메뉴 건너뛰기




Volumn 94, Issue 10, 2004, Pages 1290-1300

Myosin crossbridge activation of cardiac thin filaments: Implications for myocardial function in health and disease

Author keywords

Ca2+ regulation; Cardiac contractility; Cardiomyopathy; Cooperativity

Indexed keywords

ADENOSINE DIPHOSPHATE; CALCIUM ION; MYOSIN; TROPOMYOSIN; TROPONIN C; TROPONIN T;

EID: 2642583071     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.0000127125.61647.4F     Document Type: Review
Times cited : (128)

References (92)
  • 2
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M. Regulation of contraction in striated muscle. Physiol Rev. 2000;80:853-924.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 3
    • 0021646425 scopus 로고
    • 2+-activation of striated muscle contraction
    • 2+-activation of striated muscle contraction. Biophys J. 1984;46:541-543.
    • (1984) Biophys J , vol.46 , pp. 541-543
    • Shiner, J.S.1    Solaro, R.J.2
  • 5
    • 0025174179 scopus 로고
    • Calcium binds cooperatively to the regulatory sites of the cardiac thin filaments
    • Tobacman LS, Sawyer D. Calcium binds cooperatively to the regulatory sites of the cardiac thin filaments. J Biol Chem. 1990;265:931-939.
    • (1990) J Biol Chem , vol.265 , pp. 931-939
    • Tobacman, L.S.1    Sawyer, D.2
  • 7
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman LS. Thin filament-mediated regulation of cardiac contraction. Annu Rev Physiol. 1996;58:447-481.
    • (1996) Annu Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 8
    • 0033574547 scopus 로고    scopus 로고
    • 2+, cross-bridge kinetics or molecular cooperation
    • 2+, cross-bridge kinetics or molecular cooperation. Circ Res. 1999;84:862-865.
    • (1999) Circ Res , vol.84 , pp. 862-865
    • Moss, R.L.1
  • 9
    • 0023747148 scopus 로고
    • Cooperative turning on of myosin subfragment 1 adenosinetriphosphatase activity by the troponin-tropomyosin-actin complex
    • Williams DL, Greene LE, Eisenberg E. Cooperative turning on of myosin subfragment 1 adenosinetriphosphatase activity by the troponin-tropomyosin-actin complex. Biochemistry. 1988;27:6987-6993.
    • (1988) Biochemistry , vol.27 , pp. 6987-6993
    • Williams, D.L.1    Greene, L.E.2    Eisenberg, E.3
  • 10
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • Geeves MA, Lehrer SS. Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys J. 1994;67:273-282.
    • (1994) Biophys J , vol.67 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 11
    • 0029840598 scopus 로고    scopus 로고
    • Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils
    • Swartz DR, Moss RL, Greaser ML. Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils. Biophys J. 1996;71:1891-1904.
    • (1996) Biophys J , vol.71 , pp. 1891-1904
    • Swartz, D.R.1    Moss, R.L.2    Greaser, M.L.3
  • 12
    • 0026774946 scopus 로고
    • Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers
    • Swartz DR, Moss RL. Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers. J Biol Chem. 1992;267:20497-20506.
    • (1992) J Biol Chem , vol.267 , pp. 20497-20506
    • Swartz, D.R.1    Moss, R.L.2
  • 13
    • 0035862210 scopus 로고    scopus 로고
    • Cross-bridge interaction kinetics in rat myocardium are accelerated by strong binding of myosin to the thin filament
    • Fitzsimons DP, Patel JR, Moss RL. Cross-bridge interaction kinetics in rat myocardium are accelerated by strong binding of myosin to the thin filament. J Physiol. 2001;530:263-272.
    • (2001) J Physiol , vol.530 , pp. 263-272
    • Fitzsimons, D.P.1    Patel, J.R.2    Moss, R.L.3
  • 14
    • 0034123345 scopus 로고    scopus 로고
    • Different myofilament nearest-neighbor interactions have distinctive effects on contractile behavior
    • Razumova MV, Bukatina AE, Campbell KB. Different myofilament nearest-neighbor interactions have distinctive effects on contractile behavior. Biophys J. 2000;78:3120-3137.
    • (2000) Biophys J , vol.78 , pp. 3120-3137
    • Razumova, M.V.1    Bukatina, A.E.2    Campbell, K.B.3
  • 15
    • 0033579814 scopus 로고    scopus 로고
    • Cooperativity and switching within the three-state model of muscle regulation
    • Maytum R, Lehrer SS, Geeves MA. Cooperativity and switching within the three-state model of muscle regulation. Biochemistry. 1999;38:1102-1110.
    • (1999) Biochemistry , vol.38 , pp. 1102-1110
    • Maytum, R.1    Lehrer, S.S.2    Geeves, M.A.3
  • 16
    • 21844517087 scopus 로고
    • 2+ regulatory protein complex in cardiac muscle
    • 2+ regulatory protein complex in cardiac muscle. News Physiol Sci. 1995;10:6-12.
    • (1995) News Physiol Sci , vol.10 , pp. 6-12
    • Fuchs, F.1
  • 17
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel RD, Weber A. Cooperation within actin filament in vertebrate skeletal muscle. Nat New Biol. 1972;238:97-101.
    • (1972) Nat New Biol , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 18
    • 0023644924 scopus 로고
    • Calcium-binding properties of troponin C in detergent-skinned heart muscle fibers
    • Pan B-S, Solaro RJ. Calcium-binding properties of troponin C in detergent-skinned heart muscle fibers. J Biol Chem. 1987;262:7839-7849.
    • (1987) J Biol Chem , vol.262 , pp. 7839-7849
    • Pan, B.-S.1    Solaro, R.J.2
  • 19
    • 0023645610 scopus 로고
    • 2+-specific regulatory sites in skinned rabbit psoas muscles
    • 2+-specific regulatory sites in skinned rabbit psoas muscles. J Biol Chem. 1987;262:13627-13635.
    • (1987) J Biol Chem , vol.262 , pp. 13627-13635
    • Guth, K.1    Potter, J.D.2
  • 20
    • 0026803026 scopus 로고
    • Effects of cycling and rigor crossbridges on the conformation of cardiac troponin C
    • Hannon JD, Martyn DA, Gordon AM. Effects of cycling and rigor crossbridges on the conformation of cardiac troponin C. Circ Res. 1992;71:984-991.
    • (1992) Circ Res , vol.71 , pp. 984-991
    • Hannon, J.D.1    Martyn, D.A.2    Gordon, A.M.3
  • 21
    • 0032589143 scopus 로고    scopus 로고
    • 2+ and cross-bridge-induced changes in troponin C in skinned skeletal muscle fibers: Effect of force inhibition
    • 2+ and cross-bridge-induced changes in troponin C in skinned skeletal muscle fibers: effect of force inhibition. Biophys J. 1999;76:1480-1493.
    • (1999) Biophys J , vol.76 , pp. 1480-1493
    • Martyn, D.A.1    Freitag, C.J.2    Chase, P.B.3    Gordon, A.M.4
  • 22
    • 0023472695 scopus 로고
    • Extra calcium on shortening in barnacle muscle: Is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length?
    • Gordon AM, Ridgway EB. Extra calcium on shortening in barnacle muscle: is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length? J Gen Physiol. 1987;90:321-340.
    • (1987) J Gen Physiol , vol.90 , pp. 321-340
    • Gordon, A.M.1    Ridgway, E.B.2
  • 23
    • 0024242326 scopus 로고
    • Calcium concentration in the myoplasm of skinned ferret ventricular muscle following changes in muscle length
    • Allen DG, Kentish JC. Calcium concentration in the myoplasm of skinned ferret ventricular muscle following changes in muscle length. J Physiol. 1988;407:489-503.
    • (1988) J Physiol , vol.407 , pp. 489-503
    • Allen, D.G.1    Kentish, J.C.2
  • 25
    • 0026319614 scopus 로고
    • 2+-troponin C affinity in skeletal muscle
    • 2+-troponin C affinity in skeletal muscle. Am J Physiol. 1991;261:C787-C792.
    • (1991) Am J Physiol , vol.261
    • Fuchs, F.1    Wang, Y.-P.2
  • 26
    • 0027974349 scopus 로고
    • 2+-troponin C affinity in cardiac and slow skeletal muscle
    • 2+-troponin C affinity in cardiac and slow skeletal muscle. Am J Physiol. 1994; 266:C1077-C1082.
    • (1994) Am J Physiol , vol.266
    • Wang, Y.-P.1    Fuchs, F.2
  • 27
    • 0036409388 scopus 로고    scopus 로고
    • Activation of striated muscle: Nearest-neighbor regulatory unit and cross-bridge influence on myofilament kinetics
    • Robinson JM, Wang Y, Kerrick GL, Kawai R, Cheung HC. Activation of striated muscle: nearest-neighbor regulatory unit and cross-bridge influence on myofilament kinetics. J Mol Biol. 2002;322:1065-1088.
    • (2002) J Mol Biol , vol.322 , pp. 1065-1088
    • Robinson, J.M.1    Wang, Y.2    Kerrick, G.L.3    Kawai, R.4    Cheung, H.C.5
  • 28
    • 0025605176 scopus 로고
    • Regulation of binding of subfragment 1 in isolated rigor myofibrils
    • Swartz DR, Greaser ML, Marsh BB. Regulation of binding of subfragment 1 in isolated rigor myofibrils. J Cell Biol. 1990;111:2989-3001.
    • (1990) J Cell Biol , vol.111 , pp. 2989-3001
    • Swartz, D.R.1    Greaser, M.L.2    Marsh, B.B.3
  • 29
    • 0034084355 scopus 로고    scopus 로고
    • Influence of ADP on cross-bridge-dependent activation of myofibrillar thin filaments
    • Zhang D, Yancey KW, Swartz DR. Influence of ADP on cross-bridge-dependent activation of myofibrillar thin filaments. Biophys J. 2000;78:3103-3111.
    • (2000) Biophys J , vol.78 , pp. 3103-3111
    • Zhang, D.1    Yancey, K.W.2    Swartz, D.R.3
  • 30
    • 0027315793 scopus 로고
    • Tension transients initiated by photogeneration of MgADP in skinned skeletal muscle fibers
    • Lu Z, Moss RL, Walker JW. Tension transients initiated by photogeneration of MgADP in skinned skeletal muscle fibers. J Gen Physiol. 1993;101:867-888.
    • (1993) J Gen Physiol , vol.101 , pp. 867-888
    • Lu, Z.1    Moss, R.L.2    Walker, J.W.3
  • 31
    • 0034961156 scopus 로고    scopus 로고
    • Regulation of force development studied by photolysis of caged ADP in rabbit skinned psoas fibers
    • Lu Z, Swartz DR, Metzger JM, Moss RL, Walker JW. Regulation of force development studied by photolysis of caged ADP in rabbit skinned psoas fibers. Biophys J. 2001;81:334-344.
    • (2001) Biophys J , vol.81 , pp. 334-344
    • Lu, Z.1    Swartz, D.R.2    Metzger, J.M.3    Moss, R.L.4    Walker, J.W.5
  • 32
    • 0028053976 scopus 로고
    • Kinetics of relaxation from rigor or permeabilized fast-twitch skeletal fibers from rabbit using a novel caged ATP and apyrase
    • Thirwell H, Corrie JET, Reid GP, Trentham DR, Ferenczi MA. Kinetics of relaxation from rigor or permeabilized fast-twitch skeletal fibers from rabbit using a novel caged ATP and apyrase. Biophys J. 1994;67:2346-2447.
    • (1994) Biophys J , vol.67 , pp. 2346-2447
    • Thirwell, H.1    Corrie, J.E.T.2    Reid, G.P.3    Trentham, D.R.4    Ferenczi, M.A.5
  • 33
    • 0026067741 scopus 로고
    • Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibers
    • Dantzig JA, Hibberd MG, Trentham DR, Goldman YE. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibers, J Physiol. 1991;432:639-680.
    • (1991) J Physiol , vol.432 , pp. 639-680
    • Dantzig, J.A.1    Hibberd, M.G.2    Trentham, D.R.3    Goldman, Y.E.4
  • 34
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers
    • Dantzig JA, Goldman YE, Millar NC, Lacktis J, Homsher E. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers. J Physiol. 1992;451:247-278.
    • (1992) J Physiol , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Millar, N.C.3    Lacktis, J.4    Homsher, E.5
  • 35
    • 0026609631 scopus 로고
    • 2+ on the kinetics of phosphate release in skeletal muscle
    • 2+ on the kinetics of phosphate release in skeletal muscle. J Biol Chem. 1992;267:2459-2466.
    • (1992) J Biol Chem , vol.267 , pp. 2459-2466
    • Walker, J.W.1    Lu, Z.2    Moss, R.L.3
  • 36
    • 0020024384 scopus 로고
    • Studies on co-operative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment 1
    • Nagashima H, Asakura S. Studies on co-operative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment 1. J Mol Biol. 1982;155:409-428.
    • (1982) J Mol Biol , vol.155 , pp. 409-428
    • Nagashima, H.1    Asakura, S.2
  • 37
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DFA, Geeves MA. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J. 1993;65:693-701.
    • (1993) Biophys J , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 38
    • 0031038445 scopus 로고    scopus 로고
    • Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics
    • Campbell K. Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics. Biophys J. 1997;72:254-262.
    • (1997) Biophys J , vol.72 , pp. 254-262
    • Campbell, K.1
  • 39
    • 0030965265 scopus 로고    scopus 로고
    • Cooperative effect of calcium binding to adjacent troponin molecules on the thin filament-myosin subfragment 1 MgATPase rate
    • Butters CA, Tobacman JB, Tobacman LS. Cooperative effect of calcium binding to adjacent troponin molecules on the thin filament-myosin subfragment 1 MgATPase rate. J Biol Chem. 1997;272:13196-13202.
    • (1997) J Biol Chem , vol.272 , pp. 13196-13202
    • Butters, C.A.1    Tobacman, J.B.2    Tobacman, L.S.3
  • 40
    • 0032540229 scopus 로고    scopus 로고
    • The muscle thin filament as a classical cooperative/allosteric regulatory system
    • Lehrer SS, Geeves MA. The muscle thin filament as a classical cooperative/allosteric regulatory system. J Mol Biol. 1998;277:1081-1089.
    • (1998) J Mol Biol , vol.277 , pp. 1081-1089
    • Lehrer, S.S.1    Geeves, M.A.2
  • 41
    • 0035002723 scopus 로고    scopus 로고
    • Cooperative mechanisms in the activation dependence of the rate of force development in rabbit skinned skeletal muscle fibers
    • Fitzsimons DP, Patel JR, Campbell KS, Moss RL. Cooperative mechanisms in the activation dependence of the rate of force development in rabbit skinned skeletal muscle fibers. J Gen Physiol. 2001;117:133-148.
    • (2001) J Gen Physiol , vol.117 , pp. 133-148
    • Fitzsimons, D.P.1    Patel, J.R.2    Campbell, K.S.3    Moss, R.L.4
  • 42
    • 0035109415 scopus 로고    scopus 로고
    • Pathophysiology of cardiac muscle contraction and relaxation as a result of alterations in thin filament regulation
    • Hernandez OM, Housmans PR, Potter JD. Pathophysiology of cardiac muscle contraction and relaxation as a result of alterations in thin filament regulation. J Appl Physiol. 2001;90:1125-1136.
    • (2001) J Appl Physiol , vol.90 , pp. 1125-1136
    • Hernandez, O.M.1    Housmans, P.R.2    Potter, J.D.3
  • 43
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomyosin ATPase activity in solution
    • Brenner B, Eisenberg E. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc Natl Acad Sci U S A. 1986;83:3542-3546.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 44
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff MR, McDonald KS, Moss RL. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ Res. 1995;76:154-160.
    • (1995) Circ Res , vol.76 , pp. 154-160
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.3
  • 45
    • 0032572414 scopus 로고    scopus 로고
    • 2+ activation and relaxation in rat and guinea pig skinned trabeculae
    • 2+ activation and relaxation in rat and guinea pig skinned trabeculae. Circ Res. 1998;83:179-186.
    • (1998) Circ Res , vol.83 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 46
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc Natl Acad Sci U S A. 1988;85:3265-3269.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 47
    • 0028005290 scopus 로고
    • Coupling calcium binding to troponin C and cross-bridge cycling in skinned cardiac cells
    • Landesberg A, Sideman S. Coupling calcium binding to troponin C and cross-bridge cycling in skinned cardiac cells. Am J Physiol. 1994;266: H1260-H1271.
    • (1994) Am J Physiol , vol.266
    • Landesberg, A.1    Sideman, S.2
  • 48
    • 0022393454 scopus 로고
    • Suppression of muscle contraction by vanadate
    • Dantzig JA, Goldman YE. Suppression of muscle contraction by vanadate. J Gen Physiol. 1985;86:305-327.
    • (1985) J Gen Physiol , vol.86 , pp. 305-327
    • Dantzig, J.A.1    Goldman, Y.E.2
  • 49
    • 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
    • Brenner B, Chalovich JM. 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. 1999;77:2692-2708.
    • (1999) Biophys J , vol.77 , pp. 2692-2708
    • Brenner, B.1    Chalovich, J.M.2
  • 50
    • 0021755958 scopus 로고
    • The thin filament of vertebrate skeletal muscle co-operatively activates as a unit
    • Brandt PW, Diamond MS, Schachat FH. The thin filament of vertebrate skeletal muscle co-operatively activates as a unit. J Mol Biol. 1984;180:379-384.
    • (1984) J Mol Biol , vol.180 , pp. 379-384
    • Brandt, P.W.1    Diamond, M.S.2    Schachat, F.H.3
  • 51
    • 0022412866 scopus 로고
    • The effects of partial extraction of TnC upon the tension-pCa relationship in rabbit skinned skeletal muscle fibers
    • Moss RL, Giulian GG, Greaser ML. The effects of partial extraction of TnC upon the tension-pCa relationship in rabbit skinned skeletal muscle fibers. J Gen Physiol. 1985;86:585-600.
    • (1985) J Gen Physiol , vol.86 , pp. 585-600
    • Moss, R.L.1    Giulian, G.G.2    Greaser, M.L.3
  • 52
    • 0028178083 scopus 로고
    • α-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, Vosberg H-P, Seidman CE. α-Tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere. Cell. 1994;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    Vosberg, H.-P.6    Seidman, C.E.7
  • 53
    • 0032555955 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy: From mutations to functional deficits
    • Bonne G, Carrier L, Richard P, Hainque B, Schwartz K. Familial hypertrophic cardiomyopathy: from mutations to functional deficits. Circ Res. 1998;83:580-593.
    • (1998) Circ Res , vol.83 , pp. 580-593
    • Bonne, G.1    Carrier, L.2    Richard, P.3    Hainque, B.4    Schwartz, K.5
  • 54
    • 0036787237 scopus 로고    scopus 로고
    • Molecular mechanisms of inherited cardiomyopathies
    • Fatkin D, Graham RM. Molecular mechanisms of inherited cardiomyopathies. Physiol Rev. 2002;82:945-980.
    • (2002) Physiol Rev , vol.82 , pp. 945-980
    • Fatkin, D.1    Graham, R.M.2
  • 55
    • 0346120211 scopus 로고    scopus 로고
    • Modulafion of thin filament activation by breakdown or isoform switching of thin filament proteins
    • Marston SB, Redwood CS. Modulafion of thin filament activation by breakdown or isoform switching of thin filament proteins. Circ Res. 2003;93:1170-1178.
    • (2003) Circ Res , vol.93 , pp. 1170-1178
    • Marston, S.B.1    Redwood, C.S.2
  • 56
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert P, Craig R, Lehman W. Steric-model for activation of muscle thin filaments. J Mol Biol. 1997;266:8-14.
    • (1997) J Mol Biol , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 57
    • 0035979730 scopus 로고    scopus 로고
    • Crossbridge and tropomyosin positions observed in native, interacting thick and thin filaments
    • Craig R, Lehman W. Crossbridge and tropomyosin positions observed in native, interacting thick and thin filaments. J Mol Biol. 2001;311:1027-1036.
    • (2001) J Mol Biol , vol.311 , pp. 1027-1036
    • Craig, R.1    Lehman, W.2
  • 58
    • 0038637756 scopus 로고    scopus 로고
    • The role of tropomyosin in the regulation of myocardial contraction and relaxation
    • Wolska BM, Wieczorek DF. The role of tropomyosin in the regulation of myocardial contraction and relaxation. Pflugers Arch. 2003;446:1-8.
    • (2003) Pflugers Arch , vol.446 , pp. 1-8
    • Wolska, B.M.1    Wieczorek, D.F.2
  • 59
    • 0024349096 scopus 로고
    • Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle
    • Pan B-S, Gordon AM, Luo Z. Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle. J Biol Chem. 1989;264:8495-8498.
    • (1989) J Biol Chem , vol.264 , pp. 8495-8498
    • Pan, B.-S.1    Gordon, A.M.2    Luo, Z.3
  • 64
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro RJ, Rarick HM. Troponin and tropomyosin: proteins that switch on and tune in the activity of cardiac myofilaments. Circ Res. 1998;83:471-480.
    • (1998) Circ Res , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.M.2
  • 66
    • 0037119477 scopus 로고    scopus 로고
    • A modulatory role for the troponin T tail domain in thin filament regulation
    • Maytum R, Geeves MA, Lehrer SS. A modulatory role for the troponin T tail domain in thin filament regulation. J Biol Chem. 2002;277:29774-29780.
    • (2002) J Biol Chem , vol.277 , pp. 29774-29780
    • Maytum, R.1    Geeves, M.A.2    Lehrer, S.S.3
  • 67
    • 0037008682 scopus 로고    scopus 로고
    • The troponin tail domain promotes a conformational state of the thin filament that suppresses myosin activity
    • Tobacman LS, Nihli M, Butters C, Heller M, Hatch V, Craig R, Lehman W, Homsher E. The troponin tail domain promotes a conformational state of the thin filament that suppresses myosin activity. J Biol Chem. 2002;277:27636-27642.
    • (2002) J Biol Chem , vol.277 , pp. 27636-27642
    • Tobacman, L.S.1    Nihli, M.2    Butters, C.3    Heller, M.4    Hatch, V.5    Craig, R.6    Lehman, W.7    Homsher, E.8
  • 68
    • 0033214347 scopus 로고    scopus 로고
    • Fast skeletal muscle troponin T increases the cooperativity of transgenic mouse cardiac muscle contraction
    • Huang Q-Q, Brozovich FV, Jin J-P. Fast skeletal muscle troponin T increases the cooperativity of transgenic mouse cardiac muscle contraction. J Physiol. 1999;520:231-242.
    • (1999) J Physiol , vol.520 , pp. 231-242
    • Huang, Q.-Q.1    Brozovich, F.V.2    Jin, J.-P.3
  • 69
    • 0037414799 scopus 로고    scopus 로고
    • Folding and function of the troponin tail domain
    • Hinkle A, Tobacman LS. Folding and function of the troponin tail domain. J Biol Chem. 2003;278:506-513.
    • (2003) J Biol Chem , vol.278 , pp. 506-513
    • Hinkle, A.1    Tobacman, L.S.2
  • 73
    • 0026453190 scopus 로고
    • Complete nucleotide sequence and structural organization of rat cardiac troponin T gene
    • Jin JP, Huang QQ, Yeh HI, Lin JJC. Complete nucleotide sequence and structural organization of rat cardiac troponin T gene. 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.C.4
  • 74
    • 0030598902 scopus 로고    scopus 로고
    • Alternative RNA splicing-generated cardiac troponin T isoform switching: A non-heart-restricted genetic programming synchronized in developing cardiac and skeletal muscles
    • Jin J-P. Alternative RNA splicing-generated cardiac troponin T isoform switching: a non-heart-restricted genetic programming synchronized in developing cardiac and skeletal muscles. Biochem Biophys Res Commun. 1996;225:883-889.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 883-889
    • Jin, J.-P.1
  • 75
    • 0025216711 scopus 로고
    • 2+ binding associated with troponin T isoform switching in developing rabbit heart
    • 2+ binding associated with troponin T isoform switching in developing rabbit heart. Circ Res. 1990;66:1204-1216.
    • (1990) Circ Res , vol.66 , pp. 1204-1216
    • McAuliffe, J.J.1    Gao, L.2    Solaro, R.J.3
  • 77
    • 0028135302 scopus 로고
    • Tension production and thin filament protein isoforms in developing rat myocardium
    • Reiser PJ, Westfall MV, Schiaffino S, Solaro RJ. Tension production and thin filament protein isoforms in developing rat myocardium. Am J Physiol. 1994;267:H1589-H1596.
    • (1994) Am J Physiol , vol.267
    • Reiser, P.J.1    Westfall, M.V.2    Schiaffino, S.3    Solaro, R.J.4
  • 81
    • 0033548486 scopus 로고    scopus 로고
    • Roles for the troponin tail domain in thin filament assembly and regulation
    • Hinkle A, Goranson A, Butters CA, Tobacman LS. Roles for the troponin tail domain in thin filament assembly and regulation. J Biol Chem. 1999;274:7157-7164.
    • (1999) J Biol Chem , vol.274 , pp. 7157-7164
    • Hinkle, A.1    Goranson, A.2    Butters, C.A.3    Tobacman, L.S.4
  • 82
    • 0036278593 scopus 로고    scopus 로고
    • Isometric force kinetics upon rapid activation and relaxation of mouse, guinea pig and human heart muscle studied on the subcellular myofibrillar level
    • Stehle R, Kruger M, Scherer P, Brixius K, Schwinger RHG, Pfitzer G. Isometric force kinetics upon rapid activation and relaxation of mouse, guinea pig and human heart muscle studied on the subcellular myofibrillar level. Basic Res Cardiol. 2002;97:127-135.
    • (2002) Basic Res Cardiol , vol.97 , pp. 127-135
    • Stehle, R.1    Kruger, M.2    Scherer, P.3    Brixius, K.4    Schwinger, R.H.G.5    Pfitzer, G.6
  • 83
    • 0014797705 scopus 로고
    • A quick phase in the series-elastic component of striated muscle, demonstrated in isolated fibres from the frog
    • Huxley AF, Simmons RM. A quick phase in the series-elastic component of striated muscle, demonstrated in isolated fibres from the frog. J Physiol. 1970;208:52P-53P.
    • (1970) J Physiol , vol.208
    • Huxley, A.F.1    Simmons, R.M.2
  • 85
    • 0032518823 scopus 로고    scopus 로고
    • 2+ concentration after length changes in isolated rat ventricular trabeculae
    • 2+ concentration after length changes in isolated rat ventricular trabeculae. J Physiol. 1998;506:431-444.
    • (1998) J Physiol , vol.506 , pp. 431-444
    • Kentish, J.C.1    Wrzosek, A.2
  • 86
    • 0036795565 scopus 로고    scopus 로고
    • Length-dependent activation in three striated muscle types of the rat
    • Konhilas JP, Irving TC, deTombe PP. Length-dependent activation in three striated muscle types of the rat. J Physiol. 2002;544:225-236.
    • (2002) J Physiol , vol.544 , pp. 225-236
    • Konhilas, J.P.1    Irving, T.C.2    DeTombe, P.P.3
  • 87
    • 0037059456 scopus 로고    scopus 로고
    • Myofilament calcium sensitivity in skinned rat cardiac trabeculae: Role of interfilament spacing
    • Konhilas JP, Irving TC, de Tombe PP. Myofilament calcium sensitivity in skinned rat cardiac trabeculae: role of interfilament spacing. Circ Res. 2002;90:59-65.
    • (2002) Circ Res , vol.90 , pp. 59-65
    • Konhilas, J.P.1    Irving, T.C.2    De Tombe, P.P.3
  • 88
    • 0032555957 scopus 로고    scopus 로고
    • 2+ activation of rat ventricular myocytes
    • 2+ activation of rat ventricular myocytes. Circ Res. 1998;83:602-607.
    • (1998) Circ Res , vol.83 , pp. 602-607
    • Fitzsimons, D.P.1    Moss, R.L.2
  • 89
    • 0035977144 scopus 로고    scopus 로고
    • The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation
    • Davis JA, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, Aletras AH, Wen H, Epstein ND. The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation. Cell. 2001;107:631-641.
    • (2001) Cell , vol.107 , pp. 631-641
    • Davis, J.A.1    Hassanzadeh, S.2    Winitsky, S.3    Lin, H.4    Satorius, C.5    Vemuri, R.6    Aletras, A.H.7    Wen, H.8    Epstein, N.D.9
  • 90
    • 0018260965 scopus 로고
    • Stretch activation of muscle: Function and mechanism
    • Pringle JWS. Stretch activation of muscle: function and mechanism. Proc R Soc Lond B Biol Sci. 1978;201:107-130.
    • (1978) Proc R Soc Lond B Biol Sci , vol.201 , pp. 107-130
    • Pringle, J.W.S.1
  • 91
    • 0027517018 scopus 로고
    • Interplay between passive tension and strong and weak binding cross-bridges in insect indirect flight muscle
    • Granzier HL, Wang K. Interplay between passive tension and strong and weak binding cross-bridges in insect indirect flight muscle. J Gen Physiol. 1993;101:235-270.
    • (1993) J Gen Physiol , vol.101 , pp. 235-270
    • Granzier, H.L.1    Wang, K.2
  • 92
    • 0036623918 scopus 로고    scopus 로고
    • Cardiac titin: An adjustable multi-functional spring
    • Granzier H, Labeit S. Cardiac titin: an adjustable multi-functional spring. J Physiol. 2002;541:335-342.
    • (2002) J Physiol , vol.541 , pp. 335-342
    • Granzier, H.1    Labeit, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.