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Volumn 36, Issue 5, 2008, Pages 1077-1082

Mass spectrometric analysis of HOCl- and free-radical-induced damage to lipids and proteins

Author keywords

Biomarker; Chlorohydrin; Chlorotyrosine; Free radical; Oxidative stress; Precursor ion scanning

Indexed keywords

ALPHA CHLOROHYDRIN; CHLORINE; HYPOCHLOROUS ACID; MYELOPEROXIDASE; PHOSPHOLIPID; SULFONAMIDE; UNSATURATED FATTY ACID;

EID: 53849111214     PISSN: 03005127     EISSN: None     Source Type: Journal    
DOI: 10.1042/BST0361077     Document Type: Conference Paper
Times cited : (33)

References (51)
  • 1
    • 30544453005 scopus 로고    scopus 로고
    • Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride
    • Senthilmohan, R. and Kettle, A.J. (2006) Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Arch. Biochem. Biophys. 445, 235-244
    • (2006) Arch. Biochem. Biophys , vol.445 , pp. 235-244
    • Senthilmohan, R.1    Kettle, A.J.2
  • 2
    • 0029760021 scopus 로고    scopus 로고
    • Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid: A novel mechanism for nitric oxide-mediated protein modification
    • Eiserich, J.P., Cross, C.E., Jones, A.D., Halliwell, B. and van der Vliet, A. (1996) Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid: a novel mechanism for nitric oxide-mediated protein modification. J. Biol. Chem. 271, 19199-19208
    • (1996) J. Biol. Chem , vol.271 , pp. 19199-19208
    • Eiserich, J.P.1    Cross, C.E.2    Jones, A.D.3    Halliwell, B.4    van der Vliet, A.5
  • 3
    • 33646757884 scopus 로고    scopus 로고
    • Myeloperoxidase and its contributory role in inflammatory vascular disease
    • Lau, D. and Balcus, S. (2006) Myeloperoxidase and its contributory role in inflammatory vascular disease. Pharmacol. Ther. 111, 16-26
    • (2006) Pharmacol. Ther , vol.111 , pp. 16-26
    • Lau, D.1    Balcus, S.2
  • 4
    • 0344514747 scopus 로고    scopus 로고
    • Myeloperoxidase in kidney disease
    • Malle, E., Buch, T. and Grone, H.J. (2003) Myeloperoxidase in kidney disease. Kidney Int. 64, 1956-1967
    • (2003) Kidney Int , vol.64 , pp. 1956-1967
    • Malle, E.1    Buch, T.2    Grone, H.J.3
  • 5
    • 33845712621 scopus 로고    scopus 로고
    • Chlorinative stress: An under appreciated mediator of neurodegeneration?
    • Yap, Y.W., Whiteman, M. and Cheung, N.S. (2007) Chlorinative stress: an under appreciated mediator of neurodegeneration? Cell. Signalling 19, 219-228
    • (2007) Cell. Signalling , vol.19 , pp. 219-228
    • Yap, Y.W.1    Whiteman, M.2    Cheung, N.S.3
  • 6
    • 0001059250 scopus 로고    scopus 로고
    • 2/halide system in human atherosclerotic lesions: Colocalization of myeloperoxidase and hypochlorite-modified proteins
    • 2/halide system in human atherosclerotic lesions: colocalization of myeloperoxidase and hypochlorite-modified proteins. Eur. J. Biochem. 267, 4495-4503
    • (2000) Eur. J. Biochem , vol.267 , pp. 4495-4503
    • Malle, E.1    Waeg, G.2    Schreiber, R.3    Grone, E.F.4    Sattler, W.5    Grone, H.J.6
  • 7
    • 0030803161 scopus 로고    scopus 로고
    • Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: A sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation
    • Hazen, S.L., Crowley, J.R., Mueller, D.M. and Heinecke, J.W. (1997) Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation. Free Radical Biol. Med. 23, 909-916
    • (1997) Free Radical Biol. Med , vol.23 , pp. 909-916
    • Hazen, S.L.1    Crowley, J.R.2    Mueller, D.M.3    Heinecke, J.W.4
  • 8
    • 0348049466 scopus 로고    scopus 로고
    • Identification of a-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions
    • Thukkani, A.K., McHowat, J., Hsu, F.F., Brennan, M.L., Hazen, S.L. and Ford, D.A. (2003) Identification of a-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions. Circulation 108, 3128-3133
    • (2003) Circulation , vol.108 , pp. 3128-3133
    • Thukkani, A.K.1    McHowat, J.2    Hsu, F.F.3    Brennan, M.L.4    Hazen, S.L.5    Ford, D.A.6
  • 9
    • 0037184780 scopus 로고    scopus 로고
    • Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid
    • Winterbourn, C.C. (2002) Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid. Toxicology 181-182, 223-227
    • (2002) Toxicology , vol.181-182 , pp. 223-227
    • Winterbourn, C.C.1
  • 10
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • Pattison, D.I. and Davies, M.J. (2006) Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases. Curr. Med. Chem. 13, 3271-3290
    • (2006) Curr. Med. Chem , vol.13 , pp. 3271-3290
    • Pattison, D.I.1    Davies, M.J.2
  • 11
    • 0037104667 scopus 로고    scopus 로고
    • Formation of lysophospholipids from unsaturated phosphatidylcholines under the influence of hypochlorous acid
    • Arnhold, J., Osipov, A.N., Spalteholz, H., Panasenko, O.M. and Schiller, J. (2002) Formation of lysophospholipids from unsaturated phosphatidylcholines under the influence of hypochlorous acid. Biochim. Biophys. Acta 1572, 91-100
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 91-100
    • Arnhold, J.1    Osipov, A.N.2    Spalteholz, H.3    Panasenko, O.M.4    Schiller, J.5
  • 12
    • 0002019504 scopus 로고    scopus 로고
    • Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated Sterols
    • Hazen, S.L., Hsu, F.F., Duffin, K. and Heinecke, J.W. (1996) Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated Sterols. J. Biol. Chem, 271, 23080-23088
    • (1996) J. Biol. Chem , vol.271 , pp. 23080-23088
    • Hazen, S.L.1    Hsu, F.F.2    Duffin, K.3    Heinecke, J.W.4
  • 13
    • 0030220416 scopus 로고    scopus 로고
    • Chlorination of cholesterol in cell membranes by hypochlorous acid
    • Carr, A.C., van den Berg, J.J. and Winterbourn, C.C. (1996) Chlorination of cholesterol in cell membranes by hypochlorous acid. Arch. Biochem. Biophys. 332, 63-69
    • (1996) Arch. Biochem. Biophys , vol.332 , pp. 63-69
    • Carr, A.C.1    van den Berg, J.J.2    Winterbourn, C.C.3
  • 14
    • 0035968168 scopus 로고    scopus 로고
    • Reactive chlorinating species produced by myeloperoxidase target the vinyl ether bond of plasmalogens: Identification of 2-chlorohexadecanal
    • Albert, C.J., Crowley, J.R., Hsu, F.F., Thukkani, A.K. and Ford, D.A. (2001) Reactive chlorinating species produced by myeloperoxidase target the vinyl ether bond of plasmalogens: identification of 2-chlorohexadecanal. J. Brol. Chem. 276, 23733-23741
    • (2001) J. Brol. Chem , vol.276 , pp. 23733-23741
    • Albert, C.J.1    Crowley, J.R.2    Hsu, F.F.3    Thukkani, A.K.4    Ford, D.A.5
  • 15
    • 33749568573 scopus 로고    scopus 로고
    • Selective plasmenylcholine oxidation by hypochlorous acid: Formation of lysophosphatidylcholine chlorohydrins
    • Messner, M.C., Albert, C.J., Hsu, F.F. and Ford, D.A. (2006) Selective plasmenylcholine oxidation by hypochlorous acid: formation of lysophosphatidylcholine chlorohydrins. Chem. Phys. Lipids 144, 34-44
    • (2006) Chem. Phys. Lipids , vol.144 , pp. 34-44
    • Messner, M.C.1    Albert, C.J.2    Hsu, F.F.3    Ford, D.A.4
  • 16
    • 0037398256 scopus 로고    scopus 로고
    • Hypochlorous acid-mediated oxidation of lipid components and antioxidants present in low-density lipoproteins: Absolute rate constants, product analysis, and computational modeling
    • Pattison, D.I., Hawkins, C.L. and Davies, M.J. (2003) Hypochlorous acid-mediated oxidation of lipid components and antioxidants present in low-density lipoproteins: absolute rate constants, product analysis, and computational modeling. Chem. Res. Toxicol. 16, 439-449
    • (2003) Chem. Res. Toxicol , vol.16 , pp. 439-449
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 17
    • 33751584261 scopus 로고    scopus 로고
    • Hypochlorous acid-derived modification of phospholipids: Characterization of aminophospholipids as regulatory molecules for lipid peroxidation
    • Kawai, Y., Kiyokawa, H., Kimura, Y., Kato, Y., Tsuchiya, K. and Terao, J. (2006) Hypochlorous acid-derived modification of phospholipids: characterization of aminophospholipids as regulatory molecules for lipid peroxidation. Biochemistry 45, 14201-14211
    • (2006) Biochemistry , vol.45 , pp. 14201-14211
    • Kawai, Y.1    Kiyokawa, H.2    Kimura, Y.3    Kato, Y.4    Tsuchiya, K.5    Terao, J.6
  • 18
    • 0141653274 scopus 로고    scopus 로고
    • Global analyses of cellular lipidomes directly from crude extracts of biological samples by ESI mass spectrometry: A bridge to lipidomics
    • Han, X. and Gross, R.W. (2003) Global analyses of cellular lipidomes directly from crude extracts of biological samples by ESI mass spectrometry: a bridge to lipidomics. J. Lipid Res. 44, 1071-1079
    • (2003) J. Lipid Res , vol.44 , pp. 1071-1079
    • Han, X.1    Gross, R.W.2
  • 19
    • 28744455623 scopus 로고    scopus 로고
    • Studies of phospholipid oxidation by electrospray mass spectrometry: From analysis in cells to biological effects
    • Spickett, C.M. and Dever, G. (2005) Studies of phospholipid oxidation by electrospray mass spectrometry: from analysis in cells to biological effects. Biofactors 24, 17-31
    • (2005) Biofactors , vol.24 , pp. 17-31
    • Spickett, C.M.1    Dever, G.2
  • 20
    • 0030962474 scopus 로고    scopus 로고
    • Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry
    • Brugger, B., Erben, G., Sandhoff, R., Wieland, F.T. and Lehmann, W.D. (1997) Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 94, 2339-2344
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 2339-2344
    • Brugger, B.1    Erben, G.2    Sandhoff, R.3    Wieland, F.T.4    Lehmann, W.D.5
  • 21
    • 0034020050 scopus 로고    scopus 로고
    • Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS
    • Jerlich, A., Pitt, A.R., Schaur, R.J. and Spickett, C.M. (2000) Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS. Free Radical Biol. Med. 28, 673-682
    • (2000) Free Radical Biol. Med , vol.28 , pp. 673-682
    • Jerlich, A.1    Pitt, A.R.2    Schaur, R.J.3    Spickett, C.M.4
  • 22
    • 0035870893 scopus 로고    scopus 로고
    • Detection of phospholipid oxidation in oxidatively stressed cells by reversed-phase HPLC coupled with positive-ionization electrospray MS
    • Spickett, C.M., Rennie, N., Winter, H., Zambonin, L., Landr, L., Jerlich, A., Schaur, R.J. and Pitt, A.R. (2001) Detection of phospholipid oxidation in oxidatively stressed cells by reversed-phase HPLC coupled with positive-ionization electrospray MS. Biochem. J. 355, 449-457
    • (2001) Biochem. J , vol.355 , pp. 449-457
    • Spickett, C.M.1    Rennie, N.2    Winter, H.3    Zambonin, L.4    Landr, L.5    Jerlich, A.6    Schaur, R.J.7    Pitt, A.R.8
  • 23
    • 1442348379 scopus 로고    scopus 로고
    • Evaluation of products upon the reaction of hypohalous acid with unsaturated phosphatidylcholines
    • Spalteholz, H., Wenske, K., Panasenko, O.M., Schiller, J. and Arnhold, J. (2004) Evaluation of products upon the reaction of hypohalous acid with unsaturated phosphatidylcholines. Chem. Phys. Lipids 129, 85-96
    • (2004) Chem. Phys. Lipids , vol.129 , pp. 85-96
    • Spalteholz, H.1    Wenske, K.2    Panasenko, O.M.3    Schiller, J.4    Arnhold, J.5
  • 25
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • Hawkins, C.L., Pattison, D.I. and Davies, M.J. (2003) Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids 25, 259-274
    • (2003) Amino Acids , vol.25 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Davies, M.J.3
  • 26
    • 0036292867 scopus 로고    scopus 로고
    • Myeloperoxidase-mediated protein oxidation: Its possible biological functions
    • Naskalski, J.W., Marcinkiewicz, J. and Drozdz, R. (2002) Myeloperoxidase-mediated protein oxidation: its possible biological functions. Clin. Chem. Lab. Med. 40, 463-468
    • (2002) Clin. Chem. Lab. Med , vol.40 , pp. 463-468
    • Naskalski, J.W.1    Marcinkiewicz, J.2    Drozdz, R.3
  • 27
    • 33646788424 scopus 로고    scopus 로고
    • Nitrotyrosine and chlorotyrosine: Clinical significance and biological functions in the vascular system
    • Mohiuddin, I., Chai, H., Lin, P.H., Lumsden, A.B., Yao, Q. and Chen, C. (2006) Nitrotyrosine and chlorotyrosine: clinical significance and biological functions in the vascular system. J. Surg. Res. 133, 143-149
    • (2006) J. Surg. Res , vol.133 , pp. 143-149
    • Mohiuddin, I.1    Chai, H.2    Lin, P.H.3    Lumsden, A.B.4    Yao, Q.5    Chen, C.6
  • 29
    • 0038825874 scopus 로고    scopus 로고
    • Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation
    • Guan, Z., Yates, N.A. and Bakhtiar, R. (2003) Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation. J. Am. Soc. Mass Spectrom. 14, 605-613
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 605-613
    • Guan, Z.1    Yates, N.A.2    Bakhtiar, R.3
  • 30
    • 40649107852 scopus 로고    scopus 로고
    • Dehydroalanine derived from cysteine is a common post-translational modification in human serum albumin
    • Bar-Or, R., Rael, L.T. and Bar-Or, D. (2008) Dehydroalanine derived from cysteine is a common post-translational modification in human serum albumin. Rapid Commun. Mass Spectrom. 22, 711-716
    • (2008) Rapid Commun. Mass Spectrom , vol.22 , pp. 711-716
    • Bar-Or, R.1    Rael, L.T.2    Bar-Or, D.3
  • 31
    • 0000540068 scopus 로고
    • Tandem mass-spectrometric characterization of a specific cysteic acid residue in oxidized human apoprotein B-100
    • Burlet, O., Yang, C.Y., Guyton, J.R. and Gaskell, S.J. (1995) Tandem mass-spectrometric characterization of a specific cysteic acid residue in oxidized human apoprotein B-100. J. Am. Soc. Mass Spectrom. 6, 242-247
    • (1995) J. Am. Soc. Mass Spectrom , vol.6 , pp. 242-247
    • Burlet, O.1    Yang, C.Y.2    Guyton, J.R.3    Gaskell, S.J.4
  • 32
    • 34249003048 scopus 로고    scopus 로고
    • Mass spectrometry-based analyses for identifying and characterizing S-nitfosylation of protein tyrosine phosphatases
    • Chen, Y.Y., Huang, Y.F., Khoo, K.H. and Meng, T.C. (2007) Mass spectrometry-based analyses for identifying and characterizing S-nitfosylation of protein tyrosine phosphatases. Methods 42, 243-249
    • (2007) Methods , vol.42 , pp. 243-249
    • Chen, Y.Y.1    Huang, Y.F.2    Khoo, K.H.3    Meng, T.C.4
  • 33
    • 0029160379 scopus 로고
    • Monitoring reactions of nitric oxide with peptides and proteins by electro-spray ionization-mass spectrometry
    • Mirza, U.A., Chait, B.T. and Lander, H.M. (1995) Monitoring reactions of nitric oxide with peptides and proteins by electro-spray ionization-mass spectrometry. J. Biol. Chem. 270, 17185-17188
    • (1995) J. Biol. Chem , vol.270 , pp. 17185-17188
    • Mirza, U.A.1    Chait, B.T.2    Lander, H.M.3
  • 35
    • 0031791713 scopus 로고    scopus 로고
    • Identification of tryptophan oxidation products in bovine α-crystallin
    • Finley, E.L., Dillon, J., Crouch, R.K. and Schey, K.L. (1998) Identification of tryptophan oxidation products in bovine α-crystallin. Protein Sci. 7, 2391-2397
    • (1998) Protein Sci , vol.7 , pp. 2391-2397
    • Finley, E.L.1    Dillon, J.2    Crouch, R.K.3    Schey, K.L.4
  • 37
    • 0029952814 scopus 로고    scopus 로고
    • First direct evidence for lipid/protein conjugation in oxidized human low density lipoprotein
    • Bolgar, M.S., Yang, C.Y. and Gaskell, S.J. (1996) First direct evidence for lipid/protein conjugation in oxidized human low density lipoprotein. J. Biol. Chem. 271, 27999-28001
    • (1996) J. Biol. Chem , vol.271 , pp. 27999-28001
    • Bolgar, M.S.1    Yang, C.Y.2    Gaskell, S.J.3
  • 38
    • 3242768438 scopus 로고    scopus 로고
    • Modification of cytochrome c by 4-hydfoxy-2-nonenal: Evidence for histidine, lysine, and arginine-aldehyde adducts
    • Isom, A.L., Barnes, S., Wilson, L., Kirk, M., Coward, L. and Darley-Usmar, V. (2004) Modification of cytochrome c by 4-hydfoxy-2-nonenal: evidence for histidine, lysine, and arginine-aldehyde adducts. J. Am. Soc. Mass Spectrom. 15, 1136-1147
    • (2004) J. Am. Soc. Mass Spectrom , vol.15 , pp. 1136-1147
    • Isom, A.L.1    Barnes, S.2    Wilson, L.3    Kirk, M.4    Coward, L.5    Darley-Usmar, V.6
  • 39
    • 0141634353 scopus 로고    scopus 로고
    • Detection of four oxidation sites in viral prolyl-4-hydroxylase by top-down mass spectrometry
    • Ge, Y,, Lawhorn, B.G., ElNaggar, M., Sze, S.K., Begley, T.P. and McLafferty, F.W. (2003) Detection of four oxidation sites in viral prolyl-4-hydroxylase by top-down mass spectrometry. Protein Sci. 12, 2320-2326
    • (2003) Protein Sci , vol.12 , pp. 2320-2326
    • Ge, Y.1    Lawhorn, B.G.2    ElNaggar, M.3    Sze, S.K.4    Begley, T.P.5    McLafferty, F.W.6
  • 40
    • 2442456741 scopus 로고    scopus 로고
    • Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and pefoxynitrite (ONOO-)
    • Khor, H.K., Fisher, M.T. and Schoneich, C. (2004) Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and pefoxynitrite (ONOO-). J. Biol. Chem. 279, 19486-19493
    • (2004) J. Biol. Chem , vol.279 , pp. 19486-19493
    • Khor, H.K.1    Fisher, M.T.2    Schoneich, C.3
  • 41
    • 0037192149 scopus 로고    scopus 로고
    • Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: A potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase
    • Fu, X., Mueller, D.M. and Heinecke, J.W. (2002) Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: a potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase. Biochemistry 41, 1293-1301
    • (2002) Biochemistry , vol.41 , pp. 1293-1301
    • Fu, X.1    Mueller, D.M.2    Heinecke, J.W.3
  • 42
    • 0035823537 scopus 로고    scopus 로고
    • Novel intra- and inter-molecular sulfinamide bonds in S100A8 produced by hypachlorite oxidation
    • Raftery, M.J., Yang, Z., Valenzuela, S.M. and Geczy, C.L. (2001) Novel intra- and inter-molecular sulfinamide bonds in S100A8 produced by hypachlorite oxidation. J. Biol. Chem. 276, 33393-33401
    • (2001) J. Biol. Chem , vol.276 , pp. 33393-33401
    • Raftery, M.J.1    Yang, Z.2    Valenzuela, S.M.3    Geczy, C.L.4
  • 43
    • 14044250955 scopus 로고    scopus 로고
    • Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxiclase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport
    • Shao, B., Bergt, C., Fu, X., Green, P., Voss, J.C., Oda, M.N., Oram, J.F. and Heinecke, J.W. (2005) Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxiclase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport. J. Biol. Chem. 280, 5983-5993
    • (2005) J. Biol. Chem , vol.280 , pp. 5983-5993
    • Shao, B.1    Bergt, C.2    Fu, X.3    Green, P.4    Voss, J.C.5    Oda, M.N.6    Oram, J.F.7    Heinecke, J.W.8
  • 44
    • 1542289811 scopus 로고    scopus 로고
    • Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein
    • Bergt, C., Fu, X., Huq, N.P., Kao, J. and Heinecke, J.W. (2004) Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein. J. Biol. Chem. 279, 7856-7866
    • (2004) J. Biol. Chem , vol.279 , pp. 7856-7866
    • Bergt, C.1    Fu, X.2    Huq, N.P.3    Kao, J.4    Heinecke, J.W.5
  • 45
    • 0242468729 scopus 로고    scopus 로고
    • Quantitative screening of advanced glycation endproducts in cellular and extracellulaf proteins by tandem mass spectrometry
    • Thornalley, P.J., Battah, S., Ahmed, N., Karachalias, N., Agalou, S., Babaei-Jadidi, R. and Dawnay, A. (2003) Quantitative screening of advanced glycation endproducts in cellular and extracellulaf proteins by tandem mass spectrometry. Biochem. J. 375, 581-592
    • (2003) Biochem. J , vol.375 , pp. 581-592
    • Thornalley, P.J.1    Battah, S.2    Ahmed, N.3    Karachalias, N.4    Agalou, S.5    Babaei-Jadidi, R.6    Dawnay, A.7
  • 47
    • 36849089644 scopus 로고    scopus 로고
    • HNE Michael adducts to histidine and histidine-containing peptides as bromarkers of lipid-derived carbonyl stress in urines: LC-MS/ MS profiling in Zucker obese rats
    • Orioli, M., Aldini, G., Benfatto, M.C., Facino, R.M. and Carini, M. (2007) HNE Michael adducts to histidine and histidine-containing peptides as bromarkers of lipid-derived carbonyl stress in urines: LC-MS/ MS profiling in Zucker obese rats. Anal. Chem. 79, 9174-9184
    • (2007) Anal. Chem , vol.79 , pp. 9174-9184
    • Orioli, M.1    Aldini, G.2    Benfatto, M.C.3    Facino, R.M.4    Carini, M.5
  • 48
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter, E. (2000) Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 32, 307-326
    • (2000) Drug Metab. Rev , vol.32 , pp. 307-326
    • Shacter, E.1
  • 49
    • 33646580362 scopus 로고    scopus 로고
    • Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells
    • Greco, T.M., Hodara, R., Pafastatidis, I., Heijnen, H.F., Dennehy, M.K., Lieblef, D.C. and Ischiropoulos, H. (2006) Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells. Proc. Natl. Acad. Sci. U.S.A. 103, 7420-7425
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 7420-7425
    • Greco, T.M.1    Hodara, R.2    Pafastatidis, I.3    Heijnen, H.F.4    Dennehy, M.K.5    Lieblef, D.C.6    Ischiropoulos, H.7
  • 50
    • 0042164949 scopus 로고    scopus 로고
    • Redox proteomics: Identification of oxidatively modified proteins
    • Ghezzi, P. and Bonetto, V. (2003) Redox proteomics: identification of oxidatively modified proteins. Proteomics 3, 1145-1153
    • (2003) Proteomics , vol.3 , pp. 1145-1153
    • Ghezzi, P.1    Bonetto, V.2
  • 51
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry
    • Roe, M.R., Xie, H., Bandhakavi, S. and Griffin, T.J. (2007) Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Anal. Chem. 79, 3747-3756
    • (2007) Anal. Chem , vol.79 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4


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