메뉴 건너뛰기




Volumn 48, Issue 5, 2010, Pages 843-850

Kinetics of cardiac sarcomeric processes and rate-limiting steps in contraction and relaxation

Author keywords

Cross bridge kinetics; Diastolic function; Myofibrillar relaxation; Sarcomere length; Systolic function; Thin filament regulation

Indexed keywords

ACTIN; CALCIUM ION; CONNECTIN; MYOSIN; REGULATOR PROTEIN; TROPOMYOSIN; TROPONIN;

EID: 77951620368     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2009.12.020     Document Type: Review
Times cited : (47)

References (85)
  • 2
    • 0036772442 scopus 로고    scopus 로고
    • Physiological determinants of contractile force generation and calcium handling in mouse myocardium
    • Stull L.B., Leppo M.K., Marban E., Janssen P.M. Physiological determinants of contractile force generation and calcium handling in mouse myocardium. J. Mol. Cell. Cardiol. 2002, 34:1367-1376.
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , pp. 1367-1376
    • Stull, L.B.1    Leppo, M.K.2    Marban, E.3    Janssen, P.M.4
  • 4
    • 39749141569 scopus 로고    scopus 로고
    • 2+ exchange with troponin C and cardiac muscle dynamics
    • 2+ exchange with troponin C and cardiac muscle dynamics. Cardiovasc. Res. 2008, 77:619-626.
    • (2008) Cardiovasc. Res. , vol.77 , pp. 619-626
    • Davis, J.P.1    Tikunova, S.B.2
  • 5
    • 44349116066 scopus 로고    scopus 로고
    • Structural basis for the regulation of muscle contraction by troponin and tropomyosin
    • Galinska-Rakoczy A., Engel P., Xu C., Jung H., Craig R., Tobacman L.S., et al. Structural basis for the regulation of muscle contraction by troponin and tropomyosin. J. Mol. Biol. 2008, 379:929-935.
    • (2008) J. Mol. Biol. , vol.379 , pp. 929-935
    • Galinska-Rakoczy, A.1    Engel, P.2    Xu, C.3    Jung, H.4    Craig, R.5    Tobacman, L.S.6
  • 6
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro R.J., Rarick H.M. 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
  • 7
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon A.M., 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
  • 8
    • 34247132324 scopus 로고    scopus 로고
    • A dominant role of cardiac molecular motors in the intrinsic regulation of ventricular ejection and relaxation
    • Hinken A.C., Solaro R.J. A dominant role of cardiac molecular motors in the intrinsic regulation of ventricular ejection and relaxation. Physiology (Bethesda) 2007, 22:73-80.
    • (2007) Physiology (Bethesda) , vol.22 , pp. 73-80
    • Hinken, A.C.1    Solaro, R.J.2
  • 9
  • 10
    • 56849111197 scopus 로고    scopus 로고
    • 2+ sensitizers
    • 2+ sensitizers. Circ. J. 2008, 72:1915-1925.
    • (2008) Circ. J. , vol.72 , pp. 1915-1925
    • Endoh, M.1
  • 11
    • 0028180467 scopus 로고
    • 2+-dependent and mechanical modulators of relaxation in mammalian myocardium
    • 2+-dependent and mechanical modulators of relaxation in mammalian myocardium. J. Mol. Cell. Cardiol. 1994, 26:243-250.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 243-250
    • Dobrunz, L.E.1    Berman, M.R.2
  • 12
    • 0036088280 scopus 로고    scopus 로고
    • Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat
    • Janssen P.M., Stull L.B., Marban E. Myofilament properties comprise the rate-limiting step for cardiac relaxation at body temperature in the rat. Am. J. Physiol. Heart. Circ. Physiol. 2002, 282:H499-507.
    • (2002) Am. J. Physiol. Heart. Circ. Physiol. , vol.282
    • Janssen, P.M.1    Stull, L.B.2    Marban, E.3
  • 13
    • 2842612680 scopus 로고    scopus 로고
    • Ser16-, but not Thr17-phosphorylation of phospholamban influences frequency-dependent force generation in human myocardium
    • Brixius K., Wollmer A., Bolck B., Mehlhorn U., Schwinger R.H. Ser16-, but not Thr17-phosphorylation of phospholamban influences frequency-dependent force generation in human myocardium. Pflugers. Arch. 2003, 447:150-157.
    • (2003) Pflugers. Arch. , vol.447 , pp. 150-157
    • Brixius, K.1    Wollmer, A.2    Bolck, B.3    Mehlhorn, U.4    Schwinger, R.H.5
  • 14
    • 33646183009 scopus 로고    scopus 로고
    • Kinetics of cardiac thin-filament activation probed by fluorescence polarization of rhodamine-labeled troponin C in skinned guinea pig trabeculae
    • Bell M.G., Lankford E.B., Gonye G.E., Ellis-Davies G.C., Martyn D.A., Regnier M., et al. Kinetics of cardiac thin-filament activation probed by fluorescence polarization of rhodamine-labeled troponin C in skinned guinea pig trabeculae. Biophys. J. 2006, 90:531-543.
    • (2006) Biophys. J. , vol.90 , pp. 531-543
    • Bell, M.G.1    Lankford, E.B.2    Gonye, G.E.3    Ellis-Davies, G.C.4    Martyn, D.A.5    Regnier, M.6
  • 17
    • 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 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. 1999, 77:2692-2708.
    • (1999) Biophys. J. , vol.77 , pp. 2692-2708
    • Brenner, B.1    Chalovich, J.M.2
  • 18
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit
    • Geeves M.A., Lehrer S.S. 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
  • 19
    • 0028928124 scopus 로고
    • Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases
    • Lionne C., Brune M., Webb M.R., Travers F., Barman T. Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases. FEBS. Lett. 1995, 364:59-62.
    • (1995) FEBS. Lett. , vol.364 , pp. 59-62
    • Lionne, C.1    Brune, M.2    Webb, M.R.3    Travers, F.4    Barman, T.5
  • 20
    • 0029924005 scopus 로고    scopus 로고
    • Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calcium
    • Araujo A., Walker J.W. Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calcium. Biophys. J. 1996, 70:2316-2326.
    • (1996) Biophys. J. , vol.70 , pp. 2316-2326
    • Araujo, A.1    Walker, J.W.2
  • 21
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd M.G., Dantzig J.A., Trentham D.R., Goldman Y.E. Phosphate release and force generation in skeletal muscle fibers. Science 1985, 228:1317-1319.
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Trentham, D.R.3    Goldman, Y.E.4
  • 22
    • 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 R.H., 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:I127-135.
    • (2002) Basic. Res. Cardiol. , vol.97
    • Stehle, R.1    Kruger, M.2    Scherer, P.3    Brixius, K.4    Schwinger, R.H.5    Pfitzer, G.6
  • 23
    • 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
  • 24
    • 33646365872 scopus 로고    scopus 로고
    • ATP splitting by half the cross-bridges can explain the twitch energetics of mouse papillary muscle
    • Widen C., Barclay C.J. ATP splitting by half the cross-bridges can explain the twitch energetics of mouse papillary muscle. J. Physiol. 2006, 573:5-15.
    • (2006) J. Physiol. , vol.573 , pp. 5-15
    • Widen, C.1    Barclay, C.J.2
  • 25
    • 1142310677 scopus 로고    scopus 로고
    • Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA
    • Martin H., Bell M.G., Ellis-Davies G.C., Barsotti R.J. Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA. Biophys. J. 2004, 86:978-990.
    • (2004) Biophys. J. , vol.86 , pp. 978-990
    • Martin, H.1    Bell, M.G.2    Ellis-Davies, G.C.3    Barsotti, R.J.4
  • 26
    • 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
  • 27
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff M.R., McDonald K.S., Moss R.L. 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
  • 29
    • 35348863108 scopus 로고    scopus 로고
    • Impact of temperature on cross-bridge cycling kinetics in rat myocardium
    • de Tombe P.P., Stienen G.J. Impact of temperature on cross-bridge cycling kinetics in rat myocardium. J. Physiol. 2007, 584:591-600.
    • (2007) J. Physiol. , vol.584 , pp. 591-600
    • de Tombe, P.P.1    Stienen, G.J.2
  • 30
    • 33847624646 scopus 로고    scopus 로고
    • Tension generation and relaxation in single myofibrils from human atrial and ventricular myocardium
    • Piroddi N., Belus A., Scellini B., Tesi C., Giunti G., Cerbai E., et al. Tension generation and relaxation in single myofibrils from human atrial and ventricular myocardium. Pflugers. Arch. 2007, 454:63-73.
    • (2007) Pflugers. Arch. , vol.454 , pp. 63-73
    • Piroddi, N.1    Belus, A.2    Scellini, B.3    Tesi, C.4    Giunti, G.5    Cerbai, E.6
  • 33
    • 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. USA. 1988, 85:3265-3269.
    • (1988) Proc. Natl. Acad. Sci. USA. , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 34
    • 26844566272 scopus 로고    scopus 로고
    • The molecular mechanism of muscle contraction
    • Geeves M.A., Holmes K.C. The molecular mechanism of muscle contraction. Adv. Protein. Chem. 2005, 71:161-193.
    • (2005) Adv. Protein. Chem. , vol.71 , pp. 161-193
    • Geeves, M.A.1    Holmes, K.C.2
  • 35
    • 25444484161 scopus 로고    scopus 로고
    • Initiation of the power stroke in muscle: insights from the phosphate analog AlF4
    • Kraft T., Mahlmann E., Mattei T., Brenner B. Initiation of the power stroke in muscle: insights from the phosphate analog AlF4. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:13861-13866.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 13861-13866
    • Kraft, T.1    Mahlmann, E.2    Mattei, T.3    Brenner, B.4
  • 36
    • 33749654402 scopus 로고    scopus 로고
    • Protein kinase A-mediated acceleration of the stretch activation response in murine skinned myocardium is eliminated by ablation of cMyBP-C
    • Stelzer J.E., Patel J.R., Moss R.L. Protein kinase A-mediated acceleration of the stretch activation response in murine skinned myocardium is eliminated by ablation of cMyBP-C. Circ. Res. 2006, 99:884-890.
    • (2006) Circ. Res. , vol.99 , pp. 884-890
    • Stelzer, J.E.1    Patel, J.R.2    Moss, R.L.3
  • 37
    • 0017729269 scopus 로고
    • Contractile and relaxation reserve of the left ventricle. I. Normal left ventricle (author's transl)
    • Bussmann W.D., Heeger J., Kaltenbach M. Contractile and relaxation reserve of the left ventricle. I. Normal left ventricle (author's transl). Z. Kardiol. 1977, 66:690-695.
    • (1977) Z. Kardiol. , vol.66 , pp. 690-695
    • Bussmann, W.D.1    Heeger, J.2    Kaltenbach, M.3
  • 40
    • 0020002214 scopus 로고
    • The effects of muscle length on intracellular calcium transients in mammalian cardiac muscle
    • Allen D.G., Kurihara S. The effects of muscle length on intracellular calcium transients in mammalian cardiac muscle. J. Physiol. 1982, 327:79-94.
    • (1982) J. Physiol. , vol.327 , pp. 79-94
    • Allen, D.G.1    Kurihara, S.2
  • 41
    • 0022393490 scopus 로고
    • The cellular basis of the length-tension relation in cardiac muscle
    • Allen D.G., Kentish J.C. The cellular basis of the length-tension relation in cardiac muscle. J. Moll. Cell. Cardiol. 1985, 17:821-840.
    • (1985) J. Moll. Cell. Cardiol. , vol.17 , pp. 821-840
    • Allen, D.G.1    Kentish, J.C.2
  • 42
    • 0032104084 scopus 로고    scopus 로고
    • Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: molecular basis for cardiac adaptation
    • Sugiura S., Kobayakawa N., Fujita H., Yamashita H., Momomura S., Chaen S., et al. Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: molecular basis for cardiac adaptation. Circ. Res. 1998, 82:1029-1034.
    • (1998) Circ. Res. , vol.82 , pp. 1029-1034
    • Sugiura, S.1    Kobayakawa, N.2    Fujita, H.3    Yamashita, H.4    Momomura, S.5    Chaen, S.6
  • 43
    • 3042700478 scopus 로고    scopus 로고
    • Mechanoenergetic estimation of multiple cross-bridge steps per ATP in a beating heart
    • Suga H. Mechanoenergetic estimation of multiple cross-bridge steps per ATP in a beating heart. Jpn. J. Physiol. 2004, 54:103-108.
    • (2004) Jpn. J. Physiol. , vol.54 , pp. 103-108
    • Suga, H.1
  • 44
    • 0030768395 scopus 로고    scopus 로고
    • Distribution and categorization of echocardiographic measurements in relation to reference limits: the Framingham Heart Study: formulation of a height- and sex-specific classification and its prospective validation
    • Vasan R.S., Larson M.G., Levy D., Evans J.C., Benjamin E.J. Distribution and categorization of echocardiographic measurements in relation to reference limits: the Framingham Heart Study: formulation of a height- and sex-specific classification and its prospective validation. Circulation 1997, 96:1863-1873.
    • (1997) Circulation , vol.96 , pp. 1863-1873
    • Vasan, R.S.1    Larson, M.G.2    Levy, D.3    Evans, J.C.4    Benjamin, E.J.5
  • 45
    • 0023738191 scopus 로고
    • Kinetics of ATP hydrolysis and tension production in skinned cardiac muscle of the guinea pig
    • Barsotti R.J., Ferenczi M.A. Kinetics of ATP hydrolysis and tension production in skinned cardiac muscle of the guinea pig. J. Biol. Chem. 1988, 263:16750-16756.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16750-16756
    • Barsotti, R.J.1    Ferenczi, M.A.2
  • 46
    • 0034011475 scopus 로고    scopus 로고
    • Force-velocity relationship and biochemical-to-mechanical energy conversion by the sarcomere
    • Landesberg A., Sideman S. Force-velocity relationship and biochemical-to-mechanical energy conversion by the sarcomere. Am. J. Physiol. Heart. Circ. Physiol. 2000, 278:H1274-1284.
    • (2000) Am. J. Physiol. Heart. Circ. Physiol. , vol.278
    • Landesberg, A.1    Sideman, S.2
  • 47
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima A., Kojima H., Funatsu T., Tokunaga M., Higuchi H., Tanaka H., et al. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 1998, 92:161-171.
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6
  • 48
    • 0033552942 scopus 로고    scopus 로고
    • A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
    • Kitamura K., Tokunaga M., Iwane A.H., Yanagida T. A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature 1999, 397:129-134.
    • (1999) Nature , vol.397 , pp. 129-134
    • Kitamura, K.1    Tokunaga, M.2    Iwane, A.H.3    Yanagida, T.4
  • 49
    • 0025748142 scopus 로고
    • Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle
    • Brenner B. Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:10490-10494.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10490-10494
    • Brenner, B.1
  • 50
    • 0027436271 scopus 로고
    • A single order-disorder transition generates tension during the Huxley-Simmons phase 2 in muscle
    • Davis J.S., Harrington W.F. A single order-disorder transition generates tension during the Huxley-Simmons phase 2 in muscle. Biophys. J. 1993, 65:1886-1898.
    • (1993) Biophys. J. , vol.65 , pp. 1886-1898
    • Davis, J.S.1    Harrington, W.F.2
  • 52
    • 0028050276 scopus 로고
    • Explaining load dependence of ventricular contractile properties with a model of excitation-contraction coupling
    • Burkhoff D. Explaining load dependence of ventricular contractile properties with a model of excitation-contraction coupling. J. Mol. Cell. Cardiol. 1994, 26:959-978.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 959-978
    • Burkhoff, D.1
  • 53
    • 0033194866 scopus 로고    scopus 로고
    • Shortening deactivation of cardiac muscle: physiological mechanisms and clinical implications
    • Leach J.K., Priola D.V., Grimes L.A., Skipper B.J. Shortening deactivation of cardiac muscle: physiological mechanisms and clinical implications. J. Investig. Med. 1999, 47:369-377.
    • (1999) J. Investig. Med. , vol.47 , pp. 369-377
    • Leach, J.K.1    Priola, D.V.2    Grimes, L.A.3    Skipper, B.J.4
  • 54
    • 0020549120 scopus 로고
    • Active shortening retards the decline of the intracellular calcium transient in mammalian heart muscle
    • Housmans P.R., Lee N.K., Blinks J.R. Active shortening retards the decline of the intracellular calcium transient in mammalian heart muscle. Science 1983, 221:159-161.
    • (1983) Science , vol.221 , pp. 159-161
    • Housmans, P.R.1    Lee, N.K.2    Blinks, J.R.3
  • 55
    • 0033383559 scopus 로고    scopus 로고
    • Troponin C regulates the rate constant for the dissociation of force-generating myosin cross-bridges in cardiac muscle
    • Wang Y., Xu Y., Guth K., Kerrick W.G. Troponin C regulates the rate constant for the dissociation of force-generating myosin cross-bridges in cardiac muscle. J. Muscle. Res. Cell. Motil. 1999, 20:645-653.
    • (1999) J. Muscle. Res. Cell. Motil. , vol.20 , pp. 645-653
    • Wang, Y.1    Xu, Y.2    Guth, K.3    Kerrick, W.G.4
  • 56
    • 0024363853 scopus 로고
    • Relaxation and diastole of the heart
    • Brutsaert D.L., Sys S.U. Relaxation and diastole of the heart. Physiol. Rev. 1989, 69:1228-1315.
    • (1989) Physiol. Rev. , vol.69 , pp. 1228-1315
    • Brutsaert, D.L.1    Sys, S.U.2
  • 57
    • 0024404919 scopus 로고
    • Determinants of force decline during relaxation in isolated cardiac muscle
    • Sys S.U., Brutsaert D.L. Determinants of force decline during relaxation in isolated cardiac muscle. Am. J. Physiol. 1989, 257:H1490-H1497.
    • (1989) Am. J. Physiol. , vol.257
    • Sys, S.U.1    Brutsaert, D.L.2
  • 59
    • 33748324700 scopus 로고    scopus 로고
    • Mechanical properties of sarcomeres during cardiac myofibrillar relaxation: stretch-induced cross-bridge detachment contributes to early diastolic filling
    • Stehle R., Solzin J., Iorga B., Gomez D., Blaudeck N., Pfitzer G. Mechanical properties of sarcomeres during cardiac myofibrillar relaxation: stretch-induced cross-bridge detachment contributes to early diastolic filling. J. Muscle. Res. Cell. Motil. 2006, 27:423-434.
    • (2006) J. Muscle. Res. Cell. Motil. , vol.27 , pp. 423-434
    • Stehle, R.1    Solzin, J.2    Iorga, B.3    Gomez, D.4    Blaudeck, N.5    Pfitzer, G.6
  • 60
    • 17444431193 scopus 로고    scopus 로고
    • Sarcomeric determinants of striated muscle relaxation kinetics
    • Poggesi C., Tesi C., Stehle R. Sarcomeric determinants of striated muscle relaxation kinetics. Pflugers. Arch. 2005, 449:505-517.
    • (2005) Pflugers. Arch. , vol.449 , pp. 505-517
    • Poggesi, C.1    Tesi, C.2    Stehle, R.3
  • 61
    • 0019013686 scopus 로고
    • Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex
    • Greene L.E., Eisenberg E. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:2616-2620.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 2616-2620
    • Greene, L.E.1    Eisenberg, E.2
  • 62
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • 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. 1993, 65:693-701.
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 63
    • 66149090351 scopus 로고    scopus 로고
    • Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state
    • Mathur M.C., Kobayashi T., Chalovich J.M. Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state. Biophys. J. 2009, 96:2237-2244.
    • (2009) Biophys. J. , vol.96 , pp. 2237-2244
    • Mathur, M.C.1    Kobayashi, T.2    Chalovich, J.M.3
  • 64
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • Kentish J.C., McCloskey D.T., Layland J., Palmer S., Leiden J.M., Martin A.F., et al. Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle. Circ. Res. 2001, 88:1059-1065.
    • (2001) Circ. Res. , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Layland, J.3    Palmer, S.4    Leiden, J.M.5    Martin, A.F.6
  • 65
    • 0037023633 scopus 로고    scopus 로고
    • Phosphorylation of troponin I controls cardiac twitch dynamics: evidence from phosphorylation site mutants expressed on a troponin I-null background in mice
    • Pi Y., Kemnitz K.R., Zhang D., Kranias E.G., Walker J.W. Phosphorylation of troponin I controls cardiac twitch dynamics: evidence from phosphorylation site mutants expressed on a troponin I-null background in mice. Circ. Res. 2002, 90:649-656.
    • (2002) Circ. Res. , vol.90 , pp. 649-656
    • Pi, Y.1    Kemnitz, K.R.2    Zhang, D.3    Kranias, E.G.4    Walker, J.W.5
  • 66
    • 34548356872 scopus 로고    scopus 로고
    • Differential roles of cardiac myosin-binding protein C and cardiac troponin I in the myofibrillar force responses to protein kinase A phosphorylation
    • Stelzer J.E., Patel J.R., Walker J.W., Moss R.L. Differential roles of cardiac myosin-binding protein C and cardiac troponin I in the myofibrillar force responses to protein kinase A phosphorylation. Circ. Res. 2007, 101:503-511.
    • (2007) Circ. Res. , vol.101 , pp. 503-511
    • Stelzer, J.E.1    Patel, J.R.2    Walker, J.W.3    Moss, R.L.4
  • 67
    • 34547951704 scopus 로고    scopus 로고
    • Cardiac transgenic and gene transfer strategies converge to support an important role for troponin I in regulating relaxation in cardiac myocytes
    • Yasuda S., Coutu P., Sadayappan S., Robbins J., Metzger J.M. Cardiac transgenic and gene transfer strategies converge to support an important role for troponin I in regulating relaxation in cardiac myocytes. Circ. Res. 2007, 101:377-386.
    • (2007) Circ. Res. , vol.101 , pp. 377-386
    • Yasuda, S.1    Coutu, P.2    Sadayappan, S.3    Robbins, J.4    Metzger, J.M.5
  • 68
    • 4444334713 scopus 로고    scopus 로고
    • Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle
    • 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. 2004, 87:1815-1824.
    • (2004) Biophys. J. , vol.87 , pp. 1815-1824
    • Regnier, M.1    Martin, H.2    Barsotti, R.J.3    Rivera, A.J.4    Martyn, D.A.5    Clemmens, E.6
  • 69
    • 58149305398 scopus 로고    scopus 로고
    • Calcium- and myosin-dependent changes in troponin structure during activation of heart muscle
    • Sun Y.B., Lou F., Irving M. Calcium- and myosin-dependent changes in troponin structure during activation of heart muscle. J. Physiol. 2009, 587:155-163.
    • (2009) J. Physiol. , vol.587 , pp. 155-163
    • Sun, Y.B.1    Lou, F.2    Irving, M.3
  • 70
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium binding to cardiac troponin C
    • Hofmann P.A., Fuchs F. Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am. J. Physiol. 1987, 253:C541-C546.
    • (1987) Am. J. Physiol. , vol.253
    • Hofmann, P.A.1    Fuchs, F.2
  • 71
    • 33846446434 scopus 로고    scopus 로고
    • Cooperative effects of rigor and cycling cross-bridges on calcium binding to troponin C
    • Cantino M.E., Quintanilla A. Cooperative effects of rigor and cycling cross-bridges on calcium binding to troponin C. Biophys. J. 2007, 92:525-534.
    • (2007) Biophys. J. , vol.92 , pp. 525-534
    • Cantino, M.E.1    Quintanilla, A.2
  • 73
    • 0018833363 scopus 로고
    • Tension development and sarcomere length in rat cardiac trabeculae. Evidence of length-dependent activation
    • ter Keurs H.E., Rijnsburger W.H., van Heuningen R., Nagelsmit M.J. Tension development and sarcomere length in rat cardiac trabeculae. Evidence of length-dependent activation. Circ. Res. 1980, 46:703-714.
    • (1980) Circ. Res. , vol.46 , pp. 703-714
    • ter Keurs, H.E.1    Rijnsburger, W.H.2    van Heuningen, R.3    Nagelsmit, M.J.4
  • 74
    • 33646205849 scopus 로고    scopus 로고
    • Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers
    • Telley I.A., Denoth J., Stussi E., Pfitzer G., Stehle R. Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers. Biophys. J. 2006, 90:514-530.
    • (2006) Biophys. J. , vol.90 , pp. 514-530
    • Telley, I.A.1    Denoth, J.2    Stussi, E.3    Pfitzer, G.4    Stehle, R.5
  • 75
    • 49549104611 scopus 로고    scopus 로고
    • Approximate model of cooperative activation and crossbridge cycling in cardiac muscle using ordinary differential equations
    • Rice J.J., Wang F., Bers D.M., de Tombe P.P. Approximate model of cooperative activation and crossbridge cycling in cardiac muscle using ordinary differential equations. Biophys. J. 2008, 95:2368-2390.
    • (2008) Biophys. J. , vol.95 , pp. 2368-2390
    • Rice, J.J.1    Wang, F.2    Bers, D.M.3    de Tombe, P.P.4
  • 76
    • 33646231760 scopus 로고    scopus 로고
    • Current perspectives in diastolic dysfunction and diastolic heart failure
    • Leite-Moreira A.F. Current perspectives in diastolic dysfunction and diastolic heart failure. Heart 2006, 92:712-718.
    • (2006) Heart , vol.92 , pp. 712-718
    • Leite-Moreira, A.F.1
  • 77
    • 34648834066 scopus 로고    scopus 로고
    • Cardiac function as assessed by echocardiography in the oldest old > or = 90 years of age
    • Masugata H., Senda S., Goda F., Yoshihara Y., Yoshikawa K., Fujita N., et al. Cardiac function as assessed by echocardiography in the oldest old > or = 90 years of age. Int. Heart. J. 2007, 48:497-504.
    • (2007) Int. Heart. J. , vol.48 , pp. 497-504
    • Masugata, H.1    Senda, S.2    Goda, F.3    Yoshihara, Y.4    Yoshikawa, K.5    Fujita, N.6
  • 78
    • 0037133660 scopus 로고    scopus 로고
    • New concepts in diastolic dysfunction and diastolic heart failure: Part I: diagnosis, prognosis, and measurements of diastolic function
    • Zile M.R., Brutsaert D.L. New concepts in diastolic dysfunction and diastolic heart failure: Part I: diagnosis, prognosis, and measurements of diastolic function. Circulation 2002, 105:1387-1393.
    • (2002) Circulation , vol.105 , pp. 1387-1393
    • Zile, M.R.1    Brutsaert, D.L.2
  • 79
    • 0016592127 scopus 로고
    • Dynamic determinants of left ventricular diastolic pressure-volume relations in man
    • Gaasch W.H., Cole J.S., Quinones M.A., Alexander J.K. Dynamic determinants of left ventricular diastolic pressure-volume relations in man. Circulation 1975, 51:317-323.
    • (1975) Circulation , vol.51 , pp. 317-323
    • Gaasch, W.H.1    Cole, J.S.2    Quinones, M.A.3    Alexander, J.K.4
  • 80
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • Helmes M., Trombitas K., Granzier H. Titin develops restoring force in rat cardiac myocytes. Circ. Res. 1996, 79:619-626.
    • (1996) Circ. Res. , vol.79 , pp. 619-626
    • Helmes, M.1    Trombitas, K.2    Granzier, H.3
  • 82
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: a major player in myocardial mechanics, signaling, and disease
    • Granzier H.L., Labeit S. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ. Res. 2004, 94:284-295.
    • (2004) Circ. Res. , vol.94 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 83
    • 0031016596 scopus 로고    scopus 로고
    • The giant protein titin. Emerging roles in physiology and pathophysiology
    • Labeit S., Kolmerer B., Linke W.A. The giant protein titin. Emerging roles in physiology and pathophysiology. Circ. Res. 1997, 80:290-294.
    • (1997) Circ. Res. , vol.80 , pp. 290-294
    • Labeit, S.1    Kolmerer, B.2    Linke, W.A.3
  • 84
    • 61449259796 scopus 로고    scopus 로고
    • Differences in intracellular calcium homeostasis between atrial and ventricular myocytes
    • Walden A.P., Dibb K.M., Trafford A.W. Differences in intracellular calcium homeostasis between atrial and ventricular myocytes. J. Mol. Cell. Cardiol. 2009, 46:463-473.
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 463-473
    • Walden, A.P.1    Dibb, K.M.2    Trafford, A.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.