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Volumn 90, Issue 5, 2006, Pages 1697-1722

A quantitative analysis of cardiac myocyte relaxation: A simulation study

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; TROPOMYOSIN; TROPONIN C; CALCIUM;

EID: 33646131626     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.069534     Document Type: Article
Times cited : (176)

References (151)
  • 1
    • 0023756766 scopus 로고
    • 2+ sensitivity and twitch relaxation induced by adrenergic and cholinergic stimulation in isolated ferret cardiac muscle
    • 2+ sensitivity and twitch relaxation induced by adrenergic and cholinergic stimulation in isolated ferret cardiac muscle. J. Gen. Physiol. 92:509-529.
    • (1988) J. Gen. Physiol. , vol.92 , pp. 509-529
    • McIvor, M.1    Orchard, C.2    Lakatta, E.3
  • 3
    • 0032520057 scopus 로고    scopus 로고
    • Calcium cycling and contractile activation in intact mouse cardiac muscle
    • Gao, W. D., N. G. Perez, and E. Marban. 1998. Calcium cycling and contractile activation in intact mouse cardiac muscle. J. Physiol. (Lond.). 507:175-184.
    • (1998) J. Physiol. (Lond.) , vol.507 , pp. 175-184
    • Gao, W.D.1    Perez, N.G.2    Marban, E.3
  • 4
    • 0028855563 scopus 로고
    • Force, not sarcomere length, correlates with prolongation of isosarcometric contraction
    • Janssen, P. M., and W. C. Hunter. 1995. Force, not sarcomere length, correlates with prolongation of isosarcometric contraction. Am. J. Physiol. 269:H676-H685.
    • (1995) Am. J. Physiol. , vol.269
    • Janssen, P.M.1    Hunter, W.C.2
  • 6
    • 0029037870 scopus 로고
    • Cardiac Troponin I phosphorylation increases the rate of cardiac muscle relaxation
    • Zhang, R., J. Zhao, A. Mandveno, and J. D. Potter. 1995. Cardiac Troponin I phosphorylation increases the rate of cardiac muscle relaxation. Circ. Res. 76:1028-1035.
    • (1995) Circ. Res. , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4
  • 7
    • 0036088280 scopus 로고    scopus 로고
    • Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat
    • Janssen, P. M. L., L. B. Stull, and E. Marban. 2002. Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat. Am. J. Physiol. 282:H499-H507.
    • (2002) Am. J. Physiol. , vol.282
    • Janssen, P.M.L.1    Stull, L.B.2    Marban, E.3
  • 8
    • 0034064353 scopus 로고    scopus 로고
    • Modeling short-term interval-force relations in cardiac muscle
    • Rice, J. J., M. S. Jafri, and R. L. Winslow. 2000. Modeling short-term interval-force relations in cardiac muscle. Am. J. Physiol. 278:H913-H931.
    • (2000) Am. J. Physiol. , vol.278
    • Rice, J.J.1    Jafri, M.S.2    Winslow, R.L.3
  • 12
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro, R.J., and H.M. Rarick. 1998. Troponin and tropomyosin: proteins that switch on and tune in the activity of cardiac myofilaments. Circ. Res. 83:471-480.
    • (1998) Circ. Res. , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.M.2
  • 13
    • 0019293605 scopus 로고
    • The calcium and magnesium binding-sites on cardiac troponin and their role in the regulation of myofibrillar adenosine-triphosphatase
    • Holroyde, M. J., S. P. Robertson, J. D. Johnson, R. J. Solaro, and J. D. Potter. 1980. The calcium and magnesium binding-sites on cardiac troponin and their role in the regulation of myofibrillar adenosine-triphosphatase. J. Biol. Chem. 255:1688-1693.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1688-1693
    • Holroyde, M.J.1    Robertson, S.P.2    Johnson, J.D.3    Solaro, R.J.4    Potter, J.D.5
  • 15
    • 17944398302 scopus 로고
    • Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum
    • Fabiato, A. 1983. Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am. J. Physiol. 245:C1-C14.
    • (1983) Am. J. Physiol. , vol.245
    • Fabiato, A.1
  • 16
    • 0016200406 scopus 로고
    • Calcium requirements for cardiac myofibrillar activation
    • Solaro, R. J., R. M. Wise, J. S. Shiner, and F. N. Briggs. 1974. Calcium requirements for cardiac myofibrillar activation. Circ. Res. 34:525-530.
    • (1974) Circ. Res. , vol.34 , pp. 525-530
    • Solaro, R.J.1    Wise, R.M.2    Shiner, J.S.3    Briggs, F.N.4
  • 20
    • 0030052282 scopus 로고    scopus 로고
    • Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle
    • Dong, W. J., S. S. Rosenfeld, C. K. Wang, A. M. Gordon, and H. C. Cheung. 1996. Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle. J. Biol. Chem. 271:688-694.
    • (1996) J. Biol. Chem. , vol.271 , pp. 688-694
    • Dong, W.J.1    Rosenfeld, S.S.2    Wang, C.K.3    Gordon, A.M.4    Cheung, H.C.5
  • 21
    • 0028966335 scopus 로고
    • Troponin-I isoforms and differential effects of acidic pH on soleus and cardiac myofilaments
    • Wattanapermpool, J., P .J. Reiser, and R. J. Solaro. 1995. Troponin-I isoforms and differential effects of acidic pH on soleus and cardiac myofilaments. Am. J. Physiol. 37:C323-C330.
    • (1995) Am. J. Physiol. , vol.37
    • Wattanapermpool, J.1    Reiser, P.J.2    Solaro, R.J.3
  • 24
    • 0036655688 scopus 로고    scopus 로고
    • Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy
    • Li, M. X., E. J. Saude, X. Wang, J. R. Pearlstone, L. B. Smillie, and B. D. Sykes. 2002. Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy. Eur. Biophys. J. 31:245-256.
    • (2002) Eur. Biophys. J. , vol.31 , pp. 245-256
    • Li, M.X.1    Saude, E.J.2    Wang, X.3    Pearlstone, J.R.4    Smillie, L.B.5    Sykes, B.D.6
  • 25
    • 4143085980 scopus 로고    scopus 로고
    • Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C
    • Tikunova, S. B., and J. P. Davis. 2004. Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C. J. Biol. Chem. 279:35341-35352.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35341-35352
    • Tikunova, S.B.1    Davis, J.P.2
  • 26
    • 0034964228 scopus 로고    scopus 로고
    • Localization of regions of troponin I important in deactivation of cardiac myofilaments by acidic pH
    • Li, G., A. F. Martin, and R. J. Solaro. 2001. Localization of regions of troponin I important in deactivation of cardiac myofilaments by acidic pH. J. Mol. Cell. Cardiol. 33:1309-1320.
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1309-1320
    • Li, G.1    Martin, A.F.2    Solaro, R.J.3
  • 27
    • 0025174179 scopus 로고
    • Calcium binds cooperatively to the regulatory sites of the cardiac thin filament
    • Tobacman, L. S., and D. Sawyer. 1990. Calcium binds cooperatively to the regulatory sites of the cardiac thin filament. J. Biol. Chem. 265:931-939.
    • (1990) J. Biol. Chem. , vol.265 , pp. 931-939
    • Tobacman, L.S.1    Sawyer, D.2
  • 28
    • 0023644924 scopus 로고
    • Calcium-binding properties of troponin-C in detergent-skinned heart muscle fibers
    • Pan, B. S., and R. J. Solaro. 1987. Calcium-binding properties of troponin-C in detergent-skinned heart muscle fibers. J. Biol. Chem. 262:7839-7849.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7839-7849
    • Pan, B.S.1    Solaro, R.J.2
  • 30
    • 0021192049 scopus 로고
    • Regulation of actomyosin ATPase by a single calcium-binding site on troponin C from crayfish
    • Wnuk, W., M. Schoechlin, and E. Stein. 1984. Regulation of actomyosin ATPase by a single calcium-binding site on troponin C from crayfish. J. Biol. Chem. 259:9017-9023.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9017-9023
    • Wnuk, W.1    Schoechlin, M.2    Stein, E.3
  • 31
    • 0023797004 scopus 로고
    • 2+ activation and the inotropic effect of pimobendan - Comparison with milrinone
    • 2+ activation and the inotropic effect of pimobendan - comparison with milrinone. Circ. Res. 63:911-922.
    • (1988) Circ. Res. , vol.63 , pp. 911-922
    • Fujino, K.1    Sperelakis, N.2    Solaro, R.J.3
  • 32
    • 0023694749 scopus 로고
    • Bound calcium and force development in skinned cardiac muscle bundles - Effect of sarcomere-length
    • Hofmann, P. A., and F. Fuchs. 1988. Bound calcium and force development in skinned cardiac muscle bundles - effect of sarcomere-length. J. Mol. Cell. Cardiol. 20:667-677.
    • (1988) J. Mol. Cell. Cardiol. , vol.20 , pp. 667-677
    • Hofmann, P.A.1    Fuchs, F.2
  • 33
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium-binding to cardiac troponin-C
    • Hofmann, P. A., and F. Fuchs. 1987. Evidence for a force-dependent component of calcium-binding to cardiac troponin-C. Am. J. Physiol. 253:C541-C546.
    • (1987) Am. J. Physiol. , vol.253
    • Hofmann, P.A.1    Fuchs, F.2
  • 34
    • 10344259253 scopus 로고
    • 2+ and force development in detergent-extracted cardiac muscle bundles - Effect of sarcomere length
    • 2+ and force development in detergent-extracted cardiac muscle bundles - effect of sarcomere length. Biophys. J. 51:A463.
    • (1987) Biophys. J. , vol.51
    • Hofmann, P.A.1    Fuchs, F.2
  • 36
    • 0017102987 scopus 로고
    • 2+ binding on troponin C. Changes in spin label mobility, extrinsic fluorescence, and sulfhydryl reactivity
    • 2+ binding on troponin C. Changes in spin label mobility, extrinsic fluorescence, and sulfhydryl reactivity. J. Biol. Chem. 251:7551-7556.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7551-7556
    • Potter, J.D.1    Seidel, J.C.2    Leavis, P.3    Lehrer, S.S.4    Gergely, J.5
  • 37
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter, J. D., and J. Gergely. 1975. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250:4628-4633.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 39
    • 33646142004 scopus 로고
    • 2+ to skinned muscle fibers at short sarcomere length - Comparison of skeletal and cardiac muscle
    • 2+ to skinned muscle fibers at short sarcomere length - comparison of skeletal and cardiac muscle. Biophys. J. 53:A566-A566.
    • (1988) Biophys. J. , vol.53
    • Fuchs, F.1    Whaley, M.E.2    Hofmann, P.A.3
  • 40
    • 33646135479 scopus 로고
    • 2+-binding in detergent-extracted cardiac muscle bundles
    • 2+-binding in detergent-extracted cardiac muscle bundles. Biophys. J. 47:A290.
    • (1985) Biophys. J. , vol.47
    • Hofmann, P.A.1    Fuchs, F.2
  • 44
    • 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. 266:C1077-C1082.
    • (1994) Am. J. Physiol. , vol.266
    • Wang, Y.P.1    Fuchs, F.2
  • 45
    • 0022627157 scopus 로고
    • Comparison between the sarcomere length-force relations of intact and skinned trabeculae from rat right ventricle - Influence of calcium concentrations on these relations
    • Kentish, J. C., H. Terkeurs, L. Ricciardi, J. J. J. Bucx, and M. I. M. Noble. 1986. Comparison between the sarcomere length-force relations of intact and skinned trabeculae from rat right ventricle - influence of calcium concentrations on these relations. Circ. Res. 58:755-768.
    • (1986) Circ. Res. , vol.58 , pp. 755-768
    • Kentish, J.C.1    Terkeurs, H.2    Ricciardi, L.3    Bucx, J.J.J.4    Noble, M.I.M.5
  • 46
    • 0036084317 scopus 로고    scopus 로고
    • Cooperative activation in cardiac muscle: Impact of sarcomere length
    • Dobesh, D. P., J. P. Konhilas, and P. P. de Tombe. 2002. Cooperative activation in cardiac muscle: impact of sarcomere length. Am. J. Physiol. 282:H1055-H1062.
    • (2002) Am. J. Physiol. , vol.282
    • Dobesh, D.P.1    Konhilas, J.P.2    De Tombe, P.P.3
  • 47
    • 0021916996 scopus 로고
    • Kinetic studies of calcium-binding to regulatory complexes from skeletal muscle
    • Rosenfeld, S. S., and E. W. Taylor. 1985. Kinetic studies of calcium-binding to regulatory complexes from skeletal muscle. J. Biol. Chem. 260:252-261.
    • (1985) J. Biol. Chem. , vol.260 , pp. 252-261
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 49
    • 0025194523 scopus 로고
    • 2+ release from cardiac troponin-C and the troponin-tropomyosin complex
    • 2+ release from cardiac troponin-C and the troponin-tropomyosin complex. Br. J. Pharmacol. 100:779-785.
    • (1990) Br. J. Pharmacol. , vol.100 , pp. 779-785
    • Smith, S.J.1    England, P.J.2
  • 51
    • 0037115194 scopus 로고    scopus 로고
    • Determinants of relaxation rate in rabbit skinned skeletal muscle fibres
    • Luo, Y., J. P. Davis, L. B. Smillie, and J. A. Rall. 2002. Determinants of relaxation rate in rabbit skinned skeletal muscle fibres. J. Physiol. (Lond.). 545:887-901.
    • (2002) J. Physiol. (Lond.) , vol.545 , pp. 887-901
    • Luo, Y.1    Davis, J.P.2    Smillie, L.B.3    Rall, J.A.4
  • 53
    • 0031793436 scopus 로고    scopus 로고
    • The kinetic cycle of cardiac troponin C: Calcium binding and dissociation at site II trigger slow conformational rearrangements
    • Hazard, A. L., S. C. Kohout, N. L. Stricker, J. A. Putkey, and J. J. Falke. 1998. The kinetic cycle of cardiac troponin C: calcium binding and dissociation at site II trigger slow conformational rearrangements. Protein Sci. 7:2451-2459.
    • (1998) Protein Sci. , vol.7 , pp. 2451-2459
    • Hazard, A.L.1    Kohout, S.C.2    Stricker, N.L.3    Putkey, J.A.4    Falke, J.J.5
  • 55
    • 0020002214 scopus 로고
    • The effects of muscle length on intracellular calcium transients in mammalian cardiac-muscle
    • Allen, D. G., and S. Kurihara. 1982. The effects of muscle length on intracellular calcium transients in mammalian cardiac-muscle. J. Physiol. (Lond.). 327:79-94.
    • (1982) J. Physiol. (Lond.) , vol.327 , pp. 79-94
    • Allen, D.G.1    Kurihara, S.2
  • 56
    • 0024242326 scopus 로고
    • Calcium-concentration in the myoplasm of skinned ferret ventricular muscle following changes in muscle length
    • Allen, D. G., and J. C. Kentish. 1988. Calcium-concentration in the myoplasm of skinned ferret ventricular muscle following changes in muscle length. J. Physiol. (Lond.). 407:489-503.
    • (1988) J. Physiol. (Lond.) , vol.407 , pp. 489-503
    • Allen, D.G.1    Kentish, J.C.2
  • 58
    • 0026048386 scopus 로고
    • EMD-53998 sensitizes the contractile proteins to calcium in intact ferret ventricular muscle
    • Lee, J. A., and D. G. Allen. 1991. EMD-53998 sensitizes the contractile proteins to calcium in intact ferret ventricular muscle. Circ. Res. 69:927-936.
    • (1991) Circ. Res. , vol.69 , pp. 927-936
    • Lee, J.A.1    Allen, D.G.2
  • 61
    • 0034788580 scopus 로고    scopus 로고
    • Protein kinase a increases the rate of relaxation but not the rate of tension development in skinned rat cardiac muscle
    • Saeki, Y., K. Takigiku, H. Iwamoto, S. Yasuda, H. Yamashita, S. Sugiura, and H. Sugi. 2001. Protein kinase A increases the rate of relaxation but not the rate of tension development in skinned rat cardiac muscle. Jpn. J. Physiol. 51:427-433.
    • (2001) Jpn. J. Physiol. , vol.51 , pp. 427-433
    • Saeki, Y.1    Takigiku, K.2    Iwamoto, H.3    Yasuda, S.4    Yamashita, H.5    Sugiura, S.6    Sugi, H.7
  • 62
    • 0032533986 scopus 로고    scopus 로고
    • Role of myosin heavy chain composition in kinetics of force development and relaxation in rat myocardium
    • Fitzsimons, D. P., J. R. Patel, and R. L. Moss. 1998. Role of myosin heavy chain composition in kinetics of force development and relaxation in rat myocardium. J. Physiol. (Lond.). 513:171-183.
    • (1998) J. Physiol. (Lond.) , vol.513 , pp. 171-183
    • Fitzsimons, D.P.1    Patel, J.R.2    Moss, R.L.3
  • 63
    • 0030611731 scopus 로고    scopus 로고
    • 2+ sensitizers caffeine and CGP 48506 on the relaxation rate of rat skinned cardiac trabeculae
    • 2+ sensitizers caffeine and CGP 48506 on the relaxation rate of rat skinned cardiac trabeculae. Circ. Res. 80:682-687.
    • (1997) Circ. Res. , vol.80 , pp. 682-687
    • Palmer, S.1    Kentish, J.C.2
  • 64
    • 0030935930 scopus 로고    scopus 로고
    • Troponin I phosphorylation does not increase the rate of relaxation following laser flash photolysis of diazo-2 in guinea-pig skinned trabeculae
    • Johns, E. C., S. J. Simnett, I. P. Mulligan, and C. C. Ashley. 1997. Troponin I phosphorylation does not increase the rate of relaxation following laser flash photolysis of diazo-2 in guinea-pig skinned trabeculae. Pflueg. Arch. Eur. J. Physiol. 433:842-844.
    • (1997) Pflueg. Arch. Eur. J. Physiol. , vol.433 , pp. 842-844
    • Johns, E.C.1    Simnett, S.J.2    Mulligan, I.P.3    Ashley, C.C.4
  • 65
    • 33750856767 scopus 로고    scopus 로고
    • Effect of pH, phosphate, and ADP on relaxation of myocardium after photolysis of diazo-2
    • Simnett, S. J., E. C. Johns, S. Lipscomb, I. P. Mulligan, and C. C. Ashley. 1998. Effect of pH, phosphate, and ADP on relaxation of myocardium after photolysis of diazo-2. Am. J. Physiol. 275:H951-H960.
    • (1998) Am. J. Physiol. , vol.275
    • Simnett, S.J.1    Johns, E.C.2    Lipscomb, S.3    Mulligan, I.P.4    Ashley, C.C.5
  • 66
    • 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. 83:179-186.
    • (1998) Circ. Res. , vol.83 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 68
    • 0029739913 scopus 로고    scopus 로고
    • Altered interactions among thin filament proteins modulate cardiac function: A clarification
    • Babu, A., E. H. Sonnenblick, and J. Gulati. 1996. Altered interactions among thin filament proteins modulate cardiac function: a clarification. J. Mol. Cell. Cardiol. 28:1829-1830.
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 1829-1830
    • Babu, A.1    Sonnenblick, E.H.2    Gulati, J.3
  • 70
    • 0023986488 scopus 로고
    • Molecular basis for the influence of muscle length on myocardial performance
    • Babu, A., E. Sonnenblick, and J. Gulati. 1988. Molecular basis for the influence of muscle length on myocardial performance. Science. 240:74-76.
    • (1988) Science , vol.240 , pp. 74-76
    • Babu, A.1    Sonnenblick, E.2    Gulati, J.3
  • 71
    • 0032555957 scopus 로고    scopus 로고
    • 2+ activation of rat ventricular myocytes
    • 2+ activation of rat ventricular myocytes. Circ. Res. 83:602-607.
    • (1998) Circ. Res. , vol.83 , pp. 602-607
    • Fitzsimons, D.P.1    Moss, R.L.2
  • 72
    • 0035797846 scopus 로고    scopus 로고
    • Length dependence of tension generation in rat skinned cardiac muscle: Role of titin in the Frank-Starling mechanism of the heart
    • Fukuda, N., D. Sasaki, S. Ishiwata, and S. Kurihara. 2001. Length dependence of tension generation in rat skinned cardiac muscle: role of titin in the Frank-Starling mechanism of the heart. Circulation. 104:1639-1645.
    • (2001) Circulation , vol.104 , pp. 1639-1645
    • Fukuda, N.1    Sasaki, D.2    Ishiwata, S.3    Kurihara, S.4
  • 73
    • 0029029477 scopus 로고
    • 2+ sensitivity of tension at short sarcomere-length
    • 2+ sensitivity of tension at short sarcomere-length. Circ. Res. 77:199-205.
    • (1995) Circ. Res. , vol.77 , pp. 199-205
    • McDonald, K.S.1    Moss, R.L.2
  • 74
    • 0037059456 scopus 로고    scopus 로고
    • Myofilament calcium sensitivity in skinned rat cardiac trabeculae: Role of interfilament spacing
    • Konhilas, J., T. Irving, and P. P. de Tombe. 2002. Myofilament calcium sensitivity in skinned rat cardiac trabeculae: role of interfilament spacing. Circ. Res. 90:59-65.
    • (2002) Circ. Res. , vol.90 , pp. 59-65
    • Konhilas, J.1    Irving, T.2    De Tombe, P.P.3
  • 75
    • 0037059562 scopus 로고    scopus 로고
    • Frank-Starling relationship: Long on importance, short on mechanism
    • Moss, R. L., and D. P. Fitzsimons. 2002. Frank-Starling relationship: long on importance, short on mechanism. Circ. Res. 90:11-13.
    • (2002) Circ. Res. , vol.90 , pp. 11-13
    • Moss, R.L.1    Fitzsimons, D.P.2
  • 76
    • 2442438820 scopus 로고    scopus 로고
    • Approaches to modeling crossbridges and calcium-dependent activation in cardiac muscle
    • Rice, J. J., and P. P. de Tombe. 2004. Approaches to modeling crossbridges and calcium-dependent activation in cardiac muscle. Prog. Biophys. Mol. Biol. 85:179-195.
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 179-195
    • Rice, J.J.1    De Tombe, P.P.2
  • 77
    • 0020000435 scopus 로고
    • Calcium-dependent and length-dependent force production in rat ventricular muscle
    • Hibberd, M. G., and B. R. Jewell. 1982. Calcium-dependent and length-dependent force production in rat ventricular muscle. J. Physiol. (Lond.). 329:527-540.
    • (1982) J. Physiol. (Lond.) , vol.329 , pp. 527-540
    • Hibberd, M.G.1    Jewell, B.R.2
  • 78
    • 33751264946 scopus 로고    scopus 로고
    • The Frank-Starling mechanism is not mediated by changes in rate of cross-bridge detachment
    • Wannenburg, T., P. M. L. Janssen, D. Fan, and P. P. De Tombe. 1997. The Frank-Starling mechanism is not mediated by changes in rate of cross-bridge detachment. Am. J. Physiol. 273:H2428-H2435.
    • (1997) Am. J. Physiol. , vol.273
    • Wannenburg, T.1    Janssen, P.M.L.2    Fan, D.3    De Tombe, P.P.4
  • 79
    • 0025606303 scopus 로고
    • 2+-sensitive force in permeabilized myocardium and skeletal muscle. Evidence for force dependence of thin filament activation
    • 2+-sensitive force in permeabilized myocardium and skeletal muscle. Evidence for force dependence of thin filament activation. J. Gen. Physiol. 96:1221-1245.
    • (1990) J. Gen. Physiol. , vol.96 , pp. 1221-1245
    • Sweitzer, N.1    Moss, R.2
  • 80
    • 0035162942 scopus 로고    scopus 로고
    • Effects of MgATP on ATP utilization and force under normal and simulated ischaemic conditions in rat cardiac trabeculae
    • Ebus, J. P., Z. Papp, R. Zaremba, and G. J. M. Stienen. 2001. Effects of MgATP on ATP utilization and force under normal and simulated ischaemic conditions in rat cardiac trabeculae. Pflueg. Arch. Eur. J. Physiol. 443:102-111.
    • (2001) Pflueg. Arch. Eur. J. Physiol. , vol.443 , pp. 102-111
    • Ebus, J.P.1    Papp, Z.2    Zaremba, R.3    Stienen, G.J.M.4
  • 81
    • 1142310677 scopus 로고    scopus 로고
    • Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA
    • Martin, H., M. G. Bell, G. C. R. Ellis-Davies, and R. J. Barsotti. 2004. Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA. Biophys. J. 86:978-990.
    • (2004) Biophys. J. , vol.86 , pp. 978-990
    • Martin, H.1    Bell, M.G.2    Ellis-Davies, G.C.R.3    Barsotti, R.J.4
  • 83
    • 0036795565 scopus 로고    scopus 로고
    • Length-dependent activation in three striated muscle types of the rat
    • Konhilas, J. P., T. C. Irving, and P. P. de Tombe. 2002. Length-dependent activation in three striated muscle types of the rat. J. Physiol. (Lond.). 544:225-236.
    • (2002) J. Physiol. (Lond.) , vol.544 , pp. 225-236
    • Konhilas, J.P.1    Irving, T.C.2    De Tombe, P.P.3
  • 84
    • 0026579874 scopus 로고
    • Effects of calcium on shortening velocity in frog chemically skinned atrial myocytes and in mechanically disrupted ventricular myocardium from rat
    • Hofmann, P. A., and R. L. Moss. 1992. Effects of calcium on shortening velocity in frog chemically skinned atrial myocytes and in mechanically disrupted ventricular myocardium from rat. Circ. Res. 70:885-892.
    • (1992) Circ. Res. , vol.70 , pp. 885-892
    • Hofmann, P.A.1    Moss, R.L.2
  • 85
    • 0032840186 scopus 로고    scopus 로고
    • Tropomyosin modulates pH dependence of isometric tension
    • Fujita, H., and S. Ishiwata. 1999. Tropomyosin modulates pH dependence of isometric tension. Biophys. J. 77:1540-1546.
    • (1999) Biophys. J. , vol.77 , pp. 1540-1546
    • Fujita, H.1    Ishiwata, S.2
  • 86
    • 0033151961 scopus 로고    scopus 로고
    • Length modulation of active force in rat cardiac myocytes: Is titin the sensor?
    • Cazorla, O., G. Vassort, D. Garnier, and J.-Y. Le Guennec. 1999. Length modulation of active force in rat cardiac myocytes: is titin the sensor? J. Mol. Cell. Cardiol. 31:1215-1227.
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 1215-1227
    • Cazorla, O.1    Vassort, G.2    Garnier, D.3    Le Guennec, J.-Y.4
  • 87
    • 0023259508 scopus 로고
    • Role of creatine kinase in force development in chemically skinned rat cardiac muscle
    • Ventura-Clapier, R., H. Mekhfi, and G. Vassort. 1987. Role of creatine kinase in force development in chemically skinned rat cardiac muscle. J. Gen. Physiol. 89:815-837.
    • (1987) J. Gen. Physiol. , vol.89 , pp. 815-837
    • Ventura-Clapier, R.1    Mekhfi, H.2    Vassort, G.3
  • 88
    • 0037101918 scopus 로고    scopus 로고
    • The mechanism of the force enhancement by MgADP under simulated ischaemic conditions in rat cardiac myocytes
    • Papp, Z., A. Szabo, J. P. Barends, and G. J. M. Stienen. 2002. The mechanism of the force enhancement by MgADP under simulated ischaemic conditions in rat cardiac myocytes. J. Physiol. (Lond.). 543:177-189.
    • (2002) J. Physiol. (Lond.) , vol.543 , pp. 177-189
    • Papp, Z.1    Szabo, A.2    Barends, J.P.3    Stienen, G.J.M.4
  • 90
  • 91
    • 0023028528 scopus 로고
    • Fast skeletal muscle skinned fibers and myofibrils reconstituted with N- Terminal fluorescent analogues of troponin C
    • Zot, H., K. Guth, and J. Potter. 1986. Fast skeletal muscle skinned fibers and myofibrils reconstituted with N- terminal fluorescent analogues of troponin C. J. Biol. Chem. 261:15883-15890.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15883-15890
    • Zot, H.1    Guth, K.2    Potter, J.3
  • 93
    • 0026322150 scopus 로고
    • Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit
    • Andrews, M., D. Maughan, T. Nosek, and R. Godt. 1991. Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit. J. Gen. Physiol. 98:1105-1125.
    • (1991) J. Gen. Physiol. , vol.98 , pp. 1105-1125
    • Andrews, M.1    Maughan, D.2    Nosek, T.3    Godt, R.4
  • 95
    • 0029028751 scopus 로고
    • 2+ responsiveness and altered diastolic function in intact ventricular muscle
    • 2+ responsiveness and altered diastolic function in intact ventricular muscle. Circ. Res. 76:1036-1048.
    • (1995) Circ. Res. , vol.76 , pp. 1036-1048
    • Gao, W.D.1    Atar, D.2    Backx, P.H.3    Marban, E.4
  • 97
    • 0033668412 scopus 로고    scopus 로고
    • Myofilament lattice spacing as a function of sarcomere length in isolated rat myocardium
    • Irving, T. C., J. Konhilas, D. Perry, R. Fischetti, and P. P. de Tombe. 2000. Myofilament lattice spacing as a function of sarcomere length in isolated rat myocardium. Am. J. Physiol. 279:H2568-2573.
    • (2000) Am. J. Physiol. , vol.279
    • Irving, T.C.1    Konhilas, J.2    Perry, D.3    Fischetti, R.4    De Tombe, P.P.5
  • 98
    • 0041426228 scopus 로고    scopus 로고
    • Relationship between isometric force and myofibrillar MgATPase at short sarcomere length in skeletal and cardiac muscle and its relevance to the concept of activation heat
    • Stephenson, D. G. 2003. Relationship between isometric force and myofibrillar MgATPase at short sarcomere length in skeletal and cardiac muscle and its relevance to the concept of activation heat. Clin. Exp. Pharmacol. Physiol. 30:570-575.
    • (2003) Clin. Exp. Pharmacol. Physiol. , vol.30 , pp. 570-575
    • Stephenson, D.G.1
  • 99
    • 0036454919 scopus 로고    scopus 로고
    • Frank-Starling law of the heart and the cellular mechanisms of length-dependent activation
    • Konhilas, J., T. Irving, and P. de Tombe. 2002. Frank-Starling law of the heart and the cellular mechanisms of length-dependent activation. Pflueg. Arch. Eur. J. Physiol. 445:305-310.
    • (2002) Pflueg. Arch. Eur. J. Physiol. , vol.445 , pp. 305-310
    • Konhilas, J.1    Irving, T.2    De Tombe, P.3
  • 101
    • 0034886046 scopus 로고    scopus 로고
    • High-throughput assessment of calcium sensitivity in skinned cardiac myocytes
    • Lim, C. C., M. H. B. Helmes, D. B. Sawyer, M. Jain, and R. Liao. 2001. High-throughput assessment of calcium sensitivity in skinned cardiac myocytes. Am. J. Physiol. 281:H969-H974.
    • (2001) Am. J. Physiol. , vol.281
    • Lim, C.C.1    Helmes, M.H.B.2    Sawyer, D.B.3    Jain, M.4    Liao, R.5
  • 102
    • 4544268959 scopus 로고    scopus 로고
    • Strain softening behaviour in nonviable rat right-ventricular trabeculae, in the presence and the absence of butanedione monoxime
    • Kirton, R. S., A. J. Taberner, P. M. F. Nielsen, A. A. Young, and D. S. Loiselle. 2004. Strain softening behaviour in nonviable rat right-ventricular trabeculae, in the presence and the absence of butanedione monoxime. Exp. Physiol. 89:593-604.
    • (2004) Exp. Physiol. , vol.89 , pp. 593-604
    • Kirton, R.S.1    Taberner, A.J.2    Nielsen, P.M.F.3    Young, A.A.4    Loiselle, D.S.5
  • 103
    • 0032078310 scopus 로고    scopus 로고
    • Length dependence of calcium- and force-transients in normal and failing human myocardium
    • Vahl, C.F., T. Timek, A. Bonz, H. Fuchs, R. Dillman, and S. Hagl. 1998. Length dependence of calcium- and force-transients in normal and failing human myocardium. J. Mol. Cell. Cardiol. 30:957-966.
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 957-966
    • Vahl, C.F.1    Timek, T.2    Bonz, A.3    Fuchs, H.4    Dillman, R.5    Hagl, S.6
  • 105
    • 0026101345 scopus 로고
    • Sarcomere dynamics in cat cardiac trabeculae
    • de Tombe, P. P., and H. ter Keurs. 1991. Sarcomere dynamics in cat cardiac trabeculae. Circ. Res. 68:588-596.
    • (1991) Circ. Res. , vol.68 , pp. 588-596
    • Tombe, P.P.1    Ter Keurs, H.2
  • 106
    • 0028303529 scopus 로고
    • Effects of acidosis on maximum shortening velocity and force-velocity relation of skinned rat cardiac muscle
    • Ricciardi, L., R. Bottinelli, M. Canepari, and C. Reggiani. 1994. Effects of acidosis on maximum shortening velocity and force-velocity relation of skinned rat cardiac muscle. J. Mol. Cell. Cardiol. 26:601-607.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 601-607
    • Ricciardi, L.1    Bottinelli, R.2    Canepari, M.3    Reggiani, C.4
  • 107
    • 0026709820 scopus 로고
    • An internal viscous element limits unloaded velocity of sarcomere shortening in rat myocardium
    • de Tombe, P. P., and H. ter Keurs. 1992. An internal viscous element limits unloaded velocity of sarcomere shortening in rat myocardium. J. Physiol. (Lond.). 454:619-642.
    • (1992) J. Physiol. (Lond.) , vol.454 , pp. 619-642
    • Tombe, P.P.1    Ter Keurs, H.2
  • 108
    • 0034828977 scopus 로고    scopus 로고
    • Loaded shortening and power output in cardiac myocytes are dependent on myosin heavy chain isoform expression
    • Herron, T. J., F. S. Korte, and K. S.McDonald. 2001. Loaded shortening and power output in cardiac myocytes are dependent on myosin heavy chain isoform expression. Am. J. Physiol. 281:H1217-H1222.
    • (2001) Am. J. Physiol. , vol.281
    • Herron, T.J.1    Korte, F.S.2    McDonald, K.S.3
  • 109
    • 0037405905 scopus 로고    scopus 로고
    • Altered single cell force-velocity and power properties in exercise-trained rat myocardium
    • Diffee, G. M., and E. Chung. 2003. Altered single cell force-velocity and power properties in exercise-trained rat myocardium. J. Appl. Physiol. 94:1941-1948.
    • (2003) J. Appl. Physiol. , vol.94 , pp. 1941-1948
    • Diffee, G.M.1    Chung, E.2
  • 110
    • 3242733977 scopus 로고    scopus 로고
    • Inorganic phosphate speeds loaded shortening in rat skinned cardiac myocytes
    • Hinken, A. C., and K. S. McDonald. 2004. Inorganic phosphate speeds loaded shortening in rat skinned cardiac myocytes. Am. J. Physiol. 287:C500-C507.
    • (2004) Am. J. Physiol. , vol.287
    • Hinken, A.C.1    McDonald, K.S.2
  • 111
    • 0025253704 scopus 로고
    • Force and velocity of sarcomere shortening in trabeculae from rat heart - Effects of temperature
    • de Tombe, P. P., and H. ter Keurs. 1990. Force and velocity of sarcomere shortening in trabeculae from rat heart - effects of temperature. Circ. Res. 66:1239-1254.
    • (1990) Circ. Res. , vol.66 , pp. 1239-1254
    • De Tombe, P.P.1    Ter Keurs, H.2
  • 112
    • 0024994297 scopus 로고
    • Steady-state force velocity relation in the ATP-dependent sliding movement of myosin-coated beads on actin cables in vitro studied with a centrifuge microscope
    • Oiwa, K., S. Chaen, E. Kamitsubo, T. Shimmen, and H. Sugi. 1990. Steady-state force velocity relation in the ATP-dependent sliding movement of myosin-coated beads on actin cables in vitro studied with a centrifuge microscope. Proc. Natl. Acad. Sci. U. S. A. 87:7893-7897.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 7893-7897
    • Oiwa, K.1    Chaen, S.2    Kamitsubo, E.3    Shimmen, T.4    Sugi, H.5
  • 113
    • 1842339908 scopus 로고    scopus 로고
    • The biphasic force-velocity relationship in frog muscle fibres and its evaluation in terms of cross-bridge function
    • Edman, K., A. Mansson, and C. Caputo. 1997. The biphasic force-velocity relationship in frog muscle fibres and its evaluation in terms of cross-bridge function. J. Physiol. (Lond.). 503:141-156.
    • (1997) J. Physiol. (Lond.) , vol.503 , pp. 141-156
    • Edman, K.1    Mansson, A.2    Caputo, C.3
  • 114
    • 0026026686 scopus 로고
    • Comparison of crossbridge dynamics between intact and skinned myocardium from ferret right ventricles
    • Saeki, Y., M. Kawai, and Y. Zhao. 1991. Comparison of crossbridge dynamics between intact and skinned myocardium from ferret right ventricles. Circ. Res. 68:772-781.
    • (1991) Circ. Res. , vol.68 , pp. 772-781
    • Saeki, Y.1    Kawai, M.2    Zhao, Y.3
  • 115
    • 0019308296 scopus 로고
    • Sinusoidal analysis: A high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish
    • Kawai, M., and P. Brandt. 1980. Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish. J. Muscle Res. Cell Motil. 1:279-303.
    • (1980) J. Muscle Res. Cell Motil. , vol.1 , pp. 279-303
    • Kawai, M.1    Brandt, P.2
  • 116
    • 0022764709 scopus 로고
    • Influence of V1 and V3 isomyosins on the mechanical behavior of rat papillary muscle as studied by pseudorandom binary noise-modulated length perturbations
    • Rossmanith, G. H., J. F. Y. Hoh, A. Kirman, and L. J. Kwan. 1986. Influence of V1 and V3 isomyosins on the mechanical behavior of rat papillary muscle as studied by pseudorandom binary noise-modulated length perturbations. J. Muscle Res. Cell Motil. 7:307-319.
    • (1986) J. Muscle Res. Cell Motil. , vol.7 , pp. 307-319
    • Rossmanith, G.H.1    Hoh, J.F.Y.2    Kirman, A.3    Kwan, L.J.4
  • 118
    • 0027216259 scopus 로고
    • Crossbridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret
    • Kawai, M., Y. Saeki, and Y. Zhao. 1993. crossbridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. Circ. Res. 73:35-50.
    • (1993) Circ. Res. , vol.73 , pp. 35-50
    • Kawai, M.1    Saeki, Y.2    Zhao, Y.3
  • 119
    • 0023236882 scopus 로고
    • Dynamic stiffness of barium-contractured cardiac muscles with different speeds of contraction
    • Shibata, T., W. C. Hunter, and K. Sagawa. 1987. Dynamic stiffness of barium-contractured cardiac muscles with different speeds of contraction. Circ. Res. 60:770-779.
    • (1987) Circ. Res. , vol.60 , pp. 770-779
    • Shibata, T.1    Hunter, W.C.2    Sagawa, K.3
  • 120
    • 0023280319 scopus 로고
    • Dynamic stiffness measured in central segment of excised rabbit papillary-muscles during barium contracture
    • Shibata, T., W. C. Hunter, A. Yang, and K. Sagawa. 1987. Dynamic stiffness measured in central segment of excised rabbit papillary-muscles during barium contracture. Circ. Res. 60:756-769.
    • (1987) Circ. Res. , vol.60 , pp. 756-769
    • Shibata, T.1    Hunter, W.C.2    Yang, A.3    Sagawa, K.4
  • 123
    • 0037059561 scopus 로고    scopus 로고
    • Alterations of myocardial dynamic stiffness implicating abnormal crossbridge function in human mitral regurgitation heart failure
    • Mulieri, L. A., W. Barnes, B. J. Leavitt, F. P. Ittleman, M. M. LeWinter, N. R. Alpert, and D. W. Maughan. 2002. Alterations of myocardial dynamic stiffness implicating abnormal crossbridge function in human mitral regurgitation heart failure. Circ. Res. 90:66-72.
    • (2002) Circ. Res. , vol.90 , pp. 66-72
    • Mulieri, L.A.1    Barnes, W.2    Leavitt, B.J.3    Ittleman, F.P.4    Lewinter, M.M.5    Alpert, N.R.6    Maughan, D.W.7
  • 124
    • 0023740308 scopus 로고
    • Effect of isoproterenol on force transient time course and on stiffness spectra in rabbit papillary-muscle in barium contracture
    • Berman, M. R., J. N. Peterson, D. T. Yue, and W. C. Hunter. 1988. Effect of isoproterenol on force transient time course and on stiffness spectra in rabbit papillary-muscle in barium contracture. J. Mol. Cell. Cardiol. 20:415-426.
    • (1988) J. Mol. Cell. Cardiol. , vol.20 , pp. 415-426
    • Berman, M.R.1    Peterson, J.N.2    Yue, D.T.3    Hunter, W.C.4
  • 125
    • 4244093375 scopus 로고
    • The force response to sudden length changes in rat myocardium
    • Backx, P. H., and H. ter Keurs. 1988. The force response to sudden length changes in rat myocardium. Biophys. J. 53:167a.
    • (1988) Biophys. J. , vol.53
    • Backx, P.H.1    Ter Keurs, H.2
  • 126
    • 0014103605 scopus 로고
    • ATPase activity of myosin correlated with speed of muscle shortening
    • Barany, M. 1967. ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 50:197-218.
    • (1967) J. Gen. Physiol. , vol.50 , pp. 197-218
    • Barany, M.1
  • 127
    • 0037085511 scopus 로고    scopus 로고
    • Temperature effect on isometric tension is mediated by regulatory proteins tropomyosin and troponin in bovine myocardium
    • Fujita, H., and M. Kawai. 2002. Temperature effect on isometric tension is mediated by regulatory proteins tropomyosin and troponin in bovine myocardium. J. Physiol. (Lond.). 539:267-276.
    • (2002) J. Physiol. (Lond.) , vol.539 , pp. 267-276
    • Fujita, H.1    Kawai, M.2
  • 128
    • 0026009517 scopus 로고
    • Combined inhibitory actions of acidosis and phosphate on maximum force production in rat skinned cardiac muscle
    • Kentish, J. C. 1991. Combined inhibitory actions of acidosis and phosphate on maximum force production in rat skinned cardiac muscle. Pflueg. Arch. Eur. J. Physiol. 419:310-318.
    • (1991) Pflueg. Arch. Eur. J. Physiol. , vol.419 , pp. 310-318
    • Kentish, J.C.1
  • 131
    • 0031875561 scopus 로고    scopus 로고
    • Relationships between isometric and isotonic mechanical parameters and cross-bridge kinetics
    • Rossmanith, G. H., and O. B. Tjokorda. 1998. Relationships between isometric and isotonic mechanical parameters and cross-bridge kinetics. Clin. Exp. Pharmacol. Physiol. 25:522-535.
    • (1998) Clin. Exp. Pharmacol. Physiol. , vol.25 , pp. 522-535
    • Rossmanith, G.H.1    Tjokorda, O.B.2
  • 132
    • 0034049981 scopus 로고    scopus 로고
    • Doxorubicin impairs crossbridge turnover kinetics in skinned cardiac trabeculae after acute and chronic treatment
    • de Beer, E. L., A. E. Bottone, J. van der Velden, and E. E. Voest. 2000. Doxorubicin impairs crossbridge turnover kinetics in skinned cardiac trabeculae after acute and chronic treatment. Mol. Pharmacol. 57:1152-1157.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 1152-1157
    • De Beer, E.L.1    Bottone, A.E.2    Van Der Velden, J.3    Voest, E.E.4
  • 134
    • 0024363853 scopus 로고
    • Relaxation and diastole of the heart
    • Brutsaert, D. L., and S. U. Sys. 1989. Relaxation and diastole of the heart. Physiol. Rev. 69:1228-1315.
    • (1989) Physiol. Rev. , vol.69 , pp. 1228-1315
    • Brutsaert, D.L.1    Sys, S.U.2
  • 136
    • 0027337513 scopus 로고
    • 2+ and segment length dependence of isometric force kinetics intact ferret cardiac muscle
    • 2+ and segment length dependence of isometric force kinetics intact ferret cardiac muscle. Circ. Res. 73:603-611.
    • (1993) Circ. Res. , vol.73 , pp. 603-611
    • Hancock, W.O.1    Martyn, D.A.2    Huntsman, L.L.3
  • 137
    • 0018375111 scopus 로고
    • Origin of the instantaneous elasticity in single frog muscle fibers
    • Sugi, H., and T. Tameyasu. 1979. Origin of the instantaneous elasticity in single frog muscle fibers. Experientia (Basel). 35:227-228.
    • (1979) Experientia (Basel) , vol.35 , pp. 227-228
    • Sugi, H.1    Tameyasu, T.2
  • 139
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff, M.R., K.S. McDonald, and R.L. Moss. 1995. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ. Res. 76:154.
    • (1995) Circ. Res. , vol.76 , pp. 154
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.3
  • 140
    • 4644342938 scopus 로고    scopus 로고
    • Active force inhibition and stretch-induced force enhancement in frog muscle treated with BDM
    • Rassier, D.E., and W. Herzog. 2004. Active force inhibition and stretch-induced force enhancement in frog muscle treated with BDM. J. Appl. Physiol. 97:1395-1400.
    • (2004) J. Appl. Physiol. , vol.97 , pp. 1395-1400
    • Rassier, D.E.1    Herzog, W.2
  • 141
    • 0942287710 scopus 로고    scopus 로고
    • Considerations on the history dependence of muscle contraction
    • Rassier, D. E., and W. Herzog. 2004. Considerations on the history dependence of muscle contraction. J. Appl. Physiol. 96:419-427.
    • (2004) J. Appl. Physiol. , vol.96 , pp. 419-427
    • Rassier, D.E.1    Herzog, W.2
  • 142
    • 1542343926 scopus 로고    scopus 로고
    • Frequency- and afterload-dependent cardiac modulation in vivo by Troponin I with constitutively active protein kinase a phosphorylation sites
    • Takimoto, E., D. G. Soergel, P. M. L. Janssen, L. B. Stull, D. A. Kass, and A. M. Murphy. 2004. Frequency- and afterload-dependent cardiac modulation in vivo by Troponin I with constitutively active protein kinase A phosphorylation sites. Circ. Res. 94:496-504.
    • (2004) Circ. Res. , vol.94 , pp. 496-504
    • Takimoto, E.1    Soergel, D.G.2    Janssen, P.M.L.3    Stull, L.B.4    Kass, D.A.5    Murphy, A.M.6
  • 143
    • 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. (Lond.). 506:431-444.
    • (1998) J. Physiol. (Lond.) , vol.506 , pp. 431-444
    • Kentish, J.C.1    Wrzosek, A.2
  • 144
    • 0345490810 scopus 로고    scopus 로고
    • Origin of contractile dysfunction in heart failure - Calcium cycling versus myofilaments
    • Perez, N. G., K. Hashimoto, S. McCune, R. A. Altschuld, and E. Marban. 1999. Origin of contractile dysfunction in heart failure - calcium cycling versus myofilaments. Circulation. 99:1077-1083.
    • (1999) Circulation , vol.99 , pp. 1077-1083
    • Perez, N.G.1    Hashimoto, K.2    McCune, S.3    Altschuld, R.A.4    Marban, E.5
  • 145
    • 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., M. Kruger, P. Scherer, K. Brixius, R. H. G. Schwinger, and G. Pfitzer. 2002. 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. 97:1435-1803.
    • (2002) Basic Res. Cardiol. , vol.97 , pp. 1435-1803
    • Stehle, R.1    Kruger, M.2    Scherer, P.3    Brixius, K.4    Schwinger, R.H.G.5    Pfitzer, G.6
  • 146
    • 0142187297 scopus 로고    scopus 로고
    • Mechanism of cross-bridge detachment in isometric force relaxation of skeletal and cardiac myofibrils
    • Belus, A., N. Piroddi, and C. Tesi. 2003. Mechanism of cross-bridge detachment in isometric force relaxation of skeletal and cardiac myofibrils. J. Muscle Res. Cell Motil. 24:263-269.
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 263-269
    • Belus, A.1    Piroddi, N.2    Tesi, C.3
  • 147
    • 10944234639 scopus 로고    scopus 로고
    • Integration from proteins to organs: The IUPS Physiome Project
    • Hunter, P., N. Smith, J. Fernandez, and M. Tawhai. 2005. Integration from proteins to organs: the IUPS Physiome Project. Mech. Ageing Dev. 126:187-192.
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 187-192
    • Hunter, P.1    Smith, N.2    Fernandez, J.3    Tawhai, M.4
  • 149
    • 0026093402 scopus 로고
    • Lack of effect of isoproterenol on unloaded velocity of sarcomere shortening in rat cardiac trabeculae
    • de Tombe, P. P., and H. ter Keurs. 1991. Lack of effect of isoproterenol on unloaded velocity of sarcomere shortening in rat cardiac trabeculae. Circ. Res. 68:382-391.
    • (1991) Circ. Res. , vol.68 , pp. 382-391
    • De Tombe, P.P.1    Ter Keurs, H.2
  • 150
    • 0032169429 scopus 로고    scopus 로고
    • Force-velocity and power-load curves in rat skinned cardiac myocytes
    • McDonald, K. S., M. R. Wolff, and R. L. Moss. 1998. Force-velocity and power-load curves in rat skinned cardiac myocytes. J. Physiol. (Lond.). 511:519-531.
    • (1998) J. Physiol. (Lond.) , vol.511 , pp. 519-531
    • McDonald, K.S.1    Wolff, M.R.2    Moss, R.L.3
  • 151
    • 0036156643 scopus 로고    scopus 로고
    • Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins
    • Fujita, H., D. Sasaki, S.I. Ishiwata, and M. Kawai. 2002. Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins. Biophys. J. 82:915-928.
    • (2002) Biophys. J. , vol.82 , pp. 915-928
    • Fujita, H.1    Sasaki, D.2    Ishiwata, S.I.3    Kawai, M.4


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