  • 55
    • 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
  • 58
    • 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
  • 60
    • 0034101725 scopus 로고    scopus 로고
    • Synergism analysis of biochemical systems. I. Conceptual framework
    • DOI 10.1016/S0025-5564(99)00056-5, PII S0025556499000565
    • A. Salvador Synergism analysis of metabolic processes. I. Conceptual framework Math. Biosci. 163 2000 105 129 (Pubitemid 30117478)
    • (2000) Mathematical Biosciences , vol.163 , Issue.2 , pp. 105-129
    • Salvador, A.1
  • 61
    • 0034092624 scopus 로고    scopus 로고
    • Synergism analysis of biochemical systems. II. Tensor formulation and treatment of stoichiometric constraints
    • DOI 10.1016/S0025-5564(99)00057-7, PII S0025556499000577
    • A. Salvador Synergism analysis of metabolic processes. II. Tensor formulation and treatment of stoichiometric constraints Math. Biosci. 163 2000 131 158 (Pubitemid 30117479)
    • (2000) Mathematical Biosciences , vol.163 , Issue.2 , pp. 131-158
    • Salvador, A.1
  • 65
    • 84977586068 scopus 로고
    • Über die von der molekularkinetischen Theorie der Wärme geforderte Bewegung von in ruhenden Flüssigkeiten suspendierten Teilchen
    • A. Einstein Über die von der molekularkinetischen Theorie der Wärme geforderte Bewegung von in ruhenden Flüssigkeiten suspendierten Teilchen Ann. Phys. 322 1905 549 560
    • (1905) Ann. Phys. , vol.322 , pp. 549-560
    • Einstein, A.1
  • 66
    • 84978694892 scopus 로고
    • Zur kinetischen Theorie der Brownschen Molekularbewegung und der Suspensionen
    • M.V. Smoluchowski Zur kinetischen Theorie der Brownschen Molekularbewegung und der Suspensionen Ann. Phys. 326 1906 756 780
    • (1906) Ann. Phys. , vol.326 , pp. 756-780
    • Smoluchowski, M.V.1
  • 67
    • 0027533592 scopus 로고
    • Diffusion coefficients of oxygen, hydrogen peroxide and glucose in a hydrogel
    • DOI 10.1016/0003-2670(93)80202-V
    • S.A.M. vanStroe-Biezen, F.M. Everaerts, L.J.J. Janssen, and R.A. Tacken Diffusion coefficients of oxygen, hydrogen peroxide and glucose in a hydrogel Anal. Chim. Acta 273 1993 553 560 (Pubitemid 23058479)
    • (1993) Analytica Chimica Acta , vol.273 , Issue.1-2 , pp. 553-560
    • Van Stroe-Biezen, S.A.M.1    Everaerts, F.M.2    Janssen, L.J.J.3    Tacken, R.A.4
  • 68
    • 0000476830 scopus 로고
    • Oxidative hemolysis and erythrocyte metabolism in hereditary acatalasia
    • H.S. Jacob, S.H. Ingbar, and J.H. Jandl Oxidative hemolysis and erythrocyte metabolism in hereditary acatalasia J. Clin. Invest. 44 1965 1187 1199
    • (1965) J. Clin. Invest. , vol.44 , pp. 1187-1199
    • Jacob, H.S.1    Ingbar, S.H.2    Jandl, J.H.3
  • 69
    • 77953004335 scopus 로고    scopus 로고
    • Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia
    • C.-S. Cho, G.J. Kato, S.H. Yang, S.W. Bae, J.S. Lee, M.T. Gladwin, and S.G. Rhee Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia Antioxid. Redox Signaling 13 2010 1 11
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 1-11
    • Cho, C.-S.1    Kato, G.J.2    Yang, S.H.3    Bae, S.W.4    Lee, J.S.5    Gladwin, M.T.6    Rhee, S.G.7
  • 70
    • 0025092182 scopus 로고
    • Purification and measurement of calpromotin, the cytoplasmic protein which activates calcium-dependent potassium transport
    • DOI 10.1016/0006-291X(90)91923-G
    • R.B. Moore, G.A. Plishker, and S.K. Shriver Purification and measurement of calpromotin, the cytoplasmic protein which activates calcium-dependent potassium transport Biochem. Biophys. Res. Commun. 166 1990 146 153 (Pubitemid 20040164)
    • (1990) Biochemical and Biophysical Research Communications , vol.166 , Issue.1 , pp. 146-153
    • Moore, R.B.1    Plishker, G.A.2    Shriver, S.K.3
  • 71
    • 0027530060 scopus 로고
    • Identification of a natural killer enhancing factor (NKEF) from human erythroid cells
    • DOI 10.1006/cimm.1993.1043
    • H. Shau, R.K. Gupta, and S.H. Golub Identification of a natural killer enhancing factor (NKEF) from human erythroid cells Cell. Immunol. 147 1993 1 11 (Pubitemid 23100961)
    • (1993) Cellular Immunology , vol.147 , Issue.1 , pp. 1-11
    • Shau, H.1    Gupta, R.K.2    Golub, S.H.3
  • 73
    • 84861235219 scopus 로고    scopus 로고
    • Structural and functional analysis of native peroxiredoxin 2 in human red blood cells
    • Y. Ogasawara, T. Ohminato, Y. Nakamura, and K. Ishii Structural and functional analysis of native peroxiredoxin 2 in human red blood cells Int. J. Biochem. Cell Biol. 44 2012 1072 1077
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1072-1077
    • Ogasawara, Y.1    Ohminato, T.2    Nakamura, Y.3    Ishii, K.4
  • 74
    • 0026713741 scopus 로고
    • Superoxide generation by neutrophils and Kupffer cells during in vivo reperfusion after hepatic ischemia in rats
    • H. Jaeschke, A.P. Bautista, Z. Spolarics, and J.J. Spitzer Superoxide generation by neutrophils and Kupffer cells during in vivo reperfusion after hepatic ischemia in rats J. Leukocyte Biol. 52 1992 377 382
    • (1992) J. Leukocyte Biol. , vol.52 , pp. 377-382
    • Jaeschke, H.1    Bautista, A.P.2    Spolarics, Z.3    Spitzer, J.J.4
  • 75
    • 46849118983 scopus 로고    scopus 로고
    • Thermodynamics of the dimer-decamer transition of reduced human and plant 2-cys peroxiredoxin
    • DOI 10.1021/bi8002956
    • S. Barranco-Medina, S. Kakorin, J.J. Lázaro, and K.-J. Dietz Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin Biochemistry 47 2008 7196 7204 (Pubitemid 351956368)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 7196-7204
    • Barranco-Medina, S.1    Kakorin, S.2    Lazaro, J.J.3    Dietz, K.-J.4
  • 78
    • 84880081668 scopus 로고    scopus 로고
    • Hyperoxidized peroxiredoxin 2 interacts with the protein disulphide isomerase ERp46
    • P.E. Pace, A.V. Peskin, M.-H. Han, M.B. Hampton, and C.C. Winterbourn Hyperoxidized peroxiredoxin 2 interacts with the protein disulphide isomerase ERp46 Biochem. J. 453 2013 475 485
    • (2013) Biochem. J. , vol.453 , pp. 475-485
    • Pace, P.E.1    Peskin, A.V.2    Han, M.-H.3    Hampton, M.B.4    Winterbourn, C.C.5
  • 79
    • 78649632303 scopus 로고    scopus 로고
    • Human protein Atlas of redox systems - What can be learnt?
    • P. Dammeyer, and E.S.J. Arnér Human protein Atlas of redox systems - what can be learnt? Biochim. Biophys. Acta 1810 2011 111 138
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 111-138
    • Dammeyer, P.1    Arnér, E.S.J.2


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