메뉴 건너뛰기




Volumn 102, Issue 1, 2010, Pages 53-71

Inferring crossbridge properties from skeletal muscle energetics

Author keywords

[No Author keywords available]

Indexed keywords

ANURA;

EID: 76349088269     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2009.10.003     Document Type: Review
Times cited : (75)

References (82)
  • 1
    • 0030475775 scopus 로고    scopus 로고
    • Mechanical efficiency and fatigue of fast and slow muscles of the mouse
    • Barclay C.J. Mechanical efficiency and fatigue of fast and slow muscles of the mouse. J. Physiol. (Lond.) 497 (1996) 781-794
    • (1996) J. Physiol. (Lond.) , vol.497 , pp. 781-794
    • Barclay, C.J.1
  • 2
    • 0032425057 scopus 로고    scopus 로고
    • Estimation of cross-bridge stiffness from maximum thermodynamic efficiency
    • Barclay C.J. Estimation of cross-bridge stiffness from maximum thermodynamic efficiency. J. Muscle Res. Cell Motil. 19 (1998) 855-864
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 855-864
    • Barclay, C.J.1
  • 3
    • 0041886416 scopus 로고    scopus 로고
    • Models in which many cross-bridges attach simultaneously can explain the filament movement per ATP split during muscle contraction
    • Barclay C.J. Models in which many cross-bridges attach simultaneously can explain the filament movement per ATP split during muscle contraction. Int. J. Biol. Macromol 32 (2003) 139-147
    • (2003) Int. J. Biol. Macromol , vol.32 , pp. 139-147
    • Barclay, C.J.1
  • 4
    • 0027199209 scopus 로고
    • Changes in crossbridge and non-crossbridge energetics during moderate fatigue of frog muscle fibres
    • Barclay C.J., Curtin N.A., and Woledge R.C. Changes in crossbridge and non-crossbridge energetics during moderate fatigue of frog muscle fibres. J. Physiol. (Lond.) 468 (1993) 543-555
    • (1993) J. Physiol. (Lond.) , vol.468 , pp. 543-555
    • Barclay, C.J.1    Curtin, N.A.2    Woledge, R.C.3
  • 6
    • 33845326726 scopus 로고    scopus 로고
    • Structural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: stiffness and X-ray diffraction measurements
    • Brunello E., Bianco P., Piazzesi G., Linari M., Reconditi M., Panine P., Narayanan T., Helsby W.I., Irving M., and Lombardi V. Structural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: stiffness and X-ray diffraction measurements. J. Physiol. (Lond.) 577 (2006) 971-984
    • (2006) J. Physiol. (Lond.) , vol.577 , pp. 971-984
    • Brunello, E.1    Bianco, P.2    Piazzesi, G.3    Linari, M.4    Reconditi, M.5    Panine, P.6    Narayanan, T.7    Helsby, W.I.8    Irving, M.9    Lombardi, V.10
  • 9
    • 0017362413 scopus 로고
    • Structure of A-segments from frog and rabbit skeletal muscle
    • Craig R. Structure of A-segments from frog and rabbit skeletal muscle. J. Mol. Biol. 109 (1977) 69-81
    • (1977) J. Mol. Biol. , vol.109 , pp. 69-81
    • Craig, R.1
  • 10
    • 0016222057 scopus 로고
    • The effect of the performance of work on total energy output and metabolism during muscular contraction
    • Curtin N., Gilbert C., Kretzschmar K., and Wilkie D. The effect of the performance of work on total energy output and metabolism during muscular contraction. J. Physiol. (Lond.) 238 (1974) 455-472
    • (1974) J. Physiol. (Lond.) , vol.238 , pp. 455-472
    • Curtin, N.1    Gilbert, C.2    Kretzschmar, K.3    Wilkie, D.4
  • 11
    • 0018217817 scopus 로고
    • Energy changes and muscular contraction
    • Curtin N.A., and Woledge R.C. Energy changes and muscular contraction. Physiol. Rev. 58 (1978) 690-761
    • (1978) Physiol. Rev. , vol.58 , pp. 690-761
    • Curtin, N.A.1    Woledge, R.C.2
  • 12
    • 0018451348 scopus 로고
    • Chemical change and energy production during contraction of frog muscle: how are their time courses related?
    • Curtin N.A., and Woledge R.C. Chemical change and energy production during contraction of frog muscle: how are their time courses related?. J. Physiol. (Lond.) 288 (1979) 353-366
    • (1979) J. Physiol. (Lond.) , vol.288 , pp. 353-366
    • Curtin, N.A.1    Woledge, R.C.2
  • 13
    • 0019732155 scopus 로고
    • Effect of muscle length on energy balance in frog skeletal muscle
    • Curtin N.A., and Woledge R.C. Effect of muscle length on energy balance in frog skeletal muscle. J. Physiol. (Lond.) 316 (1981) 453-468
    • (1981) J. Physiol. (Lond.) , vol.316 , pp. 453-468
    • Curtin, N.A.1    Woledge, R.C.2
  • 17
    • 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 A., and Caputo C. The biphasic force-velocity relationship in frog muscle fibres and its evaluation in terms of cross-bridge function. J. Physiol. (Lond.) 503 (1997) 141-156
    • (1997) J. Physiol. (Lond.) , vol.503 , pp. 141-156
    • Edman, K.A.1    Mansson, A.2    Caputo, C.3
  • 18
    • 0017097417 scopus 로고
    • Non-hyperbolic force-velocity relationship in single muscle fibres
    • Edman K.A., Mulieri L.A., and Scubon-Mulieri B. Non-hyperbolic force-velocity relationship in single muscle fibres. Acta Physiol. Scand 98 (1976) 143-156
    • (1976) Acta Physiol. Scand , vol.98 , pp. 143-156
    • Edman, K.A.1    Mulieri, L.A.2    Scubon-Mulieri, B.3
  • 19
    • 1842599025 scopus 로고
    • A quantitative comparison between the energy liberated and the work performed by isolated sartorius muscle of the frog
    • Fenn W.O. A quantitative comparison between the energy liberated and the work performed by isolated sartorius muscle of the frog. J. Physiol. (Lond.) 58 (1923) 175-203
    • (1923) J. Physiol. (Lond.) , vol.58 , pp. 175-203
    • Fenn, W.O.1
  • 20
    • 0023162274 scopus 로고
    • The kinetics of heat production in response to active shortening in frog skeletal muscle
    • Ford L.E., and Gilbert S.H. The kinetics of heat production in response to active shortening in frog skeletal muscle. J. Physiol. (Lond.) 385 (1987) 449-470
    • (1987) J. Physiol. (Lond.) , vol.385 , pp. 449-470
    • Ford, L.E.1    Gilbert, S.H.2
  • 21
    • 0017385529 scopus 로고
    • Tension responses to sudden length change in stimulated frog muscle fibres near slack length
    • Ford L.E., Huxley A.F., and Simmons R.M. Tension responses to sudden length change in stimulated frog muscle fibres near slack length. J. Physiol. (Lond.) 269 (1977) 441-515
    • (1977) J. Physiol. (Lond.) , vol.269 , pp. 441-515
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 22
    • 0019390452 scopus 로고
    • The relation between stiffness and filament overlap in stimulated frog muscle fibres
    • Ford L.E., Huxley A.F., and Simmons R.M. The relation between stiffness and filament overlap in stimulated frog muscle fibres. J. Physiol. (Lond.) 311 (1981) 219-249
    • (1981) J. Physiol. (Lond.) , vol.311 , pp. 219-249
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 23
    • 0021895481 scopus 로고
    • Tension transients during steady shortening of frog muscle fibres
    • Ford L.E., Huxley A.F., and Simmons R.M. Tension transients during steady shortening of frog muscle fibres. J. Physiol. (Lond.) 361 (1985) 131-150
    • (1985) J. Physiol. (Lond.) , vol.361 , pp. 131-150
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 24
    • 0032411503 scopus 로고    scopus 로고
    • Efficiency of skeletal and cardiac muscle
    • Gibbs C.L., and Barclay C.J. Efficiency of skeletal and cardiac muscle. Adv. Exp. Med. Biol. 453 (1998) 527-535
    • (1998) Adv. Exp. Med. Biol. , vol.453 , pp. 527-535
    • Gibbs, C.L.1    Barclay, C.J.2
  • 25
    • 9244264224 scopus 로고
    • Heat, work and phsphorylcreatine splitting during muscular contraction. Cold Spring Harbor Symp
    • Gilbert C., Kretzschmar K.M., and Wilkie D.R. Heat, work and phsphorylcreatine splitting during muscular contraction. Cold Spring Harbor Symp. Quant. Biol. 37 (1972) 613-618
    • (1972) Quant. Biol. , vol.37 , pp. 613-618
    • Gilbert, C.1    Kretzschmar, K.M.2    Wilkie, D.R.3
  • 26
    • 0022702265 scopus 로고
    • The effect of length range on heat rate and power during shortening near in situ length in frog muscle
    • Gilbert S.H. The effect of length range on heat rate and power during shortening near in situ length in frog muscle. J. Muscle Res. Cell Motil. 7 (1986) 115-121
    • (1986) J. Muscle Res. Cell Motil. , vol.7 , pp. 115-121
    • Gilbert, S.H.1
  • 27
    • 0013947264 scopus 로고
    • An attempt at estimating extrafiber fluid in small skeletal muscles by a simple physical method
    • Goldspink G. An attempt at estimating extrafiber fluid in small skeletal muscles by a simple physical method. Can. J. Physiol. Pharmacol. 44 (1966) 765-775
    • (1966) Can. J. Physiol. Pharmacol. , vol.44 , pp. 765-775
    • Goldspink, G.1
  • 28
    • 0009946463 scopus 로고
    • The energy liberated by an isolated muscle during the performance of work
    • Hartree W., and Hill A.V. The energy liberated by an isolated muscle during the performance of work. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 104 (1928) 1-27
    • (1928) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.104 , pp. 1-27
    • Hartree, W.1    Hill, A.V.2
  • 29
    • 76349083243 scopus 로고
    • The factors determining the maximum work and the mechanical efficiency in muscle
    • Hartree W., and Hill A.V. The factors determining the maximum work and the mechanical efficiency in muscle. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 103 (1928) 234-251
    • (1928) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.103 , pp. 234-251
    • Hartree, W.1    Hill, A.V.2
  • 30
    • 0033877298 scopus 로고    scopus 로고
    • ATP consumption and efficiency of human single muscle fibers with different myosin isoform composition
    • He Z.H., Bottinelli R., Pellegrino M.A., Ferenczi M.A., and Reggiani C. ATP consumption and efficiency of human single muscle fibers with different myosin isoform composition. Biophys. J. 79 (2000) 945-961
    • (2000) Biophys. J. , vol.79 , pp. 945-961
    • He, Z.H.1    Bottinelli, R.2    Pellegrino, M.A.3    Ferenczi, M.A.4    Reggiani, C.5
  • 31
    • 0033564161 scopus 로고    scopus 로고
    • The efficiency of contraction in rabbit skeletal muscle fibres, determined from the rate of release of inorganic phosphate
    • He Z.H., Chillingworth R.K., Brune M., Corrie J.E., Webb M.R., and Ferenczi M.A. The efficiency of contraction in rabbit skeletal muscle fibres, determined from the rate of release of inorganic phosphate. J. Physiol. (Lond.) 517 (1999) 839-854
    • (1999) J. Physiol. (Lond.) , vol.517 , pp. 839-854
    • He, Z.H.1    Chillingworth, R.K.2    Brune, M.3    Corrie, J.E.4    Webb, M.R.5    Ferenczi, M.A.6
  • 32
    • 0042143675 scopus 로고
    • Methods of analysing the heat production of muscle
    • Hill A.V. Methods of analysing the heat production of muscle. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 124 (1937) 114-136
    • (1937) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.124 , pp. 114-136
    • Hill, A.V.1
  • 33
    • 0000682154 scopus 로고
    • Heat of shortening and the dynamic constants of muscle
    • Hill A.V. Heat of shortening and the dynamic constants of muscle. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 126 (1938) 136-195
    • (1938) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 35
    • 0011735948 scopus 로고
    • The heat of activation and the heat of shortening in a muscle twitch
    • Hill A.V. The heat of activation and the heat of shortening in a muscle twitch. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 136 (1949) 195-211
    • (1949) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.136 , pp. 195-211
    • Hill, A.V.1
  • 36
    • 0000660086 scopus 로고
    • The effect of load on the heat of shortening of muscle
    • Hill A.V. The effect of load on the heat of shortening of muscle. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 159 (1964) 297-318
    • (1964) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.159 , pp. 297-318
    • Hill, A.V.1
  • 37
    • 0000406551 scopus 로고
    • The efficiency of mechanical power development during muscular shortening and its relation to load
    • Hill A.V. The efficiency of mechanical power development during muscular shortening and its relation to load. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 159 (1964) 319-324
    • (1964) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.159 , pp. 319-324
    • Hill, A.V.1
  • 38
    • 0001027942 scopus 로고
    • An examination of absolute values in myothermic measurements
    • Hill A.V., and Woledge R.C. An examination of absolute values in myothermic measurements. J. Physiol. (Lond.) 162 (1962) 311-333
    • (1962) J. Physiol. (Lond.) , vol.162 , pp. 311-333
    • Hill, A.V.1    Woledge, R.C.2
  • 39
    • 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
  • 40
    • 0023161170 scopus 로고
    • Muscle enthalpy production and its relationship to actomyosin ATPase
    • Homsher E. Muscle enthalpy production and its relationship to actomyosin ATPase. Annu. Rev. Physiol. 49 (1987) 673-690
    • (1987) Annu. Rev. Physiol. , vol.49 , pp. 673-690
    • Homsher, E.1
  • 41
    • 0015741460 scopus 로고
    • Energetics of shortening muscles in twitches and tetanic contractions: I. A reinvestigation of Hill's concept of the shortening heat
    • Homsher E., and Rall J.A. Energetics of shortening muscles in twitches and tetanic contractions: I. A reinvestigation of Hill's concept of the shortening heat. J. Gen. Physiol 62 (1973) 663-676
    • (1973) J. Gen. Physiol , vol.62 , pp. 663-676
    • Homsher, E.1    Rall, J.A.2
  • 42
    • 0019731766 scopus 로고
    • High-energy phosphate metabolism and energy liberation associated with rapid shortening in frog skeletal muscle
    • Homsher E., Irving M., and Wallner A. High-energy phosphate metabolism and energy liberation associated with rapid shortening in frog skeletal muscle. J. Physiol. (Lond.) 321 (1981) 423-436
    • (1981) J. Physiol. (Lond.) , vol.321 , pp. 423-436
    • Homsher, E.1    Irving, M.2    Wallner, A.3
  • 43
    • 0023574445 scopus 로고
    • Repriming and reversal of the isometric unexplained enthalpy in frog skeletal muscle
    • Homsher E., Lacktis J., Yamada T., and Zohman G. Repriming and reversal of the isometric unexplained enthalpy in frog skeletal muscle. J. Physiol. (Lond.) 393 (1987) 157-170
    • (1987) J. Physiol. (Lond.) , vol.393 , pp. 157-170
    • Homsher, E.1    Lacktis, J.2    Yamada, T.3    Zohman, G.4
  • 44
    • 0015290096 scopus 로고
    • Activation heat, activation metabolism and tension-related heat in frog semitendinosus muscles
    • Homsher E., Mommaerts W.F., Ricchiuti N.V., and Wallner A. Activation heat, activation metabolism and tension-related heat in frog semitendinosus muscles. J. Physiol. (Lond.) 220 (1972) 601-625
    • (1972) J. Physiol. (Lond.) , vol.220 , pp. 601-625
    • Homsher, E.1    Mommaerts, W.F.2    Ricchiuti, N.V.3    Wallner, A.4
  • 45
    • 0021224691 scopus 로고
    • Energy balance studies in frog skeletal muscles shortening at one-half maximal velocity
    • Homsher E., Yamada T., Wallner A., and Tsai J. Energy balance studies in frog skeletal muscles shortening at one-half maximal velocity. J. Gen. Physiol. 84 (1984) 347-359
    • (1984) J. Gen. Physiol. , vol.84 , pp. 347-359
    • Homsher, E.1    Yamada, T.2    Wallner, A.3    Tsai, J.4
  • 46
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley A.F. Muscle structure and theories of contraction. Prog. Biophys. Biophysical Chem. 7 (1957) 255-318
    • (1957) Prog. Biophys. Biophysical Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 47
    • 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
  • 48
    • 0029801074 scopus 로고    scopus 로고
    • Filament compliance and tension transients in muscle
    • Huxley A.F., and Tideswell S. Filament compliance and tension transients in muscle. J. Muscle Res. Cell Motil. 17 (1996) 507-511
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 507-511
    • Huxley, A.F.1    Tideswell, S.2
  • 49
    • 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
  • 50
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • Huxley H.E., Stewart A., Sosa H., and Irving T. X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys. J. 67 (1994) 2411-2421
    • (1994) Biophys. J. , vol.67 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 51
    • 0019393860 scopus 로고
    • Variation in muscle stiffness with tension during tension transients and constant velocity shortening in the frog
    • Julian F.J., and Morgan D.L. Variation in muscle stiffness with tension during tension transients and constant velocity shortening in the frog. J. Physiol. (Lond.) 319 (1981) 193-203
    • (1981) J. Physiol. (Lond.) , vol.319 , pp. 193-203
    • Julian, F.J.1    Morgan, D.L.2
  • 52
    • 0016815857 scopus 로고
    • Variation of stiffness with force at increasing speeds of shortening
    • Julian F.J., and Sollins M.R. Variation of stiffness with force at increasing speeds of shortening. J. Gen. Physiol. 66 (1975) 287-302
    • (1975) J. Gen. Physiol. , vol.66 , pp. 287-302
    • Julian, F.J.1    Sollins, M.R.2
  • 53
    • 0014688993 scopus 로고
    • The chemical energetics of muscle contraction. II. The chemistry, efficiency and power of maximally working sartorius muscles. Appendix. Free energy and enthalpy of ATP hydrolysis in the sarcoplasm
    • Kushmerick M.J., and Davies R.E. The chemical energetics of muscle contraction. II. The chemistry, efficiency and power of maximally working sartorius muscles. Appendix. Free energy and enthalpy of ATP hydrolysis in the sarcoplasm. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 174 (1969) 315-353
    • (1969) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.174 , pp. 315-353
    • Kushmerick, M.J.1    Davies, R.E.2
  • 54
    • 0014688964 scopus 로고
    • The chemical energetics of muscle contraction. I. Activation heat, heat of shortening and ATP utilization for activation-relaxation processes
    • Kushmerick M.J., Larson R.E., and Davies R.E. The chemical energetics of muscle contraction. I. Activation heat, heat of shortening and ATP utilization for activation-relaxation processes. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 174 (1969) 293-313
    • (1969) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.174 , pp. 293-313
    • Kushmerick, M.J.1    Larson, R.E.2    Davies, R.E.3
  • 55
    • 0031958205 scopus 로고    scopus 로고
    • The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin. Biophys
    • Linari M., Dobbie I., Reconditi M., Koubassova N., Irving M., Piazzesi G., and Lombardi V. The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin. Biophys. J 74 (1998) 2459-2473
    • (1998) J , vol.74 , pp. 2459-2473
    • Linari, M.1    Dobbie, I.2    Reconditi, M.3    Koubassova, N.4    Irving, M.5    Piazzesi, G.6    Lombardi, V.7
  • 57
    • 58849127838 scopus 로고    scopus 로고
    • The effect of myofilament compliance on kinetics of force generation by myosin motors in muscle
    • Linari M., Piazzesi G., and Lombardi V. The effect of myofilament compliance on kinetics of force generation by myosin motors in muscle. Biophys. J. 96 (2009) 583-592
    • (2009) Biophys. J. , vol.96 , pp. 583-592
    • Linari, M.1    Piazzesi, G.2    Lombardi, V.3
  • 58
    • 0029161074 scopus 로고
    • Comparison of energy output during ramp and staircase shortening in frog-muscle fibers
    • Linari M., and Woledge R.C. Comparison of energy output during ramp and staircase shortening in frog-muscle fibers. J. Physiol. (Lond.) 487 (1995) 699-710
    • (1995) J. Physiol. (Lond.) , vol.487 , pp. 699-710
    • Linari, M.1    Woledge, R.C.2
  • 59
    • 0038069092 scopus 로고    scopus 로고
    • Energy storage during stretch of active single fibres from frog skeletal muscle
    • Linari M., Woledge R.C., and Curtin N.A. Energy storage during stretch of active single fibres from frog skeletal muscle. J. Physiol. (Lond.) 548 (2003) 461-474
    • (2003) J. Physiol. (Lond.) , vol.548 , pp. 461-474
    • Linari, M.1    Woledge, R.C.2    Curtin, N.A.3
  • 60
    • 0025690381 scopus 로고
    • The contractile response during steady lengthening of stimulated frog muscle fibres
    • Lombardi V., and Piazzesi G. The contractile response during steady lengthening of stimulated frog muscle fibres. J. Physiol. (Lond.) 431 (1990) 141-171
    • (1990) J. Physiol. (Lond.) , vol.431 , pp. 141-171
    • Lombardi, V.1    Piazzesi, G.2
  • 61
    • 0026571428 scopus 로고
    • Rapid regeneration of the actin-myosin power stoke in contracting muscle
    • Lombardi V., Piazzesi G., and Linari M. Rapid regeneration of the actin-myosin power stoke in contracting muscle. Nature 355 (1992) 638-641
    • (1992) Nature , vol.355 , pp. 638-641
    • Lombardi, V.1    Piazzesi, G.2    Linari, M.3
  • 62
    • 0016792909 scopus 로고
    • Sizes of components in frog skeletal muscle measured by methods of stereology
    • Mobley B.A., and Eisenberg B.R. Sizes of components in frog skeletal muscle measured by methods of stereology. J. Gen. Physiol. 66 (1975) 31-45
    • (1975) J. Gen. Physiol. , vol.66 , pp. 31-45
    • Mobley, B.A.1    Eisenberg, B.R.2
  • 63
    • 0027429944 scopus 로고
    • Kinetics of regeneration of cross-bridge power stroke in shortening muscle
    • Piazzesi G., Linari M., and Lombardi V. Kinetics of regeneration of cross-bridge power stroke in shortening muscle. Adv. Exp. Med. Biol. 332 (1993) 691-700
    • (1993) Adv. Exp. Med. Biol. , vol.332 , pp. 691-700
    • Piazzesi, G.1    Linari, M.2    Lombardi, V.3
  • 64
    • 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
  • 65
    • 0037112540 scopus 로고    scopus 로고
    • The size and the speed of the working stroke of muscle myosin and its dependence on the force
    • Piazzesi G., Lucii L., and Lombardi V. The size and the speed of the working stroke of muscle myosin and its dependence on the force. J. Physiol. (Lond.) 545 (2002) 145-151
    • (2002) J. Physiol. (Lond.) , vol.545 , pp. 145-151
    • Piazzesi, G.1    Lucii, L.2    Lombardi, V.3
  • 68
    • 0001625450 scopus 로고
    • Kinetics of muscular contraction: the approach to the steady state
    • Podolsky R.J. Kinetics of muscular contraction: the approach to the steady state. Nature 188 (1960) 666-668
    • (1960) Nature , vol.188 , pp. 666-668
    • Podolsky, R.J.1
  • 69
    • 0029908822 scopus 로고    scopus 로고
    • Increase in ATP consumption during shortening in skinned fibres from rabbit psoas muscle: effects of inorganic phosphate
    • Potma E., and Stienen G. Increase in ATP consumption during shortening in skinned fibres from rabbit psoas muscle: effects of inorganic phosphate. J. Physiol. (Lond.) 496 (1996) 1-12
    • (1996) J. Physiol. (Lond.) , vol.496 , pp. 1-12
    • Potma, E.1    Stienen, G.2
  • 70
    • 0017067484 scopus 로고
    • A temporal dissociation of energy liberation and high energy phosphate splitting during shortening in frog skeletal muscles
    • Rall J.A., Homsher E., Wallner A., and Mommaerts W.F. A temporal dissociation of energy liberation and high energy phosphate splitting during shortening in frog skeletal muscles. J. Gen. Physiol. 68 (1976) 13-27
    • (1976) J. Gen. Physiol. , vol.68 , pp. 13-27
    • Rall, J.A.1    Homsher, E.2    Wallner, A.3    Mommaerts, W.F.4
  • 72
    • 0030877965 scopus 로고    scopus 로고
    • Chemo-mechanical energy transduction in relation to myosin isoform composition in skeletal muscle fibres of the rat
    • Reggiani C., Potma E.J., Bottinelli R., Canepari M., Pellegrino M.A., and Stienen G.J.M. Chemo-mechanical energy transduction in relation to myosin isoform composition in skeletal muscle fibres of the rat. J. Physiol. (Lond.) 502 (1997) 449-460
    • (1997) J. Physiol. (Lond.) , vol.502 , pp. 449-460
    • Reggiani, C.1    Potma, E.J.2    Bottinelli, R.3    Canepari, M.4    Pellegrino, M.A.5    Stienen, G.J.M.6
  • 73
    • 0015296262 scopus 로고
    • Energetics of activation in frog and toad muscle
    • Smith I.C.H. Energetics of activation in frog and toad muscle. J. Physiol. (Lond.) 220 (1972) 583-599
    • (1972) J. Physiol. (Lond.) , vol.220 , pp. 583-599
    • Smith, I.C.H.1
  • 75
    • 0041557636 scopus 로고
    • Organisation and properties of the straited muscle sarcomere
    • Squire J.M. (Ed), Macmillan, London
    • Squire J.M., Luther P.K., and Morris E.P. Organisation and properties of the straited muscle sarcomere. In: Squire J.M. (Ed). Molecular Mechanisms in Muscular Contraction (1990), Macmillan, London 1-48
    • (1990) Molecular Mechanisms in Muscular Contraction , pp. 1-48
    • Squire, J.M.1    Luther, P.K.2    Morris, E.P.3
  • 76
    • 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. (Lond.) 531 (2001) 781-791
    • (2001) J. Physiol. (Lond.) , vol.531 , pp. 781-791
    • Sun, Y.B.1    Hilber, K.2    Irving, M.3
  • 77
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction
    • Wakabayashi K., Sugimoto Y., Tanaka H., Ueno Y., Takezawa Y., and Amemiya Y. X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys. J. 67 (1994) 2422-2435
    • (1994) Biophys. J. , vol.67 , pp. 2422-2435
    • Wakabayashi, K.1    Sugimoto, Y.2    Tanaka, H.3    Ueno, Y.4    Takezawa, Y.5    Amemiya, Y.6
  • 79
    • 67650911685 scopus 로고    scopus 로고
    • Temperature change as a probe of muscle crossbridge kinetics: a review and discussion
    • Woledge R.C., Barclay C.J., and Curtin N.A. Temperature change as a probe of muscle crossbridge kinetics: a review and discussion. Proc. R. Soc. Lond., Ser. B: Biol. Sci. 276 (2009) 2685-2695
    • (2009) Proc. R. Soc. Lond., Ser. B: Biol. Sci. , vol.276 , pp. 2685-2695
    • Woledge, R.C.1    Barclay, C.J.2    Curtin, N.A.3
  • 81
    • 0024044377 scopus 로고
    • Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells
    • Woledge R.C., and Reilly P.J. Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells. Biophys. J. 54 (1988) 97-104
    • (1988) Biophys. J. , vol.54 , pp. 97-104
    • Woledge, R.C.1    Reilly, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.