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Volumn 74, Issue 11, 2011, Pages 2274-2288

Proteomic detection of nitroproteins as potential biomarkers for cardiovascular disease

Author keywords

Biomarker; Cardiovascular disease; Nitroprotein

Indexed keywords

3 NITROTYROSINE; ACTIN; ALBUMIN; ALPHA SYNUCLEIN; ANGIOTENSIN II; APOLIPOPROTEIN A1; APOLIPOPROTEIN B100; BIOLOGICAL MARKER; CREATINE KINASE; CYCLOOXYGENASE 1; CYTOCHROME C; FIBRINOGEN; HISTONE; NITROPROTEIN; PROSTACYCLIN SYNTHASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SUPEROXIDE DISMUTASE; TYROSINE; UNCLASSIFIED DRUG;

EID: 80054868098     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.05.029     Document Type: Review
Times cited : (16)

References (121)
  • 1
    • 15744362013 scopus 로고    scopus 로고
    • World Health Organization
    • World Health Organization The world health report 2005.
    • (2005) The world health report
  • 2
    • 77957831897 scopus 로고    scopus 로고
    • Novel biomarkers in cardiovascular disease: update 2010
    • Hochholzer W., Morrow D.A., Giugliano R.P. Novel biomarkers in cardiovascular disease: update 2010. Am Heart J 2010, 160:583-594.
    • (2010) Am Heart J , vol.160 , pp. 583-594
    • Hochholzer, W.1    Morrow, D.A.2    Giugliano, R.P.3
  • 3
    • 21544467275 scopus 로고    scopus 로고
    • Pathophysiology of coronary artery disease
    • Libby P., Theroux P. Pathophysiology of coronary artery disease. Circulation 2005, 111:3481-3488.
    • (2005) Circulation , vol.111 , pp. 3481-3488
    • Libby, P.1    Theroux, P.2
  • 4
    • 0035100888 scopus 로고    scopus 로고
    • Biomarkers and surrogate endpoints: preferred definitions and conceptual framework. Biomarkers Definitions Working Group
    • Mar
    • Biomarkers and surrogate endpoints: preferred definitions and conceptual framework. Biomarkers Definitions Working Group. Clin Pharmacol Ther 2001, 69(3):89-95. Mar.
    • (2001) Clin Pharmacol Ther , vol.69 , Issue.3 , pp. 89-95
  • 7
    • 33947275729 scopus 로고    scopus 로고
    • Moving cancer diagnostics from bench to bedside
    • Zhang X., Li L., Wei D., Yap Y., Chen F. Moving cancer diagnostics from bench to bedside. Trends Biotechnol 2007, 25:166-173.
    • (2007) Trends Biotechnol , vol.25 , pp. 166-173
    • Zhang, X.1    Li, L.2    Wei, D.3    Yap, Y.4    Chen, F.5
  • 8
    • 0035037328 scopus 로고    scopus 로고
    • Use of biomarkers and surrogate endpoints in drug development and regulatory decision making: criteria, validation, strategies
    • Lesko L.J., Atkinson A.J. Use of biomarkers and surrogate endpoints in drug development and regulatory decision making: criteria, validation, strategies. Annu Rev Pharmacol Toxicol 2001, 41:347-366.
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 347-366
    • Lesko, L.J.1    Atkinson, A.J.2
  • 9
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: the long and uncertain path to clinical utility
    • Rifai N., Gillette M.A., Carr S.A. Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat Biotechnol 2006, 24:971-983.
    • (2006) Nat Biotechnol , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 10
    • 33846548168 scopus 로고    scopus 로고
    • Mass spectrometric detection of tissue proteins in plasma
    • Zhang H., Liu A.Y., Loriaux P., et al. Mass spectrometric detection of tissue proteins in plasma. Mol Cell Proteomics 2007, 6:64-71.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 64-71
    • Zhang, H.1    Liu, A.Y.2    Loriaux, P.3
  • 12
    • 33750469002 scopus 로고    scopus 로고
    • Cardiovascular proteomics: tools to develop novel biomarkers and potential applications
    • Arab S., Gramolini A.O., Ping P., et al. Cardiovascular proteomics: tools to develop novel biomarkers and potential applications. J Am Coll Cardiol 2006, 48:1733-1741.
    • (2006) J Am Coll Cardiol , vol.48 , pp. 1733-1741
    • Arab, S.1    Gramolini, A.O.2    Ping, P.3
  • 13
    • 0344196903 scopus 로고    scopus 로고
    • NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?
    • Schopfer F.J., Baker P.R., Freeman B.A. NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?. Trends Biochem Sci 2003, 28:646-654.
    • (2003) Trends Biochem Sci , vol.28 , pp. 646-654
    • Schopfer, F.J.1    Baker, P.R.2    Freeman, B.A.3
  • 15
    • 0030249458 scopus 로고    scopus 로고
    • Peroxynitrite reaction with carbon dioxide/bicarbonate: kinetics and influence on peroxynitrite-mediated oxidations
    • Denicola A., Freeman B.A., Trujillo M., Radi R. Peroxynitrite reaction with carbon dioxide/bicarbonate: kinetics and influence on peroxynitrite-mediated oxidations. Arch Biochem Biophys 1996, 333:49-58.
    • (1996) Arch Biochem Biophys , vol.333 , pp. 49-58
    • Denicola, A.1    Freeman, B.A.2    Trujillo, M.3    Radi, R.4
  • 16
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity
    • Van der Vliet A., Eiserich J.P., Halliwell B., Cross C.E. Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J Biol Chem 1997, 272:7617-7625.
    • (1997) J Biol Chem , vol.272 , pp. 7617-7625
    • Van der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 17
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan M.L., Wu W., Fu X., et al. A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J Biol Chem 2002, 277:17415-17427.
    • (2002) J Biol Chem , vol.277 , pp. 17415-17427
    • Brennan, M.L.1    Wu, W.2    Fu, X.3
  • 18
    • 0036801357 scopus 로고    scopus 로고
    • Spatial mapping of pulmonary and vascular nitrotyrosine reveals the pivotal role of myeloperoxidase as a catalyst for tyrosine nitration in inflammatory diseases
    • Baldus S., Eiserich J.P., Brennan M.L., Jackson R.M., Alexander C.B., Freeman B.A. Spatial mapping of pulmonary and vascular nitrotyrosine reveals the pivotal role of myeloperoxidase as a catalyst for tyrosine nitration in inflammatory diseases. Free Radic Biol Med 2002, 33:1010.
    • (2002) Free Radic Biol Med , vol.33 , pp. 1010
    • Baldus, S.1    Eiserich, J.P.2    Brennan, M.L.3    Jackson, R.M.4    Alexander, C.B.5    Freeman, B.A.6
  • 19
    • 10944234930 scopus 로고    scopus 로고
    • Recent methodological advances in the mass spectrometric analysis of free and protein-associated 3-nitrotyrosine in human plasma
    • Tsikas D., Caidahl K. Recent methodological advances in the mass spectrometric analysis of free and protein-associated 3-nitrotyrosine in human plasma. J Chromatogr B Analyt Technol Biomed Life Sci 2005, 814:1-9.
    • (2005) J Chromatogr B Analyt Technol Biomed Life Sci , vol.814 , pp. 1-9
    • Tsikas, D.1    Caidahl, K.2
  • 20
    • 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 H.A., Postma D.S., Bischoff R. Protein tyrosine nitration: selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins. J Proteome Res 2009, 8:3222-3238.
    • (2009) J Proteome Res , vol.8 , pp. 3222-3238
    • Abello, N.1    Kerstjens, H.A.2    Postma, D.S.3    Bischoff, R.4
  • 21
    • 14844311934 scopus 로고    scopus 로고
    • Candidate-based proteomics in the search for biomarkers of cardiovascular disease
    • Anderson L. Candidate-based proteomics in the search for biomarkers of cardiovascular disease. J Physiol 2005, 563:23-60.
    • (2005) J Physiol , vol.563 , pp. 23-60
    • Anderson, L.1
  • 22
    • 8844244036 scopus 로고    scopus 로고
    • The human pituitary nitroproteome: detection of nitrotyrosyl-proteins with two-dimensional Western blotting, and amino acid sequence determination with mass spectrometry
    • Zhan X., Desiderio D.M. The human pituitary nitroproteome: detection of nitrotyrosyl-proteins with two-dimensional Western blotting, and amino acid sequence determination with mass spectrometry. Biochem Biophys Res Commun 2004, 325:1180-1186.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 1180-1186
    • Zhan, X.1    Desiderio, D.M.2
  • 23
    • 0037423394 scopus 로고    scopus 로고
    • Nitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization
    • Aslan M., Ryan T.M., Townes T.M., Coward L., Kirk M.C., Barnes S., Alexander C.B., Rosenfeld S.S., Freeman B.A. Nitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization. J Biol Chem 2003, 278:4194-4204.
    • (2003) J Biol Chem , vol.278 , pp. 4194-4204
    • Aslan, M.1    Ryan, T.M.2    Townes, T.M.3    Coward, L.4    Kirk, M.C.5    Barnes, S.6    Alexander, C.B.7    Rosenfeld, S.S.8    Freeman, B.A.9
  • 24
    • 12844268120 scopus 로고    scopus 로고
    • Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages
    • Zheng L., Settle M., Brubaker G., et al. Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages. J Biol Chem 2005, 280:38-47.
    • (2005) J Biol Chem , vol.280 , pp. 38-47
    • Zheng, L.1    Settle, M.2    Brubaker, G.3
  • 25
    • 77958143488 scopus 로고    scopus 로고
    • Application of proteomics in biomarker discovery: a primer for the clinician
    • Tambor V., Fucíková A., Lenco J., et al. Application of proteomics in biomarker discovery: a primer for the clinician. Physiol Res 2010, 59:471-497.
    • (2010) Physiol Res , vol.59 , pp. 471-497
    • Tambor, V.1    Fucíková, A.2    Lenco, J.3
  • 26
    • 0141613681 scopus 로고    scopus 로고
    • Going global: protein expression profiling using shotgun mass spectrometry
    • Kislinger T., Emili A. Going global: protein expression profiling using shotgun mass spectrometry. Curr Opin Mol Ther 2003, 5:285-293.
    • (2003) Curr Opin Mol Ther , vol.5 , pp. 285-293
    • Kislinger, T.1    Emili, A.2
  • 27
    • 0037615160 scopus 로고    scopus 로고
    • Site-specific quantitation of protein nitration using liquid chromatography/tandem mass spectrometry
    • Willard B.B., Ruse C.I., Keightley J.A., Bond M., Kinter M. Site-specific quantitation of protein nitration using liquid chromatography/tandem mass spectrometry. Anal Chem 2003, 75:2370-2376.
    • (2003) Anal Chem , vol.75 , pp. 2370-2376
    • Willard, B.B.1    Ruse, C.I.2    Keightley, J.A.3    Bond, M.4    Kinter, M.5
  • 28
    • 77149136461 scopus 로고    scopus 로고
    • Current technological challenges in biomarker discovery and validation
    • Horvatovich P.L., Bischoff R. Current technological challenges in biomarker discovery and validation. Eur J Mass Spectrom (Chichester, Eng) 2010, 16:101-121.
    • (2010) Eur J Mass Spectrom (Chichester, Eng) , vol.16 , pp. 101-121
    • Horvatovich, P.L.1    Bischoff, R.2
  • 29
    • 70549113220 scopus 로고    scopus 로고
    • Perspectives of targeted mass spectrometry for protein biomarker verification
    • Hüttenhain R., Malmström J., Picotti P., Aebersold R. Perspectives of targeted mass spectrometry for protein biomarker verification. Curr Opin Chem Biol 2009, 13:518-525.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 518-525
    • Hüttenhain, R.1    Malmström, J.2    Picotti, P.3    Aebersold, R.4
  • 30
    • 71049137289 scopus 로고    scopus 로고
    • Multiple reaction monitoring-based, multiplexed, absolute quantitation of 45 proteins in human plasma
    • Kuzyk M.A., Smith D., Yang J., et al. Multiple reaction monitoring-based, multiplexed, absolute quantitation of 45 proteins in human plasma. Mol Cell Proteomics 2009, 8:1860-1877.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1860-1877
    • Kuzyk, M.A.1    Smith, D.2    Yang, J.3
  • 31
    • 70349144524 scopus 로고    scopus 로고
    • Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease
    • Danielson S.R., Held J.M., Schilling B., Oo M., Gibson B.W., Andersen J.K. Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease. Anal Chem 2009, 81:7823-7828.
    • (2009) Anal Chem , vol.81 , pp. 7823-7828
    • Danielson, S.R.1    Held, J.M.2    Schilling, B.3    Oo, M.4    Gibson, B.W.5    Andersen, J.K.6
  • 32
    • 0842323768 scopus 로고    scopus 로고
    • Structural and functional adaptations of striated muscles to CK deficiency
    • Ventura-Clapier R., Kaasik A., Veksler V. Structural and functional adaptations of striated muscles to CK deficiency. Mol Cell Biochem 2004, 256-257:29-41.
    • (2004) Mol Cell Biochem , pp. 29-41
    • Ventura-Clapier, R.1    Kaasik, A.2    Veksler, V.3
  • 33
    • 0026698727 scopus 로고
    • Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism
    • Wyss M., Smeitink J., Wevers R.A., Wallimann T. Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim Biophys Acta 1992, 1102:119-166.
    • (1992) Biochim Biophys Acta , vol.1102 , pp. 119-166
    • Wyss, M.1    Smeitink, J.2    Wevers, R.A.3    Wallimann, T.4
  • 35
    • 3342967512 scopus 로고    scopus 로고
    • Is the failing heart energy starved? On using chemical energy to support cardiac function
    • Ingwall J.S., Weiss R.G. Is the failing heart energy starved? On using chemical energy to support cardiac function. Circ Res 2004, 95:135-145.
    • (2004) Circ Res , vol.95 , pp. 135-145
    • Ingwall, J.S.1    Weiss, R.G.2
  • 36
    • 0030008105 scopus 로고    scopus 로고
    • Energetic basis for reduced contractile reserve in isolated rat hearts
    • Tian R., Ingwall J. Energetic basis for reduced contractile reserve in isolated rat hearts. Am J Physiol 1996, 270:1207-1216.
    • (1996) Am J Physiol , vol.270 , pp. 1207-1216
    • Tian, R.1    Ingwall, J.2
  • 37
    • 0029098914 scopus 로고
    • Inhibition of the creatine kinase reaction decreases the contractile reserve of isolated rat hearts
    • Hamman B.L., Bittl J.A., Jacobus W.E., et al. Inhibition of the creatine kinase reaction decreases the contractile reserve of isolated rat hearts. Am J Physiol 1995, 269:1030-1036.
    • (1995) Am J Physiol , vol.269 , pp. 1030-1036
    • Hamman, B.L.1    Bittl, J.A.2    Jacobus, W.E.3
  • 38
    • 0022270940 scopus 로고
    • The creatine kinase system in normal and diseased human myocardium
    • Ingwall J.S., Kramer M.F., Fifer M.A., et al. The creatine kinase system in normal and diseased human myocardium. N Engl J Med 1985, 313:1050-1054.
    • (1985) N Engl J Med , vol.313 , pp. 1050-1054
    • Ingwall, J.S.1    Kramer, M.F.2    Fifer, M.A.3
  • 39
    • 0029800446 scopus 로고    scopus 로고
    • Creatine kinase system in failing and nonfailing human myocardium
    • Nascimben L., Ingwall J.S., Pauletto P., et al. Creatine kinase system in failing and nonfailing human myocardium. Circulation 1996, 94:1894-1901.
    • (1996) Circulation , vol.94 , pp. 1894-1901
    • Nascimben, L.1    Ingwall, J.S.2    Pauletto, P.3
  • 40
    • 0242712993 scopus 로고    scopus 로고
    • Proton magnetic resonance spectroscopy can detect creatine depletion associated with the progression of heart failure in cardiomyopathy
    • Nakae I., Mitsunami K., Omura T., et al. Proton magnetic resonance spectroscopy can detect creatine depletion associated with the progression of heart failure in cardiomyopathy. J Am Coll Cardiol 2003, 42:1587-1593.
    • (2003) J Am Coll Cardiol , vol.42 , pp. 1587-1593
    • Nakae, I.1    Mitsunami, K.2    Omura, T.3
  • 41
    • 0030819144 scopus 로고    scopus 로고
    • Myocardial phosphocreatine-to-ATP ratio is a predictor of mortality in patients with dilated cardiomyopathy
    • Neubauer S., Horn M., Cramer M., et al. Myocardial phosphocreatine-to-ATP ratio is a predictor of mortality in patients with dilated cardiomyopathy. Circulation 1997, 96:2190-2196.
    • (1997) Circulation , vol.96 , pp. 2190-2196
    • Neubauer, S.1    Horn, M.2    Cramer, M.3
  • 42
    • 0035110310 scopus 로고    scopus 로고
    • Peroxynitrite induced nitration and inactivation of myofibrillar creatine kinase in experimental heart failure
    • Mihm M.J., Coyle C.M., Schanbacher B.L., Weinstein D.M., Bauer J.A. Peroxynitrite induced nitration and inactivation of myofibrillar creatine kinase in experimental heart failure. Cardiovasc Res 2001, 49:798-807.
    • (2001) Cardiovasc Res , vol.49 , pp. 798-807
    • Mihm, M.J.1    Coyle, C.M.2    Schanbacher, B.L.3    Weinstein, D.M.4    Bauer, J.A.5
  • 43
    • 0035838399 scopus 로고    scopus 로고
    • Impaired myofibrillar energetics and oxidative injury during human atrial fibrillation
    • Mihm M.J., Yu F., Carnes C.A., Reiser P.J., McCarthy P.M., VanWagoner D.R. Impaired myofibrillar energetics and oxidative injury during human atrial fibrillation. Circulation 2001, 104:174-180.
    • (2001) Circulation , vol.104 , pp. 174-180
    • Mihm, M.J.1    Yu, F.2    Carnes, C.A.3    Reiser, P.J.4    McCarthy, P.M.5    VanWagoner, D.R.6
  • 44
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: their role in calcium transport and disease
    • Periasamy M., Kalyanasundaram A. SERCA pump isoforms: their role in calcium transport and disease. Muscle Nerve 2007, 35:430-442.
    • (2007) Muscle Nerve , vol.35 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 46
    • 38849115741 scopus 로고    scopus 로고
    • 2+ ATPase pump expression and its relevance to cardiac muscle physiology and pathology
    • 2+ ATPase pump expression and its relevance to cardiac muscle physiology and pathology. Cardiovasc Res 2008, 77:265-273.
    • (2008) Cardiovasc Res , vol.77 , pp. 265-273
    • Periasamy, M.1    Bhupathy, P.2    Babu, G.J.3
  • 47
    • 25444450030 scopus 로고    scopus 로고
    • 3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment
    • Knyushko T.V., Sharov V.S., Williams T.D., Schöneich C., Bigelow D.J. 3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment. Biochemistry 2005, 44:13071-13081.
    • (2005) Biochemistry , vol.44 , pp. 13071-13081
    • Knyushko, T.V.1    Sharov, V.S.2    Williams, T.D.3    Schöneich, C.4    Bigelow, D.J.5
  • 49
    • 62149135339 scopus 로고    scopus 로고
    • Nitrotyrosine-modified SERCA2: a cellular sensor of reactive nitrogen species
    • Bigelow D.J. Nitrotyrosine-modified SERCA2: a cellular sensor of reactive nitrogen species. Pflugers Arch 2009, 457:701-710.
    • (2009) Pflugers Arch , vol.457 , pp. 701-710
    • Bigelow, D.J.1
  • 52
    • 0035071665 scopus 로고    scopus 로고
    • Functional specificity of actin isoforms
    • Khaitlina S.Y. Functional specificity of actin isoforms. Int Rev Cytol 2001, 202:35-98.
    • (2001) Int Rev Cytol , vol.202 , pp. 35-98
    • Khaitlina, S.Y.1
  • 53
    • 0026780174 scopus 로고
    • Vandekerckhove Structure and function of actin
    • Kabsch W., Vandekerckhove Structure and function of actin. J Annu Rev Biophys Biomol Struct 1992, 21:49-76.
    • (1992) J Annu Rev Biophys Biomol Struct , vol.21 , pp. 49-76
    • Kabsch, W.1
  • 56
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein L.R., Graceffa P., Dominguez R. The crystal structure of uncomplexed actin in the ADP state. Science 2001, 293:708-711.
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 58
    • 36248973660 scopus 로고    scopus 로고
    • Peroxynitrite inhibits myofibrillar protein function in an in vitro assay of motility
    • Snook J.H., Li J., Helmke B.P., Guilford W.H. Peroxynitrite inhibits myofibrillar protein function in an in vitro assay of motility. Free Radic Biol Med 2008, 44:14-23.
    • (2008) Free Radic Biol Med , vol.44 , pp. 14-23
    • Snook, J.H.1    Li, J.2    Helmke, B.P.3    Guilford, W.H.4
  • 59
    • 33749513188 scopus 로고    scopus 로고
    • Attenuation by metallothionein of early cardiac cell death via suppression of mitochondrial oxidative stress results in a prevention of diabetic cardiomyopathy
    • Cai L., Wang Y., Zhou G., et al. Attenuation by metallothionein of early cardiac cell death via suppression of mitochondrial oxidative stress results in a prevention of diabetic cardiomyopathy. J Am Coll Cardiol 2006, 48:1688-1697.
    • (2006) J Am Coll Cardiol , vol.48 , pp. 1688-1697
    • Cai, L.1    Wang, Y.2    Zhou, G.3
  • 60
    • 0032525207 scopus 로고    scopus 로고
    • Endothelial cells in physiology and in the pathophysiology of vascular disorders
    • Cines D.B., Pollak E.S., Buck C.A., et al. Endothelial cells in physiology and in the pathophysiology of vascular disorders. Blood 1998, 91:3527-3561.
    • (1998) Blood , vol.91 , pp. 3527-3561
    • Cines, D.B.1    Pollak, E.S.2    Buck, C.A.3
  • 61
    • 0026531078 scopus 로고
    • Prothrombotic and fibrinolytic function of normal and perturbed endothelium
    • Gertler J.P., Abbott W.M. Prothrombotic and fibrinolytic function of normal and perturbed endothelium. J Surg Res 1992, 52:89-95.
    • (1992) J Surg Res , vol.52 , pp. 89-95
    • Gertler, J.P.1    Abbott, W.M.2
  • 62
    • 0030950165 scopus 로고    scopus 로고
    • Anticoagulant properties of the vascular endothelium
    • Bombeli T., Mueller M., Haeberli A. Anticoagulant properties of the vascular endothelium. Thromb Haemost. 1997, 77:408-423.
    • (1997) Thromb Haemost. , vol.77 , pp. 408-423
    • Bombeli, T.1    Mueller, M.2    Haeberli, A.3
  • 67
    • 10744226883 scopus 로고    scopus 로고
    • Pro-thrombotic state induced by post-translational modification of fibrinogen by reactive nitrogen species
    • Vadseth C., Souza J.M., Thomson L., et al. Pro-thrombotic state induced by post-translational modification of fibrinogen by reactive nitrogen species. J Biol Chem 2004, 279:8820-8826.
    • (2004) J Biol Chem , vol.279 , pp. 8820-8826
    • Vadseth, C.1    Souza, J.M.2    Thomson, L.3
  • 68
    • 70249143888 scopus 로고    scopus 로고
    • Inflammation induces fibrinogen nitration in experimental human endotoxemia
    • Heffron S.P., Parastatidis I., Cuchel M., et al. Inflammation induces fibrinogen nitration in experimental human endotoxemia. Free Radic Biol Med 2009, 47:1140-1146.
    • (2009) Free Radic Biol Med , vol.47 , pp. 1140-1146
    • Heffron, S.P.1    Parastatidis, I.2    Cuchel, M.3
  • 69
    • 0035976575 scopus 로고    scopus 로고
    • Prostaglandins and leukotrienes: advances in eicosanoid biology
    • Funk C.D. Prostaglandins and leukotrienes: advances in eicosanoid biology. Science 2001, 294:1871-1875.
    • (2001) Science , vol.294 , pp. 1871-1875
    • Funk, C.D.1
  • 70
    • 0034665857 scopus 로고    scopus 로고
    • The productive conformation of arachidonic acid bound to prostaglandin synthase
    • Malkowski M.G., Ginell S.L., Smith W.L., Garavito R.M. The productive conformation of arachidonic acid bound to prostaglandin synthase. Science 2000, 289:1933-1937.
    • (2000) Science , vol.289 , pp. 1933-1937
    • Malkowski, M.G.1    Ginell, S.L.2    Smith, W.L.3    Garavito, R.M.4
  • 71
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot D., Loll P.J., Garavito R.M. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 1994, 367:243-249.
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 72
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: structural, cellular, and molecular biology
    • Smith W.L., DeWitt D.L., Garavito R.M. Cyclooxygenases: structural, cellular, and molecular biology. Annu Rev Biochem 2000, 69:145-182.
    • (2000) Annu Rev Biochem , vol.69 , pp. 145-182
    • Smith, W.L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 73
    • 0003071173 scopus 로고    scopus 로고
    • Metabolism of unsaturated fatty acids and eicosanoids
    • Stanford: Appleton Lange, CT, R.K. Murray, D.K. Granner, P.A. Mayes, V.W. Rodwell (Eds.)
    • Mayes P.A. Metabolism of unsaturated fatty acids and eicosanoids. Harper's biochemistry 1996, 236-244. Stanford: Appleton Lange, CT. R.K. Murray, D.K. Granner, P.A. Mayes, V.W. Rodwell (Eds.).
    • (1996) Harper's biochemistry , pp. 236-244
    • Mayes, P.A.1
  • 74
    • 0033551847 scopus 로고    scopus 로고
    • Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition
    • Marnett L.J., Rowlinson S.W., Goodwin D.C., Kalgutkar A.S., Lanzo C.A. Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition. J Biol Chem 1999, 274:22903-22906.
    • (1999) J Biol Chem , vol.274 , pp. 22903-22906
    • Marnett, L.J.1    Rowlinson, S.W.2    Goodwin, D.C.3    Kalgutkar, A.S.4    Lanzo, C.A.5
  • 75
    • 0025202767 scopus 로고
    • Tyrosine 385 of prostaglandin endoperoxide synthase is required for cyclooxygenase catalysis
    • Shimokawa T., Kulmacz R.J., DeWitt D.L., Smith W.L. Tyrosine 385 of prostaglandin endoperoxide synthase is required for cyclooxygenase catalysis. J Biol Chem 1990, 265:20073-20076.
    • (1990) J Biol Chem , vol.265 , pp. 20073-20076
    • Shimokawa, T.1    Kulmacz, R.J.2    DeWitt, D.L.3    Smith, W.L.4
  • 76
    • 0034708764 scopus 로고    scopus 로고
    • Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products
    • Thuresson E.D., Lakkides K.M., Smith W.L. Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products. J Biol Chem 2000, 275:8501-8507.
    • (2000) J Biol Chem , vol.275 , pp. 8501-8507
    • Thuresson, E.D.1    Lakkides, K.M.2    Smith, W.L.3
  • 77
    • 0023839666 scopus 로고
    • Higher oxidation states of prostaglandin H synthase. Rapid electronic spectroscopy detected two spectral intermediates during the peroxidase reaction with prostaglandin G2
    • Dietz R., Nastainczyk W., Ruf H.H. Higher oxidation states of prostaglandin H synthase. Rapid electronic spectroscopy detected two spectral intermediates during the peroxidase reaction with prostaglandin G2. Eur J Biochem 1988, 171:321-328.
    • (1988) Eur J Biochem , vol.171 , pp. 321-328
    • Dietz, R.1    Nastainczyk, W.2    Ruf, H.H.3
  • 79
    • 0029894331 scopus 로고    scopus 로고
    • Nitric oxide-mediated cyclooxygenase activation. A key event in the antiplatelet effects of nitrovasodilators
    • Salvemini D., Currie M.G., Mollace V. Nitric oxide-mediated cyclooxygenase activation. A key event in the antiplatelet effects of nitrovasodilators. J Clin Invest 1996, 97:2562-2568.
    • (1996) J Clin Invest , vol.97 , pp. 2562-2568
    • Salvemini, D.1    Currie, M.G.2    Mollace, V.3
  • 81
    • 0030475604 scopus 로고    scopus 로고
    • Peroxynitrite, the coupling product of nitric oxide and superoxide, activates prostaglandin biosynthesis
    • Landino L.M., Crews B.C., Timmons M.D., Morrow J.D., Marnett L.J. Peroxynitrite, the coupling product of nitric oxide and superoxide, activates prostaglandin biosynthesis. Proc Natl Acad Sci USA 1996, 93:15069-15074.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15069-15074
    • Landino, L.M.1    Crews, B.C.2    Timmons, M.D.3    Morrow, J.D.4    Marnett, L.J.5
  • 82
    • 33847649954 scopus 로고    scopus 로고
    • Interactions between nitric oxide and peroxynitrite during prostaglandin endoperoxide H synthase-1 catalysis: a free radical mechanism of inactivation
    • Trostchansky A., O'Donnell V.B., Goodwin D.C., et al. Interactions between nitric oxide and peroxynitrite during prostaglandin endoperoxide H synthase-1 catalysis: a free radical mechanism of inactivation. Free Radic Biol Med 2007, 42:1029-1038.
    • (2007) Free Radic Biol Med , vol.42 , pp. 1029-1038
    • Trostchansky, A.1    O'Donnell, V.B.2    Goodwin, D.C.3
  • 83
    • 30344458452 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase mediates prostaglandin h2 synthase nitration and suppresses eicosanoid production
    • Deeb R.S., Shen H., Gamss C., et al. Inducible nitric oxide synthase mediates prostaglandin h2 synthase nitration and suppresses eicosanoid production. Am J Pathol 2006, 168:349-362.
    • (2006) Am J Pathol , vol.168 , pp. 349-362
    • Deeb, R.S.1    Shen, H.2    Gamss, C.3
  • 86
    • 0038305949 scopus 로고    scopus 로고
    • Specific nitration at tyrosine 430 revealed by high resolution mass spectrometry as basis for redox regulation of bovine prostacyclin synthase
    • Schmidt P., Youhnovski N., Daiber A., et al. Specific nitration at tyrosine 430 revealed by high resolution mass spectrometry as basis for redox regulation of bovine prostacyclin synthase. J Biol Chem 2003, 278:12813-12819.
    • (2003) J Biol Chem , vol.278 , pp. 12813-12819
    • Schmidt, P.1    Youhnovski, N.2    Daiber, A.3
  • 87
    • 0032964853 scopus 로고    scopus 로고
    • Selective nitration of prostacyclin synthase and defective vasorelaxation in atherosclerotic bovine coronary arteries
    • Zou M.H., Leist M., Ullrich V. Selective nitration of prostacyclin synthase and defective vasorelaxation in atherosclerotic bovine coronary arteries. Am J Pathol 1999, 154:1359-1365.
    • (1999) Am J Pathol , vol.154 , pp. 1359-1365
    • Zou, M.H.1    Leist, M.2    Ullrich, V.3
  • 88
    • 0036098197 scopus 로고    scopus 로고
    • High glucose via peroxynitrite causes tyrosine nitration and inactivation of prostacyclin synthase that is associated with thromboxane/prostaglandin H(2) receptor-mediated apoptosis and adhesion molecule expression in cultured human aortic endothelial cells
    • Zou M.H., Shi C., Cohen R.A. High glucose via peroxynitrite causes tyrosine nitration and inactivation of prostacyclin synthase that is associated with thromboxane/prostaglandin H(2) receptor-mediated apoptosis and adhesion molecule expression in cultured human aortic endothelial cells. Diabetes 2002, 5:198-203.
    • (2002) Diabetes , vol.5 , pp. 198-203
    • Zou, M.H.1    Shi, C.2    Cohen, R.A.3
  • 89
    • 0033920731 scopus 로고    scopus 로고
    • Apolipoprotein A-I: structure-function relationships
    • Frank P.G., Marcel Y.L. Apolipoprotein A-I: structure-function relationships. J Lipid Res 2000, 41:853-872.
    • (2000) J Lipid Res , vol.41 , pp. 853-872
    • Frank, P.G.1    Marcel, Y.L.2
  • 90
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani D.W., Rogers D.P., Engler J.A., Brouillette C.G. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc Natl Acad Sci USA 1997, 94:12291-12296.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 91
    • 0025648850 scopus 로고
    • Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins
    • Jonas A., Wald J.H., Toohill K.L., Krul E.S., Kézdy K.E. Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins. J Biol Chem 1990, 265:22123-22129.
    • (1990) J Biol Chem , vol.265 , pp. 22123-22129
    • Jonas, A.1    Wald, J.H.2    Toohill, K.L.3    Krul, E.S.4    Kézdy, K.E.5
  • 93
    • 0035170229 scopus 로고    scopus 로고
    • High density lipoproteins and arteriosclerosis. Role of cholesterol efflux and reverse cholesterol transport
    • Von Eckardstein A., Nofer J.R., Assmann G. High density lipoproteins and arteriosclerosis. Role of cholesterol efflux and reverse cholesterol transport. Arterioscler Thromb Vasc Biol 2001, 21:13-27.
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 13-27
    • Von Eckardstein, A.1    Nofer, J.R.2    Assmann, G.3
  • 94
    • 0032813808 scopus 로고    scopus 로고
    • Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency
    • Brooks-Wilson A., Marcil M., Clee S.M., et al. Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency. Nat Genet 1999, 22:336-345.
    • (1999) Nat Genet , vol.22 , pp. 336-345
    • Brooks-Wilson, A.1    Marcil, M.2    Clee, S.M.3
  • 95
    • 0032813809 scopus 로고    scopus 로고
    • The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease
    • Bodzioch M., Orsó E., Klucken J., et al. The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease. Nat Genet 1999, 22:347-351.
    • (1999) Nat Genet , vol.22 , pp. 347-351
    • Bodzioch, M.1    Orsó, E.2    Klucken, J.3
  • 96
    • 0032813660 scopus 로고    scopus 로고
    • Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1
    • Rust S., Rosier M., Funke H., et al. Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1. Nat Genet 1999, 22:352-355.
    • (1999) Nat Genet , vol.22 , pp. 352-355
    • Rust, S.1    Rosier, M.2    Funke, H.3
  • 97
    • 0032323641 scopus 로고    scopus 로고
    • Evolutionary relationships among ABC transporters
    • Croop J.M. Evolutionary relationships among ABC transporters. Methods Enzymol 1998, 292:101-116.
    • (1998) Methods Enzymol , vol.292 , pp. 101-116
    • Croop, J.M.1
  • 98
    • 0034097561 scopus 로고    scopus 로고
    • Synthesis, characterization, biodegradation, and drug delivery application of biodegradable lactic/glycolic acid polymers: I. Synthesis and characterization
    • Wang N., Wu X.S., Li C., Feng M.F. Synthesis, characterization, biodegradation, and drug delivery application of biodegradable lactic/glycolic acid polymers: I. Synthesis and characterization. J Biomater Sci Polym Ed 2000, 11:301-318.
    • (2000) J Biomater Sci Polym Ed , vol.11 , pp. 301-318
    • Wang, N.1    Wu, X.S.2    Li, C.3    Feng, M.F.4
  • 99
    • 0018953911 scopus 로고
    • Coronary heart disease prevalence and other clinical features in familial high-density lipoprotein deficiency (Tangier disease)
    • Schaefer E.J., Zech L.A., Schwartz D.E., Brewer H.B. Coronary heart disease prevalence and other clinical features in familial high-density lipoprotein deficiency (Tangier disease). Ann Intern Med 1980, 93:261-266.
    • (1980) Ann Intern Med , vol.93 , pp. 261-266
    • Schaefer, E.J.1    Zech, L.A.2    Schwartz, D.E.3    Brewer, H.B.4
  • 100
    • 0027215121 scopus 로고
    • Increased plasma and renal clearance of an exchangeable pool of apolipoprotein A-I in subjects with low levels of high density lipoprotein cholesterol
    • Horowitz B.S., Goldberg I.J., Merab J., Vanni T.M., Ramakrishnan R., Ginsberg H.N. Increased plasma and renal clearance of an exchangeable pool of apolipoprotein A-I in subjects with low levels of high density lipoprotein cholesterol. J Clin Invest 1993, 91:1743-1752.
    • (1993) J Clin Invest , vol.91 , pp. 1743-1752
    • Horowitz, B.S.1    Goldberg, I.J.2    Merab, J.3    Vanni, T.M.4    Ramakrishnan, R.5    Ginsberg, H.N.6
  • 101
    • 0033593350 scopus 로고    scopus 로고
    • Apolipoprotein-mediated plasma membrane microsolubilization. Role of lipid affinity and membrane penetration in the efflux of cellular cholesterol and phospholipid
    • Gillotte K.L., Zaiou M., Lund-Katz S., et al. Apolipoprotein-mediated plasma membrane microsolubilization. Role of lipid affinity and membrane penetration in the efflux of cellular cholesterol and phospholipid. J Biol Chem 1999, 274:2021-2028.
    • (1999) J Biol Chem , vol.274 , pp. 2021-2028
    • Gillotte, K.L.1    Zaiou, M.2    Lund-Katz, S.3
  • 102
    • 0037131376 scopus 로고    scopus 로고
    • The role of apolipoprotein A-I helix 10 in apolipoprotein-mediated cholesterol efflux via the ATP-binding cassette transporter ABCA1
    • Panagotopulos S.E., Witting S.R., Horace E.M., Hui D.Y., Maiorano J.N., Davidson W.S. The role of apolipoprotein A-I helix 10 in apolipoprotein-mediated cholesterol efflux via the ATP-binding cassette transporter ABCA1. J Biol Chem 2002, 277:39477-39484.
    • (2002) J Biol Chem , vol.277 , pp. 39477-39484
    • Panagotopulos, S.E.1    Witting, S.R.2    Horace, E.M.3    Hui, D.Y.4    Maiorano, J.N.5    Davidson, W.S.6
  • 103
    • 0030047675 scopus 로고    scopus 로고
    • Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly
    • Palgunachari M.N., Mishra V.K., Lund-Katz S., et al. Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly. Arterioscler Thromb Vasc Biol 1996, 16:328-338.
    • (1996) Arterioscler Thromb Vasc Biol , vol.16 , pp. 328-338
    • Palgunachari, M.N.1    Mishra, V.K.2    Lund-Katz, S.3
  • 104
    • 0025900794 scopus 로고
    • Lecithin-cholesterol acyltransferase in the metabolism of high-density lipoproteins
    • Jonas A. Lecithin-cholesterol acyltransferase in the metabolism of high-density lipoproteins. Biochim Biophys Acta 1991, 1084:205-220.
    • (1991) Biochim Biophys Acta , vol.1084 , pp. 205-220
    • Jonas, A.1
  • 106
    • 0030610546 scopus 로고    scopus 로고
    • Role of the Arg123-Tyr166 paired helix of apolipoprotein A-I in lecithin:cholesterol acyltransferase activation
    • Dhoest A., Zhao Z., De Geest B., et al. Role of the Arg123-Tyr166 paired helix of apolipoprotein A-I in lecithin:cholesterol acyltransferase activation. J Biol Chem 1997, 272:15967-15972.
    • (1997) J Biol Chem , vol.272 , pp. 15967-15972
    • Dhoest, A.1    Zhao, Z.2    De Geest, B.3
  • 107
    • 0032578569 scopus 로고    scopus 로고
    • Importance of central alpha-helices of human apolipoprotein A-I in the maturation of high-density lipoproteins
    • Frank P.G., N'Guyen D., Franklin V., et al. Importance of central alpha-helices of human apolipoprotein A-I in the maturation of high-density lipoproteins. Biochemistry 1998, 37:13902-13909.
    • (1998) Biochemistry , vol.37 , pp. 13902-13909
    • Frank, P.G.1    N'Guyen, D.2    Franklin, V.3
  • 108
    • 14044250955 scopus 로고    scopus 로고
    • Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport
    • Shao B., Bergt C., Fu X., et al. Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport. J Biol Chem 2005, 280:5983-5993.
    • (2005) J Biol Chem , vol.280 , pp. 5983-5993
    • Shao, B.1    Bergt, C.2    Fu, X.3
  • 109
    • 4344577056 scopus 로고    scopus 로고
    • Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease
    • Zheng L., Nukuna B., Brennan M.L., et al. Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease. J Clin Invest 2004, 114:529-541.
    • (2004) J Clin Invest , vol.114 , pp. 529-541
    • Zheng, L.1    Nukuna, B.2    Brennan, M.L.3
  • 110
    • 0035084272 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in postischemic myocardium
    • Zweier J.L., Fertmann J., Wei G. Nitric oxide and peroxynitrite in postischemic myocardium. Antioxid Redox Signal 2001, 3:11-22.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 11-22
    • Zweier, J.L.1    Fertmann, J.2    Wei, G.3
  • 111
    • 34547950763 scopus 로고    scopus 로고
    • Increased protein nitration burden in the atherosclerotic lesions and plasma of apolipoprotein A-I deficient mice
    • Parastatidis I., Thomson L., Fries D.M., et al. Increased protein nitration burden in the atherosclerotic lesions and plasma of apolipoprotein A-I deficient mice. Circ Res 2007, 101:368-376.
    • (2007) Circ Res , vol.101 , pp. 368-376
    • Parastatidis, I.1    Thomson, L.2    Fries, D.M.3
  • 112
    • 0037414194 scopus 로고    scopus 로고
    • Association of nitrotyrosine levels with cardiovascular disease and modulation by statin therapy
    • Shishehbor M.H., Aviles R.J., Brennan M.L., et al. Association of nitrotyrosine levels with cardiovascular disease and modulation by statin therapy. JAMA 2003, 289:1675-1680.
    • (2003) JAMA , vol.289 , pp. 1675-1680
    • Shishehbor, M.H.1    Aviles, R.J.2    Brennan, M.L.3
  • 113
    • 58849133696 scopus 로고    scopus 로고
    • Molecular structure of low density lipoprotein: current status and future challenges
    • Prassl R., Laggner P. Molecular structure of low density lipoprotein: current status and future challenges. Eur Biophys J 2009, 38:145-158.
    • (2009) Eur Biophys J , vol.38 , pp. 145-158
    • Prassl, R.1    Laggner, P.2
  • 114
    • 0034648768 scopus 로고    scopus 로고
    • Atherosclerosis
    • Lusis A.J. Atherosclerosis. Nature 2000, 407:233-241.
    • (2000) Nature , vol.407 , pp. 233-241
    • Lusis, A.J.1
  • 115
    • 0022915911 scopus 로고
    • The complete cDNA and amino acid sequence of human apolipoprotein B-100
    • Chen S.H., Yang C.Y., Chen P.F., et al. The complete cDNA and amino acid sequence of human apolipoprotein B-100. J Biol Chem 1986, 261:12918-12921.
    • (1986) J Biol Chem , vol.261 , pp. 12918-12921
    • Chen, S.H.1    Yang, C.Y.2    Chen, P.F.3
  • 116
    • 0022995027 scopus 로고
    • Sequence, structure, receptor-binding domains and internal repeats of human apolipoprotein B-100
    • Yang C.Y., Chen S.H., Gianturco S.H., et al. Sequence, structure, receptor-binding domains and internal repeats of human apolipoprotein B-100. Nature 1986, 323:738-742.
    • (1986) Nature , vol.323 , pp. 738-742
    • Yang, C.Y.1    Chen, S.H.2    Gianturco, S.H.3
  • 117
    • 0035655157 scopus 로고    scopus 로고
    • Structure of apolipoprotein B-100 in low density lipoproteins
    • Segrest J.P., Jones M.K., De Loof H., Dashti N. Structure of apolipoprotein B-100 in low density lipoproteins. J Lipid Res 2001, 42:1346-1367.
    • (2001) J Lipid Res , vol.42 , pp. 1346-1367
    • Segrest, J.P.1    Jones, M.K.2    De Loof, H.3    Dashti, N.4
  • 118
    • 11244321987 scopus 로고    scopus 로고
    • LDL phospholipid hydrolysis produces modified electronegative particles with an unfolded apoB-100 protein
    • Asatryan L., Hamilton R.T., Isas J.M., Hwang J., Kayed R., Sevanian A. LDL phospholipid hydrolysis produces modified electronegative particles with an unfolded apoB-100 protein. J Lipid Res 2005, 46:115-122.
    • (2005) J Lipid Res , vol.46 , pp. 115-122
    • Asatryan, L.1    Hamilton, R.T.2    Isas, J.M.3    Hwang, J.4    Kayed, R.5    Sevanian, A.6
  • 119
    • 0027162279 scopus 로고
    • Peroxynitrite modification of low-density lipoprotein leads to recognition by the macrophage scavenger receptor
    • Graham A., Hogg N., Kalyanaraman B., O'Leary V., Darley-Usmar V., Moncada S. Peroxynitrite modification of low-density lipoprotein leads to recognition by the macrophage scavenger receptor. FEBS Lett 1993, 330:181-185.
    • (1993) FEBS Lett , vol.330 , pp. 181-185
    • Graham, A.1    Hogg, N.2    Kalyanaraman, B.3    O'Leary, V.4    Darley-Usmar, V.5    Moncada, S.6
  • 120
    • 53849118426 scopus 로고    scopus 로고
    • LDL protein nitration: implication for LDL protein unfolding
    • Hamilton R.T., Asatryan L., Nilsen J.T., et al. LDL protein nitration: implication for LDL protein unfolding. Arch Biochem Biophys 2008, 479:1-14.
    • (2008) Arch Biochem Biophys , vol.479 , pp. 1-14
    • Hamilton, R.T.1    Asatryan, L.2    Nilsen, J.T.3
  • 121
    • 0031035583 scopus 로고    scopus 로고
    • Reactive nitrogen intermediates promote low density lipoprotein oxidation in human atherosclerotic intima
    • Leeuwenburgh C., Hardy M.M., Hazen S.L., et al. Reactive nitrogen intermediates promote low density lipoprotein oxidation in human atherosclerotic intima. J Biol Chem 1997, 272:1433-1436.
    • (1997) J Biol Chem , vol.272 , pp. 1433-1436
    • Leeuwenburgh, C.1    Hardy, M.M.2    Hazen, S.L.3


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