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Volumn 8, Issue 12, 2013, Pages

Effects of troponin T cardiomyopathy mutations on the calcium sensitivity of the regulated thin filament and the actomyosin cross-bridge kinetics of human β-cardiac myosin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; BETA CARDIAC MYOSIN; CARDIAC MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; TROPONIN T; UNCLASSIFIED DRUG;

EID: 84893160910     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0083403     Document Type: Article
Times cited : (44)

References (72)
  • 1
    • 80052565758 scopus 로고    scopus 로고
    • The cell biology of disease: Cellular mechanisms of cardiomyopathy
    • Harvey PA, Leinwand LA (2011) The cell biology of disease: cellular mechanisms of cardiomyopathy. J Cell Biol 194: 355-365.
    • (2011) J Cell Biol , vol.194 , pp. 355-365
    • Harvey, P.A.1    Leinwand, L.A.2
  • 2
    • 0029083650 scopus 로고
    • Prevalence of hypertrophic cardiomyopathy in a general population of young adults. Echocardiographic analysis of 4111 subjects in the CARDIA Study. Coronary Artery Risk Development in (Young) Adults
    • Maron BJ, Gardin JM, Flack JM, Gidding SS, Kurosaki TT, et al. (1995) Prevalence of hypertrophic cardiomyopathy in a general population of young adults. Echocardiographic analysis of 4111 subjects in the CARDIA Study. Coronary Artery Risk Development in (Young) Adults. Circulation 92: 785-789.
    • (1995) Circulation , vol.92 , pp. 785-789
    • Maron, B.J.1    Gardin, J.M.2    Flack, J.M.3    Gidding, S.S.4    Kurosaki, T.T.5
  • 3
    • 49149125520 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: Etiology, diagnosis, and treatment
    • Ramaraj R (2008) Hypertrophic cardiomyopathy: etiology, diagnosis, and treatment. Cardiol Rev 16: 172-180.
    • (2008) Cardiol Rev , vol.16 , pp. 172-180
    • Ramaraj, R.1
  • 4
    • 78649631986 scopus 로고    scopus 로고
    • Clinical and genetic issues in dilated cardiomyopathy: A review for genetics professionals
    • Hershberger RE, Morales A, Siegfried JD (2010) Clinical and genetic issues in dilated cardiomyopathy: a review for genetics professionals. Genet Med 12: 655-667.
    • (2010) Genet Med , vol.12 , pp. 655-667
    • Hershberger, R.E.1    Morales, A.2    Siegfried, J.D.3
  • 6
    • 84864230812 scopus 로고    scopus 로고
    • Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motor
    • Moore JR, Leinwand L, Warshaw DM (2012) Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motor. Circulation Research 111: 375-385.
    • (2012) Circulation Research , vol.111 , pp. 375-385
    • Moore, J.R.1    Leinwand, L.2    Warshaw, D.M.3
  • 7
    • 77951620368 scopus 로고    scopus 로고
    • Kinetics of cardiac sarcomeric processes and rate-limiting steps in contraction and relaxation
    • Stehle R, Iorga B (2010) Kinetics of cardiac sarcomeric processes and rate-limiting steps in contraction and relaxation. J Mol Cell Cardiol 48: 843-850.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 843-850
    • Stehle, R.1    Iorga, B.2
  • 8
    • 0036793597 scopus 로고    scopus 로고
    • It takes "heart" to win: What makes the heart powerful?
    • McDonald KS, Herron TJ (2002) It takes "heart" to win: what makes the heart powerful? News Physiol Sci 17: 185-190.
    • (2002) News Physiol Sci , vol.17 , pp. 185-190
    • McDonald, K.S.1    Herron, T.J.2
  • 9
    • 77952158022 scopus 로고    scopus 로고
    • The genetics of dilated cardiomyopathy
    • Dellefave L, McNally EM (2010) The genetics of dilated cardiomyopathy. Curr Opin Cardiol 25: 198-204.
    • (2010) Curr Opin Cardiol , vol.25 , pp. 198-204
    • Dellefave, L.1    McNally, E.M.2
  • 12
    • 15544390385 scopus 로고    scopus 로고
    • Calcium, thin filaments, and the integrative biology of cardiac contractility
    • DOI 10.1146/annurev.physiol.67.040403.114025
    • Kobayashi T, Solaro RJ (2005) Calcium, thin filaments, and the integrative biology of cardiac contractility. Annu Rev Physiol 67: 39-67. (Pubitemid 40404485)
    • (2005) Annual Review of Physiology , vol.67 , pp. 39-67
    • Kobayashi, T.1    Solaro, R.J.2
  • 13
    • 26844510875 scopus 로고    scopus 로고
    • Regulation of muscle contraction by tropomyosin and troponin: How structure illuminates function
    • DOI 10.1016/S0065-3233(04)71004-9, PII S0065323304710049
    • Brown JH, Cohen C (2005) Regulation of muscle contraction by tropomyosin and troponin: how structure illuminates function. Adv Protein Chem 71: 121-159. (Pubitemid 41446928)
    • (2005) Advances in Protein Chemistry , vol.71 , pp. 121-159
    • Brown, J.H.1    Cohen, C.2
  • 14
    • 0035830841 scopus 로고    scopus 로고
    • Abnormal contractile function in transgenic mice expressing a familial hypertrophic cardiomyopathy-linked troponin T (I79N) mutation
    • Miller T, Szczesna D, Housmans PR, Zhao J, de Freitas F, et al. (2001) Abnormal contractile function in transgenic mice expressing a familial hypertrophic cardiomyopathy-linked troponin T (I79N) mutation. J Biol Chem 276: 3743-3755.
    • (2001) J Biol Chem , vol.276 , pp. 3743-3755
    • Miller, T.1    Szczesna, D.2    Housmans, P.R.3    Zhao, J.4    De Freitas, F.5
  • 16
    • 79953055654 scopus 로고    scopus 로고
    • Thin filament mutations: Developing an integrative approach to a complex disorder
    • Tardiff JC (2011) Thin filament mutations: developing an integrative approach to a complex disorder. Circ Res 108: 765-782.
    • (2011) Circ Res , vol.108 , pp. 765-782
    • Tardiff, J.C.1
  • 17
    • 77951621530 scopus 로고    scopus 로고
    • Mutations in Troponin that cause HCM, DCM AND RCM: What can we learn about thin filament function?
    • Willott RH, Gomes AV, Chang AN, Parvatiyar MS, Pinto JR, et al. (2010) Mutations in Troponin that cause HCM, DCM AND RCM: what can we learn about thin filament function? J Mol Cell Cardiol 48: 882-892.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 882-892
    • Willott, R.H.1    Gomes, A.V.2    Chang, A.N.3    Parvatiyar, M.S.4    Pinto, J.R.5
  • 18
    • 60849123177 scopus 로고    scopus 로고
    • Tropomyosin: Function follows structure
    • Hitchcock-DeGregori SE (2008) Tropomyosin: function follows structure. Adv Exp Med Biol 644: 60-72.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 60-72
    • Hitchcock-DeGregori, S.E.1
  • 19
    • 2642583071 scopus 로고    scopus 로고
    • Myosin crossbridge activation of cardiac thin filaments: Implications for myocardial function in health and disease
    • DOI 10.1161/01.RES.0000127125.61647.4F
    • Moss RL, Razumova M, Fitzsimons DP (2004) Myosin crossbridge activation of cardiac thin filaments: implications for myocardial function in health and disease. Circ Res 94: 1290-1300. (Pubitemid 38724474)
    • (2004) Circulation Research , vol.94 , Issue.10 , pp. 1290-1300
    • Moss, R.L.1    Razumova, M.2    Fitzsimons, D.P.3
  • 20
    • 0034614419 scopus 로고    scopus 로고
    • Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy
    • DOI 10.1074/jbc.275.1.624
    • Szczesna D, Zhang R, Zhao J, Jones M, Guzman G, et al. (2000) Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy. J Biol Chem 275: 624-630. (Pubitemid 30039027)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.1 , pp. 624-630
    • Szczesna, D.1    Zhang, R.2    Zhao, J.3    Jones, M.4    Guzman, G.5    Potter, J.D.6
  • 21
    • 0142180165 scopus 로고    scopus 로고
    • Different Functional Properties of Troponin T Mutants that Cause Dilated Cardiomyopathy
    • DOI 10.1074/jbc.M302148200
    • Venkatraman G, Harada K, Gomes AV, Kerrick WG, Potter JD (2003) Different functional properties of troponin T mutants that cause dilated cardiomyopathy. J Biol Chem 278: 41670-41676. (Pubitemid 37310424)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 41670-41676
    • Venkatraman, G.1    Harada, K.2    Gomes, A.V.3    Kerrick, W.G.L.4    Potter, J.D.5
  • 22
    • 23344435710 scopus 로고    scopus 로고
    • Characterization of troponin T dilated cardiomyopathy mutations in the fetal troponin isoform
    • DOI 10.1074/jbc.M409337200
    • Venkatraman G, Gomes AV, Kerrick WG, Potter JD (2005) Characterization of troponin T dilated cardiomyopathy mutations in the fetal troponin isoform. J Biol Chem 280: 17584-17592. (Pubitemid 41388992)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17584-17592
    • Venkatraman, G.1    Gomes, A.V.2    Kerrick, W.G.L.3    Potter, J.D.4
  • 23
    • 0033214054 scopus 로고    scopus 로고
    • Functional consequences of troponin T mutations found in hypertrophic cardiomyopathy
    • Tobacman LS, Lin D, Butters C, Landis C, Back N, et al. (1999) Functional consequences of troponin T mutations found in hypertrophic cardiomyopathy. J Biol Chem 274: 28363-28370.
    • (1999) J Biol Chem , vol.274 , pp. 28363-28370
    • Tobacman, L.S.1    Lin, D.2    Butters, C.3    Landis, C.4    Back, N.5
  • 24
    • 0029993918 scopus 로고    scopus 로고
    • Altered cardiac troponin T in vitro function in the presence of a mutation implicated in familial hypertrophic cardiomyopathy
    • Lin D, Bobkova A, Homsher E, Tobacman LS (1996) Altered cardiac troponin T in vitro function in the presence of a mutation implicated in familial hypertrophic cardiomyopathy. J Clin Invest 97: 2842-2848. (Pubitemid 26197097)
    • (1996) Journal of Clinical Investigation , vol.97 , Issue.12 , pp. 2842-2848
    • Lin, D.1    Bobkova, A.2    Homsher, E.3    Tobacman, L.S.4
  • 25
    • 84883704578 scopus 로고    scopus 로고
    • Cardiac Muscle Activation Blunted by a Mutation to the Regulatory Component, Troponin T
    • Kobayashi M, Debold EP, Turner MA, Kobayashi T (2013) Cardiac Muscle Activation Blunted by a Mutation to the Regulatory Component, Troponin T. J Biol Chem.
    • (2013) J Biol Chem
    • Kobayashi, M.1    Debold, E.P.2    Turner, M.A.3    Kobayashi, T.4
  • 26
    • 1242284573 scopus 로고    scopus 로고
    • Chaperone-mediated folding and assembly of myosin in striated muscle
    • DOI 10.1242/jcs.00899
    • Srikakulam R, Winkelmann DA (2004) Chaperone-mediated folding and assembly of myosin in striated muscle. J Cell Sci 117: 641-652. (Pubitemid 38240205)
    • (2004) Journal of Cell Science , vol.117 , Issue.4 , pp. 641-652
    • Srikakulam, R.1    Winkelmann, D.A.2
  • 27
    • 84870701407 scopus 로고    scopus 로고
    • Erratum to: Identification of functional differences between recombinant human alpha and beta cardiac myosin motors
    • Deacon JC, Bloemink MJ, Rezavandi H, Geeves MA, Leinwand LA (2012) Erratum to: Identification of functional differences between recombinant human alpha and beta cardiac myosin motors. Cell Mol Life Sci 69: 4239-4255.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 4239-4255
    • Deacon, J.C.1    Bloemink, M.J.2    Rezavandi, H.3    Geeves, M.A.4    Leinwand, L.A.5
  • 29
    • 0028178083 scopus 로고
    • Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: A disease of the sarcomere
    • Thierfelder L, Watkins H, MacRae C, Lamas R, McKenna W, et al. (1994) Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere. Cell 77: 701-712.
    • (1994) Cell , vol.77 , pp. 701-712
    • Thierfelder, L.1    Watkins, H.2    MacRae, C.3    Lamas, R.4    McKenna, W.5
  • 30
    • 0028902929 scopus 로고
    • Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy
    • Watkins H, McKenna WJ, Thierfelder L, Suk HJ, Anan R, et al. (1995) Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy. N Engl J Med 332: 1058-1064.
    • (1995) N Engl J Med , vol.332 , pp. 1058-1064
    • Watkins, H.1    McKenna, W.J.2    Thierfelder, L.3    Suk, H.J.4    Anan, R.5
  • 32
    • 0031873371 scopus 로고    scopus 로고
    • Ca2+-sensitizing effects of the mutations at Ile-79 and Arg-92 of troponin T in hypertrophic cardiomyopathy
    • Morimoto S, Yanaga F, Minakami R, Ohtsuki I (1998) Ca2+-sensitizing effects of the mutations at Ile-79 and Arg-92 of troponin T in hypertrophic cardiomyopathy. Am J Physiol 275: C200-207.
    • (1998) Am J Physiol , vol.275
    • Morimoto, S.1    Yanaga, F.2    Minakami, R.3    Ohtsuki, I.4
  • 33
    • 0033605422 scopus 로고    scopus 로고
    • 2+ sensitization and potentiation of the maximum level of myofibrillar ATPase activity caused by mutations of troponin T found in familial hypertrophic cardiomyopathy
    • DOI 10.1074/jbc.274.13.8806
    • Yanaga F, Morimoto S, Ohtsuki I (1999) Ca2+ sensitization and potentiation of the maximum level of myofibrillar ATPase activity caused by mutations of troponin T found in familial hypertrophic cardiomyopathy. J Biol Chem 274: 8806-8812. (Pubitemid 29164679)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8806-8812
    • Yanaga, F.1    Morimoto, S.2    Ohtsuki, I.3
  • 34
    • 84860156650 scopus 로고    scopus 로고
    • Patient-specific induced pluripotent stem cells as a model for familial dilated cardiomyopathy
    • Sun N, Yazawa M, Liu J, Han L, Sanchez-Freire V, et al. (2012) Patient-specific induced pluripotent stem cells as a model for familial dilated cardiomyopathy. Sci Transl Med 4: 130ra147.
    • (2012) Sci Transl Med , vol.4
    • Sun, N.1    Yazawa, M.2    Liu, J.3    Han, L.4    Sanchez-Freire, V.5
  • 36
    • 34247642743 scopus 로고    scopus 로고
    • Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C
    • DOI 10.1529/biophysj.106.095406
    • Davis JP, Norman C, Kobayashi T, Solaro RJ, Swartz DR, et al. (2007) Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C. Biophys J 92: 3195-3206. (Pubitemid 46684579)
    • (2007) Biophysical Journal , vol.92 , Issue.9 , pp. 3195-3206
    • Davis, J.P.1    Norman, C.2    Kobayashi, T.3    Solaro, R.J.4    Swartz, D.R.5    Tikunova, S.B.6
  • 37
    • 84881104951 scopus 로고    scopus 로고
    • Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human beta-cardiac myosin motor function
    • Sommese RF, Sung J, Nag S, Sutton S, Deacon JC, et al. (2013) Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human beta-cardiac myosin motor function. Proc Natl Acad Sci U S A 110: 12607-12612.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 12607-12612
    • Sommese, R.F.1    Sung, J.2    Nag, S.3    Sutton, S.4    Deacon, J.C.5
  • 38
    • 72449135662 scopus 로고    scopus 로고
    • A peptide tag system for facile purification and single-molecule immobilization
    • Huang J, Nagy SS, Koide A, Rock RS, Koide S (2009) A peptide tag system for facile purification and single-molecule immobilization. Biochemistry 48: 11834-11836.
    • (2009) Biochemistry , vol.48 , pp. 11834-11836
    • Huang, J.1    Nagy, S.S.2    Koide, A.3    Rock, R.S.4    Koide, S.5
  • 39
    • 0026496306 scopus 로고
    • Two genetically expressed troponin T fragments representing alpha and beta isoforms exhibit functional differences
    • Pan BS, Potter JD (1992) Two genetically expressed troponin T fragments representing alpha and beta isoforms exhibit functional differences. J Biol Chem 267: 23052-23056.
    • (1992) J Biol Chem , vol.267 , pp. 23052-23056
    • Pan, B.S.1    Potter, J.D.2
  • 40
    • 0026444089 scopus 로고
    • Isolation, expression, and mutation of a rabbit skeletal muscle cDNA clone for troponin I. The role of the NH2 terminus of fast skeletal muscle troponin I in its biological activity
    • Sheng Z, Pan BS, Miller TE, Potter JD (1992) Isolation, expression, and mutation of a rabbit skeletal muscle cDNA clone for troponin I. The role of the NH2 terminus of fast skeletal muscle troponin I in its biological activity. J Biol Chem 267: 25407-25413.
    • (1992) J Biol Chem , vol.267 , pp. 25407-25413
    • Sheng, Z.1    Pan, B.S.2    Miller, T.E.3    Potter, J.D.4
  • 41
    • 0029664399 scopus 로고    scopus 로고
    • The role of the four Ca2+ binding sites of troponin C in the regulation of skeletal muscle contraction
    • Szczesna D, Guzman G, Miller T, Zhao J, Farokhi K, et al. (1996) The role of the four Ca2+ binding sites of troponin C in the regulation of skeletal muscle contraction. J Biol Chem 271: 8381-8386.
    • (1996) J Biol Chem , vol.271 , pp. 8381-8386
    • Szczesna, D.1    Guzman, G.2    Miller, T.3    Zhao, J.4    Farokhi, K.5
  • 42
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee JD, Spudich JA (1982) Purification of muscle actin. Methods Enzymol 85 Pt B: 164-181.
    • (1982) Methods Enzymol , vol.85 , Issue.PART B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 43
    • 0020023850 scopus 로고
    • Preparation and identification of alpha- and beta-tropomyosins
    • Smillie LB (1982) Preparation and identification of alpha- and beta-tropomyosins. Methods Enzymol 85 Pt B: 234-241.
    • (1982) Methods Enzymol , vol.85 , Issue.PART B , pp. 234-241
    • Smillie, L.B.1
  • 44
    • 61849174756 scopus 로고    scopus 로고
    • Kinetic and equilibrium analysis of the myosin ATPase
    • De La Cruz EM, Ostap EM (2009) Kinetic and equilibrium analysis of the myosin ATPase. Methods Enzymol 455: 157-192.
    • (2009) Methods Enzymol , vol.455 , pp. 157-192
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 45
    • 27944491141 scopus 로고    scopus 로고
    • Expanding the range of free calcium regulation in biological solutions
    • DOI 10.1016/j.ab.2005.09.025, PII S0003269705006895
    • Dweck D, Reyes-Alfonso A, Jr., Potter JD (2005) Expanding the range of free calcium regulation in biological solutions. Anal Biochem 347: 303-315. (Pubitemid 41681818)
    • (2005) Analytical Biochemistry , vol.347 , Issue.2 , pp. 303-315
    • Dweck, D.1    Reyes-Alfonso Jr., A.2    Potter, J.D.3
  • 46
    • 0028953460 scopus 로고
    • In vitro motility analysis of actin-tropomyosin regulation by troponin and calcium. The thin filament is switched as a single cooperative unit
    • Fraser ID, Marston SB (1995) In vitro motility analysis of actin-tropomyosin regulation by troponin and calcium. The thin filament is switched as a single cooperative unit. J Biol Chem 270: 7836-7841.
    • (1995) J Biol Chem , vol.270 , pp. 7836-7841
    • Fraser, I.D.1    Marston, S.B.2
  • 47
    • 0029924132 scopus 로고    scopus 로고
    • Calcium regulation of thin filament movement in an in vitro motility assay
    • Homsher E, Kim B, Bobkova A, Tobacman LS (1996) Calcium regulation of thin filament movement in an in vitro motility assay. Biophys J 70: 1881-1892. (Pubitemid 26103961)
    • (1996) Biophysical Journal , vol.70 , Issue.4 , pp. 1881-1892
    • Homsher, E.1    Kim, B.2    Bobkova, A.3    Tobacman, L.S.4
  • 48
    • 79960315009 scopus 로고    scopus 로고
    • Tracking single particles and elongated filaments with nanometer precision
    • Ruhnow F, Zwicker D, Diez S (2011) Tracking single particles and elongated filaments with nanometer precision. Biophys J 100: 2820-2828.
    • (2011) Biophys J , vol.100 , pp. 2820-2828
    • Ruhnow, F.1    Zwicker, D.2    Diez, S.3
  • 49
    • 84861880853 scopus 로고    scopus 로고
    • Disease-related cardiac troponins alter thin filament Ca2+ association and dissociation rates
    • Liu B, Tikunova SB, Kline KP, Siddiqui JK, Davis JP (2012) Disease-related cardiac troponins alter thin filament Ca2+ association and dissociation rates. PLoS One 7: e38259.
    • (2012) PLoS One , vol.7
    • Liu, B.1    Tikunova, S.B.2    Kline, K.P.3    Siddiqui, J.K.4    Davis, J.P.5
  • 50
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama T, Mihashi K (1981) Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem 114: 33-38. (Pubitemid 11101489)
    • (1981) European Journal of Biochemistry , vol.114 , Issue.1 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 51
    • 0022356527 scopus 로고
    • Fluorescence studies of the conformation of pyrene-labeled tropomyosin: Effects of F-actin and myosin subfragment 1
    • DOI 10.1021/bi00344a050
    • Ishii Y, Lehrer SS (1985) Fluorescence studies of the conformation of pyrene-labeled tropomyosin: effects of F-actin and myosin subfragment 1. Biochemistry 24: 6631-6638. (Pubitemid 16207143)
    • (1985) Biochemistry , vol.24 , Issue.23 , pp. 6631-6638
    • Ishii, Y.1    Lehrer, S.S.2
  • 52
    • 0019321960 scopus 로고
    • The excimer fluorescence of pyrene-labeled tropomyosin. A probe of conformational dynamics
    • Graceffa P, Lehrer SS (1980) The excimer fluorescence of pyrene-labeled tropomyosin. A probe of conformational dynamics. J Biol Chem 255: 11296-11300.
    • (1980) J Biol Chem , vol.255 , pp. 11296-11300
    • Graceffa, P.1    Lehrer, S.S.2
  • 53
    • 0017112799 scopus 로고
    • N-(1-pyrene)maleimide: A fluorescent crosslinking reagent
    • Wu CW, Yarbrough LR (1976) N-(1-pyrene)maleimide: a fluorescent crosslinking reagent. Biochemistry 15: 2863-2868.
    • (1976) Biochemistry , vol.15 , pp. 2863-2868
    • Wu, C.W.1    Yarbrough, L.R.2
  • 54
    • 78650832959 scopus 로고    scopus 로고
    • Targeted aminoterminal acetylation of recombinant proteins in E. coli
    • Johnson M, Coulton AT, Geeves MA, Mulvihill DP (2010) Targeted aminoterminal acetylation of recombinant proteins in E. coli. PLoS One 5: e15801.
    • (2010) PLoS One , vol.5
    • Johnson, M.1    Coulton, A.T.2    Geeves, M.A.3    Mulvihill, D.P.4
  • 55
    • 0028177556 scopus 로고
    • Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group
    • Monteiro PB, Lataro RC, Ferro JA, Reinach Fde C (1994) Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group. J Biol Chem 269: 10461-10466.
    • (1994) J Biol Chem , vol.269 , pp. 10461-10466
    • Monteiro, P.B.1    Lataro, R.C.2    Ferro, J.A.3    Reinach Fde, C.4
  • 56
    • 0025895385 scopus 로고
    • Two-site attachment of troponin to pyrene-labeled tropomyosin
    • Ishii Y, Lehrer SS (1991) Two-site attachment of troponin to pyrene-labeled tropomyosin. J Biol Chem 266: 6894-6903. (Pubitemid 21906308)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.11 , pp. 6894-6903
    • Ishii, Y.1    Lehrer, S.S.2
  • 58
    • 0037174918 scopus 로고    scopus 로고
    • Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy
    • DOI 10.1074/jbc.M203446200
    • Robinson P, Mirza M, Knott A, Abdulrazzak H, Willott R, et al. (2002) Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy. J Biol Chem 277: 40710-40716. (Pubitemid 35215653)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40710-40716
    • Robinson, P.1    Mirza, M.2    Knott, A.3    Abdulrazzak, H.4    Willott, R.5    Marston, S.6    Hugh, W.C.R.7
  • 59
    • 0024991350 scopus 로고
    • Myosin step size - Estimation from slow sliding movement of actin over low-densities of heavy-meromyosin
    • Uyeda TQP, Kron SJ, Spudich JA (1990) Myosin step size - estimation from slow sliding movement of actin over low-densities of heavy-meromyosin. Journal of Molecular Biology 214: 699-710.
    • (1990) Journal of Molecular Biology , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 60
    • 75949123848 scopus 로고    scopus 로고
    • Insights into human beta-cardiac myosin function from single molecule and single cell studies
    • Sivaramakrishnan S, Ashley E, Leinwand L, Spudich JA (2009) Insights into human beta-cardiac myosin function from single molecule and single cell studies. J Cardiovasc Transl Res 2: 426-440.
    • (2009) J Cardiovasc Transl Res , vol.2 , pp. 426-440
    • Sivaramakrishnan, S.1    Ashley, E.2    Leinwand, L.3    Spudich, J.A.4
  • 62
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M (2000) Regulation of contraction in striated muscle. Physiol Rev 80: 853-924. (Pubitemid 30164950)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 63
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium binding to cardiac troponin C
    • Hofmann PA, Fuchs F (1987) Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am J Physiol 253: C541-546.
    • (1987) Am J Physiol , vol.253
    • Hofmann, P.A.1    Fuchs, F.2
  • 64
    • 78649886008 scopus 로고    scopus 로고
    • Effects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments
    • Sich NM, O'Donnell TJ, Coulter SA, John OA, Carter MS, et al. (2010) Effects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments. J Biol Chem 285: 39150-39159.
    • (2010) J Biol Chem , vol.285 , pp. 39150-39159
    • Sich, N.M.1    O'Donnell, T.J.2    Coulter, S.A.3    John, O.A.4    Carter, M.S.5
  • 65
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DF, Geeves MA (1993) Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 65: 693-701. (Pubitemid 23263882)
    • (1993) Biophysical Journal , vol.65 , Issue.2 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 66
    • 78651397869 scopus 로고    scopus 로고
    • Strong cross-bridges potentiate the Ca(2+) affinity changes produced by hypertrophic cardiomyopathy cardiac troponin C mutants in myofilaments: A fast kinetic approach
    • Pinto JR, Reynaldo DP, Parvatiyar MS, Dweck D, Liang J, et al. (2011) Strong cross-bridges potentiate the Ca(2+) affinity changes produced by hypertrophic cardiomyopathy cardiac troponin C mutants in myofilaments: a fast kinetic approach. J Biol Chem 286: 1005-1013.
    • (2011) J Biol Chem , vol.286 , pp. 1005-1013
    • Pinto, J.R.1    Reynaldo, D.P.2    Parvatiyar, M.S.3    Dweck, D.4    Liang, J.5
  • 67
    • 77952519774 scopus 로고    scopus 로고
    • Sarcomere control mechanisms and the dynamics of the cardiac cycle
    • Solaro RJ (2010) Sarcomere control mechanisms and the dynamics of the cardiac cycle. J Biomed Biotechnol 2010: 105648.
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 105648
    • Solaro, R.J.1
  • 68
    • 0037173015 scopus 로고    scopus 로고
    • Assessment of diastolic function with Doppler tissue imaging to predict genotype in preclinical hypertrophic cardiomyopathy
    • DOI 10.1161/01.CIR.0000019070.70491.6D
    • Ho CY, Sweitzer NK, McDonough B, Maron BJ, Casey SA, et al. (2002) Assessment of diastolic function with Doppler tissue imaging to predict genotype in preclinical hypertrophic cardiomyopathy. Circulation 105: 2992-2997. (Pubitemid 34693832)
    • (2002) Circulation , vol.105 , Issue.25 , pp. 2992-2997
    • Ho, C.Y.1    Sweitzer, N.K.2    McDonough, B.3    Maron, B.J.4    Casey, S.A.5    Seidman, J.G.6    Seidman, C.E.7    Solomon, S.D.8
  • 69
    • 77955684941 scopus 로고    scopus 로고
    • Spectrum and clinical significance of systolic function and myocardial fibrosis assessed by cardiovascular magnetic resonance in hypertrophic cardiomyopathy
    • Olivotto I, Maron BJ, Appelbaum E, Harrigan CJ, Salton C, et al. (2010) Spectrum and clinical significance of systolic function and myocardial fibrosis assessed by cardiovascular magnetic resonance in hypertrophic cardiomyopathy. Am J Cardiol 106: 261-267.
    • (2010) Am J Cardiol , vol.106 , pp. 261-267
    • Olivotto, I.1    Maron, B.J.2    Appelbaum, E.3    Harrigan, C.J.4    Salton, C.5
  • 70
    • 0002985780 scopus 로고
    • The cardiomyopathies and myocarditis: Toxic, chemical and physical damage to the heart
    • Philadelphia: W.B. Saunders
    • Wynne J BE (1992) The cardiomyopathies and myocarditis: toxic, chemical and physical damage to the heart. Braunwald's Heart Disease: A Textbook of Cardiovascular Medicine Philadelphia: W.B. Saunders. pp. 1394-1450.
    • (1992) Braunwald's Heart Disease: A Textbook of Cardiovascular Medicine , pp. 1394-1450
    • Wynne, J.B.E.1
  • 71
    • 84868626402 scopus 로고    scopus 로고
    • Subtle abnormalities in contractile function are an early manifestation of sarcomere mutations in dilated cardiomyopathy
    • Lakdawala NK, Thune JJ, Colan SD, Cirino AL, Farrohi F, et al. (2012) Subtle abnormalities in contractile function are an early manifestation of sarcomere mutations in dilated cardiomyopathy. Circ Cardiovasc Genet 5: 503-510.
    • (2012) Circ Cardiovasc Genet , vol.5 , pp. 503-510
    • Lakdawala, N.K.1    Thune, J.J.2    Colan, S.D.3    Cirino, A.L.4    Farrohi, F.5
  • 72
    • 80051983795 scopus 로고    scopus 로고
    • A model of calcium activation of the cardiac thin filament
    • Manning EP, Tardiff JC, Schwartz SD (2011) A model of calcium activation of the cardiac thin filament. Biochemistry 50: 7405-7413.
    • (2011) Biochemistry , vol.50 , pp. 7405-7413
    • Manning, E.P.1    Tardiff, J.C.2    Schwartz, S.D.3


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