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Volumn 329, Issue 1-2, 2003, Pages 23-38

Protein carbonyl groups as biomarkers of oxidative stress

Author keywords

2,4 Dinitrophenylhydrazine; Carbonyl assay; Human diseases; Oxyblot; Reactive oxygen species

Indexed keywords

2,4 DINITROPHENOL; 2,4 DINITROPHENYLHYDRAZINE; BIOLOGICAL MARKER; CARBONYL DERIVATIVE; PROTEIN;

EID: 0037363715     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-8981(03)00003-2     Document Type: Review
Times cited : (1919)

References (108)
  • 2
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324:1997;1-18.
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 3
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272:1997;20313-20316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 4
    • 0034659147 scopus 로고    scopus 로고
    • Role of reactive aldehyde in cardiovascular diseases
    • Uchida K. Role of reactive aldehyde in cardiovascular diseases. Free Radic. Biol. Med. 28:2000;1685-1696.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1685-1696
    • Uchida, K.1
  • 5
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10:1997;485-494.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 7
    • 0034524859 scopus 로고    scopus 로고
    • Human studies related to protein oxidation: Protein carbonyl content as a marker of damage
    • Chevion M., Berenshtein E., Stadtman E.R. Human studies related to protein oxidation: protein carbonyl content as a marker of damage. Free Radic. Res. 33:2000;S99-S108.
    • (2000) Free Radic. Res. , vol.33
    • Chevion, M.1    Berenshtein, E.2    Stadtman, E.R.3
  • 8
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter E. Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 32:2000;307-326.
    • (2000) Drug Metab. Rev. , vol.32 , pp. 307-326
    • Shacter, E.1
  • 9
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal M.F. Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32(9):2002;797-803.
    • (2002) Free Radic. Biol. Med. , vol.32 , Issue.9 , pp. 797-803
    • Beal, M.F.1
  • 10
    • 0029894681 scopus 로고    scopus 로고
    • Oxidative damage and motor neurone disease difficulties in the measurement of protein carbonyls in human brain tissue
    • Lyras L., Evans P.J., Shaw P.J., Ince P.G., Halliwell B. Oxidative damage and motor neurone disease difficulties in the measurement of protein carbonyls in human brain tissue. Free Radic. Res. 24(5):1996;397-406.
    • (1996) Free Radic. Res. , vol.24 , Issue.5 , pp. 397-406
    • Lyras, L.1    Evans, P.J.2    Shaw, P.J.3    Ince, P.G.4    Halliwell, B.5
  • 11
    • 0030057197 scopus 로고    scopus 로고
    • Oxidative stress, nutrition and health. Experimental strategies for optimisation of nutritional antioxidant intake in humans
    • Halliwell B. Oxidative stress, nutrition and health. Experimental strategies for optimisation of nutritional antioxidant intake in humans. Free Radic. Res. 25(1):1996;57-74.
    • (1996) Free Radic. Res. , vol.25 , Issue.1 , pp. 57-74
    • Halliwell, B.1
  • 13
    • 0024590274 scopus 로고
    • Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride
    • Lenz A., Costabel U., Shaltiel S., Levine L. Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride. Anal. Biochem. 177:1989;419-425.
    • (1989) Anal. Biochem. , vol.177 , pp. 419-425
    • Lenz, A.1    Costabel, U.2    Shaltiel, S.3    Levine, L.4
  • 14
    • 0032403864 scopus 로고    scopus 로고
    • Gel electrophoretic quantitation of protein carbonyls derivatized with tritiated sodium borohydride
    • Yan L.J., Sohal R.S. Gel electrophoretic quantitation of protein carbonyls derivatized with tritiated sodium borohydride. Anal. Biochem. 265:1998;176-182.
    • (1998) Anal. Biochem. , vol.265 , pp. 176-182
    • Yan, L.J.1    Sohal, R.S.2
  • 15
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R.L., Williams J., Stadtman E.R., Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233:1994;346-357.
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.2    Stadtman, E.R.3    Shacter, E.4
  • 17
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification. Examination by Western blot immunoassay
    • Shacter E., Williams J.A., Lim M., Levine R.L. Differential susceptibility of plasma proteins to oxidative modification. Examination by Western blot immunoassay. Free Radic. Biol. Med. 17:1994;429-437.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 20
    • 0035500775 scopus 로고    scopus 로고
    • Actin carbonylation: From a simple marker of protein oxidation to relevant signs of severe functional impairment
    • Dalle-Donne I., Rossi R., Giustarini D., Gagliano N., Lusini L., Milzani A.et al. Actin carbonylation: from a simple marker of protein oxidation to relevant signs of severe functional impairment. Free Radic. Biol. Med. 31:2001;1075-1083.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1075-1083
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3    Gagliano, N.4    Lusini, L.5    Milzani, A.6
  • 22
    • 0028239163 scopus 로고
    • Oxidative damage to proteins: Spectrophotometric method for carbonyl assay
    • Reznick A.Z., Packer L. Oxidative damage to proteins: spectrophotometric method for carbonyl assay. Methods Enzymol. 233:1994;263-357.
    • (1994) Methods Enzymol. , vol.233 , pp. 263-357
    • Reznick, A.Z.1    Packer, L.2
  • 25
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling A.C., Schulz J.B., Brown R.H. Jr., Beal M.F. Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 61(6):1993;2322-2325.
    • (1993) J. Neurochem. , vol.61 , Issue.6 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown R.H., Jr.3    Beal, M.F.4
  • 27
    • 0031708582 scopus 로고    scopus 로고
    • Oxidative stress at onset and in early stages of type 1 diabetes in children and adolescents
    • Dominguez C., Ruiz E., Gussinye M., Carrascosa A. Oxidative stress at onset and in early stages of type 1 diabetes in children and adolescents. Diabetes Care. 21(10):1998;1736-1742.
    • (1998) Diabetes Care , vol.21 , Issue.10 , pp. 1736-1742
    • Dominguez, C.1    Ruiz, E.2    Gussinye, M.3    Carrascosa, A.4
  • 30
    • 0032767481 scopus 로고    scopus 로고
    • Quantification of protease activities in synovial fluid from rheumatoid and osteoarthritis cases: Comparison with antioxidant and free radical damage markers
    • Mantle D., Falkous G., Walker D. Quantification of protease activities in synovial fluid from rheumatoid and osteoarthritis cases: comparison with antioxidant and free radical damage markers. Clin. Chim. Acta. 284(1):1999;45-58.
    • (1999) Clin. Chim. Acta , vol.284 , Issue.1 , pp. 45-58
    • Mantle, D.1    Falkous, G.2    Walker, D.3
  • 31
    • 0034660999 scopus 로고    scopus 로고
    • Protein carbonyl groups content as a useful clinical marker of antioxidant barrier impairment in plasma of children with juvenile chronic arthritis
    • Renke J., Popadiuk S., Korzon M., Bugajczyk B., Wozniak M. Protein carbonyl groups content as a useful clinical marker of antioxidant barrier impairment in plasma of children with juvenile chronic arthritis. Free Radic. Biol. Med. 29(2):2000;101-104.
    • (2000) Free Radic. Biol. Med. , vol.29 , Issue.2 , pp. 101-104
    • Renke, J.1    Popadiuk, S.2    Korzon, M.3    Bugajczyk, B.4    Wozniak, M.5
  • 32
    • 0034483226 scopus 로고    scopus 로고
    • Breath isoprene during acute respiratory exacerbation in cystic fibrosis
    • McGrath L.T., Patrick R., Mallon P., Dowey L., Silke B., Norwood W.et al. Breath isoprene during acute respiratory exacerbation in cystic fibrosis. Eur. Respir. J. 16(6):2000;1065-1069.
    • (2000) Eur. Respir. J. , vol.16 , Issue.6 , pp. 1065-1069
    • McGrath, L.T.1    Patrick, R.2    Mallon, P.3    Dowey, L.4    Silke, B.5    Norwood, W.6
  • 33
    • 0028347834 scopus 로고
    • Oxidation of proteins in neonatal lungs
    • Gladstone I.M. Jr., Levine R.L. Oxidation of proteins in neonatal lungs. Pediatrics. 93(5):1994;764-768.
    • (1994) Pediatrics , vol.93 , Issue.5 , pp. 764-768
    • Gladstone I.M., Jr.1    Levine, R.L.2
  • 34
    • 0029594475 scopus 로고
    • Differential oxidative damage to mitochondrial proteins during aging
    • Agarwal S., Sohal R.S. Differential oxidative damage to mitochondrial proteins during aging. Mech. Ageing Dev. 85(1):1995;55-63.
    • (1995) Mech. Ageing Dev. , vol.85 , Issue.1 , pp. 55-63
    • Agarwal, S.1    Sohal, R.S.2
  • 36
    • 0031795026 scopus 로고    scopus 로고
    • Protein carbonyl measurement by enzyme-linked immunosorbent assay
    • Winterbourn C.C., Buss I.H. Protein carbonyl measurement by enzyme-linked immunosorbent assay. Methods Enzymol. 300:1999;106-111.
    • (1999) Methods Enzymol. , vol.300 , pp. 106-111
    • Winterbourn, C.C.1    Buss, I.H.2
  • 37
    • 0028426899 scopus 로고
    • Oxidative damage to plasma proteins in adult respiratory distress syndrome
    • Quinlan G.J., Evans T.W., Gutteridge J.M. Oxidative damage to plasma proteins in adult respiratory distress syndrome. Free Radic. Res. 20(5):1994;289-298.
    • (1994) Free Radic. Res. , vol.20 , Issue.5 , pp. 289-298
    • Quinlan, G.J.1    Evans, T.W.2    Gutteridge, J.M.3
  • 38
    • 0034062242 scopus 로고    scopus 로고
    • Elevated protein carbonyls and lipid peroxidation products correlating with myeloperoxidase in tracheal aspirates from premature infants
    • Buss H., Darlow B.A., Winterbourn C.C. Elevated protein carbonyls and lipid peroxidation products correlating with myeloperoxidase in tracheal aspirates from premature infants. Pediatr. Res. 47(5):2000;640-645.
    • (2000) Pediatr. Res. , vol.47 , Issue.5 , pp. 640-645
    • Buss, H.1    Darlow, B.A.2    Winterbourn, C.C.3
  • 39
    • 0034990194 scopus 로고    scopus 로고
    • Oxidative stress and increased type-IV collagenase levels in bronchoalveolar lavage fluid from newborn babies
    • Schock B.C., Sweet D.G., Ennis M., Warner J.A., Young I.S., Halliday H.L. Oxidative stress and increased type-IV collagenase levels in bronchoalveolar lavage fluid from newborn babies. Pediatr. Res. 50(1):2001;29-33.
    • (2001) Pediatr. Res. , vol.50 , Issue.1 , pp. 29-33
    • Schock, B.C.1    Sweet, D.G.2    Ennis, M.3    Warner, J.A.4    Young, I.S.5    Halliday, H.L.6
  • 40
    • 0033961598 scopus 로고    scopus 로고
    • Protein carbonyl measurements show evidence of early oxidative stress in critically ill patients
    • Winterbourn C.C., Buss I.H., Chan T.P., Plank L.D., Clark M.A., Windsor J.A. Protein carbonyl measurements show evidence of early oxidative stress in critically ill patients. Crit. Care Med. 28(1):2000;143-149.
    • (2000) Crit. Care Med. , vol.28 , Issue.1 , pp. 143-149
    • Winterbourn, C.C.1    Buss, I.H.2    Chan, T.P.3    Plank, L.D.4    Clark, M.A.5    Windsor, J.A.6
  • 42
    • 0034974315 scopus 로고    scopus 로고
    • Protein carbonyls in decidua and placenta of pre-eclamptic women as markers for oxidative stress
    • Zusterzeel P.L., Rutten H., Roelofs H.M., Peters W.H., Steegers E.A. Protein carbonyls in decidua and placenta of pre-eclamptic women as markers for oxidative stress. Placenta. 22(2-3):2001;213-219.
    • (2001) Placenta , vol.22 , Issue.2-3 , pp. 213-219
    • Zusterzeel, P.L.1    Rutten, H.2    Roelofs, H.M.3    Peters, W.H.4    Steegers, E.A.5
  • 43
    • 0033230114 scopus 로고    scopus 로고
    • Oxidized proteins as a marker of oxidative stress during coronary heart surgery
    • Pantke U., Volk T., Schmutzler M., Kox W.J., Sitte N., Grune T. Oxidized proteins as a marker of oxidative stress during coronary heart surgery. Free Radic. Biol. Med. 27(9-10):1999;1080-1086.
    • (1999) Free Radic. Biol. Med. , vol.27 , Issue.9-10 , pp. 1080-1086
    • Pantke, U.1    Volk, T.2    Schmutzler, M.3    Kox, W.J.4    Sitte, N.5    Grune, T.6
  • 44
    • 0033667376 scopus 로고    scopus 로고
    • Plasma protein thiol oxidation and carbonyl formation in chronic renal failure
    • Himmelfarb J., McMonagle E., McMenamin E. Plasma protein thiol oxidation and carbonyl formation in chronic renal failure. Kidney Int. 58(6):2000;2571-2578.
    • (2000) Kidney Int. , vol.58 , Issue.6 , pp. 2571-2578
    • Himmelfarb, J.1    McMonagle, E.2    McMenamin, E.3
  • 45
    • 0032841267 scopus 로고    scopus 로고
    • Protein carbonyl formation on mucosal proteins in vitro and in dextran sulfate-induced colitis
    • Blackburn A.C., Doe W.F., Buffinton G.D. Protein carbonyl formation on mucosal proteins in vitro and in dextran sulfate-induced colitis. Free Radic. Biol. Med. 27(3/4):1999;262-270.
    • (1999) Free Radic. Biol. Med. , vol.27 , Issue.3-4 , pp. 262-270
    • Blackburn, A.C.1    Doe, W.F.2    Buffinton, G.D.3
  • 47
    • 0034812476 scopus 로고    scopus 로고
    • Comparison of protein carbonyl and antioxidant levels in brain tissue from intracerebral haemorrhage and control cases
    • Mantle D., Siddique S., Eddeb F., Mendelow A.D. Comparison of protein carbonyl and antioxidant levels in brain tissue from intracerebral haemorrhage and control cases. Clin. Chim. Acta. 312:2001;185-190.
    • (2001) Clin. Chim. Acta , vol.312 , pp. 185-190
    • Mantle, D.1    Siddique, S.2    Eddeb, F.3    Mendelow, A.D.4
  • 48
    • 0032753747 scopus 로고    scopus 로고
    • Ethanol-induced barrier dysfunction and its prevention by growth factors in human intestinal monolayers: Evidence for oxidative and cytoskeletal mechanisms
    • Banan A., Choudhary S., Zhang Y., Fields J.Z., Keshavarzian A. Ethanol-induced barrier dysfunction and its prevention by growth factors in human intestinal monolayers: evidence for oxidative and cytoskeletal mechanisms. J. Pharmacol. Exp. Ther. 291(3):1999;1075-1085.
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , Issue.3 , pp. 1075-1085
    • Banan, A.1    Choudhary, S.2    Zhang, Y.3    Fields, J.Z.4    Keshavarzian, A.5
  • 49
    • 0034069867 scopus 로고    scopus 로고
    • Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor alpha in a human colonic cell line
    • Banan A., Zhang Y., Losurdo J., Keshavarzian A. Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor alpha in a human colonic cell line. Gut. 46:2000;830-837.
    • (2000) Gut , vol.46 , pp. 830-837
    • Banan, A.1    Zhang, Y.2    Losurdo, J.3    Keshavarzian, A.4
  • 50
    • 0035254810 scopus 로고    scopus 로고
    • OPC-compounds prevent oxidant-induced carbonylation and depolymerization of the F-actin cytoskeleton and intestinal barrier hyperpermeability
    • Banan A., Fitzpatrick L., Zhang Y., Keshavarzian A. OPC-compounds prevent oxidant-induced carbonylation and depolymerization of the F-actin cytoskeleton and intestinal barrier hyperpermeability. Free Radic. Biol. Med. 30(3):2001;287-298.
    • (2001) Free Radic. Biol. Med. , vol.30 , Issue.3 , pp. 287-298
    • Banan, A.1    Fitzpatrick, L.2    Zhang, Y.3    Keshavarzian, A.4
  • 52
    • 0033938817 scopus 로고    scopus 로고
    • Protein oxidative damage
    • Shacter E. Protein oxidative damage. Methods Enzymol. 319:2000;428-436.
    • (2000) Methods Enzymol. , vol.319 , pp. 428-436
    • Shacter, E.1
  • 53
    • 0029965252 scopus 로고    scopus 로고
    • Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis
    • Nakamura A., Goto S. Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis. J. Biochem. 119(4):1996;768-774.
    • (1996) J. Biochem. , vol.119 , Issue.4 , pp. 768-774
    • Nakamura, A.1    Goto, S.2
  • 55
  • 58
    • 0035402254 scopus 로고    scopus 로고
    • Clara cell secretory protein oxidation and expression in premature infants who develop bronchopulmonary dysplasia
    • Ramsay P.L., Demayo F.J., Hegemier S.E., Wearden M.E., Smith C.V., Welty S.E. Clara cell secretory protein oxidation and expression in premature infants who develop bronchopulmonary dysplasia. Am. J. Respir. Crit. Care Med. 164(1):2001;155-161.
    • (2001) Am. J. Respir. Crit. Care Med. , vol.164 , Issue.1 , pp. 155-161
    • Ramsay, P.L.1    Demayo, F.J.2    Hegemier, S.E.3    Wearden, M.E.4    Smith, C.V.5    Welty, S.E.6
  • 59
    • 0034951428 scopus 로고    scopus 로고
    • Albumin is the major plasma protein target of oxidant stress in uremia
    • Himmelfarb J., McMonagle E. Albumin is the major plasma protein target of oxidant stress in uremia. Kidney Int. 60(1):2001;358-363.
    • (2001) Kidney Int. , vol.60 , Issue.1 , pp. 358-363
    • Himmelfarb, J.1    McMonagle, E.2
  • 60
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J., Pierce W.et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part I. Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic. Biol. Med. 33(4):2002;562-571.
    • (2002) Free Radic. Biol. Med. , vol.33 , Issue.4 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.5    Pierce, W.6
  • 61
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part II. Dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71
    • Castegna A., Aksenov M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R.et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain: Part II. Dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71. J. Neurochem. 82:2002;1524-1532.
    • (2002) J. Neurochem. , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6
  • 62
    • 0032190196 scopus 로고    scopus 로고
    • Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing
    • Yan L.J., Orr W.C., Sohal R.S. Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing. Anal. Biochem. 263:1998;67-71.
    • (1998) Anal. Biochem. , vol.263 , pp. 67-71
    • Yan, L.J.1    Orr, W.C.2    Sohal, R.S.3
  • 63
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging and disease
    • Levine R.L. Carbonyl modified proteins in cellular regulation, aging and disease. Free Radic. Biol. Med. 32(9):2002;790-796.
    • (2002) Free Radic. Biol. Med. , vol.32 , Issue.9 , pp. 790-796
    • Levine, R.L.1
  • 64
    • 0028076211 scopus 로고
    • Sequential oxidative damage, and changes in iron-binding and iron oxidising plasma antioxidants during cardiopulmonary bypass surgery
    • Pepper J.R., Mumby S., Gutteridge J.M.C. Sequential oxidative damage, and changes in iron-binding and iron oxidising plasma antioxidants during cardiopulmonary bypass surgery. Free Radic. Res. 21:1994;377-385.
    • (1994) Free Radic. Res. , vol.21 , pp. 377-385
    • Pepper, J.R.1    Mumby, S.2    Gutteridge, J.M.C.3
  • 65
    • 0033032678 scopus 로고    scopus 로고
    • Oxidatively modified proteins in bronchoalveolar lavage fluid of patients with ARDS and patients at-risk for ARDS
    • Lenz A.G., Jorens P.G., Meyer B., De Backer W., Van Overveld F., Bossaert L.et al. Oxidatively modified proteins in bronchoalveolar lavage fluid of patients with ARDS and patients at-risk for ARDS. Eur. Respir. J. 13(1):1999;169-174.
    • (1999) Eur. Respir. J. , vol.13 , Issue.1 , pp. 169-174
    • Lenz, A.G.1    Jorens, P.G.2    Meyer, B.3    De Backer, W.4    Van Overveld, F.5    Bossaert, L.6
  • 67
    • 10344264959 scopus 로고    scopus 로고
    • Increased oxidative stress and decreased antioxidant defenses in mucosa of inflammatory bowel disease
    • Lih-Brody L., Powell S.R., Collier K.P., Reddy G.M., Cerchia R., Kahn E.et al. Increased oxidative stress and decreased antioxidant defenses in mucosa of inflammatory bowel disease. Dig. Dis. Sci. 41:1996;2078-2086.
    • (1996) Dig. Dis. Sci. , vol.41 , pp. 2078-2086
    • Lih-Brody, L.1    Powell, S.R.2    Collier, K.P.3    Reddy, G.M.4    Cerchia, R.5    Kahn, E.6
  • 71
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase - A key regulator of neutrophil oxidant production
    • Kettle A.J., Winterbourn C.C. Myeloperoxidase - a key regulator of neutrophil oxidant production. Redox Rep. 3:1997;3-15.
    • (1997) Redox Rep. , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 72
    • 0029816226 scopus 로고    scopus 로고
    • Expression of inducible nitric oxide synthase and nitrotyrosine in colonic epithelium in inflammatory bowel disease
    • Singer I.I., Kawka D.W., Scott S., Weidner J.R., Mumford R.A., Riehl T.E.et al. Expression of inducible nitric oxide synthase and nitrotyrosine in colonic epithelium in inflammatory bowel disease. Gastroenterology. 111(4):1996;871-885.
    • (1996) Gastroenterology , vol.111 , Issue.4 , pp. 871-885
    • Singer, I.I.1    Kawka, D.W.2    Scott, S.3    Weidner, J.R.4    Mumford, R.A.5    Riehl, T.E.6
  • 73
    • 0032415840 scopus 로고    scopus 로고
    • Expression of nitric oxide synthases and formation of nitrotyrosine and reactive oxygen species in inflammatory bowel disease
    • Dijkstra G., Moshage H., van Dullemen H.M., de Jager-Krikken A., Tiebosch A.T., Kleibeuker J.H.et al. Expression of nitric oxide synthases and formation of nitrotyrosine and reactive oxygen species in inflammatory bowel disease. J. Pathol. 186(4):1998;416-421.
    • (1998) J. Pathol. , vol.186 , Issue.4 , pp. 416-421
    • Dijkstra, G.1    Moshage, H.2    Van Dullemen, H.M.3    De Jager-Krikken, A.4    Tiebosch, A.T.5    Kleibeuker, J.H.6
  • 74
    • 7144253803 scopus 로고    scopus 로고
    • Increased expression of an inducible isoform of nitric oxide synthase and the formation of peroxynitrite in colonic mucosa of patients with active ulcerative colitis
    • Kimura H., Hokari R., Miura S., Shigematsu T., Hirokawa M., Akiba Y.et al. Increased expression of an inducible isoform of nitric oxide synthase and the formation of peroxynitrite in colonic mucosa of patients with active ulcerative colitis. Gut. 42(2):1998;180-187.
    • (1998) Gut , vol.42 , Issue.2 , pp. 180-187
    • Kimura, H.1    Hokari, R.2    Miura, S.3    Shigematsu, T.4    Hirokawa, M.5    Akiba, Y.6
  • 76
    • 0031021944 scopus 로고    scopus 로고
    • Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques
    • Leeuwenburgh C., Rasmussen J.E., Hsu F.F., Mueller D.M., Pennathur S., Heinecke J.W. Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques. J. Biol. Chem. 272:1997;3520-3526.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3520-3526
    • Leeuwenburgh, C.1    Rasmussen, J.E.2    Hsu, F.F.3    Mueller, D.M.4    Pennathur, S.5    Heinecke, J.W.6
  • 77
    • 0032143406 scopus 로고    scopus 로고
    • Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
    • Fu S., Davies M.J., Stocker R., Dean R.T. Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque. Biochem. J. 333:1998;519-525.
    • (1998) Biochem. J. , vol.333 , pp. 519-525
    • Fu, S.1    Davies, M.J.2    Stocker, R.3    Dean, R.T.4
  • 78
    • 0031797254 scopus 로고    scopus 로고
    • Measurement of protein carbonyls in human brain tissue
    • Evans P., Lyras L., Halliwell B. Measurement of protein carbonyls in human brain tissue. Methods Enzymol. 300:1999;145-156.
    • (1999) Methods Enzymol. , vol.300 , pp. 145-156
    • Evans, P.1    Lyras, L.2    Halliwell, B.3
  • 79
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress - Role of the multicatalytic proteinase complex, proteasome
    • Grune T., Reinheckel T., Joshi M., Davies K.J.A. Proteolysis in cultured liver epithelial cells during oxidative stress - role of the multicatalytic proteinase complex, proteasome. J. Biol. Chem. 270:1995;2344-2351.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.A.4
  • 80
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • Grune T., Reinheckel T., Davies K.J.A. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J. Biol. Chem. 271:1996;15504-15509.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 81
    • 0030986162 scopus 로고    scopus 로고
    • Metabolic fate of 4-hydroxynonenal in hepatocytes: 1,4-dihydroxynonene is not the main product
    • Siems W.G., Zollner H., Grune T., Esterbauer H. Metabolic fate of 4-hydroxynonenal in hepatocytes: 1,4-dihydroxynonene is not the main product. J. Lipid Res. 38:1997;612-622.
    • (1997) J. Lipid Res. , vol.38 , pp. 612-622
    • Siems, W.G.1    Zollner, H.2    Grune, T.3    Esterbauer, H.4
  • 82
    • 0034527069 scopus 로고    scopus 로고
    • Antioxidant and protein oxidation
    • Griffiths H.R. Antioxidant and protein oxidation. Free Radic. Res. 33:2000;S47-S58.
    • (2000) Free Radic. Res. , vol.33
    • Griffiths, H.R.1
  • 84
    • 0028972851 scopus 로고
    • 2-treated actin: Assembly and polymer interactions with cross-linking proteins
    • 2-treated actin: assembly and polymer interactions with cross-linking proteins. Biophys. J. 69:1995;2710-2719.
    • (1995) Biophys. J. , vol.69 , pp. 2710-2719
    • Dalle-Donne, I.1    Milzani, A.2    Colombo, R.3
  • 85
    • 0033592425 scopus 로고    scopus 로고
    • The t-butyl hydroperoxide-induced oxidation of actin Cys-374 is coupled with structural changes in distant regions of the protein
    • Dalle-Donne I., Milzani A., Colombo R. The t-butyl hydroperoxide-induced oxidation of actin Cys-374 is coupled with structural changes in distant regions of the protein. Biochemistry. 38:1999;12471-12480.
    • (1999) Biochemistry , vol.38 , pp. 12471-12480
    • Dalle-Donne, I.1    Milzani, A.2    Colombo, R.3
  • 87
    • 0028918335 scopus 로고
    • Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation
    • Shacter E., Williams J.A., Levine R.L. Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation. Free Radic. Biol. Med. 18(4):1995;815-821.
    • (1995) Free Radic. Biol. Med. , vol.18 , Issue.4 , pp. 815-821
    • Shacter, E.1    Williams, J.A.2    Levine, R.L.3
  • 88
    • 0028807137 scopus 로고
    • Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation
    • Hensley K., Hall N., Subramaniam R., Cole P., Harris M., Aksenov M.et al. Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation. J. Neurochem. 65:1995;2146-2156.
    • (1995) J. Neurochem. , vol.65 , pp. 2146-2156
    • Hensley, K.1    Hall, N.2    Subramaniam, R.3    Cole, P.4    Harris, M.5    Aksenov, M.6
  • 89
    • 0030921729 scopus 로고    scopus 로고
    • Oxidatively induced structural alteration of glutamine synthetase assessed by analysis of spin label incorporation kinetics: Relevance to Alzheimer's disease
    • Butterfield D.A., Hensley K., Cole P., Subramaniam R., Aksenov M., Aksenova M.et al. Oxidatively induced structural alteration of glutamine synthetase assessed by analysis of spin label incorporation kinetics: relevance to Alzheimer's disease. J. Neurochem. 68:1997;2451-2457.
    • (1997) J. Neurochem. , vol.68 , pp. 2451-2457
    • Butterfield, D.A.1    Hensley, K.2    Cole, P.3    Subramaniam, R.4    Aksenov, M.5    Aksenova, M.6
  • 93
    • 0030813067 scopus 로고    scopus 로고
    • Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis
    • Ferrante R.J., Browne S.E., Shinobu L.A., Bowling A.C., Baik M.J., MacGarvey U.et al. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J. Neurochem. 69:1997;2064-2074.
    • (1997) J. Neurochem. , vol.69 , pp. 2064-2074
    • Ferrante, R.J.1    Browne, S.E.2    Shinobu, L.A.3    Bowling, A.C.4    Baik, M.J.5    MacGarvey, U.6
  • 95
    • 0032903009 scopus 로고    scopus 로고
    • Treatment of pulmonary exacerbations of cystic fibrosis leads to improved antioxidant status
    • Range S.P., Dunster C., Knox A.J., Kelly F.J. Treatment of pulmonary exacerbations of cystic fibrosis leads to improved antioxidant status. Eur. Respir. J. 13(3):1999;560-564.
    • (1999) Eur. Respir. J. , vol.13 , Issue.3 , pp. 560-564
    • Range, S.P.1    Dunster, C.2    Knox, A.J.3    Kelly, F.J.4
  • 97
    • 0028840591 scopus 로고
    • Early protein oxidation in the neonatal lung is related to development of chronic lung disease
    • Varsila E., Pesonen E., Andersson S. Early protein oxidation in the neonatal lung is related to development of chronic lung disease. Acta Paediatr. 84(11):1995;1296-1299.
    • (1995) Acta Paediatr. , vol.84 , Issue.11 , pp. 1296-1299
    • Varsila, E.1    Pesonen, E.2    Andersson, S.3
  • 99
    • 0036521996 scopus 로고    scopus 로고
    • Increase in oxidative damage to lipids and proteins in skeletal muscle of uremic patients
    • Lim P.S., Cheng Y.M., Wei Y.H. Increase in oxidative damage to lipids and proteins in skeletal muscle of uremic patients. Free Radic. Res. 36(3):2002;295-301.
    • (2002) Free Radic. Res. , vol.36 , Issue.3 , pp. 295-301
    • Lim, P.S.1    Cheng, Y.M.2    Wei, Y.H.3
  • 100
    • 0035370282 scopus 로고    scopus 로고
    • Oxidative damage to proteins and decrease of antioxidant capacity in patients with varicocele
    • Chen S.S., Chang L.S., Wei Y.H. Oxidative damage to proteins and decrease of antioxidant capacity in patients with varicocele. Free Radic. Biol. Med. 30(11):2001;1328-1334.
    • (2001) Free Radic. Biol. Med. , vol.30 , Issue.11 , pp. 1328-1334
    • Chen, S.S.1    Chang, L.S.2    Wei, Y.H.3
  • 102
    • 0036245785 scopus 로고    scopus 로고
    • Proteolysis in severe sepsis is related to oxidation of plasma protein
    • Abu-Zidan F.M., Plank L.D., Windsor J.A. Proteolysis in severe sepsis is related to oxidation of plasma protein. Eur. J. Surg. 168(2):2002;119-123.
    • (2002) Eur. J. Surg. , vol.168 , Issue.2 , pp. 119-123
    • Abu-Zidan, F.M.1    Plank, L.D.2    Windsor, J.A.3
  • 104
    • 0035838399 scopus 로고    scopus 로고
    • Impaired myofibrillar energetics and oxidative injury during human atrial fibrillation
    • Mihm M.J., Yu F., Carnes C.A., Reiser P.J., McCarthy P.M., Van Wagoner D.R.et al. Impaired myofibrillar energetics and oxidative injury during human atrial fibrillation. Circulation. 104(2):2001;174-180.
    • (2001) Circulation , vol.104 , Issue.2 , pp. 174-180
    • Mihm, M.J.1    Yu, F.2    Carnes, C.A.3    Reiser, P.J.4    McCarthy, P.M.5    Van Wagoner, D.R.6
  • 105
    • 15444353991 scopus 로고    scopus 로고
    • Differential protein oxidation in Duchenne and Becker muscular dystrophy
    • Haycock J.W., Mac Neil S., Mantle D. Differential protein oxidation in Duchenne and Becker muscular dystrophy. Neuroreport. 9(10):1998;2201-2207.
    • (1998) Neuroreport , vol.9 , Issue.10 , pp. 2201-2207
    • Haycock, J.W.1    Mac Neil, S.2    Mantle, D.3
  • 106
    • 0035027921 scopus 로고    scopus 로고
    • Increased oxidative and nitrative stress in human stomach associated with cagA+ Helicobacter pylori infection and inflammation
    • Li C.Q., Pignatelli B., Ohshima H. Increased oxidative and nitrative stress in human stomach associated with cagA+ Helicobacter pylori infection and inflammation. Dig. Dis. Sci. 46(4):2001;836-844.
    • (2001) Dig. Dis. Sci. , vol.46 , Issue.4 , pp. 836-844
    • Li, C.Q.1    Pignatelli, B.2    Ohshima, H.3
  • 107
    • 0031962268 scopus 로고    scopus 로고
    • Increased protein oxidation in human substantia nigra pars compacta in comparison with basal ganglia and prefrontal cortex measured with an improved dinitrophenylhydrazine assay
    • Floor E., Wetzel M.G. Increased protein oxidation in human substantia nigra pars compacta in comparison with basal ganglia and prefrontal cortex measured with an improved dinitrophenylhydrazine assay. J. Neurochem. 70(1):1998;268-275.
    • (1998) J. Neurochem. , vol.70 , Issue.1 , pp. 268-275
    • Floor, E.1    Wetzel, M.G.2


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