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Volumn 97, Issue 3, 2013, Pages 500-508

Myofibrillar Ca2+ sensitivity is uncoupled from troponin i phosphorylation in hypertrophic obstructive cardiomyopathy due to abnormal troponin T

Author keywords

Cardiac muscle contractility; Hypertrophic cardiomyopathy; Phosphorylation; Troponin I; Troponin T

Indexed keywords

CALCIUM; CYCLIC AMP DEPENDENT PROTEIN KINASE; SERINE; TROPONIN I; TROPONIN T;

EID: 84874257414     PISSN: 00086363     EISSN: 17553245     Source Type: Journal    
DOI: 10.1093/cvr/cvs322     Document Type: Article
Times cited : (31)

References (49)
  • 2
    • 0037630018 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy
    • Richard P, Charron P, Carrier L, Ledeuil C, Cheav T, Pichereau C et al. Hypertrophic cardiomyopathy distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy. Circulation 2003;107:2227-2232.
    • (2003) Circulation , vol.107 , pp. 2227-2232
    • Richard, P.1    Charron, P.2    Carrier, L.3    Ledeuil, C.4    Cheav, T.5    Pichereau, C.6
  • 3
    • 0041663609 scopus 로고    scopus 로고
    • Prevalence and spectrum of thin filament mutations in an outpatient referral population with hypertrophic cardiomyopathy
    • Van Driest SL, Ellsworth EG, Ommen SR, Tajik AJ, Gersh BJ, Ackerman MJ. Prevalence and spectrum of thin filament mutations in an outpatient referral population with hypertrophic cardiomyopathy. Circulation 2003;108:445-451.
    • (2003) Circulation , vol.108 , pp. 445-451
    • Van Driest, S.L.1    Ellsworth, E.G.2    Ommen, S.R.3    Tajik, A.J.4    Gersh, B.J.5    Ackerman, M.J.6
  • 4
    • 4043081356 scopus 로고    scopus 로고
    • Comprehensive analysis of the beta-myosin heavy chain gene in 389 unrelated patients with hypertrophic cardiomyopathy
    • Van Driest SL, Jaeger MA, Ommen SR, Will ML, Gersh BJ, Tajik AJ et al. Comprehensive analysis of the beta-myosin heavy chain gene in 389 unrelated patients with hypertrophic cardiomyopathy. J Am Coll Cardiol 2004;44:602-610.
    • (2004) J Am Coll Cardiol , vol.44 , pp. 602-610
    • Van Driest, S.L.1    Jaeger, M.A.2    Ommen, S.R.3    Will, M.L.4    Gersh, B.J.5    Tajik, A.J.6
  • 6
    • 79960564849 scopus 로고    scopus 로고
    • How do mutations in contractile proteins cause the primary familial cardiomyopathies?
    • Marston SB. How do mutations in contractile proteins cause the primary familial cardiomyopathies? J Cardiovasc Transl Res 2011;4:245-255.
    • (2011) J Cardiovasc Transl Res , vol.4 , pp. 245-255
    • Marston, S.B.1
  • 7
    • 77957233852 scopus 로고    scopus 로고
    • Normal passive viscoelasticity but abnormal myofibrillar force generation in human hypertrophic cardiomyopathy
    • Hoskins AC, Jacques A, Bardswell SC, McKenna WJ, Tsang V, Remedios C et al. Normal passive viscoelasticity but abnormal myofibrillar force generation in human hypertrophic cardiomyopathy. J Mol Cell Cardiol 2010;49:737-745.
    • (2010) J Mol Cell Cardiol , vol.49 , pp. 737-745
    • Hoskins, A.C.1    Jacques, A.2    Bardswell, S.C.3    McKenna, W.J.4    Tsang, V.5    Remedios, C.6
  • 8
    • 48749118698 scopus 로고    scopus 로고
    • The molecular phenotype of human cardiac myosin associated with hypertrophic obstructive cardiomyopathy
    • Jacques A, Briceno N, Messer A, Gallon C, Jalizadeh S, Garcia E et al. The molecular phenotype of human cardiac myosin associated with hypertrophic obstructive cardiomyopathy. Cardiovasc Res 2008;79:481-491.
    • (2008) Cardiovasc Res , vol.79 , pp. 481-491
    • Jacques, A.1    Briceno, N.2    Messer, A.3    Gallon, C.4    Jalizadeh, S.5    Garcia, E.6
  • 9
    • 62449192447 scopus 로고    scopus 로고
    • From genotype to phenotype: A longitudinal study of a patient with hypertrophic cardiomyopathy due to a mutation in the MYBPC3 gene
    • Jacques A, Hoskins A, Kentish J, Marston SB. From genotype to phenotype: a longitudinal study of a patient with hypertrophic cardiomyopathy due to a mutation in the MYBPC3 gene. J Musc Res Cell Motil 2009;29:239-246.
    • (2009) J Musc Res Cell Motil , vol.29 , pp. 239-246
    • Jacques, A.1    Hoskins, A.2    Kentish, J.3    Marston, S.B.4
  • 10
    • 0034494362 scopus 로고    scopus 로고
    • R403Q and L908V mutant beta-cardiac myosin from patients with familial hypertrophic cardiomyopathy exhibit enhanced mechanical performance at the single molecule level
    • Palmiter KA, Tyska MJ, Haeberle JR, Alpert NR, Fananapazir L, Warshaw DM. R403Q and L908V mutant beta-cardiac myosin from patients with familial hypertrophic cardiomyopathy exhibit enhanced mechanical performance at the single molecule level. J Musc Res Cell Motil 2000;21:609-620.
    • (2000) J Musc Res Cell Motil , vol.21 , pp. 609-620
    • Palmiter, K.A.1    Tyska, M.J.2    Haeberle, J.R.3    Alpert, N.R.4    Fananapazir, L.5    Warshaw, D.M.6
  • 11
    • 64949138383 scopus 로고    scopus 로고
    • Cardiac myosin-binding protein c mutations and hypertrophic cardiomyopathy Haploinsufficiency, deranged phosphorylation, and cardiomyocyte dysfunction
    • Van Dijk S, Dooijes D, Dos Remedios C, Michels M, Lamers J, Winegrad S et al. Cardiac myosin-binding protein c mutations and hypertrophic cardiomyopathy. Haploinsufficiency, deranged phosphorylation, and cardiomyocyte dysfunction. Circulation 2009;119:1473-1483.
    • (2009) Circulation , vol.119 , pp. 1473-1483
    • Van Dijk, S.1    Dooijes, D.2    Dos Remedios, C.3    Michels, M.4    Lamers, J.5    Winegrad, S.6
  • 12
    • 79960977475 scopus 로고    scopus 로고
    • Molecular mechanism of the Glu99lys mutation in cardiac actin (ACTC gene) that causes apical hypertrophy in man and mouse
    • Song W, Dyer E, Stuckey D, Copeland O, Leung M, Bayliss C et al. Molecular mechanism of the Glu99lys mutation in cardiac actin (ACTC gene) that causes apical hypertrophy in man and mouse. J Biol Chem 2011;286:27582-27593.
    • (2011) J Biol Chem , vol.286 , pp. 27582-27593
    • Song, W.1    Dyer, E.2    Stuckey, D.3    Copeland, O.4    Leung, M.5    Bayliss, C.6
  • 13
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: From mutation identification to mechanistic paradigms
    • Seidman JG, Seidman C. The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms. Cell 2001;104:557-567.
    • (2001) Cell , vol.104 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 14
    • 0033214976 scopus 로고    scopus 로고
    • Properties of mutant contractile proteins that cause hypertrophic cardiomyopathy
    • Redwood CS, Moolman-Smook JC, Watkins H. Properties of mutant contractile proteins that cause hypertrophic cardiomyopathy. Cardiovasc Res 1999;44:20-36.
    • (1999) Cardiovasc Res , vol.44 , pp. 20-36
    • Redwood, C.S.1    Moolman-Smook, J.C.2    Watkins, H.3
  • 15
    • 79953055654 scopus 로고    scopus 로고
    • Thin filament mutations: Developing an integrative approach to a complex disorder
    • Tardiff JC. Thin filament mutations: developing an integrative approach to a complex disorder. Circ Res 2011;108:765-782.
    • (2011) Circ Res , vol.108 , pp. 765-782
    • Tardiff, J.C.1
  • 16
    • 0016682585 scopus 로고
    • Operative treatment in hypertrophic subaortic stenosis.Techniques, and the results of pre and postoperative assessments in 83 patients
    • Morrow AG, Reitz BA, Epstein SE, Henry WL, Conkle DM, Itscoitz SB et al. Operative treatment in hypertrophic subaortic stenosis. Techniques, and the results of pre and postoperative assessments in 83 patients. Circulation 1975;52:88-102.
    • (1975) Circulation , vol.52 , pp. 88-102
    • Morrow, A.G.1    Reitz, B.A.2    Epstein, S.E.3    Henry, W.L.4    Conkle, D.M.5    Itscoitz, S.B.6
  • 17
    • 0036800523 scopus 로고    scopus 로고
    • Septal myotomy-myectomy and transcoronary septal alcohol ablation in hypertrophic obstructive cardiomyopathy A comparison of clinical, haemodynamic and exercise outcomes
    • Firoozi S, Elliott PM, Sharma S, Murday A, Brecker SJ, Hamid MS et al. Septal myotomy-myectomy and transcoronary septal alcohol ablation in hypertrophic obstructive cardiomyopathy. A comparison of clinical, haemodynamic and exercise outcomes. Eur Heart J 2002;23:1617-1624.
    • (2002) Eur Heart J , vol.23 , pp. 1617-1624
    • Firoozi, S.1    Elliott, P.M.2    Sharma, S.3    Murday, A.4    Brecker, S.J.5    Hamid, M.S.6
  • 18
    • 33748080756 scopus 로고    scopus 로고
    • Left ventricular outflow tract obstruction and sudden death risk in patients with hypertrophic cardiomyopathy
    • Elliott PM, Gimeno JR, Tome MT, Shah J, Ward D, Thaman R et al. Left ventricular outflow tract obstruction and sudden death risk in patients with hypertrophic cardiomyopathy. Eur Heart J 2006;27:1933-1941.
    • (2006) Eur Heart J , vol.27 , pp. 1933-1941
    • Elliott, P.M.1    Gimeno, J.R.2    Tome, M.T.3    Shah, J.4    Ward, D.5    Thaman, R.6
  • 19
    • 69249236883 scopus 로고    scopus 로고
    • Evidence from human myectomy samples that MYBPC3 mutations cause hypertrophic cardiomyopathy through haploinsufficiency
    • Marston S, Copeland O, Jacques A, Livesey K, Tsang V, McKenna WJ et al. Evidence from human myectomy samples that MYBPC3 mutations cause hypertrophic cardiomyopathy through haploinsufficiency. Circ Res 2009;105:219-222.
    • (2009) Circ Res , vol.105 , pp. 219-222
    • Marston, S.1    Copeland, O.2    Jacques, A.3    Livesey, K.4    Tsang, V.5    McKenna, W.J.6
  • 20
    • 48849095991 scopus 로고    scopus 로고
    • Myosin binding protein C phosphorylation in normal, hypertrophic and failing human heart muscle
    • Jacques A, Copeland O, Messer A, Gallon C, King C, McKenna W et al. Myosin binding protein C phosphorylation in normal, hypertrophic and failing human heart muscle. J Mol Cell Cardiol 2008;45:209-216.
    • (2008) J Mol Cell Cardiol , vol.45 , pp. 209-216
    • Jacques, A.1    Copeland, O.2    Messer, A.3    Gallon, C.4    King, C.5    McKenna, W.6
  • 21
    • 77957555832 scopus 로고    scopus 로고
    • Investigation of changes in skeletal muscle alpha-actin expression in normal and pathological human and mouse hearts
    • Copeland O, Nowak K, Laing N, Ravenscroft G, Messer AE, Bayliss CR et al. Investigation of changes in skeletal muscle alpha-actin expression in normal and pathological human and mouse hearts. J Musc Res Cell Motil 2010;31:207-214.
    • (2010) J Musc Res Cell Motil , vol.31 , pp. 207-214
    • Copeland, O.1    Nowak, K.2    Laing, N.3    Ravenscroft, G.4    Messer, A.E.5    Bayliss, C.R.6
  • 23
    • 77951074751 scopus 로고    scopus 로고
    • The use of phosphate-affinity SDS-PAGE to measure the troponin i phosphorylation site distribution in human heart muscle
    • Messer A, Gallon C, McKenna W, Elliott P, Dos Remedios C, Marston S. The use of phosphate-affinity SDS-PAGE to measure the troponin I phosphorylation site distribution in human heart muscle. Proteomics Clin Appl 2009;3:1371-1382.
    • (2009) Proteomics Clin Appl , vol.3 , pp. 1371-1382
    • Messer, A.1    Gallon, C.2    McKenna, W.3    Elliott, P.4    Dos Remedios, C.5    Marston, S.6
  • 24
    • 70350448975 scopus 로고    scopus 로고
    • Functional analysis of a unique troponin C mutation, Gly159Asp that causes familial dilated cardiomyopathy, studied in explanted heart muscle
    • Dyer E, Jacques A, Hoskins A, Ward D, Gallon C, Messer A et al. Functional analysis of a unique troponin C mutation, Gly159Asp that causes familial dilated cardiomyopathy, studied in explanted heart muscle. Circ Heart Fail 2009;2:456-464.
    • (2009) Circ Heart Fail , vol.2 , pp. 456-464
    • Dyer, E.1    Jacques, A.2    Hoskins, A.3    Ward, D.4    Gallon, C.5    Messer, A.6
  • 25
    • 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
    • Messer AE, Jacques AM, Marston SB. 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; 42:247-259.
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 247-259
    • Messer, A.E.1    Jacques, A.M.2    Marston, S.B.3
  • 26
    • 62449288850 scopus 로고    scopus 로고
    • Evidence for reduced troponin i phosphorylation and altered troponin function in patients with hypertrophic obstructive cardiomyopathy
    • Jacques A, Messer A, Tsang V, McKenna W, Marston S. Evidence for reduced troponin I phosphorylation and altered troponin function in patients with hypertrophic obstructive cardiomyopathy. Heart 2006;92(Supp II):A29.
    • (2006) Heart , vol.92 , Issue.SUPPL. II
    • Jacques, A.1    Messer, A.2    Tsang, V.3    McKenna, W.4    Marston, S.5
  • 28
    • 0028953460 scopus 로고
    • In Vitro motility analysis of actin-tropomyosin regulation by troponin and Ca2+: The thin filament is switched as a single cooperative unit
    • Fraser IDC, Marston SB. In Vitro motility analysis of actin-tropomyosin regulation by troponin and Ca2+: the thin filament is switched as a single cooperative unit. J Biol Chem 1995;270:7836-7841.
    • (1995) J Biol Chem , vol.270 , pp. 7836-7841
    • Fraser, I.D.C.1    Marston, S.B.2
  • 29
    • 0029822489 scopus 로고    scopus 로고
    • A simple method for automatic tracking of actin filaments in the motility assay
    • Marston SB, Fraser IDC, Wu B, Roper G. A simple method for automatic tracking of actin filaments in the motility assay. J Musc Res Cell Motil 1996;17:497-506.
    • (1996) J Musc Res Cell Motil , vol.17 , pp. 497-506
    • Marston, S.B.1    Fraser, I.D.C.2    Wu, B.3    Roper, G.4
  • 31
    • 84874279586 scopus 로고    scopus 로고
    • O-Glcnacylation in the long isoform of ZASP in human heart muscle
    • Leung M-C, Messer AE, Copeland On, Marston SB. O-Glcnacylation in the long isoform of ZASP in human heart muscle. Biophys J 2012;102:143a.
    • (2012) Biophys J , vol.102
    • Leung, M.-C.1    Messer, A.E.2    On, C.3    Marston, S.B.4
  • 32
    • 0030721473 scopus 로고    scopus 로고
    • Troponin i and troponin T interact with troponin C to produce different Ca2+-dependant effects on actin-tropomyosin filament motility
    • Bing W, Fraser IDC, Marston SB. Troponin I and troponin T interact with troponin C to produce different Ca2+-dependant effects on actin-tropomyosin filament motility. Biochem J 1997;327:335-340.
    • (1997) Biochem J , vol.327 , pp. 335-340
    • Bing, W.1    Fraser, I.D.C.2    Marston, S.B.3
  • 33
    • 0028858949 scopus 로고
    • A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction
    • Potter JD, Sheng Z, Pan B, Zhao J. A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction. J Biol Chem 1995; 270:2557-2562.
    • (1995) J Biol Chem , vol.270 , pp. 2557-2562
    • Potter, J.D.1    Sheng, Z.2    Pan, B.3    Zhao, J.4
  • 34
    • 0025934457 scopus 로고
    • Troponin T isoform expression in humans A comparison among normal and failing heart, fetal heart and adult and fetal skeletal muscle
    • Anderson PAW, Malouf NN, Oakeley AE, Pagani ED, Allen PD. Troponin T isoform expression in humans. A comparison among normal and failing heart, fetal heart and adult and fetal skeletal muscle. Circ Res 1991;69:1226-1233.
    • (1991) Circ Res , vol.69 , pp. 1226-1233
    • Anderson, P.A.W.1    Malouf, N.N.2    Oakeley, A.E.3    Pagani, E.D.4    Allen, P.D.5
  • 35
    • 0346120211 scopus 로고    scopus 로고
    • Modulation of thin filament activation by breakdown or isoform switching of thin filament proteins physiological and pathological implications
    • Marston S, Redwood CS. Modulation of thin filament activation by breakdown or isoform switching of thin filament proteins physiological and pathological implications. Circ Res 2003;93:1170-1178.
    • (2003) Circ Res , vol.93 , pp. 1170-1178
    • Marston, S.1    Redwood, C.S.2
  • 36
    • 62449191449 scopus 로고    scopus 로고
    • Single amino acid sequence polymorphisms in rat cardiac troponin revealed by top-down tandem mass spectrometry
    • Sancho Solis R, Ge Y, Walker JW. Single amino acid sequence polymorphisms in rat cardiac troponin revealed by top-down tandem mass spectrometry. J Muscle Res Cell Motil 2009;29:203-212.
    • (2009) J Muscle Res Cell Motil , vol.29 , pp. 203-212
    • Sancho Solis, R.1    Ge, Y.2    Walker, J.W.3
  • 38
    • 84874253670 scopus 로고    scopus 로고
    • Mutations in thin filament proteins that cause familial dilated cardiomyopathy uncouple troponin i phosphorylation from changes in myofibrillar Ca2+ sensitivity
    • Memo M, Messer AE, Marston SB. Mutations in thin filament proteins that cause familial dilated cardiomyopathy uncouple troponin I phosphorylation from changes in myofibrillar Ca2+ sensitivity. Circulation 2011;124:A13162.
    • (2011) Circulation , vol.124
    • Memo, M.1    Messer, A.E.2    Marston, S.B.3
  • 39
    • 34249676905 scopus 로고    scopus 로고
    • The troponin C G159D mutation blunts myofilament desensitization induced by troponin i Ser23/24 phosphorylation
    • Biesiadecki BJ, Kobayashi T, Walker JS, John Solaro R, de Tombe PP. The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation. Circ Res 2007;100:1486-1493.
    • (2007) Circ Res , vol.100 , pp. 1486-1493
    • Biesiadecki, B.J.1    Kobayashi, T.2    Walker, J.S.3    John Solaro, R.4    De Tombe5
  • 40
    • 0142257957 scopus 로고    scopus 로고
    • Phosphorylation of human cardiac troponin i G203S and K206Q linked to familial hypertrophic cardiomyopathy affects actomyosin interaction in different ways
    • Deng Y, Schmidtmann A, Kruse S, Filatov V, Heilmeyer LM Jr, Jaquet K et al. Phosphorylation of human cardiac troponin I G203S and K206Q linked to familial hypertrophic cardiomyopathy affects actomyosin interaction in different ways. J Mol Cell Cardiol 2003;35:1365-1374.
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 1365-1374
    • Deng, Y.1    Schmidtmann, A.2    Kruse, S.3    Filatov, V.4    Heilmeyer Jr., L.M.5    Jaquet, K.6
  • 41
    • 0036547621 scopus 로고    scopus 로고
    • In vitro motility analysis of thin filaments from failing and non-failing human hearts induces slower filament sliding and higher Ca2+-sensitivity
    • Knott A, Purcell IF, Marston S. In vitro motility analysis of thin filaments from failing and non-failing human hearts induces slower filament sliding and higher Ca2+-sensitivity. J Mol Cell Cardiol 2002;34:469-482.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 469-482
    • Knott, A.1    Purcell, I.F.2    Marston, S.3
  • 42
    • 79959963964 scopus 로고    scopus 로고
    • Phosphorylation, but not alternative splicing or proteolytic degradation, is conserved in human and mouse cardiac troponin T
    • Zhang J, Zhang H, Ayaz-Guner S, Chen Y-C, Dong X, Xu Q et al. Phosphorylation, but not alternative splicing or proteolytic degradation, is conserved in human and mouse cardiac troponin T. Biochemistry 2011;50:6081-6092.
    • (2011) Biochemistry , vol.50 , pp. 6081-6092
    • Zhang, J.1    Zhang, H.2    Ayaz-Guner, S.3    Chen, Y.-C.4    Dong, X.5    Xu, Q.6
  • 43
    • 0026453190 scopus 로고
    • Complete nucleotide sequence and structural organization of rat cardiac troponin T gene. A single gene generates embryonic and adult isoforms via developmentally regulated alternative splicing
    • Jin JP, Huang QQ, Yeh HI, Lin JJ. Complete nucleotide sequence and structural organization of rat cardiac troponin T gene. A single gene generates embryonic and adult isoforms via developmentally regulated alternative splicing. J Mol Biol 1992; 227:1269-1276.
    • (1992) J Mol Biol , vol.227 , pp. 1269-1276
    • Jin, J.P.1    Huang, Q.Q.2    Yeh, H.I.3    Lin, J.J.4
  • 44
    • 84874241315 scopus 로고    scopus 로고
    • Mutations in thin filament proteins that cause familial dilated cardiomyopathy uncouple troponin i phosphorylation from changes in myofibrillar Ca2+ sensitivity
    • Memo M, Messer AE, Leung M-C, Marston SB. Mutations in thin filament proteins that cause familial dilated cardiomyopathy uncouple troponin I phosphorylation from changes in myofibrillar Ca2+ sensitivity. Biophys J 2012;102:614a.
    • (2012) Biophys J , vol.102
    • Memo, M.1    Messer, A.E.2    Leung, M.-C.3    Marston, S.B.4
  • 45
    • 40849096222 scopus 로고    scopus 로고
    • The unique functions of cardiac troponin i in the control of cardiac muscle contraction and relaxation
    • Solaro RJ, 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;369:82-87.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 82-87
    • Solaro, R.J.1    Rosevear, P.2    Kobayashi, T.3
  • 46
    • 34748818674 scopus 로고    scopus 로고
    • Phosphorylationdependent conformational transition of the cardiac specific N-extension of troponin i in cardiac troponin
    • Howarth JW, Meller J, Solaro RJ, Trewhella J, Rosevear PR. Phosphorylationdependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin. J Mol Biol 2007;373:706-722.
    • (2007) J Mol Biol , vol.373 , pp. 706-722
    • Howarth, J.W.1    Meller, J.2    Solaro, R.J.3    Trewhella, J.4    Rosevear, P.R.5
  • 47
    • 77951622995 scopus 로고    scopus 로고
    • Increased myofilament Ca2+-sensitivity and arrhythmia susceptibility
    • Huke S, Knollmann BC. Increased myofilament Ca2+-sensitivity and arrhythmia susceptibility. J Mol Cell Cardiol 2010;48:824-833.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 824-833
    • Huke, S.1    Knollmann, B.C.2
  • 48
    • 34547951704 scopus 로고    scopus 로고
    • Cardiac transgenic and gene transfer strategies converge to support an important role for troponin i in regulating relaxation in cardiac myocytes
    • Yasuda S, Coutu P, Sadayappan S, Robbins J, Metzger JM. Cardiac transgenic and gene transfer strategies converge to support an important role for troponin I in regulating relaxation in cardiac myocytes. Circ Res 2007;101:377-386.
    • (2007) Circ Res , vol.101 , pp. 377-386
    • Yasuda, S.1    Coutu, P.2    Sadayappan, S.3    Robbins, J.4    Metzger, J.M.5
  • 49
    • 78650072126 scopus 로고    scopus 로고
    • Protein kinase A-induced myofilament desensitization to Ca(2+) as a result of phosphorylation of cardiac myosinbinding protein C
    • Chen PP, Patel JR, Rybakova IN,Walker JW, Moss RL. Protein kinase A-induced myofilament desensitization to Ca(2+) as a result of phosphorylation of cardiac myosinbinding protein C. J Gen Physiol 2010;136:615-627.
    • (2010) J Gen Physiol , vol.136 , pp. 615-627
    • Chen, P.P.1    Patel, J.R.2    Rybakova Inwalker, J.W.3    Moss, R.L.4


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