메뉴 건너뛰기




Volumn 370, Issue 2, 2003, Pages 729-735

Detection of HOCl-mediated protein oxidation products in the extracellular matrix of human atherosclerotic plaques

Author keywords

Atherosclerosis; Chloramine; Extracellular matrix; Hypochlorite; Myeloperoxidase; Protein oxidation

Indexed keywords

CATALYSIS; CHLORINATION; OXIDATION; TRANSITION METALS;

EID: 0037336908     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021710     Document Type: Article
Times cited : (114)

References (59)
  • 1
    • 0024603895 scopus 로고
    • Beyond cholesterol: Modifications of low-density lipoprotein that increase its atherogenicity
    • Steinberg, D., Parthasarathy, S., Carew, T. E., Khoo, J. C. and Witztum, J. L. (1989) Beyond cholesterol: modifications of low-density lipoprotein that increase its atherogenicity. N. Engl. J. Med. 320, 915-924
    • (1989) N. Engl. J. Med. , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witztum, J.L.5
  • 2
    • 0032487487 scopus 로고    scopus 로고
    • Oxidants and antioxidants in the pathogenesis of atherosclerosis: Implications for the oxidized low density lipoprotein hypothesis
    • Heinecke, J. W. (1998) Oxidants and antioxidants in the pathogenesis of atherosclerosis: implications for the oxidized low density lipoprotein hypothesis. Atherosclerosis 141, 1-15
    • (1998) Atherosclerosis , vol.141 , pp. 1-15
    • Heinecke, J.W.1
  • 4
    • 0029129908 scopus 로고
    • Human atherosclerotic p aque contains both oxidized lipids and relatively large amounts of α-tocopherol and ascorbate
    • Suarna, C., Dean, R. T., May, J. and Stocker, R. (1995) Human atherosclerotic p aque contains both oxidized lipids and relatively large amounts of α-tocopherol and ascorbate. Arterioscler. Thromb. Vasc. Biol. 15, 1616-1624
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 1616-1624
    • Suarna, C.1    Dean, R.T.2    May, J.3    Stocker, R.4
  • 5
    • 0020973547 scopus 로고
    • Receptor mediated endocytosis of low density lipoprotein in cultured cells
    • Goldstein, J. L., Basu, S. K. and Brown, M. S. (1983) Receptor mediated endocytosis of low density lipoprotein in cultured cells. Methods Enzymol. 98, 241-260
    • (1983) Methods Enzymol. , vol.98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 6
    • 0000061171 scopus 로고
    • Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids
    • Steinbrecher, U. P., Parthasarathy, S., Leake, D. S., Witztum, J. L. and Steinberg, D. (1984) Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids. Proc. Natl. Acad. Sci. U.S.A. 81, 3883-3887
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3883-3887
    • Steinbrecher, U.P.1    Parthasarathy, S.2    Leake, D.S.3    Witztum, J.L.4    Steinberg, D.5
  • 8
    • 0024987417 scopus 로고
    • The role of oxidative modification and antioxidants in LDL metabolism and atherosclerosis
    • Jessup, W., Dean, R. T., de Whalley, V. C., Rankin, S. M. and Leake, D. S. (1990) The role of oxidative modification and antioxidants in LDL metabolism and atherosclerosis. Adv. Exp. Med. Biol. 264, 139-142
    • (1990) Adv. Exp. Med. Biol. , vol.264 , pp. 139-142
    • Jessup, W.1    Dean, R.T.2    De Whalley, V.C.3    Rankin, S.M.4    Leake, D.S.5
  • 9
    • 0027170699 scopus 로고
    • Minimally modified low density lipoprotein-induced inflammatory responses in endothelial cells are mediated by cyclic adenosine monophosphate
    • Parhami, F., Fang, Z. T., Fogelman, A. M., Andalibi, A., Territo, M. C. and Berliner, J. A. (1993) Minimally modified low density lipoprotein-induced inflammatory responses in endothelial cells are mediated by cyclic adenosine monophosphate. J. Clin. Invest. 92, 471-478
    • (1993) J. Clin. Invest. , vol.92 , pp. 471-478
    • Parhami, F.1    Fang, Z.T.2    Fogelman, A.M.3    Andalibi, A.4    Territo, M.C.5    Berliner, J.A.6
  • 10
    • 0029096946 scopus 로고
    • Transcriptional activation of the macrophage-colony stimulating factor gene by minimally modified LDL. Involvement of nuclear factor-κB
    • Rajavashisth, T. B., Yamada, H. and Mishra, N. K. (1995) Transcriptional activation of the macrophage-colony stimulating factor gene by minimally modified LDL. Involvement of nuclear factor-κB. Arterioscl. Thromb. Vasc. Biol. 15, 1591-1598
    • (1995) Arterioscl. Thromb. Vasc. Biol. , vol.15 , pp. 1591-1598
    • Rajavashisth, T.B.1    Yamada, H.2    Mishra, N.K.3
  • 11
    • 0028361104 scopus 로고
    • Enhanced LDL oxidation by murine macrophage foam cells and their failure to secrete nitric oxide
    • Bolton, E. J., Jessup, W., Stanley, K. K. and Dean, R. T. (1994) Enhanced LDL oxidation by murine macrophage foam cells and their failure to secrete nitric oxide. Atherosclerosis 106, 213-223
    • (1994) Atherosclerosis , vol.106 , pp. 213-223
    • Bolton, E.J.1    Jessup, W.2    Stanley, K.K.3    Dean, R.T.4
  • 12
    • 0016008049 scopus 로고
    • Components of the protein-lipid complex of arterial elastin: Their role in the retention of lipid in atherosclerotic lesions
    • Kramsch, D. M., Franzblau, C. and Hollander, W. (1974) Components of the protein-lipid complex of arterial elastin: their role in the retention of lipid in atherosclerotic lesions. Adv. Exp. Med. Biol. 43, 193-210
    • (1974) Adv. Exp. Med. Biol. , vol.43 , pp. 193-210
    • Kramsch, D.M.1    Franzblau, C.2    Hollander, W.3
  • 13
    • 0021705548 scopus 로고
    • Interaction between elastin and elastases and its role in the aging of the arterial wall, skin and other connective tissues. A review
    • Robert, L., Jacob, M. P., Frances, C., Godeau, G. and Hornebeck, W. (1984) Interaction between elastin and elastases and its role in the aging of the arterial wall, skin and other connective tissues. A review. Mech. Ageing Dev. 28, 155-166
    • (1984) Mech. Ageing Dev. , vol.28 , pp. 155-166
    • Robert, L.1    Jacob, M.P.2    Frances, C.3    Godeau, G.4    Hornebeck, W.5
  • 14
    • 0031728107 scopus 로고    scopus 로고
    • Elastin-elastase-atherosclerosis revisited
    • Robert, L., Robert, A. M. and Jacotot, B. (1998) Elastin-elastase-atherosclerosis revisited. Atherosclerosis 140, 281-295
    • (1998) Atherosclerosis , vol.140 , pp. 281-295
    • Robert, L.1    Robert, A.M.2    Jacotot, B.3
  • 15
    • 0015577538 scopus 로고
    • The interaction of serum and arterial lipoproteins with elastin of the arterial intima and its role in the lipid accumulation in atherosclerotic plaques
    • Kramsch, D. M. and Hollander, W. (1973) The interaction of serum and arterial lipoproteins with elastin of the arterial intima and its role in the lipid accumulation in atherosclerotic plaques. J. Clin. Invest. 52, 236-247
    • (1973) J. Clin. Invest. , vol.52 , pp. 236-247
    • Kramsch, D.M.1    Hollander, W.2
  • 16
    • 0022442783 scopus 로고
    • A proposed structure of chondroitin 6-sulfate proteoglycan of human normal and adiacent atherosclerotic plaque
    • Wagner, W. D., Salisbury, B. G. J. and Rowe, H. A. (1987) A proposed structure of chondroitin 6-sulfate proteoglycan of human normal and adiacent atherosclerotic plaque. Arteriosclerosis 6, 407-417
    • (1987) Arteriosclerosis , vol.6 , pp. 407-417
    • Wagner, W.D.1    Salisbury, B.G.J.2    Rowe, H.A.3
  • 17
    • 0017366929 scopus 로고
    • Structure and metabolism of arterial elastin
    • Rucker, R. B. and Tinker, D. (1977) Structure and metabolism of arterial elastin. Int. Rev. Exp. Pathol. 17, 1-47
    • (1977) Int. Rev. Exp. Pathol. , vol.17 , pp. 1-47
    • Rucker, R.B.1    Tinker, D.2
  • 18
    • 0016010583 scopus 로고
    • Arterial mesenchyme and arteriosclerosis. Enzymic vs non-enzymic factors in the deterioration of connective tissue
    • LaBella, F. S. (1974) Arterial mesenchyme and arteriosclerosis. Enzymic vs non-enzymic factors in the deterioration of connective tissue. Adv. Exp. Med. Biol. 43, 377-402
    • (1974) Adv. Exp. Med. Biol. , vol.43 , pp. 377-402
    • LaBella, F.S.1
  • 19
    • 0025980710 scopus 로고
    • Oxidative damage to fibronectin. 1. The effects of the neutrophil myeloperoxidase system and HOCl
    • Vissers, M. C. M. and Winterbourn, C. C. (1991) Oxidative damage to fibronectin. 1. The effects of the neutrophil myeloperoxidase system and HOCl. Arch. Biochem. Biophys. 285, 53-59
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 53-59
    • Vissers, M.C.M.1    Winterbourn, C.C.2
  • 20
    • 0032487563 scopus 로고    scopus 로고
    • Inhibition of endothelial cell adhesion and proliferation by extracellular matrix from vascular smooth muscle cells: Role of type V collagen
    • Underwood, P. A., Bean, P. A. and Whitelock, J. M. (1998) Inhibition of endothelial cell adhesion and proliferation by extracellular matrix from vascular smooth muscle cells: role of type V collagen. Atherosclerosis 141, 141-152
    • (1998) Atherosclerosis , vol.141 , pp. 141-152
    • Underwood, P.A.1    Bean, P.A.2    Whitelock, J.M.3
  • 21
    • 0032450295 scopus 로고    scopus 로고
    • Heparin fails to inhibit the proliferation of human vascular smooth muscle cells in the presence of human serum
    • Underwood, P. A., Mitchell, S. M. and Whitelock, J. M. (1998) Heparin fails to inhibit the proliferation of human vascular smooth muscle cells in the presence of human serum. J. Vasc. Res. 35, 449-460
    • (1998) J. Vasc. Res. , vol.35 , pp. 449-460
    • Underwood, P.A.1    Mitchell, S.M.2    Whitelock, J.M.3
  • 22
    • 0030979720 scopus 로고    scopus 로고
    • 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalysed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima
    • Hazen, S. L. and Heinecke, J. W. (1997) 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalysed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J. Clin. Invest. 99, 2075-2081
    • (1997) J. Clin. Invest. , vol.99 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 23
    • 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. and Dean, R. T. (1998) Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque. Biochem. J. 333, 519-525
    • (1998) Biochem. J. , vol.333 , pp. 519-525
    • Fu, S.1    Davies, M.J.2    Stocker, R.3    Dean, R.T.4
  • 26
    • 0027417395 scopus 로고
    • Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages
    • Heinecke, J. W., Li, W., Daehnke, H. L. and Goldstein, J. A. (1993) Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages. J. Biol. Chem. 268, 4069-4077
    • (1993) J. Biol. Chem. , vol.268 , pp. 4069-4077
    • Heinecke, J.W.1    Li, W.2    Daehnke, H.L.3    Goldstein, J.A.4
  • 27
    • 0030046117 scopus 로고    scopus 로고
    • Neutrophils convert tyrosyl residues in albumin to chlorotyrosine
    • Kettle, A. J. (1996) Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett. 379, 103-106
    • (1996) FEBS Lett. , vol.379 , pp. 103-106
    • Kettle, A.J.1
  • 28
    • 0033429334 scopus 로고    scopus 로고
    • Stable markers of oxidant damage to proteins and their application in the study of human disease
    • Davies, M. J., Fu, S., Wang, H. and Dean, R. T. (1999) Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radic. Biol. Med. 27, 1151-1163
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1151-1163
    • Davies, M.J.1    Fu, S.2    Wang, H.3    Dean, R.T.4
  • 29
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant production
    • Kettle, A. J. and Winterbourn, C. C. (1997) Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Rep. 3, 3-15
    • (1997) Redox Rep. , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 30
    • 0028292033 scopus 로고
    • Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions
    • Daugherty, A., Dunn, J. L., Rateri, D. L. and Heinecke, J. W. (1994) Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J. Clin. Invest. 94, 437-444
    • (1994) J. Clin. Invest. , vol.94 , pp. 437-444
    • Daugherty, A.1    Dunn, J.L.2    Rateri, D.L.3    Heinecke, J.W.4
  • 32
    • 0034904840 scopus 로고    scopus 로고
    • A functional myeloperoxidase polymorphic variant is associated with coronary artery disease in French-Canadians
    • Nikpoor, B., Turecki, G., Fournier, C., Theroux, P. and Rouleau, G. A. (2001) A functional myeloperoxidase polymorphic variant is associated with coronary artery disease in French-Canadians. Am. Heart. J. 142, 336-369
    • (2001) Am. Heart. J. , vol.142 , pp. 336-369
    • Nikpoor, B.1    Turecki, G.2    Fournier, C.3    Theroux, P.4    Rouleau, G.A.5
  • 34
    • 0025395487 scopus 로고
    • Mechanisms of extracellular matrix proteoglycan degradation by human neutrophils
    • McGowan, S. E. (1990) Mechanisms of extracellular matrix proteoglycan degradation by human neutrophils. Am. J. Respir. Cell. Mol. Biol. 2, 271-279
    • (1990) Am. J. Respir. Cell. Mol. Biol. , vol.2 , pp. 271-279
    • McGowan, S.E.1
  • 35
    • 0034731356 scopus 로고    scopus 로고
    • Myeloperoxidase binds to low-density lipoprotein: Potential implications for atherosclerosis
    • Carr, A. C., Myzak, M. C., Stocker, R., McCall, M. R. and Frei, B. (2000) Myeloperoxidase binds to low-density lipoprotein: potential implications for atherosclerosis. FEBS Lett. 487, 176-180
    • (2000) FEBS Lett. , vol.487 , pp. 176-180
    • Carr, A.C.1    Myzak, M.C.2    Stocker, R.3    McCall, M.R.4    Frei, B.5
  • 36
    • 0032868955 scopus 로고    scopus 로고
    • Oxidation of heparin-treated low density lipoprotein by peroxidases
    • Upritchard, J. E. and Sutherland, W. H. (1999) Oxidation of heparin-treated low density lipoprotein by peroxidases. Atherosclerosis 146, 211-219
    • (1999) Atherosclerosis , vol.146 , pp. 211-219
    • Upritchard, J.E.1    Sutherland, W.H.2
  • 37
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman, E. R. (1993) Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62, 797-821
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 38
    • 0031800368 scopus 로고    scopus 로고
    • Association of myeloperoxidase with heparin: Oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme
    • Daphna, E. M., Michaela, S., Eynat, P., Irit, A. and Rimon, S. (1998) Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme Mol. Cell. Biochem. 183, 55-61
    • (1998) Mol. Cell. Biochem. , vol.183 , pp. 55-61
    • Daphna, E.M.1    Michaela, S.2    Eynat, P.3    Irit, A.4    Rimon, S.5
  • 39
    • 0029932445 scopus 로고    scopus 로고
    • Presence of hypochlorite-modified proteins in human atherosclerotic lesions
    • Hazell, L. J., Arnold, L., Flowers, D., Waeg, G., Malle, E. and Stocker, R. (1996) Presence of hypochlorite-modified proteins in human atherosclerotic lesions. J. Clin. Invest. 97, 1535-1544
    • (1996) J. Clin. Invest. , vol.97 , pp. 1535-1544
    • Hazell, L.J.1    Arnold, L.2    Flowers, D.3    Waeg, G.4    Malle, E.5    Stocker, R.6
  • 40
    • 0035890124 scopus 로고    scopus 로고
    • Correlation between intima-to-media ratio, apolipoprotein B-100, myeloperoxidase, and hypochlorite-oxidized proteins in human atherosclerosis
    • Hazell, L. J., Baernthaler, G. and Stocker, R. (2001) Correlation between intima-to-media ratio, apolipoprotein B-100, myeloperoxidase, and hypochlorite-oxidized proteins in human atherosclerosis. Free Radic. Biol. Med. 31, 1254-1262
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1254-1262
    • Hazell, L.J.1    Baernthaler, G.2    Stocker, R.3
  • 42
    • 0033151902 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of proteins in plasma: Formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation
    • Hawkins, C. L. and Davies, M. J. (1999) Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation. Biochem. J. 340, 539-548
    • (1999) Biochem. J. , vol.340 , pp. 539-548
    • Hawkins, C.L.1    Davies, M.J.2
  • 43
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: Formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
    • Hawkins, C. L. and Davies, M. J. (1998) Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochem. J. 332, 617-625
    • (1998) Biochem. J. , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 44
    • 0037005896 scopus 로고    scopus 로고
    • Superoxide radicals can act synergistically with hypochlorite to induce damage to proteins
    • Hawkins, C. L., Rees, M. D. and Davies, M. J. (2002) Superoxide radicals can act synergistically with hypochlorite to induce damage to proteins. FEBS Lett. 510, 41-44
    • (2002) FEBS Lett. , vol.510 , pp. 41-44
    • Hawkins, C.L.1    Rees, M.D.2    Davies, M.J.3
  • 45
    • 0015858165 scopus 로고
    • New method for quantitative determination of uronic acids
    • Blumencrantz, N. and Asboe-Hansen, G. (1973) New method for quantitative determination of uronic acids. Anal. Biochem. 54, 484-489
    • (1973) Anal. Biochem. , vol.54 , pp. 484-489
    • Blumencrantz, N.1    Asboe-Hansen, G.2
  • 46
    • 0031005562 scopus 로고    scopus 로고
    • Structural characterization of the products of hydroxyl-radical damage to leucine and their detection on proteins
    • Fu, S. L. and Dean, R. T. (1997) Structural characterization of the products of hydroxyl-radical damage to leucine and their detection on proteins. Biochem. J. 324, 41-48
    • (1997) Biochem. J. , vol.324 , pp. 41-48
    • Fu, S.L.1    Dean, R.T.2
  • 47
    • 0029119267 scopus 로고
    • Structural identification of valine hydroperoxides and hydroxides on radical-damaged amino acid, peptide, and protein molecules
    • Fu, S., Hick, L. A., Sheil, M. M. and Dean, R. T. (1995) Structural identification of valine hydroperoxides and hydroxides on radical-damaged amino acid, peptide, and protein molecules. Free Radic. Biol. Med. 19, 281-292
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 281-292
    • Fu, S.1    Hick, L.A.2    Sheil, M.M.3    Dean, R.T.4
  • 49
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean, R. T., Fu, S., Stocker, R. and Davies, M. J. (1997) Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324, 1-18
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 50
    • 0036802227 scopus 로고    scopus 로고
    • Recent developments in the intracellular degradation of oxidized proteins
    • Dunlop, R. A., Rodgers, K. J. and Dean, R. T. (2002) Recent developments in the intracellular degradation of oxidized proteins. Free Radic. Biol. Med. 33, 894-906
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 894-906
    • Dunlop, R.A.1    Rodgers, K.J.2    Dean, R.T.3
  • 51
    • 0033117503 scopus 로고    scopus 로고
    • Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders
    • Heinecke, J. W. (1999) Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders. J. Lab. Clin. Med. 133, 321-325
    • (1999) J. Lab. Clin. Med. , vol.133 , pp. 321-325
    • Heinecke, J.W.1
  • 52
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds
    • Pattison, D. I. and Davies, M. J. (2001) Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds. Chem. Res. Toxicol. 14, 1453-1464
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 53
    • 0027292790 scopus 로고
    • Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins
    • Heinecke, J. W., Li, W., Francis, G. A. and Goldstein, J. A. (1993) Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins. J. Clin. Invest. 91, 2866-2872
    • (1993) J. Clin. Invest. , vol.91 , pp. 2866-2872
    • Heinecke, J.W.1    Li, W.2    Francis, G.A.3    Goldstein, J.A.4
  • 54
    • 0034646718 scopus 로고    scopus 로고
    • Reaction of hypochlorous acid with tyrosine and peptidyl-tyrosyl residues gives dichlorinated and aldehydic products in addition to 3-chlorotyrosine
    • Fu, S., Wang, H., Davies, M. J. and Dean, R. T. (2000) Reaction of hypochlorous acid with tyrosine and peptidyl-tyrosyl residues gives dichlorinated and aldehydic products in addition to 3-chlorotyrosine. J. Biol. Chem. 275, 10851-10858
    • (2000) J. Biol. Chem. , vol.275 , pp. 10851-10858
    • Fu, S.1    Wang, H.2    Davies, M.J.3    Dean, R.T.4
  • 55
    • 0020574002 scopus 로고
    • Long-lived oxidants generated by human neutrophils: Characterization and bioactivity
    • Weiss, S. J., Lampert, M. B. and Test, S. T. (1983) Long-lived oxidants generated by human neutrophils: characterization and bioactivity. Science 222, 625-628
    • (1983) Science , vol.222 , pp. 625-628
    • Weiss, S.J.1    Lampert, M.B.2    Test, S.T.3
  • 57
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins, C. L. and Davies, M. J. (2001) Generation and propagation of radical reactions on proteins. Biochim. Biophys. Acta 1504, 196-219
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 58
    • 0032521011 scopus 로고    scopus 로고
    • The protein oxidation product 3,4-dihydroxyphenylalanine (DOPA) mediates oxidative DNA damage
    • Morin, B., Davies, M. J. and Dean, R. T. (1998) The protein oxidation product 3,4-dihydroxyphenylalanine (DOPA) mediates oxidative DNA damage. Biochem. J 330, 1059-1067
    • (1998) Biochem. J. , vol.330 , pp. 1059-1067
    • Morin, B.1    Davies, M.J.2    Dean, R.T.3
  • 59
    • 0036680051 scopus 로고    scopus 로고
    • Oxidation of DNA, proteins and lipids by DOPA, protein-bound DOPA, and related catechols and catecholamines
    • Pattison, D. I., Dean, R. T. and Davies, M. J. (2002) Oxidation of DNA, proteins and lipids by DOPA, protein-bound DOPA, and related catechols and catecholamines. Toxicology 177, 23-37
    • (2002) Toxicology , vol.177 , pp. 23-37
    • Pattison, D.I.1    Dean, R.T.2    Davies, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.