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Volumn 10, Issue 9, 2011, Pages 4054-4065

Top-down quantitative proteomics identified phosphorylation of cardiac troponin i as a candidate biomarker for chronic heart failure

Author keywords

cardiac troponin I; heart failure; phosphorylation; post translational modification; quantitative proteomics; top down mass spectrometry

Indexed keywords

BIOLOGICAL MARKER; TROPONIN I;

EID: 80052438941     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200258m     Document Type: Article
Times cited : (161)

References (76)
  • 1
    • 39749168495 scopus 로고    scopus 로고
    • Tackling heart failure in the twenty-first century
    • DOI 10.1038/nature06798, PII NATURE06798
    • Mudd, J. O.; Kass, D. A. Tackling heart failure in the twenty-first century Nature 2008, 451 (7181) 919-928 (Pubitemid 351301747)
    • (2008) Nature , vol.451 , Issue.7181 , pp. 919-928
    • Mudd, J.O.1    Kass, D.A.2
  • 2
    • 2542421760 scopus 로고    scopus 로고
    • The global burden of chronic diseases: Overcoming impediments to prevention and control
    • DOI 10.1001/jama.291.21.2616
    • Yach, D.; Hawkes, C.; Gould, C. L.; Hofman, K. J. The global burden of chronic diseases-Overcoming impediments to prevention and control J. Am. Med. Assoc. 2004, 291 (21) 2616-2622 (Pubitemid 38702780)
    • (2004) Journal of the American Medical Association , vol.291 , Issue.21 , pp. 2616-2622
    • Yach, D.1    Hawkes, C.2    Gould, C.L.3    Hofman, K.J.4
  • 3
    • 77953021953 scopus 로고    scopus 로고
    • Early detection of myocardial dysfunction and heart failure
    • de Couto, G.; Ouzounian, M.; Liu, P. P. Early detection of myocardial dysfunction and heart failure Nat. Rev. Cardiol. 2010, 7 (6) 334-344
    • (2010) Nat. Rev. Cardiol. , vol.7 , Issue.6 , pp. 334-344
    • De Couto, G.1    Ouzounian, M.2    Liu, P.P.3
  • 4
    • 77953578271 scopus 로고    scopus 로고
    • Early identification of cardiovascular risk using genomics and proteomics
    • Kullo, I. J.; Cooper, L. T. Early identification of cardiovascular risk using genomics and proteomics Nat. Rev. Cardiol. 2010, 7 (6) 309-317
    • (2010) Nat. Rev. Cardiol. , vol.7 , Issue.6 , pp. 309-317
    • Kullo, I.J.1    Cooper, L.T.2
  • 6
    • 33745004785 scopus 로고    scopus 로고
    • Biomarkers of cardiovascular disease: Molecular basis and practical considerations
    • DOI 10.1161/CIRCULATIONAHA.104.482570, PII 0000301720060516000014
    • Vasan, R. S. Biomarkers of cardiovascular disease-Molecular basis and practical considerations Circulation 2006, 113 (19) 2335-2362 (Pubitemid 43947980)
    • (2006) Circulation , vol.113 , Issue.19 , pp. 2335-2362
    • Vasan, R.S.1
  • 7
    • 33748745369 scopus 로고    scopus 로고
    • Proteomics-based development of biomarkers in cardiovascular disease: Mechanistic, clinical, and therapeutic insights
    • DOI 10.1074/mcp.R600007-MCP200
    • Mayr, M.; Zhang, J.; Greene, A. S.; Gutterman, D.; Perloff, J.; Ping, P. P. Proteomics-based development of biomarkers in cardiovascular disease-Mechanistic, clinical, and therapeutic insights Mol. Cell. Proteomics 2006, 5 (10) 1853-1864 (Pubitemid 44688194)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.10 , pp. 1853-1864
    • Mayr, M.1    Zhang, J.2    Greene, A.S.3    Gutterman, D.4    Perloff, J.5    Ping, P.6
  • 8
    • 41649100689 scopus 로고    scopus 로고
    • Mining the plasma proteome for cancer biomarkers
    • DOI 10.1038/nature06916, PII NATURE06916
    • Hanash, S. M.; Pitteri, S. J.; Faca, V. M. Mining the plasma proteome for cancer biomarkers Nature 2008, 452 (7187) 571-579 (Pubitemid 351483371)
    • (2008) Nature , vol.452 , Issue.7187 , pp. 571-579
    • Hanash, S.M.1    Pitteri, S.J.2    Faca, V.M.3
  • 10
    • 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 (4) 583-594
    • (2010) Am. Heart J. , vol.160 , Issue.4 , pp. 583-594
    • Hochholzer, W.1    Morrow, D.A.2    Giugliano, R.P.3
  • 11
    • 33750619876 scopus 로고    scopus 로고
    • Posttranslational protein modifications: Current implications for cancer detection, prevention, and therapeutics
    • DOI 10.1074/mcp.R600009-MCP200
    • Krueger, K. E.; Srivastava, S. Posttranslational protein modifications-Current implications for cancer detection, prevention, and therapeutics Mol. Cell. Proteomics 2006, 5 (10) 1799-1810 (Pubitemid 44688189)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.10 , pp. 1799-1810
    • Krueger, K.E.1    Srivastava, S.2
  • 12
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • DOI 10.1038/nbt0303-255
    • Mann, M.; Jensen, O. N. Proteomic analysis of post-translational modifications Nat. Biotechnol. 2003, 21 (3) 255-261 (Pubitemid 36314808)
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 13
    • 11144256932 scopus 로고    scopus 로고
    • Developing the next generation of cardiac markers: Disease-induced modifications of troponin I
    • DOI 10.1016/j.pcad.2004.07.001, PII S0033062004000532
    • McDonough, J. L.; Van Eyk, J. E. Developing the next generation of cardiac markers: Disease-induced modifications of Troponin I Prog. Cardiovasc. Dis. 2004, 47 (3) 207-216 (Pubitemid 40037320)
    • (2004) Progress in Cardiovascular Diseases , vol.47 , Issue.3 , pp. 207-216
    • McDonough, J.L.1    Van Eyk, J.E.2
  • 14
  • 19
    • 33749606981 scopus 로고    scopus 로고
    • Extending top-down mass spectrometry to proteins with masses great than 200 kilodaltons
    • DOI 10.1126/science.1128868
    • Han, X. M.; Jin, M.; Breuker, K.; McLafferty, F. W. Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons Science 2006, 314, 109-112 (Pubitemid 44547751)
    • (2006) Science , vol.314 , Issue.5796 , pp. 109-112
    • Han, X.1    Jin, M.2    Breuker, K.3    McLafferty, F.W.4
  • 20
    • 55049123817 scopus 로고    scopus 로고
    • Unraveling molecular complexity of phosphorylated human cardiac troponin i by top down electron capture dissociation/electron transfer dissociation mass spectrometry
    • Zabrouskov, V.; Ge, Y.; Schwartz, J.; Walker, J. W. Unraveling molecular complexity of phosphorylated human cardiac troponin I by top down electron capture dissociation/electron transfer dissociation mass spectrometry Mol. Cell. Proteomics 2008, 7 (10) 1838-1849
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.10 , pp. 1838-1849
    • Zabrouskov, V.1    Ge, Y.2    Schwartz, J.3    Walker, J.W.4
  • 21
    • 69249106065 scopus 로고    scopus 로고
    • In vivo phosphorylation site mapping in mouse cardiac troponin i by high resolution top-down electron capture dissociation mass spectrometry: Ser22/23 are the only sites basally phosphorylated
    • Ayaz-Guner, S.; Zhang, J.; Li, L.; Walker, J. W.; Ge, Y. In vivo phosphorylation site mapping in mouse cardiac troponin I by high resolution top-down electron capture dissociation mass spectrometry: Ser22/23 are the only sites basally phosphorylated Biochemistry 2009, 48 (34) 8161-8170
    • (2009) Biochemistry , vol.48 , Issue.34 , pp. 8161-8170
    • Ayaz-Guner, S.1    Zhang, J.2    Li, L.3    Walker, J.W.4    Ge, Y.5
  • 22
    • 69149100342 scopus 로고    scopus 로고
    • Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state
    • Ge, Y.; Rybakova, I. N.; Xu, Q. G.; Moss, R. L. Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state Proc. Natl. Acad. Sci. U.S.A. 2009, 106 (31) 12658-12663
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , Issue.31 , pp. 12658-12663
    • Ge, Y.1    Rybakova, I.N.2    Xu, Q.G.3    Moss, R.L.4
  • 23
    • 80051552668 scopus 로고    scopus 로고
    • Top-down high-resolution electron capture dissociation mass spectrometry for comprehensive characterization of post-translational modifications in rhesus monkey cardiac troponin i
    • doi:10.1016/j.ijms.2010.09.007
    • Xu, F.; Xu, Q.; Dong, X.; Guy, M.; Guner, H.; Hacker, T. A.; Ge, Y. Top-down high-resolution electron capture dissociation mass spectrometry for comprehensive characterization of post-translational modifications in rhesus monkey cardiac troponin I Int. J. Mass Spectrom. 2010, doi:10.1016/j.ijms.2010. 09.007
    • (2010) Int. J. Mass Spectrom.
    • Xu, F.1    Xu, Q.2    Dong, X.3    Guy, M.4    Guner, H.5    Hacker, T.A.6    Ge, Y.7
  • 24
    • 77952878403 scopus 로고    scopus 로고
    • Deciphering modifications in swine cardiac troponin i by top-down high-resolution tandem mass spectrometry
    • Zhang, J.; Dong, X.; Hacker, T. A.; Ge, Y. Deciphering modifications in swine cardiac troponin I by top-down high-resolution tandem mass spectrometry J. Am. Soc. Mass Spectrom. 2010, 21) 940-948
    • (2010) J. Am. Soc. Mass Spectrom. , Issue.21 , pp. 940-948
    • Zhang, J.1    Dong, X.2    Hacker, T.A.3    Ge, Y.4
  • 25
    • 66349099312 scopus 로고    scopus 로고
    • Delineating Anopheles gambiae coactivator associated arginine methyltransferase 1 automethylation using top-down high resolution tandem mass spectrometry
    • Kuhn, P.; Xu, Q. G.; Cline, E.; Zhang, D.; Ge, Y.; Xu, W. Delineating Anopheles gambiae coactivator associated arginine methyltransferase 1 automethylation using top-down high resolution tandem mass spectrometry Protein Sci. 2009, 18 (6) 1272-1280
    • (2009) Protein Sci. , vol.18 , Issue.6 , pp. 1272-1280
    • Kuhn, P.1    Xu, Q.G.2    Cline, E.3    Zhang, D.4    Ge, Y.5    Xu, W.6
  • 28
    • 33749615256 scopus 로고    scopus 로고
    • Mass spectrometry: Bottom-up or top-down?
    • DOI 10.1126/science.1133987
    • Chait, B. T. Mass Spectrometry: Bottom-up or Top-Down? Science 2006, 314, 65-66 (Pubitemid 44547738)
    • (2006) Science , vol.314 , Issue.5796 , pp. 65-66
    • Chait, B.T.1
  • 29
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • DOI 10.1038/nmeth1097, PII NMETH1097
    • Siuti, N.; Kelleher, N. L. Decoding protein modifications using top-down mass spectrometry Nat. Methods 2007, 4, 817-821 (Pubitemid 350055578)
    • (2007) Nature Methods , vol.4 , Issue.10 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 31
    • 0035173029 scopus 로고    scopus 로고
    • Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry
    • Shi, S. D. H.; Hemling, M. E.; Carr, S. A.; Horn, D. M.; Lindh, I.; McLafferty, F. W. Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry Anal. Chem. 2001, 73 (1) 19-22
    • (2001) Anal. Chem. , vol.73 , Issue.1 , pp. 19-22
    • Shi, S.D.H.1    Hemling, M.E.2    Carr, S.A.3    Horn, D.M.4    Lindh, I.5    McLafferty, F.W.6
  • 32
    • 14744299376 scopus 로고    scopus 로고
    • The role of electron capture dissociation in biomolecular analysis
    • DOI 10.1002/mas.20014
    • Cooper, H. J.; Hakansson, K.; Marshall, A. G. The role of electron capture dissociation in biomolecular analysis Mass Spectrom. Rev. 2005, 24 (2) 201-222 (Pubitemid 40328974)
    • (2005) Mass Spectrometry Reviews , vol.24 , Issue.2 , pp. 201-222
    • Cooper, H.J.1    Hakansson, K.2    Marshall, A.G.3
  • 33
    • 33745700686 scopus 로고    scopus 로고
    • Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry: Human histone H4
    • Pesavento, J. J.; Mizzen, C. A.; Kelleher, N. L. Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry: Human histone H4 Anal. Chem. 2006, 78 (13) 4271-4280
    • (2006) Anal. Chem. , vol.78 , Issue.13 , pp. 4271-4280
    • Pesavento, J.J.1    Mizzen, C.A.2    Kelleher, N.L.3
  • 34
    • 31044442964 scopus 로고    scopus 로고
    • Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry
    • DOI 10.1021/bi0517584
    • Zabrouskov, V.; Han, X. M.; Welker, E.; Zhai, H. L.; Lin, C.; van Wijk, K. J.; Scheraga, H. A.; McLafferty, F. W. Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry Biochemistry 2006, 45 (3) 987-992 (Pubitemid 43122262)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 987-992
    • Zabrouskov, V.1    Han, X.2    Welker, E.3    Zhai, H.4    Lin, C.5    Van Wijk, K.J.6    Scheraga, H.A.7    McLafferty, F.W.8
  • 35
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: The long and uncertain path to clinical utility
    • DOI 10.1038/nbt1235, PII NBT1235
    • 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 (8) 971-983 (Pubitemid 44215392)
    • (2006) Nature Biotechnology , vol.24 , Issue.8 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 36
    • 65249147185 scopus 로고    scopus 로고
    • Tissue proteomics and metabolomics: An excellent start and a promising future
    • Veenstra, T. D.; Zhou, M. Tissue proteomics and metabolomics: An excellent start and a promising future J. Proteome Res. 2009, 8 (4) 1617-1617
    • (2009) J. Proteome Res. , vol.8 , Issue.4 , pp. 1617-1617
    • Veenstra, T.D.1    Zhou, M.2
  • 37
    • 77957372670 scopus 로고    scopus 로고
    • Galectin-3 Is a candidate biomarker for amyotrophic lateral sclerosis: Discovery by a proteomics approach
    • Zhou, J. Y.; Afjehi-Sadat, L.; Asress, S.; Duong, D. M.; Cudkowicz, M.; Glass, J. D.; Peng, J. Galectin-3 Is a candidate biomarker for amyotrophic lateral sclerosis: Discovery by a proteomics approach J. Proteome Res. 2010, 9 (10) 5133-5141
    • (2010) J. Proteome Res. , vol.9 , Issue.10 , pp. 5133-5141
    • Zhou, J.Y.1    Afjehi-Sadat, L.2    Asress, S.3    Duong, D.M.4    Cudkowicz, M.5    Glass, J.D.6    Peng, J.7
  • 38
    • 17844396912 scopus 로고    scopus 로고
    • Antibody-based proteomics for human tissue profiling
    • DOI 10.1074/mcp.R500009-MCP200
    • Uhlen, M.; Ponten, F. Antibody-based proteomics for human tissue profiling Mol. Cell. Proteomics 2005, 4 (4) 384-393 (Pubitemid 40590558)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.4 , pp. 384-393
    • Uhlen, M.1    Ponten, F.2
  • 39
    • 33749455064 scopus 로고    scopus 로고
    • Capillary separations enabling tissue proteomics-based biomarker discovery
    • DOI 10.1002/elps.200600094
    • Guo, T.; Lee, C. S.; Wang, W. J.; DeVoe, D. L.; Balgley, B. M. Capillary separations enabling tissue proteomics-based biomarker discovery Electrophoresis 2006, 27 (18) 3523-3532 (Pubitemid 44515590)
    • (2006) Electrophoresis , vol.27 , Issue.18 , pp. 3523-3532
    • Guo, T.1    Lee, C.S.2    Wang, W.3    DeVoe, D.L.4    Balgley, B.M.5
  • 40
    • 77951757994 scopus 로고    scopus 로고
    • Multiplex assays for biomarker research and clinical application: Translational science coming of age
    • Fu, Q.; Schoenhoff, F. S.; Savage, W. J.; Zhang, P. B.; Van Eyk, J. E. Multiplex assays for biomarker research and clinical application: Translational science coming of age Proteomics Clin. Appl. 2010, 4 (3) 271-284
    • (2010) Proteomics Clin. Appl. , vol.4 , Issue.3 , pp. 271-284
    • Fu, Q.1    Schoenhoff, F.S.2    Savage, W.J.3    Zhang, P.B.4    Van Eyk, J.E.5
  • 41
    • 27844583398 scopus 로고    scopus 로고
    • Troponin: The biomarker of choice for the detection of cardiac injury
    • DOI 10.1503/cmaj/051291
    • Babuin, L.; Jaffe, A. S. Troponin: the biomarker of choice for the detection of cardiac injury Can. Med. Assoc. J. 2005, 173 (10) 1191-1202 (Pubitemid 41637819)
    • (2005) Canadian Medical Association Journal , vol.173 , Issue.10 , pp. 1191-1202
    • Babuin, L.1    Jaffe, A.S.2
  • 43
    • 40849096222 scopus 로고    scopus 로고
    • The unique functions of cardiac troponin i in the control of cardiac muscle contraction and relaxation
    • Solaro, R. J.; Rosevear, P.; Kobayashi, T. The unique functions of cardiac troponin I in the control of cardiac muscle contraction and relaxation Biochem. Biophys. Res. Commun. 2008, 369 (1) 82-87
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , Issue.1 , pp. 82-87
    • Solaro, R.J.1    Rosevear, P.2    Kobayashi, T.3
  • 45
    • 0034641649 scopus 로고    scopus 로고
    • Extensive troponin i and T modification detected in serum from patients with acute myocardial infarction
    • Labugger, R.; Organ, L.; Collier, C.; Atar, D.; Van Eyk, J. E. Extensive troponin I and T modification detected in serum from patients with acute myocardial infarction Circulation 2000, 102 (11) 1221-1226
    • (2000) Circulation , vol.102 , Issue.11 , pp. 1221-1226
    • Labugger, R.1    Organ, L.2    Collier, C.3    Atar, D.4    Van Eyk, J.E.5
  • 48
    • 33845778948 scopus 로고    scopus 로고
    • Troponin phosphorylation and regulatory function in human heart muscle: Dephosphorylation of Ser23/24 on troponin I could account for the contractile defect in end-stage heart failure
    • DOI 10.1016/j.yjmcc.2006.08.017, PII S0022282806007760
    • Messer, A. E.; Jacques, A. M.; Marston, S. B. Troponin phosphorylation and regulatory function in human heart muscle: Dephosphorylation of Ser23/24 on troponin I could account for the contractile defect in end-stage heart failure J. Mol. Cell. Cardiol. 2007, 42 (1) 247-259 (Pubitemid 44970468)
    • (2007) Journal of Molecular and Cellular Cardiology , vol.42 , Issue.1 , pp. 247-259
    • Messer, A.E.1    Jacques, A.M.2    Marston, S.B.3
  • 49
    • 24744463882 scopus 로고    scopus 로고
    • Mutations in human cardiac troponin I that are associated with restrictive cardiomyopathy affect basal ATPase activity and the calcium sensitivity of force development
    • DOI 10.1074/jbc.M500287200
    • Gomes, A. V.; Liang, J. S.; Potter, J. D. Mutations in human cardiac Troponin I that are associated with restrictive cardiomyopathy affect basal ATPase activity and the calcium sensitivity of force development J. Biol. Chem. 2005, 280 (35) 30909-30915 (Pubitemid 41291822)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 30909-30915
    • Gomes, A.V.1    Liang, J.2    Potter, J.D.3
  • 52
    • 14844344027 scopus 로고    scopus 로고
    • Regulation of cardiac contractile function by troponin I phosphorylation
    • DOI 10.1016/j.cardiores.2004.12.022
    • Layland, J.; Solaro, R. J.; Shah, A. M. Regulation of cardiac contractile function by troponin I phosphorylation Cardiovasc. Res. 2005, 66 (1) 12-21 (Pubitemid 40357865)
    • (2005) Cardiovascular Research , vol.66 , Issue.1 , pp. 12-21
    • Layland, J.1    Solaro, R.J.2    Shah, A.M.3
  • 53
    • 55249123610 scopus 로고    scopus 로고
    • Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins
    • Solaro, R. J. Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins J. Biol. Chem. 2008, 283 (40) 26829-26833
    • (2008) J. Biol. Chem. , vol.283 , Issue.40 , pp. 26829-26833
    • Solaro, R.J.1
  • 54
    • 0038581576 scopus 로고    scopus 로고
    • Myocyte adrenoceptor signaling pathways
    • DOI 10.1126/science.1079206
    • Xiang, Y.; Kobilka, B. K. Myocyte adrenoceptor signaling pathways Science 2003, 300 (5625) 1530-1532 (Pubitemid 36682874)
    • (2003) Science , vol.300 , Issue.5625 , pp. 1530-1532
    • Xiang, Y.1    Kobilka, B.K.2
  • 58
    • 0032498523 scopus 로고    scopus 로고
    • Breakdown and release of myofilament proteins during ischemia and ischemia/reperfusion in rat hearts identification of degradation products and effects on the pCa-force relation
    • Van Eyk, J. E.; Powers, F.; Law, W.; Larue, C.; Hedges, R. S.; Solaro, R. J. Breakdown and release of myofilament proteins during ischemia and ischemia/reperfusion in rat hearts-Identification of degradation products and effects on the pCa-force relation Circ. Res. 1998, 82 (2) 261-271 (Pubitemid 28080109)
    • (1998) Circulation Research , vol.82 , Issue.2 , pp. 261-271
    • Van Eyk, J.E.1    Powers, F.2    Law, W.3    Larue, C.4    Hodges, R.S.5    Solaro, R.J.6
  • 59
    • 0033593593 scopus 로고    scopus 로고
    • Troponin I degradation and covalent complex formation accompanies myocardial ischemia/reperfusion injury
    • McDonough, J. L.; Arrell, D. K.; Van Eyk, J. E. Troponin I degradation and covalent complex formation accompanies myocardial ischemia/reperfusion injury Circ. Res. 1999, 84 (1) 9-20 (Pubitemid 29074876)
    • (1999) Circulation Research , vol.84 , Issue.1 , pp. 9-20
    • McDonough, J.L.1    Arrell, D.K.2    Van Eyk, J.E.3
  • 61
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall, D. E.; Demartino, G. N. Calcium-activated neutral protease (calpain) system: structure, function, and regulation Physiol. Rev. 1991, 71 (3) 813-847
    • (1991) Physiol. Rev. , vol.71 , Issue.3 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 62
    • 0036549817 scopus 로고    scopus 로고
    • Troponin i proteolysis and myocardial stunning: Now you see it - Now you don't
    • Canty, J. M.; Lee, T. C. Troponin I proteolysis and myocardial stunning: Now you see it-Now you don't J. Mol. Cell. Cardiol. 2002, 34 (4) 375-377
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , Issue.4 , pp. 375-377
    • Canty, J.M.1    Lee, T.C.2
  • 63
    • 0346120211 scopus 로고    scopus 로고
    • Modulation of thin filament activation by breakdown or isoform switching of thin filament proteins: Physiological and pathological implications
    • DOI 10.1161/01.RES.0000105088.06696.17
    • Marston, S. B.; Redwood, C. S. Modulation of thin filament activation by breakdown or isoform switching of thin filament proteins-Physiological and pathological implications Circ. Res. 2003, 93 (12) 1170-1178 (Pubitemid 37543057)
    • (2003) Circulation Research , vol.93 , Issue.12 , pp. 1170-1178
    • Marston, S.B.1    Redwood, C.S.2
  • 64
    • 3142600673 scopus 로고    scopus 로고
    • Stunned peri-infarct canine myocardium is characterized by degradation of troponin T, not troponin I
    • DOI 10.1016/j.cardiores.2004.04.006, PII S0008636304001658
    • Colantonio, D. A.; Van Eyk, J. E.; Przyklenk, K. Stunned peri-infarct canine myocardium is characterized by degradation of troponin T, not troponin I Cardiovasc. Res. 2004, 63 (2) 217-225 (Pubitemid 38900836)
    • (2004) Cardiovascular Research , vol.63 , Issue.2 , pp. 217-225
    • Colantonio, D.A.1    Van Eyk, J.E.2    Przyklenk, K.3
  • 65
    • 0038359388 scopus 로고    scopus 로고
    • Strategy for analysis of cardiac troponins in biological samples with a combination of affinity chromatography and mass spectrometry
    • DOI 10.1373/49.6.873
    • Labugger, R.; Simpson, J. A.; Quick, M.; Brown, H. A.; Collier, C. E.; Neverova, I.; Van Eyk, J. E. Strategy for analysis of cardiac troponins in biological samples with a combination of affinity chromatography and mass spectrometry Clin. Chem. 2003, 49 (6) 873-879 (Pubitemid 36623465)
    • (2003) Clinical Chemistry , vol.49 , Issue.6 , pp. 873-879
    • Labugger, R.1    Simpson, J.A.2    Quick, M.3    Brown, H.A.4    Collier, C.E.5    Neverova, I.6    Van Eyk, J.E.7
  • 66
    • 77951529849 scopus 로고    scopus 로고
    • Why does troponin i have so many phosphorylation sites? Fact and fancy
    • Solaro, R. J.; van der Velden, J. Why does troponin I have so many phosphorylation sites? Fact and fancy J. Mol. Cell. Cardiol. 2010, 48 (5) 810-816
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , Issue.5 , pp. 810-816
    • Solaro, R.J.1    Van Der Velden, J.2
  • 67
    • 0242637601 scopus 로고    scopus 로고
    • What Is the Role of β-Adrenergic Signaling in Heart Failure?
    • DOI 10.1161/01.RES.0000102042.83024.CA
    • Lohse, M. J.; Engelhardt, S.; Eschenhagen, T. What is the role of beta-adrenergic signaling in heart failure? Circ. Res. 2003, 93 (10) 896-906 (Pubitemid 37433227)
    • (2003) Circulation Research , vol.93 , Issue.10 , pp. 896-906
    • Lohse, M.J.1    Engelhardt, S.2    Eschenhagen, T.3
  • 68
    • 33947527882 scopus 로고    scopus 로고
    • Cardiac GPCRs: GPCR signaling in healthy and failing hearts
    • DOI 10.1016/j.bbamem.2007.02.010, PII S0005273607000582
    • Salazar, N. C.; Chen, J.; Rockman, H. A. Cardiac GPCRs: GPCR signaling in healthy and failing hearts Biochim. Biophys. Acta 2007, 1768 (4) 1006-1018 (Pubitemid 46463942)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.4 , pp. 1006-1018
    • Salazar, N.C.1    Chen, J.2    Rockman, H.A.3
  • 70
    • 33750728385 scopus 로고    scopus 로고
    • Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications
    • DOI 10.1074/mcp.M600162-MCP200
    • Qian, W. J.; Jacobs, J. M.; Liu, T.; Camp, D. G.; Smith, R. D. Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications Mol. Cell. Proteomics 2006, 5 (10) 1727-1744 (Pubitemid 44696109)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.10 , pp. 1727-1744
    • Qian, W.-J.1    Jacobs, J.M.2    Liu, T.3    Camp II, D.G.4    Smith, R.D.5
  • 71
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome - History, character, and diagnostic prospects
    • Anderson, N. L.; Anderson, N. G. The human plasma proteome-History, character, and diagnostic prospects Mol. Cell. Proteomics 2002, 1 (11) 845-867
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.11 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 73
    • 0032895673 scopus 로고    scopus 로고
    • Affinity chromatography: A review of clinical applications
    • Hage, D. S. Affinity chromatography: A review of clinical applications Clin. Chem. 1999, 45 (5) 593-615 (Pubitemid 29220320)
    • (1999) Clinical Chemistry , vol.45 , Issue.5 , pp. 593-615
    • Hage, D.S.1
  • 74
    • 77952876849 scopus 로고    scopus 로고
    • Quantitative top-down proteomics of SILAC labeled human embryonic stem cells
    • Collier, T. S.; Sarkar, P.; Rao, B.; Muddiman, D. C. Quantitative top-down proteomics of SILAC labeled human embryonic stem cells J. Am. Soc. Mass Spectrom. 2010, 21 (6) 879-889
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , Issue.6 , pp. 879-889
    • Collier, T.S.1    Sarkar, P.2    Rao, B.3    Muddiman, D.C.4
  • 76
    • 78649406605 scopus 로고    scopus 로고
    • Achievements and perspectives of top-down proteomics
    • Armirotti, A.; Damonte, G. Achievements and perspectives of top-down proteomics Proteomics 2010, 10 (20) 3566-3576
    • (2010) Proteomics , vol.10 , Issue.20 , pp. 3566-3576
    • Armirotti, A.1    Damonte, G.2


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