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Volumn 259, Issue 4, 2009, Pages 714-726

A multisegmental cross-bridge kinetics model of the myofibril

Author keywords

Actomyosin kinetics; Muscle modeling; Sarcomere dynamics; Sarcomere length inhomogeneity; Skeletal muscle

Indexed keywords

ADENOSINE TRIPHOSPHATE;

EID: 67650720444     PISSN: 00225193     EISSN: 10958541     Source Type: Journal    
DOI: 10.1016/j.jtbi.2009.03.032     Document Type: Article
Times cited : (29)

References (66)
  • 2
    • 0031595248 scopus 로고    scopus 로고
    • ATPase and shortening rates in frog fast skeletal myofibrils by time-resolved measurements of protein-bound and free Pi
    • Barman T., Brune M., Lionne C., Piroddi N., Poggesi C., Stehle R., Tesi C., Travers F., and Webb M.R. ATPase and shortening rates in frog fast skeletal myofibrils by time-resolved measurements of protein-bound and free Pi. Biophys. J. 74 (1998) 3120-3130
    • (1998) Biophys. J. , vol.74 , pp. 3120-3130
    • Barman, T.1    Brune, M.2    Lionne, C.3    Piroddi, N.4    Poggesi, C.5    Stehle, R.6    Tesi, C.7    Travers, F.8    Webb, M.R.9
  • 3
    • 0142187297 scopus 로고    scopus 로고
    • Mechanism of cross-bridge detachment in isometric force relaxation of skeletal and cardiac myofibrils
    • Belus A., Piroddi N., and Tesi C. Mechanism of cross-bridge detachment in isometric force relaxation of skeletal and cardiac myofibrils. J. Muscle Res. Cell Motil. 24 (2003) 261-267
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 261-267
    • Belus, A.1    Piroddi, N.2    Tesi, C.3
  • 4
    • 24944571056 scopus 로고    scopus 로고
    • Endothermic force generation, temperature-jump experiments and effects of increased [MgADP] in rabbit psoas muscle fibres
    • Coupland M.E., Pinniger G.J., and Ranatunga K.W. Endothermic force generation, temperature-jump experiments and effects of increased [MgADP] in rabbit psoas muscle fibres. J. Physiol. 567 (2005) 471-492
    • (2005) J. Physiol. , vol.567 , pp. 471-492
    • Coupland, M.E.1    Pinniger, G.J.2    Ranatunga, K.W.3
  • 5
    • 0036301893 scopus 로고    scopus 로고
    • Single muscle fiber contraction is dictated by inter-sarcomere dynamics
    • Denoth J., Stussi E., Csucs G., and Danuser G. Single muscle fiber contraction is dictated by inter-sarcomere dynamics. J. Theor. Biol. 216 (2002) 101-122
    • (2002) J. Theor. Biol. , vol.216 , pp. 101-122
    • Denoth, J.1    Stussi, E.2    Csucs, G.3    Danuser, G.4
  • 6
    • 33845292922 scopus 로고    scopus 로고
    • Structural transition of the inhibitory region of troponin I within the regulated cardiac thin filament
    • Dong W.J., An J., Xing J., and Cheung H.C. Structural transition of the inhibitory region of troponin I within the regulated cardiac thin filament. Arch. Biochem. Biophys. 456 (2006) 135-142
    • (2006) Arch. Biochem. Biophys. , vol.456 , pp. 135-142
    • Dong, W.J.1    An, J.2    Xing, J.3    Cheung, H.C.4
  • 8
    • 20444443609 scopus 로고    scopus 로고
    • Contractile properties of mouse single muscle fibers, a comparison with amphibian muscle fibers
    • Edman K.A. Contractile properties of mouse single muscle fibers, a comparison with amphibian muscle fibers. J. Exp. Biol. 208 (2005) 1905-1913
    • (2005) J. Exp. Biol. , vol.208 , pp. 1905-1913
    • Edman, K.A.1
  • 9
    • 0021287452 scopus 로고
    • Redistribution of sarcomere length during isometric contraction of frog muscle fibres and its relation to tension creep
    • Edman K.A., and Reggiani C. Redistribution of sarcomere length during isometric contraction of frog muscle fibres and its relation to tension creep. J. Physiol. 351 (1984) 169-198
    • (1984) J. Physiol. , vol.351 , pp. 169-198
    • Edman, K.A.1    Reggiani, C.2
  • 10
    • 0014268849 scopus 로고
    • The adenosine triphosphatase activity of acto-heavy meromyosin. A kinetic analysis of actin activation
    • Eisenberg E., and Moos C. The adenosine triphosphatase activity of acto-heavy meromyosin. A kinetic analysis of actin activation. Biochemistry 7 (1968) 1486-1489
    • (1968) Biochemistry , vol.7 , pp. 1486-1489
    • Eisenberg, E.1    Moos, C.2
  • 11
    • 0017851095 scopus 로고
    • A cross-bridge model of muscle contraction
    • Eisenberg E., and Hill T.L. A cross-bridge model of muscle contraction. Prog. Biophys. Mol. Biol. 33 (1978) 55-82
    • (1978) Prog. Biophys. Mol. Biol. , vol.33 , pp. 55-82
    • Eisenberg, E.1    Hill, T.L.2
  • 12
    • 0018816862 scopus 로고
    • The relation of muscle biochemistry to muscle physiology
    • Eisenberg E., and Greene L.E. The relation of muscle biochemistry to muscle physiology. Annu. Rev. Physiol. 42 (1980) 293-309
    • (1980) Annu. Rev. Physiol. , vol.42 , pp. 293-309
    • Eisenberg, E.1    Greene, L.E.2
  • 14
    • 0029926524 scopus 로고    scopus 로고
    • Mechanical characterization of skeletal muscle myofibrils
    • Friedman A.L., and Goldman Y.E. Mechanical characterization of skeletal muscle myofibrils. Biophys. J. 71 (1996) 2774-2785
    • (1996) Biophys. J. , vol.71 , pp. 2774-2785
    • Friedman, A.L.1    Goldman, Y.E.2
  • 15
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in vertebrate muscle fibres
    • Gordon A.M., Huxley A.F., and Julian F.J. The variation in isometric tension with sarcomere length in vertebrate muscle fibres. J. Physiol. 184 (1966) 170-192
    • (1966) J. Physiol. , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 16
    • 0025378983 scopus 로고
    • The descending limb of the force-sarcomere length relation of the frog revisited
    • Granzier H.L., and Pollack G.H. The descending limb of the force-sarcomere length relation of the frog revisited. J. Physiol. 421 (1990) 595-615
    • (1990) J. Physiol. , vol.421 , pp. 595-615
    • Granzier, H.L.1    Pollack, G.H.2
  • 17
    • 0024536652 scopus 로고
    • Sarcomere length dependence of the force-velocity relation in single frog muscle fibers
    • Granzier H.L., Burns D.H., and Pollack G.H. Sarcomere length dependence of the force-velocity relation in single frog muscle fibers. Biophys. J. 55 (1989) 499-507
    • (1989) Biophys. J. , vol.55 , pp. 499-507
    • Granzier, H.L.1    Burns, D.H.2    Pollack, G.H.3
  • 18
    • 0033995883 scopus 로고    scopus 로고
    • The history dependence of force production in mammalian skeletal muscle following stretch-shortening and shortening-stretch cycles
    • Herzog W., and Leonard T.R. The history dependence of force production in mammalian skeletal muscle following stretch-shortening and shortening-stretch cycles. J. Biomech. 33 (2000) 531-542
    • (2000) J. Biomech. , vol.33 , pp. 531-542
    • Herzog, W.1    Leonard, T.R.2
  • 20
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of muscle
    • Hill A.V. The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. Ser. B 126 (1938) 136-195
    • (1938) Proc. R. Soc. Ser. B , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 21
    • 0016180488 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle, part I
    • Hill T.L. Theoretical formalism for the sliding filament model of contraction of striated muscle, part I. Prog. Biophys. Mol. Biol. 28 (1974) 267-340
    • (1974) Prog. Biophys. Mol. Biol. , vol.28 , pp. 267-340
    • Hill, T.L.1
  • 22
    • 0016422610 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle, part II
    • Hill T.L. Theoretical formalism for the sliding filament model of contraction of striated muscle, part II. Prog. Biophys. Mol. Biol. 29 (1975) 105-159
    • (1975) Prog. Biophys. Mol. Biol. , vol.29 , pp. 105-159
    • Hill, T.L.1
  • 23
    • 0017282704 scopus 로고
    • Free energy levels and entropy production in muscle contraction and in related solution systems
    • Hill T.L., and Simmons R.M. Free energy levels and entropy production in muscle contraction and in related solution systems. Proc. Natl. Acad. Sci. USA 73 (1976) 336-340
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 336-340
    • Hill, T.L.1    Simmons, R.M.2
  • 24
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley A.F. Muscle structure and theories of contraction. Prog. Biophys. Mol. Biol. 7 (1957) 255-318
    • (1957) Prog. Biophys. Mol. Biol. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 25
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley A.F., and Simmons R.M. Proposed mechanism of force generation in striated muscle. Nature 233 (1971) 533-538
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 26
    • 0031018999 scopus 로고    scopus 로고
    • Rapid regeneration of power stroke in contracting muscle by attachment of second myosin head
    • Huxley A.F., and Tideswell S. Rapid regeneration of power stroke in contracting muscle by attachment of second myosin head. J. Muscle Res. Cell Motil. 18 (1997) 111-114
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 111-114
    • Huxley, A.F.1    Tideswell, S.2
  • 27
    • 43249125319 scopus 로고    scopus 로고
    • Residual force enhancement in myofibrils and sarcomeres
    • Joumaa V., Leonard T.R., and Herzog W. Residual force enhancement in myofibrils and sarcomeres. Proc. Biol. Sci. 275 (2008) 1411-1419
    • (2008) Proc. Biol. Sci. , vol.275 , pp. 1411-1419
    • Joumaa, V.1    Leonard, T.R.2    Herzog, W.3
  • 29
    • 0018720081 scopus 로고
    • Intersarcomere dynamics during fixed-end tetanic contractions of frog muscle fibres
    • Julian F.J., and Morgan D.L. Intersarcomere dynamics during fixed-end tetanic contractions of frog muscle fibres. J. Physiol. 293 (1979) 365-378
    • (1979) J. Physiol. , vol.293 , pp. 365-378
    • Julian, F.J.1    Morgan, D.L.2
  • 30
    • 0018701747 scopus 로고
    • The effect on tension of non-uniform distribution of length changes applied to frog muscle fibres
    • Julian F.J., and Morgan D.L. The effect on tension of non-uniform distribution of length changes applied to frog muscle fibres. J. Physiol. 293 (1979) 379-392
    • (1979) J. Physiol. , vol.293 , pp. 379-392
    • Julian, F.J.1    Morgan, D.L.2
  • 31
    • 0030022007 scopus 로고    scopus 로고
    • Calcium-dependent inhibition of in vitro thin-filament motility by native titin
    • Kellermayer M.S., and Granzier H.L. Calcium-dependent inhibition of in vitro thin-filament motility by native titin. FEBS Lett. 380 (1996) 281-286
    • (1996) FEBS Lett. , vol.380 , pp. 281-286
    • Kellermayer, M.S.1    Granzier, H.L.2
  • 32
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer M.S., Smith S.B., Granzier H.L., and Bustamante C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276 (1997) 1112-1116
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 33
    • 0031029605 scopus 로고    scopus 로고
    • Cross-bridge kinetics studied with staircase shortening in single fibres from frog skeletal muscle
    • Linari M., Lombardi V., and Piazzesi G. Cross-bridge kinetics studied with staircase shortening in single fibres from frog skeletal muscle. J. Muscle Res. Cell Motil. 18 (1997) 91-101
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 91-101
    • Linari, M.1    Lombardi, V.2    Piazzesi, G.3
  • 34
    • 34047208553 scopus 로고    scopus 로고
    • Stiffness and fraction of myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas
    • Linari M., Caremani M., Piperio C., Brandt P., and Lombardi V. Stiffness and fraction of myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas. Biophys. J. 92 (2007) 2476-2490
    • (2007) Biophys. J. , vol.92 , pp. 2476-2490
    • Linari, M.1    Caremani, M.2    Piperio, C.3    Brandt, P.4    Lombardi, V.5
  • 35
    • 0033928461 scopus 로고    scopus 로고
    • Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle
    • Linke W.A. Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. Histol. Histopathol. 15 (2000) 799-811
    • (2000) Histol. Histopathol. , vol.15 , pp. 799-811
    • Linke, W.A.1
  • 36
    • 49649100130 scopus 로고    scopus 로고
    • Minimally invasive high-speed imaging of sarcomere contractile dynamics in mice and humans
    • Llewellyn M.E., Barretto R.P., Delp S.L., and Schnitzer M.J. Minimally invasive high-speed imaging of sarcomere contractile dynamics in mice and humans. Nature 454 (2008) 784-788
    • (2008) Nature , vol.454 , pp. 784-788
    • Llewellyn, M.E.1    Barretto, R.P.2    Delp, S.L.3    Schnitzer, M.J.4
  • 37
    • 0028601298 scopus 로고
    • Effect of series elasticity on delay in development of tension relative to stiffness during muscle activation
    • Luo Y., Cooke R., and Pate E. Effect of series elasticity on delay in development of tension relative to stiffness during muscle activation. Am. J. Physiol. 267 (1994) C1598-C1606
    • (1994) Am. J. Physiol. , vol.267
    • Luo, Y.1    Cooke, R.2    Pate, E.3
  • 38
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn R.W., and Taylor E.W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10 (1971) 4617-4624
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 39
    • 0036554815 scopus 로고    scopus 로고
    • Titin-based contribution to shortening velocity of rabbit skeletal myofibrils
    • Minajeva A., Neagoe C., Kulke M., and Linke W.A. Titin-based contribution to shortening velocity of rabbit skeletal myofibrils. J. Physiol. 540 (2002) 177-188
    • (2002) J. Physiol. , vol.540 , pp. 177-188
    • Minajeva, A.1    Neagoe, C.2    Kulke, M.3    Linke, W.A.4
  • 40
    • 0028907268 scopus 로고
    • A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle
    • Piazzesi G., and Lombardi V. A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle. Biophys. J. 68 (1995) 1966-1979
    • (1995) Biophys. J. , vol.68 , pp. 1966-1979
    • Piazzesi, G.1    Lombardi, V.2
  • 41
    • 0029893494 scopus 로고    scopus 로고
    • Simulation of the rapid regeneration of the actin-myosin working stroke with a tight coupling model of muscle contraction
    • Piazzesi G., and Lombardi V. Simulation of the rapid regeneration of the actin-myosin working stroke with a tight coupling model of muscle contraction. J. Muscle Res. Cell Motil. 17 (1996) 45-53
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 45-53
    • Piazzesi, G.1    Lombardi, V.2
  • 42
    • 33744931426 scopus 로고    scopus 로고
    • Crossbridge and non-crossbridge contributions to tension in lengthening muscle: force-induced reversal of the power stroke
    • Pinniger G.J., Ranatunga K.W., and Offer G.W. Crossbridge and non-crossbridge contributions to tension in lengthening muscle: force-induced reversal of the power stroke. J. Physiol. 573 (2006) 627-643
    • (2006) J. Physiol. , vol.573 , pp. 627-643
    • Pinniger, G.J.1    Ranatunga, K.W.2    Offer, G.W.3
  • 44
    • 54249146868 scopus 로고    scopus 로고
    • Pre-power stroke cross bridges contribute to force during stretch of skeletal muscle myofibrils
    • Rassier D.E. Pre-power stroke cross bridges contribute to force during stretch of skeletal muscle myofibrils. Proc. Biol. Sci. 275 (2008) 2577-2586
    • (2008) Proc. Biol. Sci. , vol.275 , pp. 2577-2586
    • Rassier, D.E.1
  • 45
    • 0041876435 scopus 로고    scopus 로고
    • Dynamics of individual sarcomeres during and after stretch in activated single myofibrils
    • Rassier D.E., Herzog W., and Pollack G.H. Dynamics of individual sarcomeres during and after stretch in activated single myofibrils. Proc. R. Soc. London Ser. B Biol. Sci. 270 (2003) 1735-1740
    • (2003) Proc. R. Soc. London Ser. B Biol. Sci. , vol.270 , pp. 1735-1740
    • Rassier, D.E.1    Herzog, W.2    Pollack, G.H.3
  • 46
    • 0036803262 scopus 로고    scopus 로고
    • Force enhancement above the initial isometric force on the descending limb of the force-length relationship
    • Schachar R., Herzog W., and Leonard T. Force enhancement above the initial isometric force on the descending limb of the force-length relationship. J. Biomech. 35 (2002) 1299-1306
    • (2002) J. Biomech. , vol.35 , pp. 1299-1306
    • Schachar, R.1    Herzog, W.2    Leonard, T.3
  • 48
    • 38749117238 scopus 로고    scopus 로고
    • Nonlinearities make a difference: comparison of two common Hill-type models with real muscle
    • Siebert T., Rode C., Herzog W., Till O., and Blickhan R. Nonlinearities make a difference: comparison of two common Hill-type models with real muscle. Biol. Cybernet. 98 (2008) 133-143
    • (2008) Biol. Cybernet. , vol.98 , pp. 133-143
    • Siebert, T.1    Rode, C.2    Herzog, W.3    Till, O.4    Blickhan, R.5
  • 49
    • 15844429778 scopus 로고    scopus 로고
    • The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle
    • Sleep J., Irving M., and Burton K. The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle. J. Physiol. 563 (2005) 671-687
    • (2005) J. Physiol. , vol.563 , pp. 671-687
    • Sleep, J.1    Irving, M.2    Burton, K.3
  • 50
    • 49049092336 scopus 로고    scopus 로고
    • Toward a unified theory of muscle contraction. II: predictions with the mean-field approximation
    • Smith D.A., and Mijailovich S.M. Toward a unified theory of muscle contraction. II: predictions with the mean-field approximation. Ann. Biomed. Eng. 36 (2008) 1353-1371
    • (2008) Ann. Biomed. Eng. , vol.36 , pp. 1353-1371
    • Smith, D.A.1    Mijailovich, S.M.2
  • 51
    • 51549107300 scopus 로고    scopus 로고
    • Towards a unified theory of muscle contraction. I: foundations
    • Smith D.A., Geeves M.A., Sleep J., and Mijailovich S.M. Towards a unified theory of muscle contraction. I: foundations. Ann. Biomed. Eng. 36 (2008) 1624-1640
    • (2008) Ann. Biomed. Eng. , vol.36 , pp. 1624-1640
    • Smith, D.A.1    Geeves, M.A.2    Sleep, J.3    Mijailovich, S.M.4
  • 52
    • 0036789489 scopus 로고    scopus 로고
    • Force kinetics and individual sarcomere dynamics in cardiac myofibrils after rapid Ca(2+) changes
    • Stehle R., Krüger M., and Pfitzer G. Force kinetics and individual sarcomere dynamics in cardiac myofibrils after rapid Ca(2+) changes. Biophys. J. 83 (2002) 2152-2161
    • (2002) Biophys. J. , vol.83 , pp. 2152-2161
    • Stehle, R.1    Krüger, M.2    Pfitzer, G.3
  • 53
    • 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., Krüger M., Scherer P., Brixius K., Schwinger R.H., and 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. 97 Suppl. 1 (2002) 127-135
    • (2002) Basic Res. Cardiol. , vol.97 , Issue.SUPPL. 1 , pp. 127-135
    • Stehle, R.1    Krüger, M.2    Scherer, P.3    Brixius, K.4    Schwinger, R.H.5    Pfitzer, G.6
  • 54
    • 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., and 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. 27 (2006) 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
  • 56
    • 0035868791 scopus 로고    scopus 로고
    • Effect of active shortening on the rate of ATP utilisation by rabbit psoas muscle fibres
    • Sun Y.B., Hilber K., and Irving M. Effect of active shortening on the rate of ATP utilisation by rabbit psoas muscle fibres. J. Physiol. 531 (2001) 781-791
    • (2001) J. Physiol. , vol.531 , pp. 781-791
    • Sun, Y.B.1    Hilber, K.2    Irving, M.3
  • 57
    • 0031942848 scopus 로고    scopus 로고
    • The effects of stretch parameters on eccentric exercise-induced damage to toad skeletal muscle
    • Talbot J.A., and Morgan D.L. The effects of stretch parameters on eccentric exercise-induced damage to toad skeletal muscle. J. Muscle Res. Cell Motil. 19 (1998) 237-245
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 237-245
    • Talbot, J.A.1    Morgan, D.L.2
  • 58
    • 34250190961 scopus 로고    scopus 로고
    • Sarcomere dynamics during muscular contraction and their implications to muscle function
    • Telley I.A., and Denoth J. Sarcomere dynamics during muscular contraction and their implications to muscle function. J. Muscle Res. Cell Motil. 28 (2007) 89-104
    • (2007) J. Muscle Res. Cell Motil. , vol.28 , pp. 89-104
    • Telley, I.A.1    Denoth, J.2
  • 59
    • 1842474900 scopus 로고    scopus 로고
    • Inter-sarcomere dynamics in muscle fibres. A neglected subject?
    • Telley I.A., Denoth J., and Ranatunga K.W. Inter-sarcomere dynamics in muscle fibres. A neglected subject?. Adv. Exp. Med. Biol. 538 (2003) 481-500
    • (2003) Adv. Exp. Med. Biol. , vol.538 , pp. 481-500
    • Telley, I.A.1    Denoth, J.2    Ranatunga, K.W.3
  • 60
    • 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., and Stehle R. Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers. Biophys. J. 90 (2006) 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
  • 61
    • 33646339394 scopus 로고    scopus 로고
    • Dynamic behaviour of half-sarcomeres during and after stretch in activated psoas myofibrils: sarcomere asymmetry but no 'sarcomere popping'
    • Telley I.A., Stehle R., Ranatunga K.W., Pfitzer G., Stussi E., and Denoth J. Dynamic behaviour of half-sarcomeres during and after stretch in activated psoas myofibrils: sarcomere asymmetry but no 'sarcomere popping'. J. Physiol. 573 (2006) 173-185
    • (2006) J. Physiol. , vol.573 , pp. 173-185
    • Telley, I.A.1    Stehle, R.2    Ranatunga, K.W.3    Pfitzer, G.4    Stussi, E.5    Denoth, J.6
  • 62
    • 0018168049 scopus 로고
    • The sarcomere length-tension relation in skeletal muscle
    • ter Keurs H.E., Iwazumi T., and Pollack G.H. The sarcomere length-tension relation in skeletal muscle. J. Gen. Physiol. 72 (1978) 565-592
    • (1978) J. Gen. Physiol. , vol.72 , pp. 565-592
    • ter Keurs, H.E.1    Iwazumi, T.2    Pollack, G.H.3
  • 63
    • 0037095908 scopus 로고    scopus 로고
    • Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles
    • Tesi C., Colomo F., Piroddi N., and Poggesi C. Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles. J. Physiol. 541 (2002) 187-199
    • (2002) J. Physiol. , vol.541 , pp. 187-199
    • Tesi, C.1    Colomo, F.2    Piroddi, N.3    Poggesi, C.4
  • 64
    • 0019592007 scopus 로고
    • A distribution-moment approximation for kinetic theories of muscular-contraction
    • Zahalak G.I. A distribution-moment approximation for kinetic theories of muscular-contraction. Math. Biosci. 55 (1981) 89-114
    • (1981) Math. Biosci. , vol.55 , pp. 89-114
    • Zahalak, G.I.1
  • 65
    • 0031280314 scopus 로고    scopus 로고
    • Can muscle fibers be stable on the descending limbs of their sarcomere length-tension relations?
    • Zahalak G.I. Can muscle fibers be stable on the descending limbs of their sarcomere length-tension relations?. J. Biomech. 30 (1997) 1179-1182
    • (1997) J. Biomech. , vol.30 , pp. 1179-1182
    • Zahalak, G.I.1
  • 66
    • 0034616454 scopus 로고    scopus 로고
    • The two-state cross-bridge model of muscle is an asymptotic limit of multi-state models
    • Zahalak G.I. The two-state cross-bridge model of muscle is an asymptotic limit of multi-state models. J. Theor. Biol. 204 (2000) 67-82
    • (2000) J. Theor. Biol. , vol.204 , pp. 67-82
    • Zahalak, G.I.1


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