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Volumn 50, Issue 1, 2011, Pages 165-174

Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscle

Author keywords

Calcium binding kinetics; Cardiac muscle; Contraction; Cooperative activation; Relaxation; Troponin C

Indexed keywords

CALCIUM ION; PHOSPHATE; TROPONIN C;

EID: 78650848080     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2010.10.025     Document Type: Article
Times cited : (62)

References (48)
  • 1
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Apr
    • Gordon A.M., Homsher E., Regnier M. Regulation of contraction in striated muscle. Physiol Rev Apr. 2000, 80(2):853-924.
    • (2000) Physiol Rev , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 2
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium binding to cardiac troponin C
    • Oct
    • Hofmann P.A., Fuchs F. Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am J Physiol Oct. 1987, 253(4 Pt 1):C541-C546.
    • (1987) Am J Physiol , vol.253 , Issue.4 PART 1
    • Hofmann, P.A.1    Fuchs, F.2
  • 3
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • Aug
    • McKillop D.F., Geeves M.A. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J Aug. 1993, 65(2):693-701.
    • (1993) Biophys J , vol.65 , Issue.2 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 4
    • 17444431193 scopus 로고    scopus 로고
    • Sarcomeric determinants of striated muscle relaxation kinetics
    • Mar
    • Poggesi C., Tesi C., Stehle R. Sarcomeric determinants of striated muscle relaxation kinetics. Pflugers Arch Mar. 2005, 449(6):505-517.
    • (2005) Pflugers Arch , vol.449 , Issue.6 , pp. 505-517
    • Poggesi, C.1    Tesi, C.2    Stehle, R.3
  • 5
    • 4444334713 scopus 로고    scopus 로고
    • Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle
    • Sep
    • Regnier M., Martin H., Barsotti R.J., Rivera A.J., Martyn D.A., Clemmens E. Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle. Biophys J Sep. 2004, 87(3):1815-1824.
    • (2004) Biophys J , vol.87 , Issue.3 , pp. 1815-1824
    • Regnier, M.1    Martin, H.2    Barsotti, R.J.3    Rivera, A.J.4    Martyn, D.A.5    Clemmens, E.6
  • 6
    • 0031920485 scopus 로고    scopus 로고
    • Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle
    • Apr
    • Regnier M., Martyn D.A., Chase P.B. Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle. Biophys J Apr. 1998, 74(4):2005-2015.
    • (1998) Biophys J , vol.74 , Issue.4 , pp. 2005-2015
    • Regnier, M.1    Martyn, D.A.2    Chase, P.B.3
  • 7
    • 0034705580 scopus 로고    scopus 로고
    • 2-Deoxy-ATP enhances contractility of rat cardiac muscle
    • Jun
    • Regnier M., Rivera A.J., Chen Y., Chase P.B. 2-Deoxy-ATP enhances contractility of rat cardiac muscle. Circ Res Jun. 23 2000, 86(12):1211-1217.
    • (2000) Circ Res , vol.86 , Issue.12 , pp. 1211-1217
    • Regnier, M.1    Rivera, A.J.2    Chen, Y.3    Chase, P.B.4
  • 8
    • 34147172853 scopus 로고    scopus 로고
    • Investigation of thin filament near-neighbor regulatory unit interactions during skinned rat cardiac muscle force development
    • Gillis T.E., Martyn D.A., Rivera A.J., Regnier M. Investigation of thin filament near-neighbor regulatory unit interactions during skinned rat cardiac muscle force development. J Physiol Feb. 22 2007, 580(Pt 2):561-576.
    • (2007) J Physiol , vol.580 , Issue.PART 2 , pp. 561-576
    • Gillis, T.E.1    Martyn, D.A.2    Rivera, A.J.3    Regnier, M.4
  • 9
    • 0037092230 scopus 로고    scopus 로고
    • Thin filament near-neighbour regulatory unit interactions affect rabbit skeletal muscle steady-state force-Ca(2+) relations
    • Apr
    • Regnier M., Rivera A.J., Wang C.K., Bates M.A., Chase P.B., Gordon A.M. Thin filament near-neighbour regulatory unit interactions affect rabbit skeletal muscle steady-state force-Ca(2+) relations. J Physiol Apr. 15 2002, 540(Pt 2):485-497.
    • (2002) J Physiol , vol.540 , Issue.PART 2 , pp. 485-497
    • Regnier, M.1    Rivera, A.J.2    Wang, C.K.3    Bates, M.A.4    Chase, P.B.5    Gordon, A.M.6
  • 10
    • 0033614841 scopus 로고    scopus 로고
    • Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C
    • Jun
    • Li M.X., Spyracopoulos L., Sykes B.D. Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C. Biochemistry Jun. 29 1999, 38(26):8289-8298.
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8289-8298
    • Li, M.X.1    Spyracopoulos, L.2    Sykes, B.D.3
  • 11
    • 0242475138 scopus 로고    scopus 로고
    • Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils
    • Nov
    • Piroddi N., Tesi C., Pellegrino M.A., Tobacman L.S., Homsher E., Poggesi C. Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils. J Physiol Nov. 1 2003, 552(Pt 3):917-931.
    • (2003) J Physiol , vol.552 , Issue.PART 3 , pp. 917-931
    • Piroddi, N.1    Tesi, C.2    Pellegrino, M.A.3    Tobacman, L.S.4    Homsher, E.5    Poggesi, C.6
  • 12
    • 13844272490 scopus 로고    scopus 로고
    • Cardiac troponin C (TnC) and a site I skeletal TnC mutant alter Ca2+ versus crossbridge contribution to force in rabbit skeletal fibres
    • Feb
    • Moreno-Gonzalez A., Fredlund J., Regnier M. Cardiac troponin C (TnC) and a site I skeletal TnC mutant alter Ca2+ versus crossbridge contribution to force in rabbit skeletal fibres. J Physiol Feb. 1 2005, 562(Pt 3):873-884.
    • (2005) J Physiol , vol.562 , Issue.PART 3 , pp. 873-884
    • Moreno-Gonzalez, A.1    Fredlund, J.2    Regnier, M.3
  • 13
    • 33847672617 scopus 로고    scopus 로고
    • Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres
    • Mar
    • Moreno-Gonzalez A., Gillis T.E., Rivera A.J., Chase P.B., Martyn D.A., Regnier M. Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres. J Physiol Mar. 1 2007, 579(Pt 2):313-326.
    • (2007) J Physiol , vol.579 , Issue.PART 2 , pp. 313-326
    • Moreno-Gonzalez, A.1    Gillis, T.E.2    Rivera, A.J.3    Chase, P.B.4    Martyn, D.A.5    Regnier, M.6
  • 14
    • 34547852341 scopus 로고    scopus 로고
    • Influence of enhanced troponin C Ca2+ binding affinity on cooperative thin filament activation in rabbit skeletal muscle
    • Jun
    • Kreutziger K.L., Gillis T.E., Davis J.P., Tikunova S.B., Regnier M. Influence of enhanced troponin C Ca2+ binding affinity on cooperative thin filament activation in rabbit skeletal muscle. J Physiol Jun. 21 2007, 583(1):337-350.
    • (2007) J Physiol , vol.583 , Issue.1 , pp. 337-350
    • Kreutziger, K.L.1    Gillis, T.E.2    Davis, J.P.3    Tikunova, S.B.4    Regnier, M.5
  • 15
    • 48549085587 scopus 로고    scopus 로고
    • Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle
    • Aug
    • Kreutziger K.L., Piroddi N., Scellini B., Tesi C., Poggesi C., Regnier M. Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle. J Physiol Aug. 1 2008, 586(Pt 15):3683-3700.
    • (2008) J Physiol , vol.586 , Issue.PART 15 , pp. 3683-3700
    • Kreutziger, K.L.1    Piroddi, N.2    Scellini, B.3    Tesi, C.4    Poggesi, C.5    Regnier, M.6
  • 16
    • 4143085980 scopus 로고    scopus 로고
    • Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C
    • Aug
    • Tikunova S.B., Davis J.P. Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C. J Biol Chem Aug. 20 2004, 279(34):35341-35352.
    • (2004) J Biol Chem , vol.279 , Issue.34 , pp. 35341-35352
    • Tikunova, S.B.1    Davis, J.P.2
  • 17
    • 35348992614 scopus 로고    scopus 로고
    • Modulation of the rate of cardiac muscle contraction by troponin C constructs with various calcium binding affinities
    • Oct
    • Norman C., Rall J.A., Tikunova S.B., Davis J.P. Modulation of the rate of cardiac muscle contraction by troponin C constructs with various calcium binding affinities. Am J Physiol Heart Circ Physiol Oct. 2007, 293(4):H2580-H2587.
    • (2007) Am J Physiol Heart Circ Physiol , vol.293 , Issue.4
    • Norman, C.1    Rall, J.A.2    Tikunova, S.B.3    Davis, J.P.4
  • 18
    • 4143056326 scopus 로고    scopus 로고
    • Engineering cardiac troponin C (cTnC) mutants with dramatically altered Ca2+ dissociation rates as molecular tools to study cardiac muscle relaxation
    • Tikunova S.B., Davis J.P., Rall J.A. Engineering cardiac troponin C (cTnC) mutants with dramatically altered Ca2+ dissociation rates as molecular tools to study cardiac muscle relaxation. Biophys J 2004, 86(1):394a.
    • (2004) Biophys J , vol.86 , Issue.1
    • Tikunova, S.B.1    Davis, J.P.2    Rall, J.A.3
  • 19
    • 78650844997 scopus 로고    scopus 로고
    • Ca2+-binding kinetics of troponin C influence force generation kinetics in cardiac muscle
    • Kreutziger K.L., Piroddi N., Belus A., Poggesi C., Regnier M. Ca2+-binding kinetics of troponin C influence force generation kinetics in cardiac muscle. Biophys J 2007, 92:477a.
    • (2007) Biophys J , vol.92
    • Kreutziger, K.L.1    Piroddi, N.2    Belus, A.3    Poggesi, C.4    Regnier, M.5
  • 21
    • 0030052282 scopus 로고    scopus 로고
    • Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle
    • Jan
    • Dong W., Rosenfeld S.S., Wang C.K., Gordon A.M., Cheung H.C. Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle. J Biol Chem Jan. 12 1996, 271(2):688-694.
    • (1996) J Biol Chem , vol.271 , Issue.2 , pp. 688-694
    • Dong, W.1    Rosenfeld, S.S.2    Wang, C.K.3    Gordon, A.M.4    Cheung, H.C.5
  • 22
    • 0037188409 scopus 로고    scopus 로고
    • Effect of hydrophobic residue substitutions with glutamine on Ca(2+) binding and exchange with the N-domain of troponin C
    • May
    • Tikunova S.B., Rall J.A., Davis J.P. Effect of hydrophobic residue substitutions with glutamine on Ca(2+) binding and exchange with the N-domain of troponin C. Biochemistry May. 28 2002, 41(21):6697-6705.
    • (2002) Biochemistry , vol.41 , Issue.21 , pp. 6697-6705
    • Tikunova, S.B.1    Rall, J.A.2    Davis, J.P.3
  • 23
    • 9644281066 scopus 로고    scopus 로고
    • Cardiac troponin T isoforms affect the Ca(2+) sensitivity of force development in the presence of slow skeletal troponin I: insights into the role of troponin T isoforms in the fetal heart
    • Nov
    • Gomes A.V., Venkatraman G., Davis J.P., Tikunova S.B., Engel P., Solaro R.J., et al. Cardiac troponin T isoforms affect the Ca(2+) sensitivity of force development in the presence of slow skeletal troponin I: insights into the role of troponin T isoforms in the fetal heart. J Biol Chem Nov. 26 2004, 279(48):49579-49587.
    • (2004) J Biol Chem , vol.279 , Issue.48 , pp. 49579-49587
    • Gomes, A.V.1    Venkatraman, G.2    Davis, J.P.3    Tikunova, S.B.4    Engel, P.5    Solaro, R.J.6
  • 24
    • 17544393835 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy mutations in troponin I (K183Delta, G203S, K206Q) enhance filament sliding
    • Jul
    • Kohler J., Chen Y., Brenner B., Gordon A.M., Kraft T., Martyn D.A., et al. Familial hypertrophic cardiomyopathy mutations in troponin I (K183Delta, G203S, K206Q) enhance filament sliding. Physiol Genomics Jul. 7 2003, 14(2):117-128.
    • (2003) Physiol Genomics , vol.14 , Issue.2 , pp. 117-128
    • Kohler, J.1    Chen, Y.2    Brenner, B.3    Gordon, A.M.4    Kraft, T.5    Martyn, D.A.6
  • 25
    • 33645344861 scopus 로고    scopus 로고
    • No direct effect of creatine phosphate on the cross-bridge cycle in cardiac myofibrils
    • Apr
    • Piroddi N., Belus A., Eiras S., Tesi C., van der Velden J., Poggesi C., et al. No direct effect of creatine phosphate on the cross-bridge cycle in cardiac myofibrils. Pflugers Arch Apr. 2006, 452(1):3-6.
    • (2006) Pflugers Arch , vol.452 , Issue.1 , pp. 3-6
    • Piroddi, N.1    Belus, A.2    Eiras, S.3    Tesi, C.4    van der Velden, J.5    Poggesi, C.6
  • 26
    • 0031594197 scopus 로고    scopus 로고
    • Force regulation by Ca2+ in skinned single cardiac myocytes of frog
    • Apr
    • Brandt P.W., Colomo F., Piroddi N., Poggesi C., Tesi C. Force regulation by Ca2+ in skinned single cardiac myocytes of frog. Biophys J Apr. 1998, 74(4):1994-2004.
    • (1998) Biophys J , vol.74 , Issue.4 , pp. 1994-2004
    • Brandt, P.W.1    Colomo, F.2    Piroddi, N.3    Poggesi, C.4    Tesi, C.5
  • 27
    • 0028114442 scopus 로고
    • Unloaded shortening of skinned muscle fibers from rabbit activated with and without Ca2+
    • Nov
    • Martyn D.A., Chase P.B., Hannon J.D., Huntsman L.L., Kushmerick M.J., Gordon A.M. Unloaded shortening of skinned muscle fibers from rabbit activated with and without Ca2+. Biophys J Nov. 1994, 67(5):1984-1993.
    • (1994) Biophys J , vol.67 , Issue.5 , pp. 1984-1993
    • Martyn, D.A.1    Chase, P.B.2    Hannon, J.D.3    Huntsman, L.L.4    Kushmerick, M.J.5    Gordon, A.M.6
  • 28
    • 0034084354 scopus 로고    scopus 로고
    • The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle
    • Jun
    • Tesi C., Colomo F., Nencini S., Piroddi N., Poggesi C. The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle. Biophys J Jun. 2000, 78(6):3081-3092.
    • (2000) Biophys J , vol.78 , Issue.6 , pp. 3081-3092
    • Tesi, C.1    Colomo, F.2    Nencini, S.3    Piroddi, N.4    Poggesi, C.5
  • 29
    • 0036787723 scopus 로고    scopus 로고
    • Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle
    • Oct
    • Tesi C., Piroddi N., Colomo F., Poggesi C. Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle. Biophys J Oct. 2002, 83(4):2142-2151.
    • (2002) Biophys J , vol.83 , Issue.4 , pp. 2142-2151
    • Tesi, C.1    Piroddi, N.2    Colomo, F.3    Poggesi, C.4
  • 30
    • 34247642743 scopus 로고    scopus 로고
    • Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C
    • May
    • Davis J.P., Norman C., Kobayashi T., Solaro R.J., Swartz D.R., Tikunova S.B. Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C. Biophys J May 1 2007, 92(9):3195-3206.
    • (2007) Biophys J , 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
  • 31
    • 77749286325 scopus 로고    scopus 로고
    • Effect of calcium-sensitizing mutations on calcium binding and exchange with troponin C in increasingly complex biochemical systems
    • May
    • Tikunova S.B., Liu B., Swindle N., Little S.C., Gomes A.V., Swartz D.R., et al. Effect of calcium-sensitizing mutations on calcium binding and exchange with troponin C in increasingly complex biochemical systems. Biochemistry Mar. 9 2010, 49(9):1975-1984.
    • (2010) Biochemistry , vol.49 , Issue.9 , pp. 1975-1984
    • Tikunova, S.B.1    Liu, B.2    Swindle, N.3    Little, S.C.4    Gomes, A.V.5    Swartz, D.R.6
  • 32
    • 0035006418 scopus 로고    scopus 로고
    • Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle
    • Jun
    • Martyn D.A., Gordon A.M. Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle. Biophys J Jun. 2001, 80(6):2798-2808.
    • (2001) Biophys J , vol.80 , Issue.6 , pp. 2798-2808
    • Martyn, D.A.1    Gordon, A.M.2
  • 33
    • 0034746350 scopus 로고    scopus 로고
    • Ca2+- and cross-bridge-dependent changes in N- and C-terminal structure of troponin C in rat cardiac muscle
    • Jan
    • Martyn D.A., Regnier M., Xu D., Gordon A.M. Ca2+- and cross-bridge-dependent changes in N- and C-terminal structure of troponin C in rat cardiac muscle. Biophys J Jan. 2001, 80(1):360-370.
    • (2001) Biophys J , vol.80 , Issue.1 , pp. 360-370
    • Martyn, D.A.1    Regnier, M.2    Xu, D.3    Gordon, A.M.4
  • 34
    • 0027974349 scopus 로고
    • Length, force, and Ca(2+)-troponin C affinity in cardiac and slow skeletal muscle
    • Apr
    • Wang Y.P., Fuchs F. Length, force, and Ca(2+)-troponin C affinity in cardiac and slow skeletal muscle. Am J Physiol Apr. 1994, 266(4 Pt 1):C1077-C1082.
    • (1994) Am J Physiol , vol.266 , Issue.4 PART 1
    • Wang, Y.P.1    Fuchs, F.2
  • 35
    • 2342422415 scopus 로고    scopus 로고
    • Mutations of hydrophobic residues in the N-terminal domain of troponin C affect calcium binding and exchange with the troponin C-troponin I96-148 complex and muscle force production
    • Apr
    • Davis J.P., Rall J.A., Alionte C., Tikunova S.B. Mutations of hydrophobic residues in the N-terminal domain of troponin C affect calcium binding and exchange with the troponin C-troponin I96-148 complex and muscle force production. J Biol Chem Apr. 23 2004, 279(17):17348-17360.
    • (2004) J Biol Chem , vol.279 , Issue.17 , pp. 17348-17360
    • Davis, J.P.1    Rall, J.A.2    Alionte, C.3    Tikunova, S.B.4
  • 36
    • 77951218082 scopus 로고    scopus 로고
    • Phosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments
    • Apr
    • Lu Q.W., Hinken A.C., Patrick S.E., Solaro R.J., Kobayashi T. Phosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments. J Biol Chem Apr. 16 2010, 285(16):11810-11817.
    • (2010) J Biol Chem , vol.285 , Issue.16 , pp. 11810-11817
    • Lu, Q.W.1    Hinken, A.C.2    Patrick, S.E.3    Solaro, R.J.4    Kobayashi, T.5
  • 37
    • 0032734506 scopus 로고    scopus 로고
    • Kinetics of thin filament activation probed by fluorescence of N-((2-(Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1, 3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle contraction
    • Nov
    • Brenner B., Chalovich J.M. Kinetics of thin filament activation probed by fluorescence of N-((2-(Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1, 3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle contraction. Biophys J Nov. 1999, 77(5):2692-2708.
    • (1999) Biophys J , vol.77 , Issue.5 , pp. 2692-2708
    • Brenner, B.1    Chalovich, J.M.2
  • 38
    • 0035002723 scopus 로고    scopus 로고
    • Cooperative mechanisms in the activation dependence of the rate of force development in rabbit skinned skeletal muscle fibers
    • Feb
    • Fitzsimons D.P., Patel J.R., Campbell K.S., Moss R.L. Cooperative mechanisms in the activation dependence of the rate of force development in rabbit skinned skeletal muscle fibers. J Gen Physiol Feb. 2001, 117(2):133-148.
    • (2001) J Gen Physiol , vol.117 , Issue.2 , pp. 133-148
    • Fitzsimons, D.P.1    Patel, J.R.2    Campbell, K.S.3    Moss, R.L.4
  • 39
    • 0034123345 scopus 로고    scopus 로고
    • Different myofilament nearest-neighbor interactions have distinctive effects on contractile behavior
    • Jun
    • Razumova M.V., Bukatina A.E., Campbell K.B. Different myofilament nearest-neighbor interactions have distinctive effects on contractile behavior. Biophys J Jun. 2000, 78(6):3120-3137.
    • (2000) Biophys J , vol.78 , Issue.6 , pp. 3120-3137
    • Razumova, M.V.1    Bukatina, A.E.2    Campbell, K.B.3
  • 40
    • 0024007477 scopus 로고
    • Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction
    • May
    • Brenner B. Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc Natl Acad Sci USA May 1988, 85(9):3265-3269.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.9 , pp. 3265-3269
    • Brenner, B.1
  • 41
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction
    • Apr
    • Kress M., Huxley H.E., Faruqi A.R., Hendrix J. Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction. J Mol Biol Apr. 5 1986, 188(3):325-342.
    • (1986) J Mol Biol , vol.188 , Issue.3 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3    Hendrix, J.4
  • 42
    • 0014843604 scopus 로고
    • Rapid 'give' and the tension 'shoulder' in the relaxation of frog muscle fibres
    • Sep
    • Huxley A.F., Simmons R.M. Rapid 'give' and the tension 'shoulder' in the relaxation of frog muscle fibres. J Physiol Sep. 1970, 210(1):32P-33P.
    • (1970) J Physiol , vol.210 , Issue.1
    • Huxley, A.F.1    Simmons, R.M.2
  • 43
    • 1842579533 scopus 로고    scopus 로고
    • Myofibrillar determinants of rate of relaxation in skinned skeletal muscle fibers
    • discussion 81-2
    • Luo Y., Davis J.P., Tikunova S.B., Smillie L.B., Rall J.A. Myofibrillar determinants of rate of relaxation in skinned skeletal muscle fibers. Adv Exp Med Biol 2003, 538:573-581. discussion 81-2.
    • (2003) Adv Exp Med Biol , vol.538 , pp. 573-581
    • Luo, Y.1    Davis, J.P.2    Tikunova, S.B.3    Smillie, L.B.4    Rall, J.A.5
  • 44
    • 43649089498 scopus 로고    scopus 로고
    • A novel mutant cardiac troponin C disrupts molecular motions critical for calcium binding affinity and cardiomyocyte contractility
    • May
    • Lim C.C., Yang H., Yang M., Wang C.K., Shi J., Berg E.A., et al. A novel mutant cardiac troponin C disrupts molecular motions critical for calcium binding affinity and cardiomyocyte contractility. Biophys J May 1 2008, 94(9):3577-3589.
    • (2008) Biophys J , vol.94 , Issue.9 , pp. 3577-3589
    • Lim, C.C.1    Yang, H.2    Yang, M.3    Wang, C.K.4    Shi, J.5    Berg, E.A.6
  • 45
    • 43049104563 scopus 로고    scopus 로고
    • The familial hypertrophic cardiomyopathy related cardiac troponin C mutation L29Q affects Ca2+ binding and myofilament contractility
    • Feb
    • Liang B., Chung F., Qu Y., Pavlov D., Gillis T.E., Tikunova S.B., et al. The familial hypertrophic cardiomyopathy related cardiac troponin C mutation L29Q affects Ca2+ binding and myofilament contractility. Physiol Genomics Feb. 19 2008, 33(2):257-266.
    • (2008) Physiol Genomics , vol.33 , Issue.2 , pp. 257-266
    • Liang, B.1    Chung, F.2    Qu, Y.3    Pavlov, D.4    Gillis, T.E.5    Tikunova, S.B.6
  • 46
    • 48849100715 scopus 로고    scopus 로고
    • Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C
    • aug
    • Landstrom A.P., Parvatiyar M.S., Pinto J.R., Marquardt M.L., Bos J.M., Tester D.J., et al. Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C. J Mol Cell Cardiol Aug. 2008, 45(2):281-288.
    • (2008) J Mol Cell Cardiol , vol.45 , Issue.2 , pp. 281-288
    • Landstrom, A.P.1    Parvatiyar, M.S.2    Pinto, J.R.3    Marquardt, M.L.4    Bos, J.M.5    Tester, D.J.6
  • 47
    • 70349652425 scopus 로고    scopus 로고
    • The cardiac troponin C mutation Leu29Gln found in a patient with hypertrophic cardiomyopathy does not alter contractile parameters in skinned murine myocardium
    • Jun
    • Neulen A., Stehle R., Pfitzer G. The cardiac troponin C mutation Leu29Gln found in a patient with hypertrophic cardiomyopathy does not alter contractile parameters in skinned murine myocardium. Basic Res Cardiol Jun. 9 2009, 104(6):751-760.
    • (2009) Basic Res Cardiol , vol.104 , Issue.6 , pp. 751-760
    • Neulen, A.1    Stehle, R.2    Pfitzer, G.3
  • 48
    • 34249676905 scopus 로고    scopus 로고
    • The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation
    • May
    • Biesiadecki B.J., Kobayashi T., Walker J.S., John Solaro R., de Tombe P.P. The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation. Circ Res May 25 2007, 100(10):1486-1493.
    • (2007) Circ Res , vol.100 , Issue.10 , pp. 1486-1493
    • Biesiadecki, B.J.1    Kobayashi, T.2    Walker, J.S.3    John Solaro, R.4    de Tombe, P.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.