메뉴 건너뛰기




Volumn 15, Issue 26, 2009, Pages 3052-3062

Mitochondrial-targeted antioxidants and oxidative stress: A proteomic prospective study

Author keywords

Antioxidant; Cardiovascular disease; Free radicals; Mitochondria; Oxidative stress; Proteomics

Indexed keywords

ALPHA TOCOPHEROL; ANTIOXIDANT; FLUPIRTINE; HIGH DENSITY LIPOPROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LOW DENSITY LIPOPROTEIN; MITOCHONDRIAL DNA; NITRIC OXIDE; PROTEOME; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; TRANSCRIPTOME; TROLOX C; TROPONIN; UBIQUINONE;

EID: 70449431374     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209789058138     Document Type: Review
Times cited : (10)

References (105)
  • 1
    • 0024417667 scopus 로고
    • International mortality from heart disease: Rates and trends
    • Thom TJ. International mortality from heart disease: rates and trends. Int J Epidemiol 1989; 18: 20-28
    • (1989) Int J Epidemiol , vol.18 , pp. 20-28
    • Thom, T.J.1
  • 2
    • 0032563824 scopus 로고    scopus 로고
    • Trends in the incidence of myocardial infarction and in mortality due to coronary heart disease, 1987 to 1994
    • Rosamond WD, Chambless LE, Folsom AR, Cooper LS, Conwill DE, Clegg L et al. Trends in the incidence of myocardial infarction and in mortality due to coronary heart disease, 1987 to 1994. N Engl J Med 1998; 339: 861-867
    • (1998) N Engl J Med , vol.339 , pp. 861-867
    • Rosamond, W.D.1    Chambless, L.E.2    Folsom, A.R.3    Cooper, L.S.4    Conwill, D.E.5    Clegg, L.6
  • 3
    • 17144431795 scopus 로고    scopus 로고
    • What have we learnt about microarray analyses of atherogenesis?
    • Tuomisto TT, Yla-Herttuala S. What have we learnt about microarray analyses of atherogenesis?. Curr Opin Lipidol 2005; 16: 201-205
    • (2005) Curr Opin Lipidol , vol.16 , pp. 201-205
    • Tuomisto, T.T.1    Yla-Herttuala, S.2
  • 4
    • 33745047836 scopus 로고    scopus 로고
    • Genome-wide expression studies of atherosclerosis: Critical issues in methodology, analysis, interpretation of transcriptomics data
    • Bijnens AP, Lutgens E, Ayoubi T, Kuiper J, Horrevoets AJ, Daemen MJ. Genome-wide expression studies of atherosclerosis: critical issues in methodology, analysis, interpretation of transcriptomics data. Arterioscler Thromb Vasc Biol 2006; 26: 1226-1235
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 1226-1235
    • Bijnens, A.P.1    Lutgens, E.2    Ayoubi, T.3    Kuiper, J.4    Horrevoets, A.J.5    Daemen, M.J.6
  • 5
    • 0033052884 scopus 로고    scopus 로고
    • Redox imbalance in critical ill
    • Gutteridge JM, Mitchell J. Redox imbalance in critical ill. Br Med Bull 1999; 55: 49-75.
    • (1999) Br Med Bull , vol.55 , pp. 49-75
    • Gutteridge, J.M.1    Mitchell, J.2
  • 6
    • 0028792111 scopus 로고
    • Lipid peroxidation and antioxidants as biomarkers of tissue damage
    • Gutteridge JM. Lipid peroxidation and antioxidants as biomarkers of tissue damage. Clin Chem 1995; 41: 1819-1828
    • (1995) Clin Chem , vol.41 , pp. 1819-1828
    • Gutteridge, J.M.1
  • 7
    • 0342424181 scopus 로고    scopus 로고
    • Prognostic impact of coronary vasodilator dysfunction on adverse long- Term outcome of coronary heart disease
    • Schachinger V, Britten MB, Zeiher AM. Prognostic impact of coronary vasodilator dysfunction on adverse long-term outcome of coronary heart disease. Circulation 2000; 101: 1899-1906 (Pubitemid 30225269)
    • (2000) Circulation , vol.101 , Issue.16 , pp. 1899-1906
    • Schachinger, V.1    Britten, M.B.2    Zeiher, A.M.3
  • 8
    • 15944383403 scopus 로고    scopus 로고
    • Gene-environment interactions in human diseases
    • Hunter DJ. Gene-environment interactions in human diseases. Nat Rev Genet 2005; 6: 287-298
    • (2005) Nat Rev Genet , vol.6 , pp. 287-298
    • Hunter, D.J.1
  • 9
    • 25644460981 scopus 로고    scopus 로고
    • Genetics, genomics and proteomics in atherosclerosis research
    • DOI 10.1080/07853890510011949
    • Tuomisto TT, Binder BR, Yla-Herttuala S. Genetics, genomics and proteomics in atherosclerosis research. Ann Med 2005; 37: 323-332 (Pubitemid 41379839)
    • (2005) Annals of Medicine , vol.37 , Issue.5 , pp. 323-332
    • Tuomisto, T.T.1    Binder, B.R.2    Yla-Herttuala, S.3
  • 10
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • DOI 10.1016/S0962-8924(98)01273-2
    • Green D, Kroemer G. The central executioners of apoptosis: caspases or mitochondria?. Trends Cell Biol 1998; 8: 267-271 (Pubitemid 28310224)
    • (1998) Trends in Cell Biology , vol.8 , Issue.7 , pp. 267-271
    • Green, D.1    Kroemer, G.2
  • 11
    • 0032924757 scopus 로고    scopus 로고
    • Mitochondrial damage induced by conditions of oxidative stress
    • DOI 10.1016/S0891-5849(98)00216-0, PII S0891584998002160
    • Kowaltowski AJ, Vercesi AE. Mitochondrial damage induced by conditions of oxidative stress. Free Radic Biol Med 1999; 26: 463-471 (Pubitemid 29013479)
    • (1999) Free Radical Biology and Medicine , vol.26 , Issue.3-4 , pp. 463-471
    • Kowaltowski, A.J.1    Vercesi, A.E.2
  • 12
    • 0141504202 scopus 로고    scopus 로고
    • N-acetylcysteine protects-mice from lethal endotoxemia by regulating the redox state of immune cells
    • DOI 10.1080/1071576031000148727
    • Victor VM, Rocha M, De la Fuente M. N-acetylcysteine protects mice from lethal endotoxemia by regulating the redox state of immune cells. Free Radic Res 2003; 37: 919-929 (Pubitemid 37221024)
    • (2003) Free Radical Research , vol.37 , Issue.9 , pp. 919-929
    • Victor, V.M.1    Rocha, M.2    De La Fuente, M.3
  • 13
    • 1642295733 scopus 로고    scopus 로고
    • Immune cells: Free radicals and antioxidants in sepsis
    • DOI 10.1016/j.intimp.2004.01.020, PII S1567576904000487
    • Victor VM, Rocha M, De la Fuente M. Immune cells: free radicals and antioxidants in sepsis. Int Immunopharmacol 2004; 4: 327-347 (Pubitemid 38375967)
    • (2004) International Immunopharmacology , vol.4 , Issue.3 , pp. 327-347
    • Victor, V.M.1    Rocha, M.2    De La Fuente, M.3
  • 16
    • 29344446328 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria: A new therapeutic direction
    • Sheu SS, Nauduri D, Anders MW. Targeting antioxidants to mitochondria: a new therapeutic direction. Biochim Biophys Acta 2006; 1762: 256-265
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 256-265
    • Sheu, S.S.1    Nauduri, D.2    Anders, M.W.3
  • 19
    • 0037007227 scopus 로고    scopus 로고
    • Mitochondria are morphologically and functionally heterogeneous within cells
    • DOI 10.1093/emboj/21.7.1616
    • Collins TJ, Berridge MJ, Lipp P, Bootman MD. Mitochondria are morphologically and functionally heterogeneous within cells. EMBO J 2002; 21: 1616-1627 (Pubitemid 34614618)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1616-1627
    • Collins, T.J.1    Berridge, M.J.2    Lipp, P.3    Bootman, M.D.4
  • 20
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner F, Foster LJ, Campanaro S, Valle G, Mann M. Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol Cell Proteomics 2006; 5: 608-619
    • (2006) Mol Cell Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 21
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro S, Schon EA. Mitochondrial respiratory-chain diseases. N Engl J Med 2003; 348: 2656-2668
    • (2003) N Engl J Med , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 24
    • 13844281067 scopus 로고    scopus 로고
    • The powerhouse takes control of the cell: Is the mitochondrial permeability transition a viable therapeutic target against neuronal dysfunction and death?
    • Stavrovskaya IG, Kristal BS. The powerhouse takes control of the cell: is the mitochondrial permeability transition a viable therapeutic target against neuronal dysfunction and death?. Free Radic Biol Med 2005; 38: 687-697
    • (2005) Free Radic Biol Med , vol.38 , pp. 687-697
    • Stavrovskaya, I.G.1    Kristal, B.S.2
  • 25
    • 16344374718 scopus 로고    scopus 로고
    • Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition
    • Di Lisa F, Bernardi P. Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition. Cardiovasc Res 2005; 66: 222-232
    • (2005) Cardiovasc Res , vol.66 , pp. 222-232
    • Di Lisa, F.1    Bernardi, P.2
  • 26
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • DOI 10.1073/pnas.94.2.514
    • Yakes FM, Van Houten B. Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc Natl Acad Sci USA 1997; 94: 514-519 (Pubitemid 27053665)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.2 , pp. 514-519
    • Yakes, F.M.1    Van Houten, B.2
  • 27
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutasedeficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume AG, Elliott JL, Hoffman EK, Kowal NW, Ferrante RJ, Siwek DF, et al. Motor neurons in Cu/Zn superoxide dismutasedeficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat Genet 1996; 13: 43-47
    • (1996) Nat Genet , vol.13 , pp. 43-47
    • Reaume, A.G.1    Elliott, J.L.2    Hoffman, E.K.3    Kowal, N.W.4    Ferrante, R.J.5    Siwek, D.F.6
  • 30
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of Intracellular Oxygen in Hypoxia by Nitric Oxide: Effect on HIF1 alpha
    • DOI 10.1126/science.1088805
    • Hagen T, Taylor CT, Lam F, Moncada S. Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1 alpha. Science 2003; 302:1975-1978 (Pubitemid 37523507)
    • (2003) Science , vol.302 , Issue.5652 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 31
    • 0027363407 scopus 로고
    • NF-kappa B activation by ultraviolet light not dependent on a nuclear signal
    • Devary Y, Rosette C, DiDonato JA, Karin M. NF-kappa B activation by ultraviolet light not dependent on a nuclear signal. Science 1993; 261: 1442-1445 (Pubitemid 23334264)
    • (1993) Science , vol.261 , Issue.5127 , pp. 1442-1445
    • Devary, Y.1    Rosette, C.2    Didonato, J.A.3    Karin, M.4
  • 32
    • 0027328056 scopus 로고
    • Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF
    • Schulze-Osthoff K, Beyaert R, Vandervoorde V, Haegeman G, Fiers W. Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF. EMBO J 1993; 12: 3095-3104. (Pubitemid 23232740)
    • (1993) EMBO Journal , vol.12 , Issue.8 , pp. 3095-3104
    • Schulze-Osthoff, K.1    Beyaert, R.2    Vandevoorde, V.3    Haegeman, G.4    Fiers, W.5
  • 33
    • 0035849714 scopus 로고    scopus 로고
    • S-nitrosylation is emerging as a specific fundamental posttranslational protein modification: Head to head comparison with O-phosphorylation
    • Review
    • Lane P, Hao G, Gross SS. S-nitrosylation is emerging as a specific fundamental posttranslational protein modification: head to head comparison with O-phosphorylation. Sci STKE 2001; 2001(86): RE1 (Review).
    • (2001) Sci STKE , vol.2001 , Issue.86
    • Lane, P.1    Hao, G.2    Gross, S.S.3
  • 35
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • DOI 10.1016/j.sbi.2004.09.012, PII S0959440X04001769
    • Barford D. The role of cysteine residues as redox-sensitive regulatory switches. Curr Opin Struct Biol 2004; 14: 679-686 (Pubitemid 39592578)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.6 , pp. 679-686
    • Barford, D.1
  • 36
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • DOI 10.1038/nature01681
    • VanMontfort RL, Congreve M, Tisi D, Carr R, Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 2003; 423: 773-777 (Pubitemid 36735702)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 773-777
    • Van Montfort, R.L.M.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 37
    • 0033529591 scopus 로고    scopus 로고
    • Responses of cardiac protein kinase C isoforms to distinct pathological stimuli are differentially regulated
    • Takeishi Y, Jalili T, Ball NA, Walsh RA. Responses of cardiac protein kinase C isoforms to distinct pathological stimuli are differentially regulated. Circ Res 1999; 85: 264-271 (Pubitemid 29377298)
    • (1999) Circulation Research , vol.85 , Issue.3 , pp. 264-271
    • Takeishi, Y.1    Jalili, T.2    Ball, N.A.3    Walsh, R.A.4
  • 38
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. Protein oxidation and aging. Science 1992; 257: 1220-1224
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 39
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • DOI 10.1016/S0531-5565(01)00139-5, PII S0531556501001395
    • Squier TC. Oxidative stress and protein aggregation during biological aging. Exp Gerontol 2001; 36: 1539-1550 (Pubitemid 32768730)
    • (2001) Experimental Gerontology , vol.36 , Issue.9 , pp. 1539-1550
    • Squier, T.C.1
  • 40
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida K, Stadtman ER. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc Natl Acad Sci USA 1992; 89: 4544-4548
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 41
    • 0036310246 scopus 로고    scopus 로고
    • Protein tyrosine nitration and peroxynitrite
    • Beckman JS. Protein tyrosine nitration and peroxynitrite. FASEB J 2002; 16: 1144.
    • (2002) FASEB J , vol.16 , pp. 1144
    • Beckman, J.S.1
  • 42
    • 0034891783 scopus 로고    scopus 로고
    • Oxidative modification of proteins during aging
    • Levine RL, Stadtman ER. Oxidative modification of proteins during aging. Exp Gerontol 2001; 36: 1495-1502
    • (2001) Exp Gerontol , vol.36 , pp. 1495-1502
    • Levine, R.L.1    Stadtman, E.R.2
  • 43
    • 0035793088 scopus 로고    scopus 로고
    • Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins
    • Requena JR, Chao CC, Levine RL, Stadtman ER. Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proc Natl Acad Sci USA 2001; 98: 69-74.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 69-74
    • Requena, J.R.1    Chao, C.C.2    Levine, R.L.3    Stadtman, E.R.4
  • 44
    • 4244218956 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism
    • DOI 10.1023/A:1015916831583
    • Stadtman ER, Moskovitz J, Berlett BS, Levine RL. Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol Cell Biochem 2002; 234-235: 3-9. (Pubitemid 34777836)
    • (2002) Molecular and Cellular Biochemistry , vol.234-235 , pp. 3-9
    • Stadtman, E.R.1    Moskovitz, J.2    Berlett, B.S.3    Levine, R.L.4
  • 46
    • 0343986284 scopus 로고    scopus 로고
    • Drug delivery to mitochondria: The key to mitochondrial medicine
    • Murphy MP, Smith RA. Drug delivery to mitochondria: the key to mitochondrial medicine. Adv Drug Deliv Rev 2000; 41: 235-250
    • (2000) Adv Drug Deliv Rev , vol.41 , pp. 235-250
    • Murphy, M.P.1    Smith, R.A.2
  • 48
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace DC. Mitochondrial diseases in man and mouse. Science 1999; 283: 1482-1488
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 49
    • 0028609520 scopus 로고
    • Advanced Maillard reaction end products, free radicals, and protein oxidation in Alzheimer's disease
    • Smith MA, Richey PL, Taneda S, Kutty RK, Sayre LM, Monnier VM, et al. Advanced Maillard reaction end products, free radicals, and protein oxidation in Alzheimer's disease. Ann NY Acad Sci 1994; 738: 447-454
    • (1994) Ann NY Acad Sci , vol.738 , pp. 447-454
    • Smith, Ma.1    Richey, P.L.2    Taneda, S.3    Kutty, R.K.4    Sayre, L.M.5    Monnier, V.M.6
  • 50
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • DOI 10.1081/DMR-100102336
    • Shacter E. Quantification and significance of protein oxidation in biological samples. Drug Metab Rev 2000; 32: 307-326 (Pubitemid 32001909)
    • (2000) Drug Metabolism Reviews , vol.32 , Issue.3-4 , pp. 307-326
    • Shacter, E.1
  • 53
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
    • DOI 10.1016/j.ejphar.2006.06.026, PII S0014299906006467
    • Butterfield DA, Perluigi M, Sultana R. Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. Eur J Pharmacol 2006; 545: 39-50. (Pubitemid 44215876)
    • (2006) European Journal of Pharmacology , vol.545 , Issue.1 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 55
    • 17044378603 scopus 로고    scopus 로고
    • Proteomics of ischemia/reperfusion injury in rabbit myocardium reveals alterations to proteins of essential functional systems
    • DOI 10.1002/pmic.200400995
    • White MY, Cordwell SJ, McCarron HC, Prasan AM, Craft G, Hambly BD, et al. Proteomics of ischemia/reperfusion injury in rabbit myocardium reveals alterations to proteins of essential functional systems. Proteomics 2005; 5: 1395-1410 (Pubitemid 40503055)
    • (2005) Proteomics , vol.5 , Issue.5 , pp. 1395-1410
    • White, M.Y.1    Cordwell, S.J.2    McCarron, H.C.K.3    Prasan, A.M.4    Craft, G.5    Hambly, B.D.6    Jeremy, R.W.7
  • 58
    • 33750431664 scopus 로고    scopus 로고
    • Analyzing the cardiac muscle proteome by liquid chromatography-mass spectrometry-based expression proteomics
    • Gramolini AO, Kislinger T, Liu PP, MacLennan DH, Emili A. Analyzing the cardiac muscle proteome by liquid chromatography-mass spectrometry-based expression proteomics. Methods Mol Biol 2007; 357: 15-31.
    • (2007) Methods Mol Biol , vol.357 , pp. 15-31
    • Gramolini, A.O.1    Kislinger, T.2    Liu, P.P.3    MacLennan, D.H.4    Emili, A.5
  • 59
  • 60
    • 3042771387 scopus 로고    scopus 로고
    • Detection of regional changes in protein levels in the in vivo canine model of acute heart failure following ischemia-reperfusion injury: Functional proteomics studies
    • Sawicki G, Jugdutt BI. Detection of regional changes in protein levels in the in vivo canine model of acute heart failure following ischemia-reperfusion injury: functional proteomics studies. Proteomics 2004; 4: 2195-2202
    • (2004) Proteomics , vol.4 , pp. 2195-2202
    • Sawicki, G.1    Jugdutt, B.I.2
  • 61
    • 0028289443 scopus 로고
    • A definition of initial, fatty streak, and intermediate lesions of atherosclerosis. A report from the Committee on Vascular Lesions of the Council on Arteriosclerosis
    • American Heart Association
    • Stary HC, Chandler AB, Glagov S, Guyton JR, Insull W Jr, Rosenfeld ME, et al. A definition of initial, fatty streak, and intermediate lesions of atherosclerosis. A report from the Committee on Vascular Lesions of the Council on Arteriosclerosis. American Heart Association. Circulation 1994; 89: 2462-2478
    • (1994) Circulation , vol.89 , pp. 2462-2478
    • Stary, H.C.1    Chandler, A.B.2    Glagov, S.3    Guyton, J.R.4    Insull Jr., W.5    Rosenfeld, M.E.6
  • 63
    • 0022502722 scopus 로고
    • Human aortic intima protein composition during initial stages of atherogenesis
    • Stastny J, Fosslien E, Robertson AL Jr. Human aortic intima protein composition during initial stages of atherogenesis. Atherosclerosis 1986; 60: 131-139
    • (1986) Atherosclerosis , vol.60 , pp. 131-139
    • Stastny, J.1    Fosslien, E.2    Robertson Jr., A.L.3
  • 65
    • 0027082524 scopus 로고
    • Quantitative alteration of some aortic intima proteins in fatty streaks and fibro-fatty lesions
    • Stastny JJ, Fosslien E. Quantitative alteration of some aortic intima proteins in fatty streaks and fibro-fatty lesions. Exp Mol Pathol 1992; 57: 205-214
    • (1992) Exp Mol Pathol , vol.57 , pp. 205-214
    • Stastny, J.J.1    Fosslien, E.2
  • 66
    • 0022370877 scopus 로고
    • Effect of aging on human aortic protein composition: II. Two-dimensional polyacrylamide gel electrophoretic analysis
    • Song J, Stastny J, Fosslien E, Robertson AL Jr. Effect of aging on human aortic protein composition: II. Two-dimensional polyacrylamide gel electrophoretic analysis. Exp Mol Pathol 1985; 43: 297-304.
    • (1985) Exp Mol Pathol , vol.43 , pp. 297-304
    • Song, J.1    Stastny, J.2    Fosslien, E.3    Robertson Jr., A.L.4
  • 67
    • 0037453132 scopus 로고    scopus 로고
    • Proteomic approach to coronary atherosclerosis shows ferritin light chain as a significant marker: Evidence consistent with iron hypothesis in atherosclerosis
    • You SA, Archacki SR, Angheloiu G, Moravec CS, Rao S, Kinter M, et al. Proteomic approach to coronary atherosclerosis shows ferritin light chain as a significant marker: evidence consistent with iron hypothesis in atherosclerosis. Physiol Genomics 2003; 13: 25-30.
    • (2003) Physiol Genomics , vol.13 , pp. 25-30
    • You, S.A.1    Archacki, S.R.2    Angheloiu, G.3    Moravec, C.S.4    Rao, S.5    Kinter, M.6
  • 69
    • 8744294747 scopus 로고    scopus 로고
    • Analysis of proteome and transcriptome of tumor necrosis factor alpha stimulated vascular smooth muscle cells with or without alpha lipoic acid
    • Jang WG, Kim HS, Park KG, Park YB, Yoon KH, Han SW, et al. Analysis of proteome and transcriptome of tumor necrosis factor alpha stimulated vascular smooth muscle cells with or without alpha lipoic acid. Proteomics 2004; 4: 3383-3393
    • (2004) Proteomics , vol.4 , pp. 3383-3393
    • Jang, W.G.1    Kim, H.S.2    Park, K.G.3    Park, Y.B.4    Yoon, K.H.5    Han, S.W.6
  • 70
    • 13844306306 scopus 로고    scopus 로고
    • Lipoproteomics I: Mapping of proteins in low-density lipoprotein using two-dimensional gel electrophoresis and mass spectrometry
    • DOI 10.1002/pmic.200300938
    • Karlsson H, Leanderson P, Tagesson C, Lindahl M. Lipoproteomics I: mapping of proteins in low-density lipoprotein using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2005; 5: 551-565 (Pubitemid 40262072)
    • (2005) Proteomics , vol.5 , Issue.2 , pp. 551-565
    • Karlsson, H.1    Leanderson, P.2    Tagesson, C.3    Lindahl, M.4
  • 71
    • 0035928838 scopus 로고    scopus 로고
    • Immunopathogenesis of atherosclerosis: Endotoxin accelerates atherosclerosis in rabbits on hypercholesterolemic diet
    • Lehr HA, Sagban TA, Ihling C, Zähringer U, Hungerer KD, Blumrich M, et al. Immunopathogenesis of atherosclerosis: endotoxin accelerates atherosclerosis in rabbits on hypercholesterolemic diet. Circulation 2001; 104: 914-920
    • (2001) Circulation , vol.104 , pp. 914-920
    • Lehr, H.A.1    Sagban, T.A.2    Ihling, C.3    Zähringer, U.4    Hungerer, K.D.5    Blumrich, M.6
  • 75
    • 0141864397 scopus 로고    scopus 로고
    • Identification of novel signaling complexes by functional proteomics
    • DOI 10.1161/01.RES.0000093221.98213.E0
    • Ping P. Identification of novel signaling complexes by functional proteomics. Circ Res 2003; 93: 595-603. (Pubitemid 37222155)
    • (2003) Circulation Research , vol.93 , Issue.7 , pp. 595-603
    • Ping, P.1
  • 77
    • 4744351348 scopus 로고    scopus 로고
    • Heart disease, clinical proteomics and mass spectrometry
    • Stanley BA, Gundry RL, Cotter RJ, Van Eyk JE. Heart disease, clinical proteomics and mass spectrometry. Dis Markers 2004; 20: 167-178 (Pubitemid 39314347)
    • (2004) Disease Markers , vol.20 , Issue.3 , pp. 167-178
    • Stanley, B.A.1    Gundry, R.L.2    Cotter, R.J.3    Van Eyk, J.E.4
  • 78
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • DOI 10.1002/pmic.200401031
    • Gorg A, Weiss W, Dunn MJ. Current two-dimensional electrophoresis technology for proteomics. Proteomics 2004; 4: 3665-3685 (Pubitemid 39657447)
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 80
    • 26044474872 scopus 로고    scopus 로고
    • Validation and quality control of protein microarray-based analytical methods
    • Kricka LJ, Master SR. Validation and quality control of protein microarray-based analytical methods. Methods Mol Med 2005; 114: 233-255
    • (2005) Methods Mol Med , vol.114 , pp. 233-255
    • Kricka, L.J.1    Master, S.R.2
  • 81
    • 0036194529 scopus 로고    scopus 로고
    • Mitochondria as a pharmacological target
    • Szewczyk A, Wojtczak L. Mitochondria as a pharmacological target. Pharmacol Rev 2002; 54: 101-127
    • (2002) Pharmacol Rev , vol.54 , pp. 101-127
    • Szewczyk, A.1    Wojtczak, L.2
  • 82
    • 0348136710 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect Friedreich Ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants
    • Jauslin ML, Meier T, Smith RA, Murphy MP. Mitochondria-targeted antioxidants protect Friedreich Ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants. FASEB J 2003; 17: 1972-1974
    • (2003) FASEB J , vol.17 , pp. 1972-1974
    • Jauslin, M.L.1    Meier, T.2    Smith, R.A.3    Murphy, M.P.4
  • 91
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • DOI 10.1038/13690
    • Gipy SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R. Quantitaive analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 1999; 17: 994-999 (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
  • 92
    • 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, Cohen RA. Isotope-coded affinity tag (ICAT) approach to identify and quantify oxidant-sensitive protein thiols. Mol Cell Proteomics 2004; 3: 273-278 (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
  • 95
    • 0035566429 scopus 로고    scopus 로고
    • Analysis of peptides and proteins containing nitrotyrosine by matrix-assisted laser desorption/ionization mass spectrometry
    • DOI 10.1016/S1044-0305(01)00213-6, PII S1044030501002136
    • Sarver A, Scheffler NK, Shetlar MD, Gibson BW. Analysis of peptides and proteins containing nitrotyrosine by matrix-assisted laser desorption/ionization mass spectrometry. J Am Soc Mass Spectrom 2001; 12: 439-448 (Pubitemid 34546613)
    • (2001) Journal of the American Society for Mass Spectrometry , vol.12 , Issue.4 , pp. 439-448
    • Sarver, A.1    Scheffler, N.K.2    Shetlar, M.D.3    Gibson, B.W.4
  • 96
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex I due to peroxynitrite: Identification of reactive tyrosines by mass spectrometry
    • DOI 10.1074/jbc.M305694200
    • Murray J, Taylor SW, Zhang B, Ghosh SS, Capaldi RA. Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry. J Biol Chem 2003; 278: 37223-37230 (Pubitemid 37175238)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 97
    • 0346788870 scopus 로고    scopus 로고
    • Quantitative screening of protein biomarkers of early glycation, advanced glycation, oxidation and nitrosation in cellular and extracellular proteins by tandem mass spectrometry multiple reaction monitoring
    • Ahmed N, Thornalley PJ. Quantitative screening of protein biomarkers of early glycation, advanced glycation, oxidation and nitrosation in cellular and extracellular protein by tandem mass spectrometry multiple reaction monitoring. Biochem Soc Trans 2003; 31: 1417-1422 (Pubitemid 38030990)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1417-1422
    • Ahmed, N.1    Thornalley, P.J.2
  • 99
    • 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, Yang AJ. High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. Pharm Res 2003; 20: 1713-1720 (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
  • 100
    • 33845991485 scopus 로고    scopus 로고
    • Proteomic analysis reveals higher demand for antioxidant protection in embryonic stem cell-derived smooth muscle cells
    • DOI 10.1002/pmic.200600351
    • Yin X, Mayr M, Xiao Q, Wang W, Xu Q. Proteomic analysis reveals higher demand for antioxidant protection in embryonic stem cell-derived smooth muscle cells. Proteomics 2006; 6: 6437-6446 (Pubitemid 46048384)
    • (2006) Proteomics , vol.6 , Issue.24 , pp. 6437-6446
    • Yin, X.1    Mayr, M.2    Xiao, Q.3    Wang, W.4    Xu, Q.5
  • 101
    • 10644248275 scopus 로고    scopus 로고
    • Vascular proteomics: Linking proteomic and metabolomic changes
    • DOI 10.1002/pmic.200400947
    • Mayr M, Mayr U, Chung YL, Yin X, Griffiths JR, Xu Q. Vascular proteomics: linking proteomic and metabolomic changes. Proteomics 2004; 4: 3751-3761 (Pubitemid 39657452)
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3751-3761
    • Mayr, M.1    Mayr, U.2    Chung, Y.-L.3    Yin, X.4    Griffiths, J.R.5    Xu, Q.6
  • 102
    • 0035523363 scopus 로고    scopus 로고
    • Identification and mapping of human saphenous vein medial smooth muscle proteins by two-dimensional polyacrylamide gel electrophoresis
    • McGregor E, Kempster L, Wait R, Welson SY, Gosling M, Dunn MJ, et al. Identification and mapping of human saphenous vein medial smooth muscle proteins by two-dimensional polyacrylamide gel electrophoresis. Proteomics 2001; 1: 1405-1414 (Pubitemid 33587896)
    • (2001) Proteomics , vol.1 , Issue.11 , pp. 1405-1414
    • McGregor, E.1    Kempster, L.2    Wait, R.3    Welson, S.Y.4    Gosling, M.5    Dunn, M.J.6    Powell, J.T.7
  • 104
    • 42049094453 scopus 로고    scopus 로고
    • The protective role of steroids in ischemia- reperfusion injury of the liver
    • Pulitano C, Aldrighetti L. The protective role of steroids in ischemia- reperfusion injury of the liver. Curr Pharm Des 2008; 14(5): 496-503.
    • (2008) Curr Pharm Des , vol.14 , Issue.5 , pp. 496-503
    • Pulitano, C.1    Aldrighetti, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.