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7. References
Bagni, M. A., Cecchi, G., Colomo, F. and Garzella P., 1992, Are weakly binding bridges present in resting intact muscle fibers?, Biophys. J. 63: 1412–1415.
Bagni, M. A., Cecchi, G., Colomo, F. and Garzella P., 1995, Absence of mechanical evidence for attached weakly binding cross-bridges in frog relaxed muscle fibers, J. Physiol. 482: 391–400.
Bagshaw, C. R., 1994. Muscle Contraction, Chapman & Hall, London.
Cecchi, G., Griffiths, P. J., and Taylor, S., 1982, Muscular contraction: kinetics of cross-bridge attachment studied by high-frequency stiffness measurements, Science. 217: 70–72.
Cecchi, G., Griffiths, P. J., and Taylor, S., 1984, The kinetics of cross-bridge attachment and detachment studied by high frequency stiffness measurements, in: Contractile Mechanisms in Muscle, H, Sugi, G. H. Pollack eds., Plenum, New York, pp. 641–655.
Cecchi, G., Griffiths, P. J., and Taylor, S., 1986, Stiffness and force in activated frog skeletal muscle fibers, Biophys. J. 49: 437–451.
Civan, M. M., and Podolsky, R. J., 1966, Contractile kinetics of striated muscle fibres following quick changes in load, J. Physiol. 184: 511–534.
Ford, L. E., Huxley, A. F., and Simmons, R.M., 1971, Tension responses to sudden length change in stimulated frog muscle fibres near slack length, J. Physiol. 269: 441–515.
Goldman, Y. E., Hibberd, M. G., and Trentham, D. R., 1984, Relaxation of rabbit psoas muscle fibers from rigor by photochemical generation of adenosine-5′-triphosphate, J. Physiol. 354: 577–604.
Gordon, A. M., Huxley, A. F., and Julian, F. J., 1966, Tension development in highly stretched vertebrate muscle fibres, J. Physiol. 184: 143–169.
Gordon, A. M., Huxley, A. F., and Julian, F. J., 1966, The variation in isometric tension with sarcomere length in vertebrate muscle fibres, J. Physiol. 184: 170–192.
Harada, Y., Sakurada, K., Aoki, T., Tohmas, D. D., and Yanagida, T., 1990, Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay, J. Mol. Biol. 216: 49–68.
Harrington, W. F., Ueno, H., and Davis, J. S., 1988, Helix-coil melting in rigor and activated cross-bridges of skeletal muscle, in: Molecular Mechanism of Muscle Contraction, H, Sugi, G. H. Pollack eds., Plenum, New York, pp. 307–318.
Hatta, I., Sugi, H., and Tamura, Y., 1988, Stiffness changes in frog skeletal muscle during contraction recorded using ultrasonic waves, J. Physiol. 403: 193–209.
He, Z-H., Chillingworth, R. K., Brune, M, Corrie, J. E. T., Webb, M. R., and Ferenczi, M. A., 1999, The efficiency of contraction in rabbit skeletal muscle fibers, determined from the rate of release of inorganic phosphate, J. Physiol. 517: 839–854.
Higuchi, H., and Goldman, Y. E., 1991, Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres, Nature. 352: 352–354.
Hill, A. V., 1938, The heat of shortening and the dynamic constants of muscle, Proc. Roy. Soc. Lond. B126: 136–195
Howard, J., 1997, Molecular motors: structural adaptations to cellular functions, Nature. 389: 561–567.
Huxley, A. F., 1957, Muscle structure and theories of contraction, Prog. Biophys. Biophys. Chem. 7: 255–318.
Huxley, A. F., 1974, Muscular contraction, J. Physiol. 243: 1–43.
Huxley, A. F., and Simmons, R.M., 1971, Proposed mechanism of force generation in striated muscle. Nature. 233:533–538.
Huxley, H. E., and Faruqi, A. R., 1983, Time-resolved X-ray diffraction studies on vertebrate striated muscle, Annl Rev. Biophys. Bioeng. 12: 381–417.
Huxley, H. E., and Hanson, J., 1954, Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation, Nature. 173: 973–976.
Julian, F. J., and Sollins, M. R., 1975, Variation of muscle stiffness with force at increasing speeds of shortening, J. Gen. Physiol. 66: 282–302.
Kinosita, K. Jr., Yasuda, R., Noji, H., and Adachi, K., 2000, A rotary molecular motor that can work at near 100% efficiency, Phil. Trans. R. Soc. B. 355: 473–489.
Kobayashi, T., Kosuge, S., Karr, T., and Sugi, H., 1998, Evidence for bidirectional functional communication between myosin subfragments 1 and 2 in skeletal muscle fibers, Biochem. Biophys. Res. Commun. 246: 539–542.
Kron, S. J., and Spudich, J. A., 1986, Fluorescent actin filament move on myosin fixed to a glass surface, Proc. Natl. Acad. Sci. USA. 83: 6272–6276.
Oiwa, K., Chaen. S., and Sugi, H., 1991, Measurment of work done by ATP-indiced sliding between rabbit muscle myosin and algal cell actin cables in vitro, J. Physiol. 437: 715–763.
Oiwa, K., Kawakami, T., and Sugi, H., 1993, Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis, J. Biochem. 114: 28–32.
Podolsky, R. J., Nolan, A. C, and Zavaler, S. A., 1969, Cross-bridge properties derived from muscle isotonic velocity transients, Proc. Natl. Acad. Sci. USA. 64: 504–511.
Reggiani, C, Potma, E. J., Bottinelli, R., Canepari, M., Pellegrino, M. A., and Stienen, G. J. M., 1997, Chemo-mechanical energy transduction in relation to myosin isoform composition in skeletal muscle fibers of the rat, J. Physiol. 502: 449–460.
Stehle, R., and Brenner B., 2000, Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament shortening, Biophys. J. 78: 1458–1473.
Sugi, H., 1992, Molecular mechanisms of actin-myosin interaction in muscle contraction, in: Muscle, Contraction and Cell Motility, H. Sugi, ed., Springer, Berlin and Heidelberg, pp. 131–171.
Sugi, H., 1993, Molecular mechanism of ATP dependent actin-myosin interaction in muscle contraction, Jpn. J. Physiol. 43: 435–454.
Sugi, H., Akimoto T., Sutoh, K., Chaen, S., Oishi, N., and Suzuki, S., 1997, Dynamic electron microscopy of ATP-induced myosin head movement in living muscle thick filaments, Proc. Natl. Acad. Sci. USA. 94: 4378–4382.
Sugi, H., Iwamoto, H., Akimoto T., and Kishi, H., 2003, High mechanical efficiency of the cross-bridge powerstroke in skeletal muscle, J. Exp. Biol. 206: 1201–1206.
Sugi, H., Iwamoto, H., Akimoto T., and Ushitani, H., 1998, Evidence for the load-dependent mechanical efficiency of individual myosin heads in skeletal muscle fibers activated by laser flash photolysis of caged calcium in the presence of a limited amount of ATP, Proc. Natl. Acad. Sci. 95: 2273–2278.
Sugi, H., and Kobayashi, T, 1983, Sarcomere length and tension changes in tetanized frog muscle fibers after quick stretches and releases, Proc. Natl. Acad. Sci. USA. 80: 6422–6425.
Sugi, H., and Tsuchiya, T., 1981, Isotonic velocity transients in frog muscle fibres following quick changes in load, J. Physiol. 319: 239–252.
Sugi, H., and Tsuchiya, T., 1988, Stiffness changes during enhancement and deficit of isometric force by slow length changes in frog skeletal muscle fibres, J. Physiol. 407: 215–229.
Sugi, H., and Tsuchiya, T, 1998, Muscle mechanics I: intact single muscle fibres, in: Current Methods in Muscle Physiology; Advantages, Problems and Limitations, H, Sugi, ed., Oxford University Press, Oxford, pp. 3–31.
Sun, Y-B., Hilber K., and Irving, M., 2001, Effect of active shortening on the rate of ATP utilization by rabbit psoas muscle fibers, J. Physiol. 531: 781–791.
Tamura, Y., Hatta, I., Matsuda, T., Sugi, H., and Tsuchiya, T., 1982, Changes in muscle stiffness during contraction recorded using ultrasonic waves, Nature. 299: 631–633.
Toyoshima, Y. Y., Kron, S. J., and Spudich, J. A., 1990, The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro motility assay, Proc. Natl. Acad. Sci. USA. 87: 7130–7134.
Uyeda, T. P. Q., Kron, S. J., and Spudich, J. A, 1990, Myosin step size estimation from slow sliding movement of actin over low densities of heavy meromyosin, J. Mol. Biol. 214: 699–710.
Vale, R. D., and Osawa, F., 1990, Protein motors and Maxwell’s demons: does mechanochemical transduction involve a thermal rachet, Adv. Biophys. 26: 97–134.
Yamada, T., Abe, O., Kobayashi, T., and Sugi, H., 1993, Myofilament sliding per ATP molecule in rabbit muscle fibres studied using laser flash photolysis of caged ATP, J. Physiol. 466: 229–243.
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Sugi, H., Chaen, S., Shirakawa, I. (2005). Mysteries about Amplitude and Efficiency of Cross-Bridge Powerstroke. In: Sugi, H. (eds) Sliding Filament Mechanism in Muscle Contraction. Advances in Experimental Medicine and Biology, vol 565. Springer, Boston, MA. https://doi.org/10.1007/0-387-24990-7_8
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