메뉴 건너뛰기




Volumn 17, Issue 11, 2012, Pages 1528-1559

Cardiovascular redox and ox stress proteomics

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DERIVATIVE; ANTIBODY; BIOLOGICAL MARKER; CYSTEINE; DISULFIDE; HISTIDINE; LYSINE; METHIONINE; PHENYLALANINE; THYRONINE; TRYPTOPHAN;

EID: 84866871142     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4706     Document Type: Review
Times cited : (22)

References (314)
  • 1
    • 80054001981 scopus 로고    scopus 로고
    • Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2
    • Aachmann FL, Kwak GH, Del Conte R, Kim HY, Gladyshev VN, and Dikiy A. Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2. Proteins 79: 3123-3131, 2011.
    • (2011) Proteins , vol.79 , pp. 3123-3131
    • Aachmann, F.L.1    Kwak, G.H.2    Del Conte, R.3    Kim, H.Y.4    Gladyshev, V.N.5    Dikiy, A.6
  • 2
    • 67650354415 scopus 로고    scopus 로고
    • Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins
    • Abello N, Kerstjens HA, Postma DS, and Bischoff R. Protein tyrosine nitration: selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins. J Proteome Res 8: 3222-3238, 2009.
    • (2009) J Proteome Res , vol.8 , pp. 3222-3238
    • Abello, N.1    Kerstjens, H.A.2    Postma, D.S.3    Bischoff, R.4
  • 3
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • DOI 10.1074/jbc.M313320200
    • Adachi T, Pimentel DR, Heibeck T, Hou X, Lee YJ, Jiang B, Ido Y, and Cohen RA. S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem 279: 29857-29862, 2004. (Pubitemid 38915870)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.28 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 4
    • 9144266981 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • DOI 10.1038/nm1119
    • Adachi T, Weisbrod RM, Pimentel DR, Ying J, Sharov VS, Schoneich C, and Cohen RA. S-Glutathiolation by perox-ynitrite activates SERCA during arterial relaxation by nitric oxide. Nat Med 10: 1200-1207, 2004. (Pubitemid 39540436)
    • (2004) Nature Medicine , vol.10 , Issue.11 , pp. 1200-1207
    • Adachi, T.1    Weisbrod, R.M.2    Pimentel, D.R.3    Ying, J.4    Sharov, V.S.5    Schoneich, C.6    Cohen, R.A.7
  • 5
    • 78650806850 scopus 로고    scopus 로고
    • Thioredoxin 1 enhances neovascularization and reduces ventricular remodeling during chronic myocardial infarction: A study using thioredoxin 1 transgenic mice
    • Adluri RS, Thirunavukkarasu M, Zhan L, Akita Y, Samuel SM, Otani H, Ho YS, Maulik G, and Maulik N. Thioredoxin 1 enhances neovascularization and reduces ventricular remodeling during chronic myocardial infarction: a study using thioredoxin 1 transgenic mice. J Mol Cell Cardiol 50: 239-247, 2011.
    • (2011) J Mol Cell Cardiol , vol.50 , pp. 239-247
    • Adluri, R.S.1    Thirunavukkarasu, M.2    Zhan, L.3    Akita, Y.4    Samuel, S.M.5    Otani, H.6    Ho, Y.S.7    Maulik, G.8    Maulik, N.9
  • 6
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold R and Mann M. Mass spectrometry-based proteomics. Nature 422: 198-207, 2003. (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 7
    • 44649184557 scopus 로고    scopus 로고
    • A Redox-Dependent Pathway for Regulating Class II HDACs and Cardiac Hypertrophy
    • DOI 10.1016/j.cell.2008.04.041, PII S0092867408006156
    • Ago T, Liu T, Zhai P, Chen W, Li H, Molkentin JD, Vatner SF, and Sadoshima J. A redox-dependent pathway for regulating class II HDACs and cardiac hypertrophy. Cell 133: 978-993, 2008. (Pubitemid 351787743)
    • (2008) Cell , vol.133 , Issue.6 , pp. 978-993
    • Ago, T.1    Liu, T.2    Zhai, P.3    Chen, W.4    Li, H.5    Molkentin, J.D.6    Vatner, S.F.7    Sadoshima, J.8
  • 9
    • 0001637467 scopus 로고
    • Formation and reactions of sulfenic acids in proteins
    • Allison WS. Formation and reactions of sulfenic acids in proteins. Acc Chem Res 9: 293-299, 1976.
    • (1976) Acc Chem Res , vol.9 , pp. 293-299
    • Allison, W.S.1
  • 10
    • 33847643676 scopus 로고    scopus 로고
    • Bidimensional tandem mass spectrometry for selective identification of nitration sites in proteins
    • DOI 10.1021/ac0620361
    • Amoresano A, Chiappetta G, Pucci P, D'Ischia M, and Marino G. Bidimensional tandem mass spectrometry for selective identification of nitration sites in proteins. Anal Chem 79: 2109-2117, 2007. (Pubitemid 46355246)
    • (2007) Analytical Chemistry , vol.79 , Issue.5 , pp. 2109-2117
    • Amoresano, A.1    Chiappetta, G.2    Pucci, P.3    D'Ischia, M.4    Marino, G.5
  • 11
    • 33646259481 scopus 로고    scopus 로고
    • Selective detection and identification of phosphopeptides by dansyl MS/MS/MS fragmentation
    • Amoresano A, Monti G, Cirulli C, and Marino G. Selective detection and identification of phosphopeptides by dansyl MS/MS/MS fragmentation. Rapid Commun Mass Spectrom 20: 1400-1404, 2006.
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 1400-1404
    • Amoresano, A.1    Monti, G.2    Cirulli, C.3    Marino, G.4
  • 12
    • 0031417973 scopus 로고    scopus 로고
    • Activation of the NADPH oxidase in human fibroblasts by mechanical intrusion of a single cell with an ultramicroelectrode
    • DOI 10.1093/carcin/18.3.569
    • Arbault S, Pantano P, Sojic N, Amatore C, Best-Belpomme M, Sarasin A, and Vuillaume M. Activation of the NADPH oxidase in human fibroblasts by mechanical intrusion of a single cell with an ultramicroelectrode. Carcinogenesis 18: 569-574, 1997. (Pubitemid 28132496)
    • (1997) Carcinogenesis , vol.18 , Issue.3 , pp. 569-574
    • Arbault, S.1    Pantano, P.2    Sojic, N.3    Amatore, C.4    Best-Belpomme, M.5    Sarasin, A.6    Vuillaume, M.7
  • 13
    • 79957578430 scopus 로고    scopus 로고
    • Aldose reductase (AKR1B3) regulates the accumulation of advanced glycosylation end products (AGEs) and the expression of AGE receptor (RAGE)
    • Baba SP, Hellmann J, Srivastava S, and Bhatnagar A. Aldose reductase (AKR1B3) regulates the accumulation of advanced glycosylation end products (AGEs) and the expression of AGE receptor (RAGE). Chem Biol Interact 191: 357-363, 2011.
    • (2011) Chem Biol Interact , vol.191 , pp. 357-363
    • Baba, S.P.1    Hellmann, J.2    Srivastava, S.3    Bhatnagar, A.4
  • 14
    • 84866607741 scopus 로고    scopus 로고
    • Vascular aging: Chronic oxidative stress and impairment of redox signaling-consequences for vascular homeostasis and disease
    • Epub ahead of print DOI: 10.3109/07853890.2011.645498
    • Bachschmid MM, Schildknecht S, Matsui R, Zee R, Haeussler D, A Cohen R, Pimental D, and Loo BV. Vascular aging: chronic oxidative stress and impairment of redox signaling-consequences for vascular homeostasis and disease. Ann Med 2012 [Epub ahead of print]; DOI: 10.3109/07853890.2011.645498.
    • (2012) Ann Med
    • Bachschmid, M.M.1    Schildknecht, S.2    Matsui, R.3    Zee, R.4    Haeussler, D.5    Cohen R, A.6    Pimental, D.7    Loo, B.V.8
  • 15
    • 77956174156 scopus 로고    scopus 로고
    • Attenuated cardiovascular hypertrophy and oxidant generation in response to angiotensin II infusion in glutaredoxin-1 knockout mice
    • Bachschmid MM, Xu S, Maitland-Toolan KA, Ho YS, Cohen RA, and Matsui R. Attenuated cardiovascular hypertrophy and oxidant generation in response to angiotensin II infusion in glutaredoxin-1 knockout mice. Free Radic Biol Med 49: 1221-1229, 2010.
    • (2010) Free Radic Biol Med , vol.49 , pp. 1221-1229
    • Bachschmid, M.M.1    Xu, S.2    Maitland-Toolan, K.A.3    Ho, Y.S.4    Cohen, R.A.5    Matsui, R.6
  • 16
    • 78650692177 scopus 로고    scopus 로고
    • Posttranslational modification and regulation of glutamatecysteine ligase by the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal
    • BackosDS, FritzKS, Roede JR, PetersenDR, and FranklinCC. Posttranslational modification and regulation of glutamatecysteine ligase by the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal. Free Radic Biol Med 50: 14-26, 2011.
    • (2011) Free Radic Biol Med , vol.50 , pp. 14-26
    • Backos, D.S.1    Fritz, K.S.2    Roede, J.R.3    Petersen, D.R.4    Franklin, C.C.5
  • 17
    • 0037462277 scopus 로고    scopus 로고
    • Kynurenines and the respiratory parameters on rat heart mitochondria
    • DOI 10.1016/S0024-3205(02)02365-2, PII S0024320502023652
    • Baran H, Staniek K, Kepplinger B, Stur J, Draxler M, and Nohl H. Kynurenines and the respiratory parameters on rat heart mitochondria. Life Sci 72: 1103-1115, 2003. (Pubitemid 36050794)
    • (2003) Life Sciences , vol.72 , Issue.10 , pp. 1103-1115
    • Baran, H.1    Staniek, K.2    Kepplinger, B.3    Stur, J.4    Draxler, M.5    Nohl, H.6
  • 18
    • 75149149380 scopus 로고    scopus 로고
    • Protein carbonylation in skeletal muscles: Impact on function
    • Barreiro E and Hussain SN. Protein carbonylation in skeletal muscles: impact on function. Antioxid Redox Signal 12: 417-429, 2010.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 417-429
    • Barreiro, E.1    Hussain, S.N.2
  • 19
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty JW, Hampton MB, and Winterbourn CC. Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2: 1261-1266, 2002.
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 20
    • 0025345820 scopus 로고
    • Application of avidin-biotin technology to affinity-based separations
    • DOI 10.1016/S0021-9673(01)93733-1
    • Bayer EA and Wilchek M. Application of avidin-biotin technology to affinity-based separations. J Chromatogr 510: 3-11, 1990. (Pubitemid 20197875)
    • (1990) Journal of Chromatography , vol.510 , pp. 3-11
    • Bayer, E.A.1    Wilchek, M.2
  • 23
    • 0019193338 scopus 로고
    • Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids
    • Benedetti A, Comporti M, and Esterbauer H. Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids. Biochim Biophys Acta 620: 281-296, 1980. (Pubitemid 11216247)
    • (1980) Biochimica et Biophysica Acta , vol.620 , Issue.2 , pp. 281-296
    • Benedetti, A.1    Comporti, M.2    Esterbauer, H.3
  • 24
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • DOI 10.1126/science.1158265
    • Benhar M, Forrester MT, Hess DT, and Stamler JS. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320: 1050-1054, 2008. (Pubitemid 351929542)
    • (2008) Science , vol.320 , Issue.5879 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 25
    • 77955576782 scopus 로고    scopus 로고
    • Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach
    • Benhar M, Thompson JW, Moseley MA, and Stamler JS. Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach. Biochemistry 49: 6963-6969, 2010.
    • (2010) Biochemistry , vol.49 , pp. 6963-6969
    • Benhar, M.1    Thompson, J.W.2    Ma, M.3    Stamler, J.S.4
  • 26
    • 0016256290 scopus 로고
    • The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins
    • Benitez LV and Allison WS. The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins. J Biol Chem 249: 6234-6243, 1974.
    • (1974) J Biol Chem , vol.249 , pp. 6234-6243
    • Benitez, L.V.1    Allison, W.S.2
  • 27
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • DOI 10.1074/jbc.272.33.20313
    • Berlett BS and Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272: 20313-20316, 1997. (Pubitemid 27355575)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 28
    • 0028899620 scopus 로고
    • Electrophysiological effects of 4-hydroxynonenal, an aldehydic product of lipid peroxidation, on isolated rat ventricular myocytes
    • Bhatnagar A. Electrophysiological effects of 4-hydroxynonenal, an aldehydic product of lipid peroxidation, on isolated rat ventricular myocytes. Circ Res 76: 293-304, 1995.
    • (1995) Circ Res , vol.76 , pp. 293-304
    • Bhatnagar, A.1
  • 32
    • 4744363388 scopus 로고    scopus 로고
    • Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis
    • DOI 10.1074/jbc.M403827200
    • Brennan JP, Wait R, Begum S, Bell JR, Dunn MJ, and Eaton P. Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis. J Biol Chem 279: 41352-41360, 2004. (Pubitemid 39313574)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41352-41360
    • Brennan, J.P.1    Wait, R.2    Begum, S.3    Bell, J.R.4    Dunn, M.J.5    Eaton, P.6
  • 33
    • 0037047414 scopus 로고    scopus 로고
    • The local electrostatic environment determines cysteine reactivity of tubulin
    • Britto PJ, Knipling L, and Wolff J. The local electrostatic environment determines cysteine reactivity of tubulin. J Biol Chem 277: 29018-29027, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 29018-29027
    • Britto, P.J.1    Knipling, L.2    Wolff, J.3
  • 35
    • 0026663037 scopus 로고
    • A novel hypothesis of lipofuscinogenesis and cellular aging based on interactions between oxidative stress and autophagocytosis
    • Brunk UT, Jones CB, and Sohal RS. A novel hypothesis of lipofuscinogenesis and cellular aging based on interactions between oxidative stress and autophagocytosis. Mutat Res 275: 395-403, 1992.
    • (1992) Mutat Res , vol.275 , pp. 395-403
    • Brunk, U.T.1    Jones, C.B.2    Sohal, R.S.3
  • 37
    • 77953257870 scopus 로고    scopus 로고
    • Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease
    • Butterfield DA, Bader Lange ML, and Sultana R. Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease. Biochim Biophys Acta 1801: 924-929, 2010.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 924-929
    • Butterfield, D.A.1    Bader Lange, M.L.2    Sultana, R.3
  • 38
    • 34548152584 scopus 로고    scopus 로고
    • A novel approach to identify proteins modified by nitric oxide: The HIS-TAG switch method
    • DOI 10.1021/pr0701456
    • Camerini S, Polci ML, Restuccia U, Usuelli V, Malgaroli A, and Bachi A. A novel approach to identify proteins modified by nitric oxide: the HIS-TAG switch method. J Proteome Res 6: 3224-3231, 2007. (Pubitemid 47310207)
    • (2007) Journal of Proteome Research , vol.6 , Issue.8 , pp. 3224-3231
    • Camerini, S.1    Polci, M.L.2    Restuccia, U.3    Usuelli, V.4    Malgaroli, A.5    Bachi, A.6
  • 39
    • 33744988762 scopus 로고    scopus 로고
    • Angiotensin type-1 receptor A1166C gene polymorphism correlates with oxidative stress levels in human heart failure
    • DOI 10.1161/01.HYP.0000222893.85662.cd, PII 0000426820060600000021
    • Cameron VA, Mocatta TJ, Pilbrow AP, Frampton CM, Troughton RW, Richards AM, and Winterbourn CC. Angiotensin type-1 receptor A1166C gene polymorphism correlates with oxidative stress levels in human heart failure. Hypertension 47: 1155-1161, 2006. (Pubitemid 44289173)
    • (2006) Hypertension , vol.47 , Issue.6 , pp. 1155-1161
    • Cameron, V.A.1    Mocatta, T.J.2    Pilbrow, A.P.3    Frampton, C.M.4    Troughton, R.W.5    Richards, A.M.6    Winterbourn, C.C.7
  • 40
    • 0029743817 scopus 로고    scopus 로고
    • Redox modulation of L-type calcium channels in ferret ventricular myocytes: Dual mechanism regulation by nitric oxide and S-nitrosothiols
    • Campbell DL, Stamler JS, and Strauss HC. Redox modulation of L-type calcium channels in ferret ventricular myocytes. Dual mechanism regulation by nitric oxide and S-nitrosothiols. J Gen Physiol 108: 277-293, 1996. (Pubitemid 26332539)
    • (1996) Journal of General Physiology , vol.108 , Issue.4 , pp. 277-293
    • Campbell, D.L.1    Stamler, J.S.2    Strauss, H.C.3
  • 43
    • 0036702810 scopus 로고    scopus 로고
    • Cellular thiols redox status: A switch for NF-κB activation during myocardial post-ischaemic reperfusion
    • DOI 10.1006/jmcc.2002.2046
    • Cargnoni A, Ceconi C, Gaia G, Agnoletti L, and Ferrari R. Cellular thiols redox status: a switch for NF-kappaB activation during myocardial post-ischaemic reperfusion. J Mol Cell Cardiol 34: 997-1005, 2002. (Pubitemid 35316147)
    • (2002) Journal of Molecular and Cellular Cardiology , vol.34 , Issue.8 , pp. 997-1005
    • Cargnoni, A.1    Ceconi, C.2    Gaia, G.3    Agnoletti, L.4    Ferrari, R.5
  • 45
    • 77955640917 scopus 로고    scopus 로고
    • Mapping protein cysteine sulfonic acid modifications with specific enrichment and mass spectrometry: An integrated approach to explore the cysteine oxidation
    • Chang YC, Huang CN, Lin CH, Chang HC, and Wu CC. Mapping protein cysteine sulfonic acid modifications with specific enrichment and mass spectrometry: an integrated approach to explore the cysteine oxidation. Proteomics 10: 2961-2971, 2010.
    • (2010) Proteomics , vol.10 , pp. 2961-2971
    • Chang, Y.C.1    Huang, C.N.2    Chang, C.H.3    Chang, H.C.4    Wu, C.C.5
  • 47
    • 33749457861 scopus 로고    scopus 로고
    • New role for an old probe: Affinity labeling of oxylipid protein conjugates by N'-aminooxymethylcarbonylhydrazino D-biotin
    • DOI 10.1021/ac0607257
    • Chavez J, Wu J, Han B, Chung W-G, and Maier CS. New role for an old probe: affinity labeling of oxylipid protein conjugates by N¢- aminooxymethylcarbonylhydrazino dbiotin. Anal Chem 78: 6847-6854, 2006. (Pubitemid 44522535)
    • (2006) Analytical Chemistry , vol.78 , Issue.19 , pp. 6847-6854
    • Chavez, J.1    Wu, J.2    Han, B.3    Chung, W.-G.4    Maier, C.S.5
  • 49
    • 0035196175 scopus 로고    scopus 로고
    • Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart
    • DOI 10.1006/jmcc.2001.1454
    • Chen J, Henderson GI, and Freeman GL. Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart. J Mol Cell Cardiol 33: 1919-1927, 2001. (Pubitemid 33097271)
    • (2001) Journal of Molecular and Cellular Cardiology , vol.33 , Issue.11 , pp. 1919-1927
    • Chen, J.1    Henderson, G.I.2    Freeman, G.L.3
  • 50
    • 80955158726 scopus 로고    scopus 로고
    • Thioredoxin reductase inhibition reduces relaxation by increasing oxidative stress and s-nitrosylation in mouse aorta
    • Choi H, Tostes RC, and Webb RC. Thioredoxin reductase inhibition reduces relaxation by increasing oxidative stress and s-nitrosylation in mouse aorta. J Cardiovasc Pharmacol 58: 522-527, 2011.
    • (2011) J Cardiovasc Pharmacol , vol.58 , pp. 522-527
    • Choi, H.1    Tostes, R.C.2    Webb, R.C.3
  • 51
    • 77955492720 scopus 로고    scopus 로고
    • Identification of S-nitrosated mitochondrial proteins by Snitrosothiol difference in gel electrophoresis (SNO-DIGE): Implications for the regulation of mitochondrial function by reversible S-nitrosation
    • Chouchani ET, Hurd TR, Nadtochiy SM, Brookes PS, Fearnley IM, Lilley KS, Smith RA, and Murphy MP. Identification of S-nitrosated mitochondrial proteins by Snitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation. Biochem J 430: 49-59, 2010.
    • (2010) Biochem J , vol.430 , pp. 49-59
    • Chouchani, E.T.1    Hurd, T.R.2    Nadtochiy, S.M.3    Brookes, P.S.4    Fearnley, I.M.5    Lilley, K.S.6    Smith, R.A.7    Murphy, M.P.8
  • 52
    • 27744449782 scopus 로고    scopus 로고
    • S-nitrosylation in Parkinson's disease and related neurodegenerative disorders
    • DOI 10.1016/S0076-6879(05)96014-X, PII S007668790596014X, Nitric Oxide
    • Chung KK, Dawson VL, and Dawson TM. S-nitrosylation in Parkinson's disease and related neurodegenerative disorders. Methods Enzymol 396: 139-150, 2005. (Pubitemid 41603545)
    • (2005) Methods in Enzymology , vol.396 , pp. 139-150
    • Chung, K.K.K.1    Dawson, V.L.2    Dawson, T.M.3
  • 53
    • 33645806282 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells
    • DOI 10.1096/fj.05-4875fje
    • Clavreul N, Adachi T, Pimental DR, Ido Y, Schoneich C, and Cohen RA. S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J 20: 518-520, 2006. (Pubitemid 46671235)
    • (2006) FASEB Journal , vol.20 , Issue.3 , pp. 518-520
    • Clavreul, N.1    Adachi, T.2    Pimental, D.R.3    Ido, Y.4    Schoneich, C.5    Cohen, R.A.6
  • 55
    • 0023235798 scopus 로고
    • S-thiolation of cytoplasmic cardiac creatine kinase in heart cells treated with diamide
    • DOI 10.1016/0167-4889(87)90112-1
    • Collison MW and Thomas JA. S-thiolation of cytoplasmic cardiac creatine kinase in heart cells treated with diamide. Biochim Biophys Acta 928: 121-129, 1987. (Pubitemid 17063341)
    • (1987) Biochimica et Biophysica Acta - Molecular Cell Research , vol.928 , Issue.2 , pp. 121-129
    • Collison, M.W.1    Thomas, J.A.2
  • 56
    • 80054732682 scopus 로고    scopus 로고
    • Quantitative proteomics of complex mixtures
    • Coombs KM. Quantitative proteomics of complex mixtures. Expert Rev Proteomics 8: 659-677, 2011.
    • (2011) Expert Rev Proteomics , vol.8 , pp. 659-677
    • Coombs, K.M.1
  • 57
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • DOI 10.1038/nature06525, PII NATURE06525
    • Cravatt BF, Simon GM, and Yates JR, 3rd. The biological impact of mass-spectrometry-based proteomics. Nature 450: 991-1000, 2007. (Pubitemid 350273629)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates III, J.R.3
  • 58
    • 0000111712 scopus 로고
    • The oxidation of amino-acids with the production of substances of biological importance
    • Dakin HD. The oxidation of amino-acids with the production of substances of biological importance. J Biol Chem 1: 171-176, 1905.
    • (1905) J Biol Chem , vol.1 , pp. 171-176
    • Dakin, H.D.1
  • 60
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. general aspects
    • Davies KJ. Protein damage and degradation by oxygen radicals. I. general aspects. J Biol Chem 262: 9895-9901, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.1
  • 63
    • 33845967456 scopus 로고    scopus 로고
    • Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples
    • DOI 10.1002/mas.20109
    • DiMarco T and Giulivi C. Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples. Mass Spectrom Rev 26: 108-120, 2007. (Pubitemid 46051815)
    • (2007) Mass Spectrometry Reviews , vol.26 , Issue.1 , pp. 108-120
    • DiMarco, T.1    Giulivi, C.2
  • 65
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B and Aebersold R. Mass spectrometry and protein analysis. Science 312: 212-217, 2006.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 66
    • 78049288138 scopus 로고    scopus 로고
    • Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation
    • Doulias PT, Greene JL, Greco TM, Tenopoulou M, Seeholzer SH, Dunbrack RL, and Ischiropoulos H. Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation. Proc Natl Acad Sci USA 107: 16958-16963, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16958-16963
    • Doulias, P.T.1    Greene, J.L.2    Greco, T.M.3    Tenopoulou, M.4    Seeholzer, S.H.5    Dunbrack, R.L.6    Ischiropoulos, H.7
  • 67
    • 33646745126 scopus 로고    scopus 로고
    • Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures
    • DOI 10.1016/j.freeradbiomed.2005.12.037, PII S0891584906001614
    • Eaton P. Protein thiol oxidation in health and disease: techniques for measuring disulfides and related modifica-tions in complex protein mixtures. Free Radic Biol Med 40: 1889-1899, 2006. (Pubitemid 43744434)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.11 , pp. 1889-1899
    • Eaton, P.1
  • 68
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • DOI 10.1074/jbc.M111454200
    • Eaton P, Byers HL, Leeds N, Ward MA, and Shattock MJ. Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 277: 9806-9811, 2002. (Pubitemid 34968084)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 71
    • 0032464635 scopus 로고    scopus 로고
    • Pathophysiology of nitric oxide and related species: Free radical reactions and modification of biomolecules
    • DOI 10.1016/S0098-2997(99)00002-3, PII S0098299799000023
    • Eiserich JP, Patel RP, and O'Donnell VB. Pathophysiology of nitric oxide and related species: free radical reactions and modification of biomolecules. Mol Aspects Med 19: 221-357, 1998. (Pubitemid 29184931)
    • (1998) Molecular Aspects of Medicine , vol.19 , Issue.4-5 , pp. 221-357
    • Eiserich, J.P.1    Patel, R.P.2    O'Donnell, V.B.3
  • 72
    • 0030778083 scopus 로고    scopus 로고
    • Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase
    • DOI 10.1021/bi972191x
    • Ellis HR and Poole LB. Novel application of 7-chloro-4-nitrobenzo-2-oxa- 1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry 36: 15013-15018, 1997. (Pubitemid 27524428)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 15013-15018
    • Ellis, H.R.1    Poole, L.B.2
  • 75
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H, Schaur RJ, and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 11: 81-128, 1991. (Pubitemid 121003917)
    • (1991) Free Radical Biology and Medicine , vol.11 , Issue.1 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 77
    • 33845183951 scopus 로고
    • Long-range electron transfer between tyrosine and tryptophan in peptides
    • Faraggi M, DeFelippis MR, and Klapper MH. Long-range electron transfer between tyrosine and tryptophan in peptides. J Am Chem Soc 111: 5141-5145, 1989.
    • (1989) J Am Chem Soc , vol.111 , pp. 5141-5145
    • Faraggi, M.1    Defelippis, M.R.2    Klapper, M.H.3
  • 78
    • 77954692363 scopus 로고    scopus 로고
    • Quantitative evaluation of tryptophan oxidation in actin and troponin i from skeletal muscles using a rat model of acute oxidative stress
    • Fedorova M, Todorovsky T, Kuleva N, and Hoffmann R. Quantitative evaluation of tryptophan oxidation in actin and troponin I from skeletal muscles using a rat model of acute oxidative stress. Proteomics 10: 2692-2700, 2010.
    • (2010) Proteomics , vol.10 , pp. 2692-2700
    • Fedorova, M.1    Todorovsky, T.2    Kuleva, N.3    Hoffmann, R.4
  • 79
    • 0346634902 scopus 로고    scopus 로고
    • Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry
    • DOI 10.1021/ac020443g
    • Fenaille F, Tabet J-C, and Guy PA. Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal-and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry. Anal Chem 74: 6298-6304, 2002. (Pubitemid 36025176)
    • (2002) Analytical Chemistry , vol.74 , Issue.24 , pp. 6298-6304
    • Fenaille, F.1    Tabet, J.-C.2    Guy, P.A.3
  • 80
    • 55249122494 scopus 로고    scopus 로고
    • Functional diversity of cysteine residues in proteins and unique features of catalytic redox-active cysteines in thiol oxidoreductases
    • Fomenko DE, Marino SM, and Gladyshev VN. Functional diversity of cysteine residues in proteins and unique features of catalytic redox-active cysteines in thiol oxidoreductases. Mol Cells 26: 228-235, 2008.
    • (2008) Mol Cells , vol.26 , pp. 228-235
    • De, F.1    Marino, S.M.2    Gladyshev, V.N.3
  • 81
  • 82
    • 33846635882 scopus 로고    scopus 로고
    • High-throughput identification of catalytic redox-active cystein residues
    • DOI 10.1126/science.1133114
    • Fomenko DE, Xing W, Adair BM, Thomas DJ, and Gladyshev VN. High-throughput identification of catalytic redoxactive cysteine residues. Science 315: 387-389, 2007. (Pubitemid 46175521)
    • (2007) Science , vol.315 , Issue.5810 , pp. 387-389
    • Fomenko, D.E.1    Xing, W.2    Adair, B.M.3    Thomas, D.J.4    Gladyshev, V.N.5
  • 83
  • 85
    • 84859857110 scopus 로고    scopus 로고
    • 4-HNE Adduct stability characterized by collision-induced dissociation and electron transfer dissociation mass spectrometry
    • Fritz KS, Kellersberger KA, Gomez JD, and Petersen DR. 4-HNE Adduct stability characterized by collision-induced dissociation and electron transfer dissociation mass spectrometry. Chem Res Toxicol 25: 965-970, 2012.
    • (2012) Chem Res Toxicol , vol.25 , pp. 965-970
    • Fritz, K.S.1    Kellersberger, K.A.2    Gomez, J.D.3    Petersen, D.R.4
  • 86
    • 55249116799 scopus 로고    scopus 로고
    • Quantitative analysis of redox-sensitive proteome with DIGE and ICAT
    • Fu C, Hu J, Liu T, Ago T, Sadoshima J, and Li H. Quantitative analysis of redox-sensitive proteome with DIGE and ICAT. J Proteome Res 7: 3789-3802, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 3789-3802
    • Fu, C.1    Hu, J.2    Liu, T.3    Ago, T.4    Sadoshima, J.5    Li, H.6
  • 88
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • DOI 10.1016/j.coph.2007.06.003, PII S1471489207001038, Cancer/Immunomodulation
    • Gallogly MM and Mieyal JJ. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr Opin Pharmacol 7: 381-391, 2007. (Pubitemid 47304000)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.4 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 89
    • 0033818040 scopus 로고    scopus 로고
    • Troglitazone reduces reactive oxygen species generation by leukocytes and lipid peroxidation and improves flow-mediated vasodilatation in obese subjects
    • Garg R, Kumbkarni Y, Aljada A, Mohanty P, Ghanim H, Hamouda W, and Dandona P. Troglitazone reduces reactive oxygen species generation by leukocytes and lipid peroxidation and improves flow-mediated vasodilatation in obese subjects. Hypertension 36: 430-435, 2000.
    • (2000) Hypertension , vol.36 , pp. 430-435
    • Garg, R.1    Kumbkarni, Y.2    Aljada, A.3    Mohanty, P.4    Ghanim, H.5    Hamouda, W.6    Dandona, P.7
  • 90
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • Garrison WM. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem Rev 87: 381-398, 1987.
    • (1987) Chem Rev , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 92
    • 0027319565 scopus 로고
    • Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins
    • DOI 10.1021/bi00069a012
    • Gieseg SP, Simpson JA, Charlton TS, Duncan MW, and Dean RT. Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry 32: 4780-4786, 1993. (Pubitemid 23162033)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4780-4786
    • Gieseg, S.P.1    Simpson, J.A.2    Charlton, T.S.3    Duncan, M.W.4    Dean, R.T.5
  • 93
    • 0036277906 scopus 로고    scopus 로고
    • Malondialdehyde: A possible marker of ageing
    • DOI 10.1159/000058352
    • Gil P, Farinas F, Casado A, and Lopez-Fernandez E. Malondialdehyde: a possible marker of ageing. Gerontology 48: 209-214, 2002. (Pubitemid 34621617)
    • (2002) Gerontology , vol.48 , Issue.4 , pp. 209-214
    • Gil, P.1    Farinas, F.2    Casado, A.3    Lopez-Fernandez, E.4
  • 94
    • 34548148201 scopus 로고    scopus 로고
    • Hydrogen peroxide: A metabolic by-product or a common mediator of ageing signals?
    • DOI 10.1038/nrm2240, PII NRM2240
    • Giorgio M, Trinei M, Migliaccio E, and Pelicci PG. Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? Nat Rev Mol Cell Biol 8: 722-728, 2007. (Pubitemid 47312827)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.9 , pp. 722-728
    • Giorgio, M.1    Trinei, M.2    Migliaccio, E.3    Pelicci, P.G.4
  • 95
    • 0031260471 scopus 로고    scopus 로고
    • General method to identify and enrich vicinal thiol proteins present in intact cells in the oxidized, disulfide state
    • DOI 10.1006/abio.1997.2294
    • Gitler C, Zarmi B, and Kalef E. General method to identify and enrich vicinal thiol proteins present in intact cells in the oxidized, disulfide state. Anal Biochem 252: 48-55, 1997. (Pubitemid 27408691)
    • (1997) Analytical Biochemistry , vol.252 , Issue.1 , pp. 48-55
    • Gitler, C.1    Zarmi, B.2    Kalef, E.3
  • 96
    • 0346731053 scopus 로고    scopus 로고
    • Tyrosine oxidation products: Analysis and biological relevance
    • DOI 10.1007/s00726-003-0013-0
    • Giulivi C, Traaseth NJ, and Davies KJ. Tyrosine oxidation products: analysis and biological relevance. Amino acids 25: 227-232, 2003. (Pubitemid 38041261)
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 227-232
    • Giulivi, C.1    Traaseth, N.J.2    Davies, K.J.A.3
  • 97
    • 60349113228 scopus 로고    scopus 로고
    • Quantification of redox conditions in the nucleus
    • Go YM, Pohl J, and Jones DP. Quantification of redox conditions in the nucleus. Methods Mol Biol 464: 303-317, 2009.
    • (2009) Methods Mol Biol , vol.464 , pp. 303-317
    • Go, Y.M.1    Pohl, J.2    Jones, D.P.3
  • 98
    • 0025948114 scopus 로고
    • Mechanism of formation of the maillard protein cross-link pentosidine: Glucose, fructose, and ascorbate as pentosidine precursors
    • Grandhee SK and Monnier VM. Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. J Biol Chem 266: 11649-11653, 1991. (Pubitemid 21906998)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.18 , pp. 11649-11653
    • Grandhee, S.K.1    Monnier, V.M.2
  • 100
    • 34247361278 scopus 로고    scopus 로고
    • Carbonylation of adipose proteins in obesity and insulin resistance: Identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal
    • DOI 10.1074/mcp.M600120-MCP200
    • Grimsrud PA, Picklo MJ, Sr., Griffin TJ, and Bernlohr DA. Carbonylation of adipose proteins in obesity and insulin resistance: identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol Cell Proteomics 6: 624-637, 2007. (Pubitemid 46630095)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.4 , pp. 624-637
    • Grimsrud, P.A.1    Picklo Sr., M.J.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 101
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • DOI 10.1016/j.biocel.2004.04.020, PII S1357272504001670
    • Grune T, Jung T, Merker K, and Davies KJ. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int J Biochem Cell Biol 36: 2519-2530, 2004. (Pubitemid 39119763)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.12 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.A.4
  • 102
    • 0041573371 scopus 로고    scopus 로고
    • Selective solid-phase isolation of methionine-containing peptides and subsequent matrix-assisted laser desorption/ionisation mass spectrometric detection of methionine- and of methionine-sulfoxide-containing peptides
    • DOI 10.1002/rcm.1110
    • Grunert T, Pock K, Buchacher A, and Allmaier G. Selective solid-phase isolation of methionine-containing peptides and subsequent matrix-assisted laser desorption/ionisation mass spectrometric detection of methionine-and of methionine-sulfoxide-containing peptides. Rapid Commun Mass Spectrom 17: 1815-1824, 2003. (Pubitemid 36980583)
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , Issue.16 , pp. 1815-1824
    • Grunert, T.1    Pock, K.2    Buchacher, A.3    Allmaier, G.4
  • 103
    • 0038825874 scopus 로고    scopus 로고
    • Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation
    • DOI 10.1016/S1044-0305(03)00201-0
    • Guan Z, Yates NA, and Bakhtiar R. Detection and characterization of methionine oxidation in peptides by collisioninduced dissociation and electron capture dissociation. J Am Soc Mass Spectrom 14: 605-613, 2003. (Pubitemid 36870969)
    • (2003) Journal of the American Society for Mass Spectrometry , vol.14 , Issue.6 , pp. 605-613
    • Guan, Z.1    Yates, N.A.2    Bakhtiar, R.3
  • 104
    • 0026496731 scopus 로고
    • Dityrosine formation in the proteins of the eye lens
    • Guptasarma P and Balasubramanian D. Dityrosine formation in the proteins of the eye lens. Curr Eye Res 11: 1121-1125, 1992.
    • (1992) Curr Eye Res , vol.11 , pp. 1121-1125
    • Guptasarma, P.1    Balasubramanian, D.2
  • 105
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • DOI 10.1038/13690
    • Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, and Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17: 994-999, 1999. (Pubitemid 29474856)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 106
    • 0028820954 scopus 로고
    • Modulation of cardiac Na( + )-K + pump current: Role of protein and nonprotein sulfhydryl redox status
    • Haddock PS, Shattock MJ, and Hearse DJ. Modulation of cardiac Na( + )-K + pump current: role of protein and nonprotein sulfhydryl redox status. Am J Physiol 269: H297-H307, 1995.
    • (1995) Am J Physiol , vol.269
    • Haddock, P.S.1    Shattock, M.J.2    Hearse, D.J.3
  • 107
    • 33845544078 scopus 로고    scopus 로고
    • Relationship of metabolic risk factors and development of cardiovascular disease and diabetes
    • Haffner SM. Relationship of metabolic risk factors and development of cardiovascular disease and diabetes. Obesity 14 Suppl 3: 121S-127S, 2006.
    • (2006) Obesity , vol.14 , Issue.SUPPL. 3
    • Haffner, S.M.1
  • 108
    • 34047111193 scopus 로고    scopus 로고
    • Alterations in the diabetic myocardial proteome coupled with increased myocardial oxidative stress underlies diabetic cardiomyopathy
    • DOI 10.1016/j.yjmcc.2006.12.018, PII S0022282806010789
    • Hamblin M, Friedman DB, Hill S, Caprioli RM, Smith HM, and Hill MF. Alterations in the diabetic myocardial proteome coupled with increased myocardial oxidative stress underlies diabetic cardiomyopathy. J Mol Cell Cardiol 42: 884-895, 2007. (Pubitemid 46527591)
    • (2007) Journal of Molecular and Cellular Cardiology , vol.42 , Issue.4 , pp. 884-895
    • Hamblin, M.1    Friedman, D.B.2    Hill, S.3    Caprioli, R.M.4    Smith, H.M.5    Hill, M.F.6
  • 109
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton MB, Kettle AJ, and Winterbourn CC. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92: 3007-3017, 1998. (Pubitemid 28492304)
    • (1998) Blood , vol.92 , Issue.9 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 110
    • 34248233116 scopus 로고    scopus 로고
    • Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates
    • DOI 10.1021/ac062262a
    • Han B, Stevens JF, and Maier CS. Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates. Anal Chem 79: 3342-3354, 2007. (Pubitemid 46717165)
    • (2007) Analytical Chemistry , vol.79 , Issue.9 , pp. 3342-3354
    • Han, B.1    Stevens, J.F.2    Maier, C.S.3
  • 111
    • 24644469955 scopus 로고    scopus 로고
    • Sites and mechanisms of aconitase inactivation by peroxynitrite: Modulation by citrate and glutathione
    • DOI 10.1021/bi0509393
    • Han D, Canali R, Garcia J, Aguilera R, Gallaher TK, and Cadenas E. Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione. Biochemistry 44: 11986-11996, 2005. (Pubitemid 41285696)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 11986-11996
    • Han, D.1    Canali, R.2    Garcia, J.3    Aguilera, R.4    Gallaher, T.K.5    Cadenas, E.6
  • 112
    • 0142210179 scopus 로고    scopus 로고
    • Effect of Glutathione Depletion on Sites and Topology of Superoxide and Hydrogen Peroxide Production in Mitochondria
    • DOI 10.1124/mol.64.5.1136
    • Han D, Canali R, Rettori D, and Kaplowitz N. Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria. Mol Pharmacol 64: 1136-1144, 2003. (Pubitemid 37310746)
    • (2003) Molecular Pharmacology , vol.64 , Issue.5 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 113
    • 33646064159 scopus 로고    scopus 로고
    • The yeast cytosolic thioredoxins are involved in the regulation of methionine sulfoxide reductase A
    • Hanbauer I and Moskovitz J. The yeast cytosolic thioredoxins are involved in the regulation of methionine sulfoxide reductase A. Free Radic Biol Med 40: 1391-1396, 2006.
    • (2006) Free Radic Biol Med , vol.40 , pp. 1391-1396
    • Hanbauer, I.1    Moskovitz, J.2
  • 114
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • DOI 10.1038/nrm1105
    • Hancock JF. Ras proteins: different signals from different locations. Nat Rev Mol Cell Biol 4: 373-384, 2003. (Pubitemid 36565569)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.5 , pp. 373-384
    • Hancock, J.F.1
  • 115
    • 0033582342 scopus 로고    scopus 로고
    • Thiolation of the gammaB-crystallins in intact bovine lens exposed to hydrogen peroxide
    • Hanson SR, Chen AA, Smith JB, and Lou MF. Thiolation of the gammaB-crystallins in intact bovine lens exposed to hydrogen peroxide. J Biol Chem 274: 4735-4742, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 4735-4742
    • Hanson, S.R.1    Chen, A.A.2    Smith, J.B.3    Lou, M.F.4
  • 117
  • 118
    • 0036591861 scopus 로고    scopus 로고
    • Beta-scission of side-chain alkoxyl radicals on peptides and proteins results in the loss of side-chains as aldehydes and ketones
    • DOI 10.1016/S0891-5849(02)00814-6, PII S0891584902008146
    • Headlam HA and Davies MJ. Beta-scission of side-chain alkoxyl radicals on peptides and proteins results in the loss of side-chains as aldehydes and ketones. Free Radic Biol Med 32: 1171-1184, 2002. (Pubitemid 34603354)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1171-1184
    • Headlam, H.A.1    Davies, M.J.2
  • 119
    • 0033712060 scopus 로고    scopus 로고
    • And Davies MJ. beta-Scission of C-3 (beta-carbon) alkoxyl radicals on peptides and proteins: A novel pathway which results in the formation of alpha-carbon radicals and the loss of amino acid side chains
    • Headlam HA, Mortimer A, Easton CJ, and Davies MJ. beta-Scission of C-3 (beta-carbon) alkoxyl radicals on peptides and proteins: a novel pathway which results in the formation of alpha-carbon radicals and the loss of amino acid side chains. Chem Res Toxicol 13: 1087-1095, 2000.
    • (2000) Chem Res Toxicol , vol.13 , pp. 1087-1095
    • Headlam, H.A.1    Mortimer, A.2    Easton, C.J.3
  • 120
    • 68749092225 scopus 로고    scopus 로고
    • Anti-atherogenic effect of statins: Role of nitric oxide, peroxynitrite and haem oxygenase-1
    • Heeba G, Moselhy ME, Hassan M, Khalifa M, Gryglewski R, and Malinski T. Anti-atherogenic effect of statins: role of nitric oxide, peroxynitrite and haem oxygenase-1. Br J Pharmacol 156: 1256-1266, 2009.
    • (2009) Br J Pharmacol , vol.156 , pp. 1256-1266
    • Heeba, G.1    Moselhy, M.E.2    Hassan, M.3    Khalifa, M.4    Gryglewski, R.5    Malinski, T.6
  • 121
    • 67649227830 scopus 로고    scopus 로고
    • Detection of protein carbonyls by means of biotin hydrazide-streptavidin affinity methods
    • Hensley K. Detection of protein carbonyls by means of biotin hydrazide-streptavidin affinity methods. Methods Mol Biol 536: 457-462, 2009.
    • (2009) Methods Mol Biol , vol.536 , pp. 457-462
    • Hensley, K.1
  • 122
    • 0036401950 scopus 로고    scopus 로고
    • Redox regulation of calcium release in skeletal and cardiac muscle
    • Hidalgo C, Aracena P, Sanchez G, and Donoso P. Redox regulation of calcium release in skeletal and cardiac muscle. Biol Res 35: 183-193, 2002. (Pubitemid 35189791)
    • (2002) Biological Research , vol.35 , Issue.2 , pp. 183-193
    • Hidalgo, C.1    Aracena, P.2    Sanchez, G.3    Donoso, P.4
  • 123
    • 70350694223 scopus 로고    scopus 로고
    • Importance of the bioenergetic reserve capacity in response to cardiomyocyte stress induced by 4-hydroxynonenal
    • Hill BG, Dranka BP, Zou L, Chatham JC, and Darley-Usmar VM. Importance of the bioenergetic reserve capacity in response to cardiomyocyte stress induced by 4-hydroxynonenal. Biochem J 424: 99-107, 2009.
    • (2009) Biochem J , vol.424 , pp. 99-107
    • Hill, B.G.1    Dranka, B.P.2    Zou, L.3    Chatham, J.C.4    Darley-Usmar, V.M.5
  • 124
    • 34548844721 scopus 로고    scopus 로고
    • Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia
    • DOI 10.1016/j.freeradbiomed.2007.07.025, PII S0891584907005047
    • Ho YS, Xiong Y, Ho DS, Gao J, Chua BH, Pai H, and Mieyal JJ. Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia. Free Radic Biol Med 43: 1299-1312, 2007. (Pubitemid 47440124)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.9 , pp. 1299-1312
    • Ho, Y.-S.1    Xiong, Y.2    Ho, D.S.3    Gao, J.4    Chua, B.H.L.5    Pai, H.6    Mieyal, J.J.7
  • 126
    • 0036859446 scopus 로고    scopus 로고
    • Identification of oxidized methionine residues in peptides containing two methionine residues by derivatization and matrix-assisted laser desorption/ionization mass spectrometry
    • DOI 10.1002/1615-9861(200211)2:11<1524::AID-PROT1524>3.0.CO;2-7
    • Hollemeyer K, Heinzle E, and Tholey A. Identification of oxidized methionine residues in peptides containing two methionine residues by derivatization and matrix-assisted laser desorption/ionization mass spectrometry. Proteomics 2: 1524-1531, 2002. (Pubitemid 35424500)
    • (2002) Proteomics , vol.2 , Issue.11 , pp. 1524-1531
    • Hollemeyer, K.1    Heinzle, E.2    Tholey, A.3
  • 127
    • 71649105292 scopus 로고    scopus 로고
    • Covalent selection of the thiol proteome on activated thiol sepharose: A robust tool for redox proteomics
    • Hu W, Tedesco S, Faedda R, Petrone G, Cacciola SO, O'Keefe A, and Sheehan D. Covalent selection of the thiol proteome on activated thiol sepharose: a robust tool for redox proteomics. Talanta 80: 1569-1575, 2010.
    • (2010) Talanta , vol.80 , pp. 1569-1575
    • Hu, W.1    Tedesco, S.2    Faedda, R.3    Petrone, G.4    Cacciola, S.O.5    O'Keefe, A.6    Sheehan, D.7
  • 128
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of Oxidative Damage
    • DOI 10.1146/annurev.micro.57.030502.090938
    • Imlay JA. Pathways of oxidative damage. Annu Rev Microbiol 57: 395-418, 2003. (Pubitemid 37392949)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 130
    • 0037379388 scopus 로고    scopus 로고
    • Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: Identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1021/bi027172o
    • Ishii T, Tatsuda E, Kumazawa S, Nakayama T, and Uchida K. Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 42: 3474-3480, 2003. (Pubitemid 36368641)
    • (2003) Biochemistry , vol.42 , Issue.12 , pp. 3474-3480
    • Ishii, T.1    Tatsuda, E.2    Kumazawa, S.3    Nakayama, T.4    Uchida, K.5
  • 131
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey SR and Snyder SH. The biotin switch method for the detection of S-nitrosylated proteins. Sci STKE 2001: pl1, 2001.
    • (2001) Sci STKE 2001
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 132
    • 78650676710 scopus 로고    scopus 로고
    • Identifying the sequence and distinguishing the oxidized-methionine from phenylalanine peptides by MALDI TOF/TOF mass spectrometry in an antarctic bacterium pseudomonas syringae
    • Jagannadham MV. Identifying the sequence and distinguishing the oxidized-methionine from phenylalanine peptides by MALDI TOF/TOF mass spectrometry in an antarctic bacterium pseudomonas syringae. Proteomics Insights 2: 27, 2009.
    • (2009) Proteomics Insights , vol.2 , pp. 27
    • Jagannadham, M.V.1
  • 133
    • 0038462137 scopus 로고    scopus 로고
    • Nitric oxide and calcium together inactivate mitochondrial complex I and induce cytochrome c release
    • DOI 10.1016/S0022-2828(03)00137-8
    • Jekabsone A, Ivanoviene L, Brown GC, and Borutaite V. Nitric oxide and calcium together inactivate mitochondrial complex I and induce cytochrome c release. J Mol Cell Cardiol 35: 803-809, 2003. (Pubitemid 36773593)
    • (2003) Journal of Molecular and Cellular Cardiology , vol.35 , Issue.7 , pp. 803-809
    • Jekabsone, A.1    Ivanoviene, L.2    Brown, G.C.3    Borutaite, V.4
  • 134
    • 0036667552 scopus 로고    scopus 로고
    • Multidrug resistance-associated protein2 (MRP2) plays an important role in the biliary excretion of glutathione conjugates of 4-hydroxynonenal
    • DOI 10.1016/S0891-5849(02)00906-1, PII S0891584902009061
    • Ji B, Ito K, Suzuki H, Sugiyama Y, and Horie T. Multidrug resistance-associated protein2 (MRP2) plays an important role in the biliary excretion of glutathione conjugates of 4-hydroxynonenal. Free Radic Biol Med 33: 370-378, 2002. (Pubitemid 34786276)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.3 , pp. 370-378
    • Ji, B.1    Ito, K.2    Suzuki, H.3    Sugiyama, Y.4    Horie, T.5
  • 136
    • 70450030685 scopus 로고    scopus 로고
    • Complete sequencing and oxidative modification of manganese superoxide dismutase in medulloblastoma cells
    • John JP, Pollak A, and Lubec G. Complete sequencing and oxidative modification of manganese superoxide dismutase in medulloblastoma cells. Electrophoresis 30: 3006-3016, 2009.
    • (2009) Electrophoresis , vol.30 , pp. 3006-3016
    • John, J.P.1    Pollak, A.2    Lubec, G.3
  • 139
    • 0242321030 scopus 로고    scopus 로고
    • Proteomic identification of age-dependent protein nitration in rat skeletal muscle
    • DOI 10.1016/S0891-5849(03)00500-8
    • Kanski J, Alterman MA, and Schoneich C. Proteomic identification of age-dependent protein nitration in rat skeletal muscle. Free Radic Biol Med 35: 1229-1239, 2003. (Pubitemid 37357248)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.10 , pp. 1229-1239
    • Kanski, J.1    Alterman, M.A.2    Schoneich, C.3
  • 143
    • 1542313980 scopus 로고    scopus 로고
    • Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases
    • DOI 10.1091/mbc.E03-08-0629
    • Kim HY and Gladyshev VN. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol Biol Cell 15: 1055-1064, 2004. (Pubitemid 38316216)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1055-1064
    • Kim, H.-Y.1    Gladyshev, V.N.2
  • 144
    • 43549109795 scopus 로고    scopus 로고
    • Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine
    • Kim HY and Kim JR. Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine. Biochem Biophys Res Commun 371: 490-494, 2008.
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 490-494
    • Kim, H.Y.1    Kim, J.R.2
  • 145
    • 22144454310 scopus 로고    scopus 로고
    • Rapid increase in serum lipid peroxide 4-hydroxynonenal (HNE) through monocyte NADPH oxidase in early endo-toxemia
    • DOI 10.1080/10715760500161546
    • Kimura H, Liu S, Yamada S, Uchida K, Matsumoto K, Mukaida M, and Yoshida K. Rapid increase in serum lipid peroxide 4-hydroxynonenal (HNE) through monocyte NADPH oxidase in early endo-toxemia. Free Radic Res 39: 845-851, 2005. (Pubitemid 40975077)
    • (2005) Free Radical Research , vol.39 , Issue.8 , pp. 845-851
    • Kimura, H.1    Liu, S.2    Yamada, S.3    Uchida, K.4    Matsumoto, K.5    Mukaida, M.6    Yoshida, K.-I.7
  • 146
    • 26844480191 scopus 로고    scopus 로고
    • Assessment of S-nitrosothiols on diaminofluorescein gels
    • DOI 10.1016/j.ab.2005.07.025, PII S000326970500535X
    • King M, Gildemeister O, Gaston B, and Mannick JB. Assessment of S-nitrosothiols on diaminofluorescein gels. Anal Biochem 346: 69-76, 2005. (Pubitemid 41456627)
    • (2005) Analytical Biochemistry , vol.346 , Issue.1 , pp. 69-76
    • King, M.1    Gildemeister, O.2    Gaston, B.3    Mannick, J.B.4
  • 148
    • 31544460928 scopus 로고    scopus 로고
    • Effective detection of peptides containing cysteine sulfonic acid using matrix-assisted laser desorption/ionization and laser desorption/ionization on porous silicon mass spectrometry
    • DOI 10.1002/jms.973
    • Kinumi T, Shimomae Y, Arakawa R, Tatsu Y, Shigeri Y, Yumoto N, and Niki E. Effective detection of peptides containing cysteine sulfonic acid using matrix-assisted laser desorption/ionization and laser desorption/ionization on porous silicon mass spectrometry. J Mass Spectrom: JMS 41: 103-112, 2006. (Pubitemid 43164841)
    • (2006) Journal of Mass Spectrometry , vol.41 , Issue.1 , pp. 103-112
    • Kinumi, T.1    Shimomae, Y.2    Arakawa, R.3    Tatsu, Y.4    Shigeri, Y.5    Yumoto, N.6    Niki, E.7
  • 150
    • 61749089821 scopus 로고    scopus 로고
    • Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion
    • Kumar V, Kitaeff N, Hampton MB, Cannell MB, and Winterbourn CC. Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion. FEBS Lett 583: 997-1000, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 997-1000
    • Kumar, V.1    Kitaeff, N.2    Hampton, M.B.3    Cannell, M.B.4    Winterbourn, C.C.5
  • 152
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • DOI 10.1126/science.1068592
    • Lando D, Peet DJ, Whelan DA, Gorman JJ, and Whitelaw ML. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 295: 858-861, 2002. (Pubitemid 34118367)
    • (2002) Science , vol.295 , Issue.5556 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 153
    • 33644637265 scopus 로고    scopus 로고
    • Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart
    • DOI 10.1016/j.freeradbiomed.2005.10.040, PII S0891584905006350
    • Lashin OM, Szweda PA, Szweda LI, and Romani AM. Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart. Free Radic Biol Med 40: 886-896, 2006. (Pubitemid 43327322)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.5 , pp. 886-896
    • Lashin, O.M.1    Szweda, P.A.2    Szweda, L.I.3    Romani, A.M.P.4
  • 154
    • 0032806289 scopus 로고    scopus 로고
    • Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine
    • DOI 10.1016/S0891-5849(99)00071-4, PII S0891584999000714
    • Leeuwenburgh C, Hansen PA, Holloszy JO, and Heinecke JW. Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine. Free Radic Biol Med 27: 186-192, 1999. (Pubitemid 29353099)
    • (1999) Free Radical Biology and Medicine , vol.27 , Issue.1-2 , pp. 186-192
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3    Heinecke, J.W.4
  • 156
    • 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
    • DOI 10.1074/jbc.272.6.3520
    • Leeuwenburgh C, Rasmussen JE, Hsu FF, Mueller DM, Pennathur S, and Heinecke JW. 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: 3520-3526, 1997. (Pubitemid 27066853)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , 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
  • 158
    • 33846425366 scopus 로고    scopus 로고
    • Tryptophan 334 oxidation in bovine cytochrome c oxidase subunit I involves free radical migration
    • DOI 10.1016/j.febslet.2006.12.054, PII S0014579307000233
    • Lemma-Gray P, Weintraub ST, Carroll CA, Musatov A, and Robinson NC. Tryptophan 334 oxidation in bovine cytochrome c oxidase subunit I involves free radical migration. FEBS Lett 581: 437-442, 2007. (Pubitemid 46149616)
    • (2007) FEBS Letters , vol.581 , Issue.3 , pp. 437-442
    • Lemma-Gray, P.1    Weintraub, S.T.2    Carroll, C.A.3    Musatov, A.4    Robinson, N.C.5
  • 159
    • 0024590274 scopus 로고
    • Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride
    • DOI 10.1016/0003-2697(89)90077-8
    • Lenz AG, Costabel U, Shaltiel S, and Levine RL. Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride. Anal Biochem 177: 419-425, 1989. (Pubitemid 19088284)
    • (1989) Analytical Biochemistry , vol.177 , Issue.2 , pp. 419-425
    • Lenz, A.-G.1    Costabel, U.2    Shaltiel, S.3    Levine, R.L.4
  • 160
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells
    • Leonard SE, Reddie KG, and Carroll KS. Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem Biol 4: 783-799, 2009.
    • (2009) ACS Chem Biol , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 163
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules - From biology to health and disease
    • DOI 10.1089/ars.2007.9.25
    • Lillig CH and Holmgren A. Thioredoxin and related molecules-from biology to health and disease. Antioxid Redox Signal 9: 25-47, 2007. (Pubitemid 44901873)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.1 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 164
    • 79960604985 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A is a stereospecific methionine oxidase
    • Lim JC, You Z, Kim G, and Levine RL. Methionine sulfoxide reductase A is a stereospecific methionine oxidase. Proc Natl Acad Sci USA 108: 10472-10477, 2011.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 10472-10477
    • Lim, J.C.1    You, Z.2    Kim, G.3    Levine, R.L.4
  • 165
    • 41649108639 scopus 로고    scopus 로고
    • Tumour maintenance is mediated by eNOS
    • DOI 10.1038/nature06778, PII NATURE06778
    • Lim KH, Ancrile BB, Kashatus DF, and Counter CM. Tumour maintenance is mediated by eNOS. Nature 452: 646-649, 2008. (Pubitemid 351483359)
    • (2008) Nature , vol.452 , Issue.7187 , pp. 646-649
    • Lim, K.-H.1    Ancrile, B.B.2    Kashatus, D.F.3    Counter, C.M.4
  • 167
    • 79955454974 scopus 로고    scopus 로고
    • Modulating fatty acid oxidation in heart failure
    • Lionetti V, Stanley WC, and Recchia FA. Modulating fatty acid oxidation in heart failure. Cardiovasc Res 90: 202-209, 2011.
    • (2011) Cardiovasc Res , vol.90 , pp. 202-209
    • Lionetti, V.1    Stanley, W.C.2    Recchia, F.A.3
  • 168
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • DOI 10.1038/35068596
    • Liu L, Hausladen A, Zeng M, Que L, Heitman J, and Stamler JS. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410: 490-494, 2001. (Pubitemid 32240051)
    • (2001) Nature , vol.410 , Issue.6827 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 170
    • 76549097437 scopus 로고    scopus 로고
    • Better score function for peptide identification with ETD MS/MS spectra
    • Liu X, Shan B, Xin L, and Ma B. Better score function for peptide identification with ETD MS/MS spectra. BMC Bioinform 11 Suppl 1: S4, 2010.
    • (2010) BMC Bioinform , vol.11 , Issue.SUPPL. 1
    • Liu, X.1    Shan, B.2    Xin, L.3    Ma, B.4
  • 171
    • 34548258281 scopus 로고    scopus 로고
    • Limitations and pitfalls in protein identifications by mass spectrometry
    • DOI 10.1021/cr068213f
    • Lubec G and Afjehi-Sadat L. Limitations and pitfalls in protein identification by mass spectrometry. Chem Rev 107: 3568-3584, 2007. (Pubitemid 47322745)
    • (2007) Chemical Reviews , vol.107 , Issue.8 , pp. 3568-3584
    • Lubec, G.1    Afjehi-Sadat, L.2
  • 173
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo S and Levine RL. Methionine in proteins defends against oxidative stress. FASEB J 23: 464-472, 2009.
    • (2009) FASEB J , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 174
    • 0032501998 scopus 로고    scopus 로고
    • Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues
    • DOI 10.1021/bi971894b
    • MacMillan-Crow LA, Crow JP, and Thompson JA. Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues. Biochemistry 37: 1613-1622, 1998. (Pubitemid 28093677)
    • (1998) Biochemistry , vol.37 , Issue.6 , pp. 1613-1622
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Thompson, J.A.3
  • 175
    • 0035062753 scopus 로고    scopus 로고
    • Invited review: Manganese superoxide dismutase in disease
    • Macmillan-Crow LA and Cruthirds DL. Invited review: manganese superoxide dismutase in disease. Free Radic Res 34: 325-336, 2001. (Pubitemid 32331659)
    • (2001) Free Radical Research , vol.34 , Issue.4 , pp. 325-336
    • Macmillan-Crow, L.A.1    Cruthirds, D.L.2
  • 176
    • 77955455232 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins and their oxidation sites
    • Madian AG and Regnier FE. Proteomic identification of carbonylated proteins and their oxidation sites. J Proteome Res 9: 3766-3780, 2010.
    • (2010) J Proteome Res , vol.9 , pp. 3766-3780
    • Madian, A.G.1    Regnier, F.E.2
  • 177
    • 53849102546 scopus 로고    scopus 로고
    • Carbonylated proteins are detectable only in a degradation-resistant aggregate state in Escherichia coli
    • Maisonneuve E, Fraysse L, Lignon S, Capron L, and Dukan S. Carbonylated proteins are detectable only in a degradation-resistant aggregate state in Escherichia coli. J Bacteriol 190: 6609-6614, 2008.
    • (2008) J Bacteriol , vol.190 , pp. 6609-6614
    • Maisonneuve, E.1    Fraysse, L.2    Lignon, S.3    Capron, L.4    Dukan, S.5
  • 180
    • 0027016046 scopus 로고
    • Lipofuscinogenesis in a model system of cultured cardiac myocytes
    • Marzabadi MR, Yin D, and Brunk UT. Lipofuscinogenesis in a model system of cultured cardiac myocytes. EXS 62: 78-88, 1992.
    • (1992) EXS , vol.62 , pp. 78-88
    • Marzabadi, M.R.1    Yin, D.2    Brunk, U.T.3
  • 182
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM and Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049-6055, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 183
    • 0015056379 scopus 로고
    • An enzymebased theory of obligate anaerobiosis: The physiological function of superoxide dismutase
    • McCord JM, Keele BB, Jr., and Fridovich I. An enzymebased theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc Natl Acad Sci USA 68: 1024-1027, 1971.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 1024-1027
    • McCord, J.M.1    Keele Jr., B.B.2    Fridovich, I.3
  • 185
    • 34247464726 scopus 로고    scopus 로고
    • Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry
    • DOI 10.1002/pmic.200600450
    • Meany DL, Xie H, Thompson LV, Arriaga EA, and Griffin TJ. Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry. Proteomics 7: 1150-1163, 2007. (Pubitemid 46649164)
    • (2007) Proteomics , vol.7 , Issue.7 , pp. 1150-1163
    • Meany, D.L.1    Xie, H.2    Thompson, L.V.3    Arriaga, E.A.4    Griffin, T.J.5
  • 187
    • 0036819362 scopus 로고    scopus 로고
    • Peroxynitrite-induced inhibition and nitration of cardiac myofibrillar creatine kinase
    • DOI 10.1016/S0300-9084(02)00005-6, PII S0300908402000056
    • Mihm MJ and Bauer JA. Peroxynitrite-induced inhibition and nitration of cardiac myofibrillar creatine kinase. Biochimie 84: 1013-1019, 2002. (Pubitemid 36040534)
    • (2002) Biochimie , vol.84 , Issue.10 , pp. 1013-1019
    • Mihm, M.J.1    Bauer, J.A.2
  • 188
    • 17644362744 scopus 로고    scopus 로고
    • Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry
    • DOI 10.1021/ac0484373
    • Mirzaei H and Regnier F. Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry. Anal Chem 77: 2386-2392, 2005. (Pubitemid 40562738)
    • (2005) Analytical Chemistry , vol.77 , Issue.8 , pp. 2386-2392
    • Mirzaei, H.1    Regnier, F.2
  • 191
    • 0030028219 scopus 로고    scopus 로고
    • Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment
    • DOI 10.1074/jbc.271.8.4209
    • Mohr S, Stamler JS, and Brune B. Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment. J Biol Chem 271: 4209-4214, 1996. (Pubitemid 26070523)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.8 , pp. 4209-4214
    • Mohr, S.1    Stamler, J.S.2    Brune, B.3
  • 193
    • 0031028437 scopus 로고    scopus 로고
    • Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4
    • Montine KS, Olson SJ, Amarnath V, Whetsell WO, Jr., Graham DG, and Montine TJ. Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4. Am J Pathol 150: 437-443, 1997. (Pubitemid 27073773)
    • (1997) American Journal of Pathology , vol.150 , Issue.2 , pp. 437-443
    • Montine, K.S.1    Oison, S.J.2    Amarnath, V.3    Whetsell Jr., W.O.4    Graham, D.G.5    Montine, T.J.6
  • 195
    • 75149114580 scopus 로고    scopus 로고
    • Protein carbonyl and the methionine sulfoxide reductase system
    • Moskovitz J and Oien DB. Protein carbonyl and the methionine sulfoxide reductase system. Antioxid Redox Signal 12: 405-415, 2010.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 405-415
    • Moskovitz, J.1    Oien, D.B.2
  • 196
  • 198
    • 84856717563 scopus 로고    scopus 로고
    • Identification and quantification of snitrosylation by cysteine reactive tandem mass tag switch assay
    • M111 013441
    • Murray CI, Uhrigshardt H, O'Meally RN, Cole RN, and Van Eyk JE. Identification and quantification of Snitrosylation by cysteine reactive tandem mass tag switch assay. Mol Cell Proteomics 11: M111 013441, 2012.
    • (2012) Mol Cell Proteomics , vol.11
    • Murray, C.I.1    Uhrigshardt, H.2    O'Meally, R.N.3    Cole, R.N.4    Van Eyk, J.E.5
  • 199
    • 67649354633 scopus 로고    scopus 로고
    • Superoxidemediated formation of tyrosine hydroperoxides and methionine sulfoxide in peptides through radical addition and intramolecular oxygen transfer
    • Nagy P, Kettle AJ, and Winterbourn CC. Superoxidemediated formation of tyrosine hydroperoxides and methionine sulfoxide in peptides through radical addition and intramolecular oxygen transfer. J Biol Chem 284: 14723-14733, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 14723-14733
    • Nagy, P.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 201
    • 78649444069 scopus 로고    scopus 로고
    • Deficiency of methionine sulfoxide reductase A causes cellular dysfunction and mitochondrial damage in cardiac myocytes under physical and oxidative stresses
    • Nan C, Li Y, Jean-Charles PY, Chen G, Kreymerman A, Prentice H, Weissbach H, and Huang X. Deficiency of methionine sulfoxide reductase A causes cellular dysfunction and mitochondrial damage in cardiac myocytes under physical and oxidative stresses. Biochem Biophys Res Commun 402: 608-613, 2010.
    • (2010) Biochem Biophys Res Commun , vol.402 , pp. 608-613
    • Nan, C.1    Li, Y.2    Jean-Charles, P.Y.3    Chen, G.4    Kreymerman, A.5    Prentice, H.6    Weissbach, H.7    Huang, X.8
  • 202
    • 0037467060 scopus 로고    scopus 로고
    • αC-H bonds in model peptides: Absolute rate constants and effect of amino acid structure
    • DOI 10.1021/ja0293599
    • Nauser T and Schoneich C. Thiyl radicals abstract hydrogen atoms from the (alpha)C-H bonds in model peptides: absolute rate constants and effect of amino acid structure. J Am Chem Soc 125: 2042-2043, 2003. (Pubitemid 36245686)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.8 , pp. 2042-2043
    • Nauser, T.1    Schoneich, C.2
  • 204
    • 0041620467 scopus 로고    scopus 로고
    • Analysis of nitrated proteins by nitrotyrosine-specific affinity probes and mass spectrometry
    • DOI 10.1016/S0003-2697(03)00359-2
    • Nikov G, Bhat V, Wishnok JS, and Tannenbaum SR. Analysis of nitrated proteins by nitrotyrosine-specific affinity probes and mass spectrometry. Anal Biochem 320: 214-222, 2003. (Pubitemid 36962845)
    • (2003) Analytical Biochemistry , vol.320 , Issue.2 , pp. 214-222
    • Nikov, G.1    Bhat, V.2    Wishnok, J.S.3    Tannenbaum, S.R.4
  • 205
    • 34447575657 scopus 로고    scopus 로고
    • Analysis of modified apolipoprotein B-100 structures formed in oxidized low-density lipoprotein using LC-MS/MS
    • DOI 10.1002/pmic.200700111
    • Obama T, Kato R, Masuda Y, Takahashi K, Aiuchi T, and Itabe H. Analysis of modified apolipoprotein B-100 structures formed in oxidized low-density lipoprotein using LCMS/MS. Proteomics 7: 2132-2141, 2007. (Pubitemid 47067199)
    • (2007) Proteomics , vol.7 , Issue.13 , pp. 2132-2141
    • Obama, T.1    Kato, R.2    Masuda, Y.3    Takahashi, K.4    Aiuchi, T.5    Itabe, H.6
  • 206
    • 64549133370 scopus 로고    scopus 로고
    • Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies
    • Oien DB, Canello T, Gabizon R, Gasset M, Lundquist BL, Burns JM, and Moskovitz J. Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies. Arch Biochem Biophys 485: 35-40, 2009.
    • (2009) Arch Biochem Biophys , vol.485 , pp. 35-40
    • Oien, D.B.1    Canello, T.2    Gabizon, R.3    Gasset, M.4    Lundquist, B.L.5    Burns, J.M.6    Moskovitz, J.7
  • 207
    • 27644504514 scopus 로고    scopus 로고
    • Quantification of urinary o,o'-dityrosine, a biomarker for oxidative damage to proteins, by high performance liquid chromatography with triple quadrupole tandem mass spectrometry: A comparison with ion-trap tandem mass spectrometry
    • DOI 10.1016/j.jchromb.2005.03.043, PII S1570023205002369, Analysis of Antioxidants and Biomarkers of Oxidative Stress
    • Orhan H, Coolen S, and Meerman JH. Quantification of urinary o,o'-dityrosine, a biomarker for oxidative damage to proteins, by high performance liquid chromatography with triple quadrupole tandem mass spectrometry. A comparison with ion-trap tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 827: 104-108, 2005. (Pubitemid 41551603)
    • (2005) Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences , vol.827 , Issue.1 , pp. 104-108
    • Orhan, H.1    Coolen, S.2    Meerman, J.H.N.3
  • 208
    • 0345096597 scopus 로고    scopus 로고
    • Simultaneous determination of tyrosine, phenylalanine and deoxyguanosine oxidation products by liquid chromatography-tandem mass spectrometry as non-invasive biomarkers for oxidative damage
    • DOI 10.1016/j.jchromb.2003.10.056
    • Orhan H, Vermeulen NP, Tump C, Zappey H, and Meerman JH. Simultaneous determination of tyrosine, phenylalanine and deoxyguanosine oxidation products by liquid chromatography-tandem mass spectrometry as non-invasive biomarkers for oxidative damage. J Chromatogr B Analyt Technol Biomed Life Sci 799: 245-254, 2004. (Pubitemid 37510227)
    • (2004) Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences , vol.799 , Issue.2 , pp. 245-254
    • Orhan, H.1    Vermeulen, N.P.E.2    Tump, C.3    Zappey, H.4    Meerman, J.H.N.5
  • 209
    • 52949106861 scopus 로고    scopus 로고
    • Membrane phospholipids, lipoxidative damage and molecular integrity: A causal role in aging and longevity
    • Pamplona R. Membrane phospholipids, lipoxidative damage and molecular integrity: a causal role in aging and longevity. Biochim Biophys Acta 1777: 1249-1262, 2008.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1249-1262
    • Pamplona, R.1
  • 210
    • 0033230114 scopus 로고    scopus 로고
    • Oxidized proteins as a marker of oxidative stress during coronary heart surgery
    • DOI 10.1016/S0891-5849(99)00144-6, PII S0891584999001446
    • Pantke U, Volk T, Schmutzler M, Kox WJ, Sitte N, and Grune T. Oxidized proteins as a marker of oxidative stress during coronary heart surgery. Free Radic Biol Med 27: 1080-1086, 1999. (Pubitemid 29507480)
    • (1999) Free Radical Biology and Medicine , 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
  • 211
    • 67349241663 scopus 로고    scopus 로고
    • The kynurenines are associated with oxidative stress, inflammation and the prevalence of cardiovascular disease in patients with end-stage renal disease
    • Pawlak K, Domaniewski T, Mysliwiec M, and Pawlak D. The kynurenines are associated with oxidative stress, inflammation and the prevalence of cardiovascular disease in patients with end-stage renal disease. Atherosclerosis 204: 309-314, 2009.
    • (2009) Atherosclerosis , vol.204 , pp. 309-314
    • Pawlak, K.1    Domaniewski, T.2    Mysliwiec, M.3    Pawlak, D.4
  • 212
    • 34250714956 scopus 로고    scopus 로고
    • Biochemistry of protein tyrosine nitration in cardiovascular pathology
    • DOI 10.1016/j.cardiores.2007.04.024, PII S000863630700209X
    • Peluffo G and Radi R. Biochemistry of protein tyrosine nitration in cardiovascular pathology. Cardiovasc Res 75: 291-302, 2007. (Pubitemid 46961930)
    • (2007) Cardiovascular Research , vol.75 , Issue.2 , pp. 291-302
    • Peluffo, G.1    Radi, R.2
  • 213
    • 0035057229 scopus 로고    scopus 로고
    • A hydroxyl radical-like species oxidizes cynomolgus monkey artery wall proteins in early diabetic vascular disease
    • Pennathur S, Wagner JD, Leeuwenburgh C, Litwak KN, and Heinecke JW. A hydroxyl radical-like species oxidizes cynomolgus monkey artery wall proteins in early diabetic vascular disease. J Clin Invest 107: 853-860, 2001. (Pubitemid 32274038)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.7 , pp. 853-860
    • Pennathur, S.1    Wagner, J.D.2    Leeuwenburgh, C.3    Litwak, K.N.4    Heinecke, J.W.5
  • 214
    • 77953911347 scopus 로고    scopus 로고
    • Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: Chemical artifact or post-translational modification?
    • Perdivara I, Deterding LJ, Przybylski M, and Tomer KB. Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: chemical artifact or post-translational modification? J Am Soc Mass Spectrom 21: 1114-1117, 2010.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1114-1117
    • Perdivara, I.1    Deterding, L.J.2    Przybylski, M.3    Tomer, K.B.4
  • 215
    • 84856728902 scopus 로고    scopus 로고
    • Regulation of cell physiology and pathology by protein S-glutathionylation Lessons learned from the cardiovascular system
    • Pimentel D, Haeussler DJ, Matsui R, Burgoyne J, Cohen RA, and Bachschmid M. Regulation of cell physiology and pathology by protein S-glutathionylation. Lessons learned from the cardiovascular system. Antioxid Redox Signal 16: 524-542, 2012.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 524-542
    • Pimentel, D.1    Haeussler, D.J.2    Matsui, R.3    Burgoyne, J.4    Cohen, R.A.5    Bachschmid, M.6
  • 217
    • 1342306400 scopus 로고    scopus 로고
    • Acrolein inhibits NADHlinked mitochondrial enzyme activity: Implications for alzheimer's disease
    • Pocernich CB and Butterfield DA. Acrolein inhibits NADHlinked mitochondrial enzyme activity: implications for Alzheimer's disease. Neurotox Res 5: 515-520, 2003.
    • (2003) Neurotox Res , vol.5 , pp. 515-520
    • Pocernich, C.B.1    Butterfield, D.A.2
  • 219
    • 0035698458 scopus 로고    scopus 로고
    • In vivo measurement of the redox state
    • Pratico D. In vivo measurement of the redox state. Lipids 36 Suppl: S45-S47, 2001. (Pubitemid 34106208)
    • (2001) Lipids , vol.36 , Issue.SUPPL.
    • Pratico, D.1
  • 222
    • 20444410779 scopus 로고    scopus 로고
    • Biomedicine: Protection from experimental asthma by an endogenous bronchodilator
    • DOI 10.1126/science.1108228
    • Que LG, Liu L, Yan Y, Whitehead GS, Gavett SH, Schwartz DA, and Stamler JS. Protection from experimental asthma by an endogenous bronchodilator. Science 308: 1618-1621, 2005. (Pubitemid 40807509)
    • (2005) Science , vol.308 , Issue.5728 , pp. 1618-1621
    • Que, L.G.1    Liu, L.2    Yan, Y.3    Whitehead, G.S.4    Gavett, S.H.5    Schwartz, D.A.6    Stamler, J.S.7
  • 223
    • 0036890524 scopus 로고    scopus 로고
    • Peroxynitrite reactions and formation in mitochondria
    • DOI 10.1016/S0891-5849(02)01111-5, PII S0891584902011115
    • Radi R, Cassina A, Hodara R, Quijano C, and Castro L. Peroxynitrite reactions and formation in mitochondria. Free Radic Biol Med 33: 1451-1464, 2002. (Pubitemid 35351588)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.11 , pp. 1451-1464
    • Radi, R.1    Cassina, A.2    Hodara, R.3    Quijano, C.4    Castro, L.5
  • 225
    • 0020668294 scopus 로고
    • Lipid peroxidation and acute myocardial ischemia
    • Rao PS and Mueller HS. Lipid peroxidation and acute myocardial ischemia. Adv Exp Med Biol 161: 347-363, 1983.
    • (1983) Adv Exp Med Biol , vol.161 , pp. 347-363
    • Rao, P.S.1    Mueller, H.S.2
  • 226
    • 35649012000 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry of covalent adducts of proteins and 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation
    • DOI 10.1007/s00216-007-1534-2, Ultrahigh Resolution Mass Spectrometry
    • Rauniyar N, Stevens SM, Jr., and Prokai L. Fourier transform ion cyclotron resonance mass spectrometry of covalent adducts of proteins and 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation. Anal Bioanal Chem 389: 1421-1428, 2007. (Pubitemid 350023666)
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , Issue.5 , pp. 1421-1428
    • Rauniyar, N.1    Stevens Jr., S.M.2    Prokai, L.3
  • 227
    • 60549083972 scopus 로고    scopus 로고
    • Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: Neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation
    • Rauniyar N, Stevens SM, Prokai-Tatrai K, and Prokai L. Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation. Anal Chem 81: 782-789, 2009.
    • (2009) Anal Chem , vol.81 , pp. 782-789
    • Rauniyar, N.1    Stevens, S.M.2    Prokai-Tatrai, K.3    Prokai, L.4
  • 228
    • 77954072854 scopus 로고    scopus 로고
    • Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids
    • Rehder DS and Borges CR. Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids. BMC Biochem 11: 25, 2010.
    • (2010) BMC Biochem , vol.11 , pp. 25
    • Rehder, D.S.1    Borges, C.R.2
  • 229
    • 0034721584 scopus 로고    scopus 로고
    • Characterization of 4-hydroxy-2-nonenal metabolism in stellate cell lines derived from normal and cirrhotic rat liver
    • Reichard JF, Vasiliou V, and Petersen DR. Characterization of 4-hydroxy-2-nonenal metabolism in stellate cell lines derived from normal and cirrhotic rat liver. Biochim Biophys Acta 1487: 222-232, 2000.
    • (2000) Biochim Biophys Acta , vol.1487 , pp. 222-232
    • Reichard, J.F.1    Vasiliou, V.2    Petersen, D.R.3
  • 230
    • 10644231762 scopus 로고    scopus 로고
    • Challenges in mass spectrometry-based proteomics
    • DOI 10.1002/pmic.200400869
    • Reinders J, Lewandrowski U, Moebius J, Wagner Y, and Sickmann A. Challenges in mass spectrometry-based proteomics. Proteomics 4: 3686-3703, 2004. (Pubitemid 39657448)
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3686-3703
    • Reinders, J.1    Lewandrowski, U.2    Moebius, J.3    Wagner, Y.4    Sickmann, A.5
  • 231
    • 77749316875 scopus 로고    scopus 로고
    • Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage
    • Requejo R, Hurd TR, Costa NJ, and Murphy MP. Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage. FEBS J 277: 1465-1480, 2010.
    • (2010) FEBS J , vol.277 , pp. 1465-1480
    • Requejo, R.1    Hurd, T.R.2    Costa, N.J.3    Murphy, M.P.4
  • 233
    • 34547441421 scopus 로고    scopus 로고
    • Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: Its discovery, mechanism of action, and biological significance
    • DOI 10.1038/sj.ki.5002380, PII 5002380
    • Rhee SG, Jeong W, Chang TS, and Woo HA. Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significance. Kidney Int Suppl S3-S8, 2007. (Pubitemid 47172555)
    • (2007) Kidney International , vol.72 , Issue.SUPPL. 106
    • Rhee, S.G.1    Jeong, W.2    Chang, T.-S.3    Woo, H.A.4
  • 234
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • DOI 10.1038/13732
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, and Seraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17: 1030-1032, 1999. (Pubitemid 29474865)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 235
    • 0014249648 scopus 로고
    • Excited-molecule reactions in the radiolysis of peptides in concentrated aqueous solution
    • Rodgers MA and Garrison WM. Excited-molecule reactions in the radiolysis of peptides in concentrated aqueous solution. J Phys Chem 72: 758-759, 1968.
    • (1968) J Phys Chem , vol.72 , pp. 758-759
    • Ma, R.1    Garrison, W.M.2
  • 236
    • 79959340042 scopus 로고    scopus 로고
    • Protein sulfenic acid formation: From cellular damage to redox regulation
    • Roos G and Messens J. Protein sulfenic acid formation: from cellular damage to redox regulation. Free Radic Biol Med 51: 314-326, 2011.
    • (2011) Free Radic Biol Med , vol.51 , pp. 314-326
    • Roos, G.1    Messens, J.2
  • 237
    • 85027925434 scopus 로고    scopus 로고
    • Evaluation of multiple biomarkers of cardiovascular stress for risk prediction and guiding medical therapy in patients with stable coronary disease
    • Sabatine MS, Morrow DA, de Lemos JA, Omland T, Sloan S, Jarolim P, Solomon SD, Pfeffer MA, and Braunwald E. Evaluation of multiple biomarkers of cardiovascular stress for risk prediction and guiding medical therapy in patients with stable coronary disease. Circulation 125: 233-240, 2012.
    • (2012) Circulation , vol.125 , pp. 233-240
    • Sabatine, M.S.1    Morrow, D.A.2    De Lemos, J.A.3    Omland, T.4    Sloan, S.5    Jarolim, P.6    Solomon, S.D.7    Ma, P.8    Braunwald, E.9
  • 240
    • 70349693474 scopus 로고    scopus 로고
    • Lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span
    • Salmon AB, Perez VI, Bokov A, Jernigan A, Kim G, Zhao H, Levine RL, and Richardson A. Lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span. FASEB J 23: 3601-3608, 2009.
    • (2009) FASEB J , vol.23 , pp. 3601-3608
    • Salmon, A.B.1    Perez, V.I.2    Bokov, A.3    Jernigan, A.4    Kim, G.5    Zhao, H.6    Levine, R.L.7    Richardson, A.8
  • 242
    • 0034033915 scopus 로고    scopus 로고
    • Identification of peptide oxidation by tandem mass spectrometry
    • Schey KL and Finley EL. Identification of peptide oxidation by tandem mass spectrometry. Acc Chem Res 33: 299-306, 2000.
    • (2000) Acc Chem Res , vol.33 , pp. 299-306
    • Schey, K.L.1    Finley, E.L.2
  • 243
    • 0343986369 scopus 로고    scopus 로고
    • Mechanisms of metal-catalyzed oxidation of histidine to 2-oxo-histidine in peptides and proteins
    • DOI 10.1016/S0731-7085(99)00182-X, PII S073170859900182X
    • Schoneich C. Mechanisms of metal-catalyzed oxidation of histidine to 2-oxo-histidine in peptides and proteins. J Pharm Biomed Anal 21: 1093-1097, 2000. (Pubitemid 30001539)
    • (2000) Journal of Pharmaceutical and Biomedical Analysis , vol.21 , Issue.6 , pp. 1093-1097
    • Schoneich, C.1
  • 244
    • 12844260763 scopus 로고    scopus 로고
    • Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease
    • DOI 10.1016/j.bbapap.2004.09.009, PII S1570963904002493, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Schoneich C. Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease. Biochim Biophys Acta 1703: 111-119, 2005. (Pubitemid 40170434)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 111-119
    • Schoneich, C.1
  • 245
    • 34748893526 scopus 로고    scopus 로고
    • Integrated biomarkers in cardiomyopathies: Cardiovascular magnetic resonance imaging combined with molecular and immunologic markers - A stepwise approach for diagnosis and treatment
    • DOI 10.1007/s00059-007-3046-4
    • Schulz-Menger J, Maisch B, Abdel-Aty H, and Pankuweit S. Integrated biomarkers in cardiomyopathies: cardiovascular magnetic resonance imaging combined with molecular and immunologic markers-a stepwise approach for diagnosis and treatment. Herz 32: 458-472, 2007. (Pubitemid 47468955)
    • (2007) Herz , vol.32 , Issue.6 , pp. 458-472
    • Schulz-Menger, J.1    Maisch, B.2    Abdel-Aty, H.3    Pankuweit, S.4
  • 246
    • 0030591436 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal in human monocytes fed with malarial pigment hemozoin. A possible clue for hemozoin toxicity
    • DOI 10.1016/0014-5793(96)00523-6
    • Schwarzer E, Muller O, Arese P, Siems WG, and Grune T. Increased levels of 4-hydroxynonenal in human monocytes fed with malarial pigment hemozoin. A possible clue for hemozoin toxicity. FEBS Lett 388: 119-122, 1996. (Pubitemid 26226343)
    • (1996) FEBS Letters , vol.388 , Issue.2-3 , pp. 119-122
    • Schwarzer, E.1    Muller, O.2    Arese, P.3    Siems, W.G.4    Grune, T.5
  • 247
    • 79551676040 scopus 로고    scopus 로고
    • Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone
    • Seo YH and Carroll KS. Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone. Angew Chem 50: 1342-1345, 2011.
    • (2011) Angew Chem , vol.50 , pp. 1342-1345
    • Seo, Y.H.1    Carroll, K.S.2
  • 248
    • 79851512689 scopus 로고    scopus 로고
    • The SNO-proteome: Causation and classifications
    • Seth D and Stamler JS. The SNO-proteome: causation and classifications. Curr Opin Chem Biol 15: 129-136, 2011.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 129-136
    • Seth, D.1    Stamler, J.S.2
  • 249
    • 2642576571 scopus 로고    scopus 로고
    • Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols
    • DOI 10.1074/mcp.T300011-MCP200
    • Sethuraman M, McComb ME, Heibeck T, Costello CE, and Cohen RA. Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols. Mol Cell Proteomics 3: 273-278, 2004. (Pubitemid 38714283)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.3 , pp. 273-278
    • Sethuraman, M.1    McCombs, M.E.2    Heibeck, T.3    Costellos, C.E.4    Cohen, R.A.5
  • 250
    • 11144252625 scopus 로고    scopus 로고
    • Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures
    • DOI 10.1021/pr049887e
    • Sethuraman M, McComb ME, Huang H, Huang S, Heibeck T, Costello CE, and Cohen RA. Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J Proteome Res 3: 1228-1233, 2004. (Pubitemid 40040377)
    • (2004) Journal of Proteome Research , vol.3 , Issue.6 , pp. 1228-1233
    • Sethuraman, M.1    McComb, M.E.2    Huang, H.3    Huang, S.4    Heibeck, T.5    Costello, C.E.6    Cohen, R.A.7
  • 251
    • 0347895099 scopus 로고    scopus 로고
    • Conserved residues in the putative catalytic triad of human bile acid coenzyme A:Amino acid N-acyltransferase
    • DOI 10.1074/jbc.M207463200
    • Sfakianos MK, Wilson L, Sakalian M, Falany CN, and Barnes S. Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase. J Biol Chem 277: 47270-47275, 2002. (Pubitemid 36159238)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 47270-47275
    • Sfakianos, M.K.1    Wilson, L.2    Sakalian, M.3    Falany, C.N.4    Barnes, S.5
  • 252
    • 84857491459 scopus 로고    scopus 로고
    • Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions
    • Shao B, Pennathur S, and Heinecke JW. Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions. J Biol Chem 287: 6375-6386, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 6375-6386
    • Shao, B.1    Pennathur, S.2    Heinecke, J.W.3
  • 255
    • 74149092499 scopus 로고    scopus 로고
    • Fluorogenic tagging of peptide and protein 3-nitrotyrosine with 4-(aminomethyl)-benzenesulfonic acid for quantitative analysis of protein tyrosine nitration
    • Sharov VS, Dremina ES, Galeva NA, Gerstenecker GS, Li X, Dobrowsky RT, Stobaugh JF, and Schoneich C. Fluorogenic tagging of peptide and protein 3-nitrotyrosine with 4-(aminomethyl)-benzenesulfonic acid for quantitative analysis of protein tyrosine nitration. Chromatographia 71: 37-53, 2010.
    • (2010) Chromatographia , vol.71 , pp. 37-53
    • Sharov, V.S.1    Dremina, E.S.2    Galeva, N.A.3    Gerstenecker, G.S.4    Li, X.5    Dobrowsky, R.T.6    Stobaugh, J.F.7    Schoneich, C.8
  • 256
    • 0032520869 scopus 로고    scopus 로고
    • Photodynamically generated bovine serum albumin radicals: Evidence for damage transfer and oxidation at cysteine and tryptophan residues
    • DOI 10.1016/S0891-5849(97)00327-4, PII S0891584997003274
    • Silvester JA, Timmins GS, and Davies MJ. Photodynamically generated bovine serum albumin radicals: evidence for damage transfer and oxidation at cysteine and tryptophan residues. Free Radic Biol Med 24: 754-766, 1998. (Pubitemid 28169563)
    • (1998) Free Radical Biology and Medicine , vol.24 , Issue.5 , pp. 754-766
    • Silvester, J.A.1    Timmins, G.S.2    Davies, M.J.3
  • 257
    • 34548681412 scopus 로고    scopus 로고
    • Identification of a denitrase activity against calmodulin in activated macrophages using high-field liquid chromatography-FTICR mass spectrometry
    • DOI 10.1021/bi7009713
    • Smallwood HS, Lourette NM, Boschek CB, Bigelow DJ, Smith RD, Pasa-Tolić L, and Squier TC. Identification of a denitrase activity against calmodulin in activated macrophages using high-field liquid chromatography-FTICR mass spectrometry. Biochemistry 46: 10498-10505, 2007. (Pubitemid 47417245)
    • (2007) Biochemistry , vol.46 , Issue.37 , pp. 10498-10505
    • Smallwood, H.S.1    Lourette, N.M.2    Boschek, C.B.3    Bigelow, D.J.4    Smith, R.D.5    Pasa-Tolic, L.6    Squier, T.C.7
  • 258
    • 0024537069 scopus 로고
    • Effect of ambient oxygen concentration on lipofuscin accumulation in cultured rat heart myocytes - A novel in vitro model of lipofuscinogenesis
    • DOI 10.1016/0891-5849(89)90155-X
    • Sohal RS, Marzabadi MR, Galaris D, and Brunk UT. Effect of ambient oxygen concentration on lipofuscin accumulation in cultured rat heart myocytes-a novel in vitro model of lipofuscinogenesis. Free Radic Biol Med 6: 23-30, 1989. (Pubitemid 19032726)
    • (1989) Free Radical Biology and Medicine , vol.6 , Issue.1 , pp. 23-30
    • Sohal, R.S.1    Marzabadi, M.R.2    Galaris, D.3    Brunk, U.T.4
  • 259
    • 0344084088 scopus 로고    scopus 로고
    • High-Throughput Proteomic-Based Identification of Oxidatively Induced Protein Carbonylation in Mouse Brain
    • DOI 10.1023/B:PHAM.0000003366.25263.78
    • Soreghan BA, Yang F, Thomas SN, Hsu J, and Yang AJ. High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. Pharm Res 20: 1713-1720, 2003. (Pubitemid 37449442)
    • (2003) Pharmaceutical Research , vol.20 , Issue.11 , pp. 1713-1720
    • Soreghan, B.A.1    Yang, F.2    Thomas, S.N.3    Hsu, J.4    Yang, A.J.5
  • 262
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • DOI 10.1074/jbc.M207217200
    • St.-Pierre J, Buckingham JA, Roebuck SJ, and Brand MD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277: 44784-44790, 2002. (Pubitemid 36159072)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 263
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • Stadtman ER. Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic Biol Med 9: 315-325, 1990. (Pubitemid 120036900)
    • (1990) Free Radical Biology and Medicine , vol.9 , Issue.4 , pp. 315-325
    • Stadtman, E.R.1
  • 264
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metalcatalyzed reactions. Annu Rev Biochem 62: 797-821, 1993. (Pubitemid 23237888)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 265
    • 84889453656 scopus 로고    scopus 로고
    • Chemical modification of proteins by reactive oxygen species
    • Series Editors: Desiderio DM and Nibbering NM). Hoboken NJ: John Wiley & Sons, Inc.
    • Stadtman ER and Levine RL. Chemical modification of proteins by reactive oxygen species. In: Redox Proteomics, edited by Dalle-Donne I, Scaloni A, and Butterfield DA (Series Editors: Desiderio DM and Nibbering NM). Hoboken, NJ: John Wiley & Sons, Inc., 2006, pp. 1-23.
    • (2006) Redox Proteomics Edited by Dalle-Donne i Scaloni A and Butterfield da , pp. 1-23
    • Stadtman, E.R.1    Levine, R.L.2
  • 266
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of Methionine Residues of Proteins: Biological Consequences
    • Stadtman ER, Moskovitz J, and Levine RL. Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal 5: 577-582, 2003. (Pubitemid 37315145)
    • (2003) Antioxidants and Redox Signaling , vol.5 , Issue.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 267
    • 34347255359 scopus 로고    scopus 로고
    • Detection of kynurenine modifications in proteins using a monoclonal antibody
    • DOI 10.1016/j.jim.2007.05.002, PII S0022175907001470
    • Staniszewska M and Nagaraj RH. Detection of kynurenine modifications in proteins using a monoclonal antibody. J Immunol Methods 324: 63-73, 2007. (Pubitemid 47001427)
    • (2007) Journal of Immunological Methods , vol.324 , Issue.1-2 , pp. 63-73
    • Staniszewska, M.1    Nagaraj, R.H.2
  • 268
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • DOI 10.1038/nrm1468
    • Steen H and Mann M. The ABC's (and XYZ's) of peptide sequencing. Nat Rev Mol Cell Biol 5: 699-711, 2004. (Pubitemid 39208180)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 269
    • 38149060199 scopus 로고    scopus 로고
    • Rapid characterization of covalent modifications to rat brain mitochondrial proteins after ex vivo exposure to 4-hydroxy-2-nonenal by liquid chromatography-tandem mass spectrometry using data-dependent and neutral loss-driven MS3 acquisition
    • Stevens SM, Jr., Rauniyar N, and Prokai L. Rapid characterization of covalent modifications to rat brain mitochondrial proteins after ex vivo exposure to 4-hydroxy-2-nonenal by liquid chromatography-tandem mass spectrometry using data-dependent and neutral loss-driven MS3 acquisition. J Mass Spectrom 42: 1599-1605, 2007.
    • (2007) J Mass Spectrom , vol.42 , pp. 1599-1605
    • Stevens Jr., S.M.1    Rauniyar, N.2    Prokai, L.3
  • 270
    • 0036286512 scopus 로고    scopus 로고
    • Detection and affinity purification of oxidant-sensitive proteins using biotinylated glutathione ethyl ester
    • DOI 10.1016/S0076-6879(02)53040-8
    • Sullivan DM, Levine RL, and Finkel T. Detection and affinity purification of oxidant-sensitive proteins using biotinylated glutathione ethyl ester. Methods Enzymol 353: 101-113, 2002. (Pubitemid 34625584)
    • (2002) Methods in Enzymology , vol.353 , pp. 101-113
    • Sullivan, D.M.1    Levine, R.L.2    Finkel, T.3
  • 273
    • 33750905662 scopus 로고    scopus 로고
    • S-nitrosylation: NO-related redox signaling to protect against oxidative stress
    • DOI 10.1089/ars.2006.8.1693
    • Sun J, Steenbergen C, and Murphy E. S-nitrosylation: NOrelated redox signaling to protect against oxidative stress. Antioxid Redox Signal 8: 1693-1705, 2006. (Pubitemid 44726342)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.9-10 , pp. 1693-1705
    • Sun, J.1    Steenbergen, C.2    Murphy, E.3
  • 276
    • 37249001753 scopus 로고    scopus 로고
    • A genetically encoded probe for cysteine sulfenic acid protein modification in vivo
    • DOI 10.1021/bi701625s
    • Takanishi CL, Ma LH, and Wood MJ. A genetically encoded probe for cysteine sulfenic acid protein modification in vivo. Biochemistry 46: 14725-14732, 2007. (Pubitemid 350276376)
    • (2007) Biochemistry , vol.46 , Issue.50 , pp. 14725-14732
    • Takanishi, C.L.1    Ma, L.H.2    Wood, M.J.3
  • 277
    • 77952071893 scopus 로고    scopus 로고
    • Plant thioredoxin CDSP32 regenerates 1-cys methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid
    • Tarrago L, Laugier E, Zaffagnini M, Marchand CH, Le Marechal P, Lemaire SD, and Rey P. Plant thioredoxin CDSP32 regenerates 1-cys methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid. J Biol Chem 285: 14964-14972, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 14964-14972
    • Tarrago, L.1    Laugier, E.2    Zaffagnini, M.3    Ch, M.4    Le Marechal, P.5    Lemaire, S.D.6    Rey, P.7
  • 278
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins
    • DOI 10.1074/jbc.C300135200
    • Taylor SW, Fahy E, Murray J, Capaldi RA, and Ghosh SS. Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins. J Biol Chem 278: 19587-19590, 2003. (Pubitemid 36799140)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4    Ghosh, S.S.5
  • 280
    • 80054801005 scopus 로고    scopus 로고
    • Mass spectrometric characterization of peptides containing different oxidized tryptophan residues
    • Todorovski T, Fedorova M, and Hoffmann R. Mass spectrometric characterization of peptides containing different oxidized tryptophan residues. J Mass Spectrom 46: 1030-1038, 2011.
    • (2011) J Mass Spectrom , vol.46 , pp. 1030-1038
    • Todorovski, T.1    Fedorova, M.2    Hoffmann, R.3
  • 281
    • 77958495432 scopus 로고    scopus 로고
    • Upregulation of Nox4 by TGF{beta}1 oxidizes SERCA and inhibits NO in arterial smooth muscle of the prediabetic Zucker rat
    • Tong X, Hou X, Jourd'heuil D, Weisbrod RM, and Cohen RA. Upregulation of Nox4 by TGF{beta}1 oxidizes SERCA and inhibits NO in arterial smooth muscle of the prediabetic Zucker rat. Circ Res 107: 975-983, 2010.
    • (2010) Circ Res , vol.107 , pp. 975-983
    • Tong, X.1    Hou, X.2    Jourd'Heuil, D.3    Weisbrod, R.M.4    Cohen, R.A.5
  • 283
    • 80051789102 scopus 로고    scopus 로고
    • Isotopecoded chemical reporter and acid-cleavable affinity reagents for monitoring protein sulfenic acids
    • Truong TH, Garcia FJ, Seo YH, and Carroll KS. Isotopecoded chemical reporter and acid-cleavable affinity reagents for monitoring protein sulfenic acids. Bioorg Med Chem Lett 21: 5015-5020, 2011.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 5015-5020
    • Truong, T.H.1    Garcia, F.J.2    Seo, Y.H.3    Carroll, K.S.4
  • 284
    • 0028938334 scopus 로고
    • Spectroscopic evidence for reaction of prostaglandin H synthase-1 tyrosyl radical with arachidonic acid
    • Tsai A, Kulmacz RJ, and Palmer G. Spectroscopic evidence for reaction of prostaglandin H synthase-1 tyrosyl radical with arachidonic acid. J Biol Chem 270: 10503-10508, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 10503-10508
    • Tsai, A.1    Kulmacz, R.J.2    Palmer, G.3
  • 292
    • 34250211138 scopus 로고    scopus 로고
    • Myocardial ischemia-reperfusion injury, antioxidant enzyme systems, and selenium: A review
    • DOI 10.2174/092986707780831078
    • Venardos KM, Perkins A, Headrick J, and Kaye DM. Myocardial ischemia-reperfusion injury, antioxidant enzyme systems, and selenium: a review. Curr Med Chem 14: 1539-1549, 2007. (Pubitemid 46902214)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.14 , pp. 1539-1549
    • Venardos, K.M.1    Kaye, D.M.2
  • 293
    • 41649118986 scopus 로고    scopus 로고
    • Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives
    • Vila A, Tallman KA, Jacobs AT, Liebler DC, Porter NA, and Marnett LJ. Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives. Chem Res Toxicol 21: 432-444, 2008.
    • (2008) Chem Res Toxicol , vol.21 , pp. 432-444
    • Vila, A.1    Tallman, K.A.2    Jacobs, A.T.3    Liebler, D.C.4    Porter, N.A.5    Marnett, L.J.6
  • 294
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic Biol Med 18: 93-105, 1995.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 296
    • 34250746414 scopus 로고    scopus 로고
    • Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP) - A general method for mapping sites of probe modification in proteomes
    • DOI 10.1038/nprot.2007.194, PII NPROT.2007.194
    • Weerapana E, Speers AE, and Cravatt BF. Tandem orthogonal proteolysis-activity-based protein profiling (TOPABPP)-a general method for mapping sites of probe modification in proteomes. Nat Protoc 2: 1414-1425, 2007. (Pubitemid 46952321)
    • (2007) Nature Protocols , vol.2 , Issue.6 , pp. 1414-1425
    • Weerapana, E.1    Speers, A.E.2    Cravatt, B.F.3
  • 298
    • 0033932346 scopus 로고    scopus 로고
    • Cardiac peroxynitrite formation and left ventricular dysfunction following doxorubicin treatment in mice
    • Weinstein DM, Mihm MJ, and Bauer JA. Cardiac peroxynitrite formation and left ventricular dysfunction following doxorubicin treatment in mice. J Pharmacol Exp Ther 294: 396-401, 2000. (Pubitemid 30434713)
    • (2000) Journal of Pharmacology and Experimental Therapeutics , vol.294 , Issue.1 , pp. 396-401
    • Weinstein, D.M.1    Mihm, M.J.2    Bauer, J.A.3
  • 299
    • 0030866161 scopus 로고    scopus 로고
    • Age-dependent increase in ortho-tyrosine and methionine sulfoxide in human skin collagen is not accelerated in diabetes - Evidence against a generalized increase in oxidative stress in diabetes
    • Wells-Knecht MC, Lyons TJ, McCance DR, Thorpe SR, and Baynes JW. Age-dependent increase in ortho-tyrosine and methionine sulfoxide in human skin collagen is not accelerated in diabetes. Evidence against a generalized increase in oxidative stress in diabetes. J Clin Invest 100: 839-846, 1997. (Pubitemid 27371702)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.4 , pp. 839-846
    • Wells-Knecht, M.C.1    Lyons, T.J.2    McCance, D.R.3    Thorpe, S.R.4    Baynes, J.W.5
  • 300
    • 68549101834 scopus 로고    scopus 로고
    • Attenuation of angiotensin II-induced vascular dysfunction and hypertension by overexpression of Thioredoxin 2
    • Widder JD, Fraccarollo D, Galuppo P, Hansen JM, Jones DP, Ertl G, and Bauersachs J. Attenuation of angiotensin II-induced vascular dysfunction and hypertension by overexpression of Thioredoxin 2. Hypertension 54: 338-344, 2009.
    • (2009) Hypertension , vol.54 , pp. 338-344
    • Widder, J.D.1    Fraccarollo, D.2    Galuppo, P.3    Hansen, J.M.4    Jones, D.P.5    Ertl, G.6    Bauersachs, J.7
  • 301
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • DOI 10.1038/nchembio.85, PII NCHEMBIO85
    • Winterbourn CC. Reconciling the chemistry and biology of reactive oxygen species. Nat Chem Biol 4: 278-286, 2008. (Pubitemid 351550893)
    • (2008) Nature Chemical Biology , vol.4 , Issue.5 , pp. 278-286
    • Winterbourn, C.C.1
  • 302
    • 75149170936 scopus 로고    scopus 로고
    • Cell signaling by protein carbonylation and decarbonylation
    • Wong CM, Marcocci L, Liu L, and Suzuki YJ. Cell signaling by protein carbonylation and decarbonylation. Antioxid Redox Signal 12: 393-404, 2010.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 393-404
    • Wong, C.M.1    Marcocci, L.2    Liu, L.3    Suzuki, Y.J.4
  • 303
    • 0032573507 scopus 로고    scopus 로고
    • 2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein
    • DOI 10.1016/S0014-5793(98)01415-X, PII S001457939801415X
    • Wu Y, Kwon KS, and Rhee SG. Probing cellular protein targets of H2O2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein. FEBS Lett 440: 111-115, 1998. (Pubitemid 28558747)
    • (1998) FEBS Letters , vol.440 , Issue.1-2 , pp. 111-115
    • Wu, Y.1    Kwon, K.-S.2    Rhee, S.G.3
  • 306
    • 0033619720 scopus 로고    scopus 로고
    • Identification of modified tryptophan residues in apolipoprotein B-100 derived from copper ion-oxidized low-density lipoprotein
    • Yang C-y, Gu Z-W, Yang M, Lin S-N, Siuzdak G, and Smith CV. Identification of modified tryptophan residues in apolipoprotein B-100 derived from copper ion-oxidized low-density lipoprotein. Biochemistry 38: 15903-15908, 1999. (Pubitemid 129520483)
    • (1999) Biochemistry , vol.38 , Issue.48 , pp. 15903-15908
    • Yang, C.-Y.1    Gu, Z.-W.2    Yang, M.3    Lin, S.-N.4    Siuzdak, G.5    Smith, C.V.6
  • 307
    • 79751513700 scopus 로고    scopus 로고
    • Thioredoxin 1 negatively regulates angiotensin II-induced cardiac hypertrophy through upregulation of miR-98/let-7
    • Yang Y, Ago T, Zhai P, Abdellatif M, and Sadoshima J. Thioredoxin 1 negatively regulates angiotensin II-induced cardiac hypertrophy through upregulation of miR-98/let-7. Circ Res 108: 305-313, 2011.
    • (2011) Circ Res , vol.108 , pp. 305-313
    • Yang, Y.1    Ago, T.2    Zhai, P.3    Abdellatif, M.4    Sadoshima, J.5
  • 308
    • 34548507495 scopus 로고    scopus 로고
    • Thiol oxidation in signaling and response to stress: Detection and quantification of physiological and pathophysiological thiol modifications
    • DOI 10.1016/j.freeradbiomed.2007.07.014, PII S0891584907004959
    • Ying J, Clavreul N, Sethuraman M, Adachi T, and Cohen RA. Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications. Free Radic Biol Med 43: 1099-1108, 2007. (Pubitemid 47374443)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.8 , pp. 1099-1108
    • Ying, J.1    Clavreul, N.2    Sethuraman, M.3    Adachi, T.4    Cohen, R.A.5
  • 309
    • 84859393607 scopus 로고    scopus 로고
    • Comprehensive analysis of protein modifications by top-down mass spectrometry
    • Zhang H and Ge Y. Comprehensive analysis of protein modifications by top-down mass spectrometry. Circ Cardiovasc Genet 4: 711, 2011.
    • (2011) Circ Cardiovasc Genet , vol.4 , pp. 711
    • Zhang, H.1    Ge, Y.2
  • 312
    • 0001434308 scopus 로고
    • Kinetics of oneelectron oxidation of thiols and hydrogen abstraction by thiyl radicals from .alpha.-amino C-H bonds
    • Zhao R, Lind J, Merenyi G, and Eriksen TE. Kinetics of oneelectron oxidation of thiols and hydrogen abstraction by thiyl radicals from .alpha.-amino C-H bonds. J Am Chem Soc 116: 12010-12015, 1994.
    • (1994) J Am Chem Soc , vol.116 , pp. 12010-12015
    • Zhao, R.1    Lind, J.2    Merenyi, G.3    Eriksen, T.E.4
  • 314
    • 33745198418 scopus 로고    scopus 로고
    • Redox regulation of cardiac calcium channels and transporters
    • Zima AV and Blatter LA. Redox regulation of cardiac calcium channels and transporters. Cardiovasc Res 71: 310-321, 2006.
    • (2006) Cardiovasc Res , vol.71 , pp. 310-321
    • Zima, A.V.1    Blatter, L.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.