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Volumn 35, Issue 2, 2014, Pages 153-160

The myosin-activated thin filament regulatory state, M- -open: A link to hypertrophic cardiomyopathy (HCM)

Author keywords

3 state; Actin; Calcium; Muscle; Myosin; Regulation; Tropomyosin; Troponin

Indexed keywords

CALCIUM; MYOSIN; TROPOMYOSIN; TROPONIN;

EID: 84904255551     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-014-9383-z     Document Type: Review
Times cited : (30)

References (56)
  • 1
    • 79951828756 scopus 로고    scopus 로고
    • Enhanced active cross-bridges during diastole: Molecular pathogenesis of tropomyosin's HCM mutations
    • 10.1016/j.bpj.2011.01.001 1:CAS:528:DC%2BC3MXhvFKgtbg%3D 3037557 21320446 10.1016/j.bpj.2011.01.001
    • Bai F, Weis A, Takeda AK, Chase PB, Kawai M (2011) Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutations. Biophys J 100(4):1014-1023. doi: 10.1016/j.bpj.2011.01.001
    • (2011) Biophys J , vol.100 , Issue.4 , pp. 1014-1023
    • Bai, F.1    Weis, A.2    Takeda, A.K.3    Chase, P.B.4    Kawai, M.5
  • 2
    • 34250174756 scopus 로고    scopus 로고
    • Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments
    • 10.1007/s10974-007-9103-z 1:CAS:528:DC%2BD2sXmtlShsbw%3D 17436057 10.1007/s10974-007-9103-z
    • Boussouf SE, Maytum R, Jaquet K, Geeves MA (2007) Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments. J Muscle Res Cell Motil 28(1):49-58. doi: 10.1007/s10974-007-9103-z
    • (2007) J Muscle Res Cell Motil , vol.28 , Issue.1 , pp. 49-58
    • Boussouf, S.E.1    Maytum, R.2    Jaquet, K.3    Geeves, M.A.4
  • 3
    • 26644464382 scopus 로고    scopus 로고
    • Functional consequences of hypertrophic and dilated cardiomyopathy- causing mutations in alpha-tropomyosin
    • 10.1074/jbc.M505014200 1:CAS:528:DC%2BD2MXhtVKitrzP 16043485 10.1074/jbc.M505014200
    • Chang AN, Harada K, Ackerman MJ, Potter JD (2005) Functional consequences of hypertrophic and dilated cardiomyopathy-causing mutations in alpha-tropomyosin. J Biol Chem 280(40):34343-34349. doi: 10.1074/jbc.M505014200
    • (2005) J Biol Chem , vol.280 , Issue.40 , pp. 34343-34349
    • Chang, A.N.1    Harada, K.2    Ackerman, M.J.3    Potter, J.D.4
  • 4
    • 0030592154 scopus 로고    scopus 로고
    • Calcium-induced conformational change in cardiac troponin C studied by fluorescence probes attached to Cys-84
    • 8695639 10.1016/0167-4838(96)00028-3
    • Dong WJ, Cheung HC (1996) Calcium-induced conformational change in cardiac troponin C studied by fluorescence probes attached to Cys-84. Biochim Biophys Acta 1295(2):139-146
    • (1996) Biochim Biophys Acta , vol.1295 , Issue.2 , pp. 139-146
    • Dong, W.J.1    Cheung, H.C.2
  • 5
    • 0033615542 scopus 로고    scopus 로고
    • Conformation of the regulatory domain of cardiac muscle troponin C in its complex with cardiac troponin i
    • 1:CAS:528:DyaK1MXntFKqtbY%3D 10531339 10.1074/jbc.274.44.31382
    • Dong WJ, Xing J, Villain M, Hellinger M, Robinson JM, Chandra M, Solaro RJ, Umeda PK, Cheung HC (1999) Conformation of the regulatory domain of cardiac muscle troponin C in its complex with cardiac troponin I. J Biol Chem 274(44):31382-31390
    • (1999) J Biol Chem , vol.274 , Issue.44 , pp. 31382-31390
    • Dong, W.J.1    Xing, J.2    Villain, M.3    Hellinger, M.4    Robinson, J.M.5    Chandra, M.6    Solaro, R.J.7    Umeda, P.K.8    Cheung, H.C.9
  • 6
    • 34548211785 scopus 로고    scopus 로고
    • Effects of PKA phosphorylation of cardiac troponin i and strong crossbridge on conformational transitions of the N-domain of cardiac troponin C in regulated thin filaments
    • 10.1021/bi700574n 1:CAS:528:DC%2BD2sXosVOqtr4%3D 2547119 17676764 10.1021/bi700574n
    • Dong WJ, Jayasundar JJ, An J, Xing J, Cheung HC (2007) Effects of PKA phosphorylation of cardiac troponin I and strong crossbridge on conformational transitions of the N-domain of cardiac troponin C in regulated thin filaments. Biochemistry 46(34):9752-9761. doi: 10.1021/bi700574n
    • (2007) Biochemistry , vol.46 , Issue.34 , pp. 9752-9761
    • Dong, W.J.1    Jayasundar, J.J.2    An, J.3    Xing, J.4    Cheung, H.C.5
  • 7
    • 0034698086 scopus 로고    scopus 로고
    • Altered regulatory properties of human cardiac troponin i mutants that cause hypertrophic cardiomyopathy
    • 1:CAS:528:DC%2BD3cXlt1ehtLc%3D 10806205 10.1074/jbc.M002502200
    • Elliott K, Watkins H, Redwood CS (2000) Altered regulatory properties of human cardiac troponin I mutants that cause hypertrophic cardiomyopathy. J Biol Chem 275(29):22069-22074
    • (2000) J Biol Chem , vol.275 , Issue.29 , pp. 22069-22074
    • Elliott, K.1    Watkins, H.2    Redwood, C.S.3
  • 8
    • 0035862210 scopus 로고    scopus 로고
    • Cross-bridge interaction kinetics in rat myocardium are accelerated by strong binding of myosin to the thin filament
    • 1:CAS:528:DC%2BD3MXit1Olu7Y%3D 2278404 11208974 10.1111/j.1469-7793.2001. 0263l.x
    • Fitzsimons DP, Patel JR, Moss RL (2001) Cross-bridge interaction kinetics in rat myocardium are accelerated by strong binding of myosin to the thin filament. J Physiol 530(Pt 2):263-272
    • (2001) J Physiol , vol.530 , Issue.PART 2 , pp. 263-272
    • Fitzsimons, D.P.1    Patel, J.R.2    Moss, R.L.3
  • 9
    • 44349116066 scopus 로고    scopus 로고
    • Structural basis for the regulation of muscle contraction by troponin and tropomyosin
    • 10.1016/j.jmb.2008.04.062 1:CAS:528:DC%2BD1cXmsFKqt7k%3D 2483953 18514658 10.1016/j.jmb.2008.04.062
    • Galinska-Rakoczy A, Engel P, Xu C, Jung H, Craig R, Tobacman LS, Lehman W (2008) Structural basis for the regulation of muscle contraction by troponin and tropomyosin. J Mol Biol 379(5):929-935. doi: 10.1016/j.jmb.2008.04.062
    • (2008) J Mol Biol , vol.379 , Issue.5 , pp. 929-935
    • Galinska-Rakoczy, A.1    Engel, P.2    Xu, C.3    Jung, H.4    Craig, R.5    Tobacman, L.S.6    Lehman, W.7
  • 10
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • 10.1016/S0006-3495(94)80478-3 1:CAS:528:DyaK2cXlsFWmtLs%3D 1225357 7918995 10.1016/S0006-3495(94)80478-3
    • Geeves MA, Lehrer SS (1994) Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys J 67(1):273-282. doi: 10.1016/S0006-3495(94)80478-3
    • (1994) Biophys J , vol.67 , Issue.1 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 11
    • 0034622584 scopus 로고    scopus 로고
    • Inhibition of actin-myosin subfragment 1 ATPase activity by troponin i and IC: Relationship to the thin filament states of muscle
    • 1:CAS:528:DC%2BD3cXksleisL0%3D 10924128 10.1021/bi0002232
    • Geeves MA, Chai M, Lehrer SS (2000) Inhibition of actin-myosin subfragment 1 ATPase activity by troponin I and IC: relationship to the thin filament states of muscle. Biochemistry 39(31):9345-9350
    • (2000) Biochemistry , vol.39 , Issue.31 , pp. 9345-9350
    • Geeves, M.A.1    Chai, M.2    Lehrer, S.S.3
  • 12
    • 0030933128 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy-causing mutations on alpha-tropomyosin structure and function
    • 10.1021/bi962970y 1:STN:280:DyaK2s3mtlOmuw%3D%3D 9109674 10.1021/bi962970y
    • Golitsina N, An Y, Greenfield NJ, Thierfelder L, Iizuka K, Seidman JG, Seidman CE, Lehrer SS, Hitchcock-DeGregori SE (1997) Effects of two familial hypertrophic cardiomyopathy-causing mutations on alpha-tropomyosin structure and function. Biochemistry 36(15):4637-4642. doi: 10.1021/bi962970y
    • (1997) Biochemistry , vol.36 , Issue.15 , pp. 4637-4642
    • Golitsina, N.1    An, Y.2    Greenfield, N.J.3    Thierfelder, L.4    Iizuka, K.5    Seidman, J.G.6    Seidman, C.E.7    Lehrer, S.S.8    Hitchcock-Degregori, S.E.9
  • 14
    • 3042791328 scopus 로고    scopus 로고
    • Role of troponin T in disease
    • 1:CAS:528:DC%2BD2cXotlCrsbk%3D 15524172 10.1023/B:MCBI.0000041853.20588. a0
    • Gomes AV, Barnes JA, Harada K, Potter JD (2004) Role of troponin T in disease. Mol Cell Biochem 263(1-2):115-129
    • (2004) Mol Cell Biochem , vol.263 , Issue.1-2 , pp. 115-129
    • Gomes, A.V.1    Barnes, J.A.2    Harada, K.3    Potter, J.D.4
  • 15
    • 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
    • 10.1074/jbc.M500287200 1:CAS:528:DC%2BD2MXpsVCmt7w%3D 15961398 10.1074/jbc.M500287200
    • Gomes AV, Liang J, Potter JD (2005) 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 280(35):30909-30915. doi: 10.1074/jbc.M500287200
    • (2005) J Biol Chem , vol.280 , Issue.35 , pp. 30909-30915
    • Gomes, A.V.1    Liang, J.2    Potter, J.D.3
  • 17
    • 84870918869 scopus 로고    scopus 로고
    • α-Tropomyosin with a D175N or E180G mutation in only one chain differs from tropomyosin with mutations in both chains
    • 10.1021/bi301323n 1:CAS:528:DC%2BC38XhslWksbfM 3711130 23170982 10.1021/bi301323n
    • Janco M, Kalyva A, Scellini B, Piroddi N, Tesi C, Poggesi C, Geeves MA (2012) α-Tropomyosin with a D175N or E180G mutation in only one chain differs from tropomyosin with mutations in both chains. Biochemistry 51(49):9880-9890. doi: 10.1021/bi301323n
    • (2012) Biochemistry , vol.51 , Issue.49 , pp. 9880-9890
    • Janco, M.1    Kalyva, A.2    Scellini, B.3    Piroddi, N.4    Tesi, C.5    Poggesi, C.6    Geeves, M.A.7
  • 18
    • 33744954871 scopus 로고    scopus 로고
    • 2+ affinity of cardiac thin filaments reconstituted with cardiomyopathy-related mutant cardiac troponin i
    • 1:CAS:528:DC%2BD28Xkt1ymtrc%3D 16531415 10.1074/jbc.M509561200
    • 2+ affinity of cardiac thin filaments reconstituted with cardiomyopathy-related mutant cardiac troponin I. J Biol Chem 281(19):13471-13477
    • (2006) J Biol Chem , vol.281 , Issue.19 , pp. 13471-13477
    • Kobayashi, T.1    Solaro, R.J.2
  • 19
    • 10044280728 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy mutations in alpha-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin
    • 10.1529/biophysj.104.048793 1:CAS:528:DC%2BD2cXhtVOmtbnK 1304903 15454401 10.1529/biophysj.104.048793
    • Kremneva E, Boussouf S, Nikolaeva O, Maytum R, Geeves MA, Levitsky DI (2004) Effects of two familial hypertrophic cardiomyopathy mutations in alpha-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin. Biophys J 87(6):3922-3933. doi: 10.1529/biophysj.104. 048793
    • (2004) Biophys J , vol.87 , Issue.6 , pp. 3922-3933
    • Kremneva, E.1    Boussouf, S.2    Nikolaeva, O.3    Maytum, R.4    Geeves, M.A.5    Levitsky, D.I.6
  • 20
    • 0037023758 scopus 로고    scopus 로고
    • Functional analysis of a troponin i (R145G) mutation associated with familial hypertrophic cardiomyopathy
    • 1:CAS:528:DC%2BD38XivVeksrw%3D 11801593 10.1074/jbc.M108912200
    • Lang R, Gomes AV, Zhao J, Housmans PR, Miller T, Potter JD (2002) Functional analysis of a troponin I (R145G) mutation associated with familial hypertrophic cardiomyopathy. J Biol Chem 277(14):11670-11678
    • (2002) J Biol Chem , vol.277 , Issue.14 , pp. 11670-11678
    • Lang, R.1    Gomes, A.V.2    Zhao, J.3    Housmans, P.R.4    Miller, T.5    Potter, J.D.6
  • 21
  • 22
    • 82955195877 scopus 로고    scopus 로고
    • The 3-state model of muscle regulation revisited: Is a fourth state involved?
    • 10.1007/s10974-011-9263-8 1:CAS:528:DC%2BC3MXhsVWksbbJ 21948173 10.1007/s10974-011-9263-8
    • Lehrer SS (2011) The 3-state model of muscle regulation revisited: is a fourth state involved? J Muscle Res Cell Motil 32(3):203-208. doi: 10.1007/s10974-011-9263-8
    • (2011) J Muscle Res Cell Motil , vol.32 , Issue.3 , pp. 203-208
    • Lehrer, S.S.1
  • 23
    • 0033614841 scopus 로고    scopus 로고
    • Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C
    • 10.1021/bi9901679 1:CAS:528:DyaK1MXjsFynsbc%3D 10387074 10.1021/bi9901679
    • Li MX, Spyracopoulos L, Sykes BD (1999) Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C. Biochemistry 38(26):8289-8298. doi: 10.1021/bi9901679
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8289-8298
    • Li, M.X.1    Spyracopoulos, L.2    Sykes, B.D.3
  • 24
    • 0027986739 scopus 로고
    • Coupling of calcium to the interaction of troponin i with troponin C from cardiac muscle
    • 1:CAS:528:DyaK2cXmsVyrtb8%3D 7918499 10.1021/bi00208a026
    • Liao R, Wang CK, Cheung HC (1994) Coupling of calcium to the interaction of troponin I with troponin C from cardiac muscle. Biochemistry 33(42):12729-12734
    • (1994) Biochemistry , vol.33 , Issue.42 , pp. 12729-12734
    • Liao, R.1    Wang, C.K.2    Cheung, H.C.3
  • 25
    • 84865119925 scopus 로고    scopus 로고
    • Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin
    • 10.1021/bi3006835 1:CAS:528:DC%2BC38XhtVWhtLjP 3447992 22794249 10.1021/bi3006835
    • Ly S, Lehrer SS (2012) Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin. Biochemistry 51(32):6413-6420. doi: 10.1021/bi3006835
    • (2012) Biochemistry , vol.51 , Issue.32 , pp. 6413-6420
    • Ly, S.1    Lehrer, S.S.2
  • 26
    • 79960564849 scopus 로고    scopus 로고
    • How do mutations in contractile proteins cause the primary familial cardiomyopathies?
    • 10.1007/s12265-011-9266-2 21424860 10.1007/s12265-011-9266-2
    • Marston SB (2011) How do mutations in contractile proteins cause the primary familial cardiomyopathies? J Cardiovasc Transl Res 4(3):245-255. doi: 10.1007/s12265-011-9266-2
    • (2011) J Cardiovasc Transl Res , vol.4 , Issue.3 , pp. 245-255
    • Marston, S.B.1
  • 27
    • 0037470225 scopus 로고    scopus 로고
    • Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms
    • 1:CAS:528:DC%2BD3sXhsVKjtLg%3D 12475978 10.1074/jbc.M210690200
    • Maytum R, Westerdorf B, Jaquet K, Geeves MA (2003) Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms. J Biol Chem 278(9):6696-6701
    • (2003) J Biol Chem , vol.278 , Issue.9 , pp. 6696-6701
    • Maytum, R.1    Westerdorf, B.2    Jaquet, K.3    Geeves, M.A.4
  • 28
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • 1:CAS:528:DyaK2cXhsFKqs7k%3D
    • McKillop DFA, Geeves MA (1993) Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biohys J 65:693-701
    • (1993) Biohys J , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 29
    • 2642583071 scopus 로고    scopus 로고
    • Myosin crossbridge activation of cardiac thin filaments: Implications for myocardial function in health and disease
    • 1:CAS:528:DC%2BD2cXktFSltbY%3D 15166116 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(10):1290-1300
    • (2004) Circ Res , vol.94 , Issue.10 , pp. 1290-1300
    • Moss, R.L.1    Razumova, M.2    Fitzsimons, D.P.3
  • 30
    • 65649150702 scopus 로고    scopus 로고
    • 2+-dependent photocrosslinking of tropomyosin residue 146 to residues 157-163 in the C-terminal domain of troponin i in reconstituted skeletal muscle thin filaments
    • 10.1016/j.jmb.2009.04.027 1:CAS:528:DC%2BD1MXms1aitb0%3D 2805953 19379756 10.1016/j.jmb.2009.04.027
    • 2+-dependent photocrosslinking of tropomyosin residue 146 to residues 157-163 in the C-terminal domain of troponin I in reconstituted skeletal muscle thin filaments. J Mol Biol 389(3):575-583. doi: 10.1016/j.jmb.2009.04.027
    • (2009) J Mol Biol , vol.389 , Issue.3 , pp. 575-583
    • Mudalige, W.A.1    Tao, T.C.2    Lehrer, S.S.3
  • 31
    • 23944457539 scopus 로고    scopus 로고
    • 2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin
    • 10.1016/j.jmb.2005.06.067 1:CAS:528:DC%2BD2MXpsVWlsLY%3D 16061251 10.1016/j.jmb.2005.06.067
    • 2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin. J Mol Biol 352(1):178-201. doi: 10.1016/j.jmb.2005.06.067
    • (2005) J Mol Biol , vol.352 , Issue.1 , pp. 178-201
    • Murakami, K.1    Yumoto, F.2    Ohki, S.Y.3    Yasunaga, T.4    Tanokura, M.5    Wakabayashi, T.6
  • 32
    • 40849094355 scopus 로고    scopus 로고
    • Troponin: Regulatory function and disorders
    • 10.1016/j.bbrc.2007.11.187 1:CAS:528:DC%2BD1cXjs12rsb4%3D 18154728 10.1016/j.bbrc.2007.11.187
    • Ohtsuki I, Morimoto S (2008) Troponin: regulatory function and disorders. Biochem Biophys Res Commun 369(1):62-73. doi: 10.1016/j.bbrc.2007.11.187
    • (2008) Biochem Biophys Res Commun , vol.369 , Issue.1 , pp. 62-73
    • Ohtsuki, I.1    Morimoto, S.2
  • 33
    • 77954558179 scopus 로고    scopus 로고
    • Cardiac troponin mutations and restrictive cardiomyopathy
    • 10.1155/2010/350706 2896668 20617149 10.1155/2010/350706
    • Parvatiyar MS, Pinto JR, Dweck D, Potter JD (2010) Cardiac troponin mutations and restrictive cardiomyopathy. J Biomed Biotechnol 2010:350706. doi: 10.1155/2010/350706
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 350706
    • Parvatiyar, M.S.1    Pinto, J.R.2    Dweck, D.3    Potter, J.D.4
  • 34
    • 84866431330 scopus 로고    scopus 로고
    • A mutation in TNNC1-encoded cardiac troponin C, TNNC1-A31S, predisposes to hypertrophic cardiomyopathy and ventricular fibrillation
    • 10.1074/jbc.M112.377713 1:CAS:528:DC%2BC38XhtlGgtr3E 3442518 22815480 10.1074/jbc.M112.377713
    • Parvatiyar MS, Landstrom AP, Figueiredo-Freitas C, Potter JD, Ackerman MJ, Pinto JR (2012) A mutation in TNNC1-encoded cardiac troponin C, TNNC1-A31S, predisposes to hypertrophic cardiomyopathy and ventricular fibrillation. J Biol Chem 287(38):31845-31855. doi: 10.1074/jbc.M112.377713
    • (2012) J Biol Chem , vol.287 , Issue.38 , pp. 31845-31855
    • Parvatiyar, M.S.1    Landstrom, A.P.2    Figueiredo-Freitas, C.3    Potter, J.D.4    Ackerman, M.J.5    Pinto, J.R.6
  • 35
    • 38349117234 scopus 로고    scopus 로고
    • 2+ sensitivity of force development and impairs the inhibitory properties of troponin
    • 10.1074/jbc.M707066200 1:CAS:528:DC%2BD1cXnsFCmsQ%3D%3D 18032382 10.1074/jbc.M707066200
    • 2+ sensitivity of force development and impairs the inhibitory properties of troponin. J Biol Chem 283(4):2156-2166. doi: 10.1074/jbc. M707066200
    • (2008) J Biol Chem , vol.283 , Issue.4 , pp. 2156-2166
    • Pinto, J.R.1    Parvatiyar, M.S.2    Jones, M.A.3    Liang, J.4    Potter, J.D.5
  • 36
    • 67650544956 scopus 로고    scopus 로고
    • A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy
    • 10.1074/jbc.M109.007021 1:CAS:528:DC%2BD1MXotVKnt7k%3D 2707221 19439414 10.1074/jbc.M109.007021
    • Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD (2009) A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy. J Biol Chem 284(28):19090-19100. doi: 10.1074/jbc.M109.007021
    • (2009) J Biol Chem , vol.284 , Issue.28 , pp. 19090-19100
    • Pinto, J.R.1    Parvatiyar, M.S.2    Jones, M.A.3    Liang, J.4    Ackerman, M.J.5    Potter, J.D.6
  • 37
    • 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
    • 10.1074/jbc.M110.168583 3020707 21056975 10.1074/jbc.M110.168583
    • Pinto JR, Reynaldo DP, Parvatiyar MS, Dweck D, Liang J, Jones MA, Sorenson MM, Potter JD (2010) 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(2):1005-1013. doi: 10.1074/jbc.M110.168583
    • (2010) J Biol Chem , vol.286 , Issue.2 , pp. 1005-1013
    • Pinto, J.R.1    Reynaldo, D.P.2    Parvatiyar, M.S.3    Dweck, D.4    Liang, J.5    Jones, M.A.6    Sorenson, M.M.7    Potter, J.D.8
  • 38
    • 84890102055 scopus 로고    scopus 로고
    • Alpha-tropomyosin mutations in inherited cardiomyopathies
    • 10.1007/s10974-013-9358-5 1:CAS:528:DC%2BC3sXhvVyiurzO 24005378 10.1007/s10974-013-9358-5
    • Redwood C, Robinson P (2013) Alpha-tropomyosin mutations in inherited cardiomyopathies. J Muscle Res Cell Motil 34(3-4):285-294. doi: 10.1007/s10974-013-9358-5
    • (2013) J Muscle Res Cell Motil , vol.34 , Issue.3-4 , pp. 285-294
    • Redwood, C.1    Robinson, P.2
  • 39
    • 84882771372 scopus 로고    scopus 로고
    • Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges
    • 10.1016/j.abb.2013.07.013 1:CAS:528:DC%2BC3sXhsVWjur%2FN 23896515 10.1016/j.abb.2013.07.013
    • Rieck DC, Li KL, Ouyang Y, Solaro RJ, Dong WJ (2013) Structural basis for the in situ Ca(2+) sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges. Arch Biochem Biophys 537(2):198-209. doi: 10.1016/j.abb.2013.07.013
    • (2013) Arch Biochem Biophys , vol.537 , Issue.2 , pp. 198-209
    • Rieck, D.C.1    Li, K.L.2    Ouyang, Y.3    Solaro, R.J.4    Dong, W.J.5
  • 40
    • 2942607388 scopus 로고    scopus 로고
    • Switching of troponin I: Ca(2+) and myosin-induced activation of heart muscle
    • 10.1016/j.jmb.2004.04.046 1:CAS:528:DC%2BD2cXkvVKmu74%3D 15201053 10.1016/j.jmb.2004.04.046
    • Robinson JM, Dong WJ, Xing J, Cheung HC (2004) Switching of troponin I: Ca(2+) and myosin-induced activation of heart muscle. J Mol Biol 340(2):295-305. doi: 10.1016/j.jmb.2004.04.046
    • (2004) J Mol Biol , vol.340 , Issue.2 , pp. 295-305
    • Robinson, J.M.1    Dong, W.J.2    Xing, J.3    Cheung, H.C.4
  • 41
    • 37349042936 scopus 로고    scopus 로고
    • Dilated and hypertrophic cardiomyopathy mutations in troponin and {alpha}-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments
    • 1:CAS:528:DC%2BD2sXhtlOjsLzK 17932326 10.1161/CIRCRESAHA.107.156380
    • Robinson P, Griffiths PJ, Watkins H, Redwood CS (2007) Dilated and hypertrophic cardiomyopathy mutations in troponin and {alpha}-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments. Circ Res 101(12):1266-1273
    • (2007) Circ Res , vol.101 , Issue.12 , pp. 1266-1273
    • Robinson, P.1    Griffiths, P.J.2    Watkins, H.3    Redwood, C.S.4
  • 42
    • 84881104951 scopus 로고    scopus 로고
    • Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human beta-cardiac myosin motor function
    • 10.1073/pnas.1309493110 1:CAS:528:DC%2BC3sXht12ht7bI 3732973 23798412 10.1073/pnas.1309493110
    • Sommese RF, Sung J, Nag S, Sutton S, Deacon JC, Choe E, Leinwand LA, Ruppel K, Spudich JA (2013) Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human beta-cardiac myosin motor function. Proc Natl Acad Sci U S A 110(31):12607-12612. doi: 10.1073/pnas.1309493110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.31 , pp. 12607-12612
    • Sommese, R.F.1    Sung, J.2    Nag, S.3    Sutton, S.4    Deacon, J.C.5    Choe, E.6    Leinwand, L.A.7    Ruppel, K.8    Spudich, J.A.9
  • 43
    • 84896509481 scopus 로고    scopus 로고
    • Hypertrophic and dilated cardiomyopathy: Four decades of basic research on muscle lead to potential therapeutic approaches to these devastating genetic diseases
    • 10.1016/j.bpj.2014.02.011 1:CAS:528:DC%2BC2cXks1Wiu74%3D 24655499 10.1016/j.bpj.2014.02.011
    • Spudich JA (2014) Hypertrophic and dilated cardiomyopathy: four decades of basic research on muscle lead to potential therapeutic approaches to these devastating genetic diseases. Biophys J 106(6):1236-1249. doi: 10.1016/j.bpj.2014.02.011
    • (2014) Biophys J , vol.106 , Issue.6 , pp. 1236-1249
    • Spudich, J.A.1
  • 44
    • 58149305398 scopus 로고    scopus 로고
    • Calcium- and myosin-dependent changes in troponin structure during activation of heart muscle
    • 10.1113/jphysiol.2008.164707 1:CAS:528:DC%2BD1MXhtVKlsL8%3D 2670030 19015190 10.1113/jphysiol.2008.164707
    • Sun YB, Lou F, Irving M (2009) Calcium- and myosin-dependent changes in troponin structure during activation of heart muscle. J Physiol 587(Pt 1):155-163. doi: 10.1113/jphysiol.2008.164707
    • (2009) J Physiol , vol.587 , Issue.PART 1 , pp. 155-163
    • Sun, Y.B.1    Lou, F.2    Irving, M.3
  • 45
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin i from white skeletal muscle of the rabbit
    • 1:CAS:528:DyaE28Xhs1Sku7s%3D 1172583 179535
    • Syska H, Wilkinson JM, Grand RJ, Perry SV (1976) The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem J 153(2):375-387
    • (1976) Biochem J , vol.153 , Issue.2 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.3    Perry, S.V.4
  • 46
    • 0034614419 scopus 로고    scopus 로고
    • Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy
    • 1:CAS:528:DC%2BD3cXjvVKgug%3D%3D 10617660 10.1074/jbc.275.1.624
    • Szczesna D, Zhang R, Zhao J, Jones M, Guzman G, Potter JD (2000) Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy. J Biol Chem 275(1):624-630
    • (2000) J Biol Chem , 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
  • 47
    • 0942276371 scopus 로고    scopus 로고
    • 2+ binding of human cardiac myosin regulatory light chain affect cardiac muscle contraction
    • 10.1074/jbc.M307092200 1:CAS:528:DC%2BD2cXmtlClsg%3D%3D 14594949 10.1074/jbc.M307092200
    • 2+ binding of human cardiac myosin regulatory light chain affect cardiac muscle contraction. J Biol Chem 279(5):3535-3542. doi: 10.1074/jbc.M307092200
    • (2004) J Biol Chem , vol.279 , Issue.5 , pp. 3535-3542
    • Szczesna-Cordary, D.1    Guzman, G.2    Ng, S.S.3    Zhao, J.4
  • 48
    • 0035695803 scopus 로고    scopus 로고
    • Functional consequences of the mutations in human cardiac troponin i gene found in familial hypertrophic cardiomyopathy
    • 1:CAS:528:DC%2BD3MXovV2msLw%3D 11735257 10.1006/jmcc.2001.1473
    • Takahashi-Yanaga F, Morimoto S, Harada K, Minakami R, Shiraishi F, Ohta M, Lu QW, Sasaguri T, Ohtsuki I (2001) Functional consequences of the mutations in human cardiac troponin I gene found in familial hypertrophic cardiomyopathy. J Mol Cell Cardiol 33(12):2095-2107
    • (2001) J Mol Cell Cardiol , vol.33 , Issue.12 , pp. 2095-2107
    • Takahashi-Yanaga, F.1    Morimoto, S.2    Harada, K.3    Minakami, R.4    Shiraishi, F.5    Ohta, M.6    Lu, Q.W.7    Sasaguri, T.8    Ohtsuki, I.9
  • 49
    • 30944444021 scopus 로고    scopus 로고
    • Sarcomeric proteins and familial hypertrophic cardiomyopathy: Linking mutations in structural proteins to complex cardiovascular phenotypes
    • 10.1007/s10741-005-5253-5 1:CAS:528:DC%2BD28XksVOmtA%3D%3D 16416046 10.1007/s10741-005-5253-5
    • Tardiff JC (2005) Sarcomeric proteins and familial hypertrophic cardiomyopathy: linking mutations in structural proteins to complex cardiovascular phenotypes. Heart Fail Rev 10(3):237-248. doi: 10.1007/s10741-005-5253-5
    • (2005) Heart Fail Rev , vol.10 , Issue.3 , pp. 237-248
    • Tardiff, J.C.1
  • 50
    • 79953055654 scopus 로고    scopus 로고
    • Thin filament mutations: Developing an integrative approach to a complex disorder
    • 10.1161/CIRCRESAHA.110.224170 1:CAS:528:DC%2BC3MXjsV2jtrs%3D 3075069 21415410 10.1161/CIRCRESAHA.110.224170
    • Tardiff JC (2011) Thin filament mutations: developing an integrative approach to a complex disorder. Circ Res 108(6):765-782. doi: 10.1161/CIRCRESAHA.110.224170
    • (2011) Circ Res , vol.108 , Issue.6 , pp. 765-782
    • Tardiff, J.C.1
  • 51
    • 0031554903 scopus 로고    scopus 로고
    • 2+-dependent regulation of muscle contraction
    • 1:CAS:528:DyaK2sXlvFymt7o%3D 9299323 10.1006/jmbi.1997.1200
    • 2+-dependent regulation of muscle contraction. J Mol Biol 271(5):728-750
    • (1997) J Mol Biol , vol.271 , Issue.5 , pp. 728-750
    • Tripet, B.1    Van Eyk, J.E.2    Hodges, R.S.3
  • 53
    • 0022367130 scopus 로고
    • Energetics of the binding of calcium and troponin i to troponin C from rabbit skeletal muscle
    • 10.1016/S0006-3495(85)83831-5 1:CAS:528:DyaL28XisVaj 1329398 4074834 10.1016/S0006-3495(85)83831-5
    • Wang CK, Cheung HC (1985) Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle. Biophys J 48(5):727-739. doi: 10.1016/S0006-3495(85)83831-5
    • (1985) Biophys J , vol.48 , Issue.5 , pp. 727-739
    • Wang, C.K.1    Cheung, H.C.2
  • 54
    • 77951621530 scopus 로고    scopus 로고
    • Mutations in Troponin that cause HCM, DCM and RCM: What can we learn about thin filament function?
    • 10.1016/j.yjmcc.2009.10.031 19914256 10.1016/j.yjmcc.2009.10.031
    • Willott RH, Gomes AV, Chang AN, Parvatiyar MS, Pinto JR, Potter JD (2009) Mutations in Troponin that cause HCM, DCM AND RCM: what can we learn about thin filament function? J Mol Cell Cardiol 48(5):882-892. doi: 10.1016/j.yjmcc.2009. 10.031
    • (2009) J Mol Cell Cardiol , vol.48 , Issue.5 , pp. 882-892
    • Willott, R.H.1    Gomes, A.V.2    Chang, A.N.3    Parvatiyar, M.S.4    Pinto, J.R.5    Potter, J.D.6
  • 55
    • 0008415922 scopus 로고
    • Troponin i and troponin I-C binding to actin-tropomyosin and dissociation by myosin S1
    • Zhou X, Morris EP, Lehrer SS (1995) Troponin I and troponin I-C binding to actin-tropomyosin and dissociation by myosin S1. Bophys J 68:A167
    • (1995) Bophys J , vol.68 , pp. 167
    • Zhou, X.1    Morris, E.P.2    Lehrer, S.S.3
  • 56
    • 0034620545 scopus 로고    scopus 로고
    • Binding of troponin i and the troponin I-troponin C complex to actin-tropomyosin: Dissociation by myosin subfragment 1
    • 1:CAS:528:DC%2BD3cXit1Wjsg%3D%3D 10653659 10.1021/bi992327m
    • Zhou X, Morris EP, Lehrer SS (2000) Binding of troponin I and the troponin I-troponin C complex to actin-tropomyosin: dissociation by myosin subfragment 1. Biochemistry 39(5):1128-1132
    • (2000) Biochemistry , vol.39 , Issue.5 , pp. 1128-1132
    • Zhou, X.1    Morris, E.P.2    Lehrer, S.S.3


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