메뉴 건너뛰기




Volumn 74, Issue 4, 1998, Pages 1611-1621

Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING SITE; ENERGY CONSUMPTION; FORCE; MATHEMATICAL MODEL; MECHANICS; MUSCLE CONTRACTION; MUSCLE FORCE; MYOFILAMENT; SKELETAL MUSCLE; SYSTEM ANALYSIS;

EID: 0031953771     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77875-0     Document Type: Article
Times cited : (134)

References (36)
  • 1
    • 0025094287 scopus 로고
    • Tension and stiffness of frog muscle fibres at full filament overlap
    • Bagni, M. A., G. Cecchi, F. Colomo, and C. Peggesi. 1990. Tension and stiffness of frog muscle fibres at full filament overlap. J. Mus. Res. Cell Motil. 11:371-377.
    • (1990) J. Mus. Res. Cell Motil. , vol.11 , pp. 371-377
    • Bagni, M.A.1    Cecchi, G.2    Colomo, F.3    Peggesi, C.4
  • 3
    • 0028934207 scopus 로고
    • Effect of physiological ADP levels on contraction of single skinned fibers from rabbit fast and slow muscles
    • Chase, P. B., and M. J. Kushmerick. 1995. Effect of physiological ADP levels on contraction of single skinned fibers from rabbit fast and slow muscles. Am. J. Physiol. 268:C480-C489.
    • (1995) Am. J. Physiol. , vol.268
    • Chase, P.B.1    Kushmerick, M.J.2
  • 4
    • 0026513219 scopus 로고
    • Dynamics of single-motor molecules: The thermal ratchet model
    • Córdova, N. J., B. Ermentrout, and G. Oster. 1992. Dynamics of single-motor molecules: the thermal ratchet model. Proc. Natl. Acad. Sci. USA. 89:339-343.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 339-343
    • Córdova, N.J.1    Ermentrout, B.2    Oster, G.3
  • 5
    • 0020040724 scopus 로고
    • Chemical energetics of slow-and fast-twitch muscle of the mouse
    • Crow, M. T., and M. J. Kushmerick. 1982. Chemical energetics of slow-and fast-twitch muscle of the mouse. J. Gen. Physiol. 79:147-166.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 147-166
    • Crow, M.T.1    Kushmerick, M.J.2
  • 6
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers
    • Dantzig, J., Y. E. Goldman, N. Lacktis, and E. Homsher. 1992. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers. J. Physiol. (Lond.). 451:247-278.
    • (1992) J. Physiol. (Lond.) , vol.451 , pp. 247-278
    • Dantzig, J.1    Goldman, Y.E.2    Lacktis, N.3    Homsher, E.4
  • 7
    • 0023729295 scopus 로고
    • Double-hyperbolic force-velocity relation in frog muscle fibres
    • Edman, K. A. P. 1988. Double-hyperbolic force-velocity relation in frog muscle fibres. J. Physiol. (Lond.). 404:301-321.
    • (1988) J. Physiol. (Lond.) , vol.404 , pp. 301-321
    • Edman, K.A.P.1
  • 8
    • 36448998595 scopus 로고
    • Theoretical foundations of Monte Carlo simulations
    • Fichthorn, K. A., and W. H. Weinberg. 1991. Theoretical foundations of Monte Carlo simulations. J. Chem. Phys. 95:1090-1096.
    • (1991) J. Chem. Phys. , vol.95 , pp. 1090-1096
    • Fichthorn, K.A.1    Weinberg, W.H.2
  • 9
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • Finer, J. T., R. M. Simmons, and J. A. Spudich. 1994. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature. 368:113-119.
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 10
    • 0017385529 scopus 로고
    • Tension responses to sudden length changes in stimulated frog muscle fibres near slack length
    • Ford, L. E., A. F. Huxley, and R. M. Simmons. 1977. Tension responses to sudden length changes in stimulated frog muscle fibres near slack length. J. Physiol. (Lond.). 269:441-515.
    • (1977) J. Physiol. (Lond.) , vol.269 , pp. 441-515
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 11
    • 0019390452 scopus 로고
    • The relationship between stiffness and filament overlap in stimulated frog muscle fibres
    • Ford, L. E., A. F. Huxley, and R. M. Simmons. 1981. The relationship between stiffness and filament overlap in stimulated frog muscle fibres. J. Physiol. (Lond.). 311:219-249.
    • (1981) J. Physiol. (Lond.) , vol.311 , pp. 219-249
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 12
    • 0021891179 scopus 로고
    • Dependence of adenosine triphosphate activity of rabbit psoas muscle fibres and myofibrils on substrate concentration
    • Glynn, H., and J. Sleep. 1985. Dependence of adenosine triphosphate activity of rabbit psoas muscle fibres and myofibrils on substrate concentration. J. Physiol. (Lond.). 365:259-276.
    • (1985) J. Physiol. (Lond.) , vol.365 , pp. 259-276
    • Glynn, H.1    Sleep, J.2
  • 13
    • 0028000070 scopus 로고
    • Actin compliance: Are you pulling my chain?
    • Goldman, Y. E., and A. F. Huxley. 1994. Actin compliance: are you pulling my chain? Biophys. J. 67:2131-2133.
    • (1994) Biophys. J. , vol.67 , pp. 2131-2133
    • Goldman, Y.E.1    Huxley, A.F.2
  • 14
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in venebrate muscle fibres
    • Gordon, A. M., A. F. Huxley, and F. J. Julian. 1966. The variation in isometric tension with sarcomere length in venebrate muscle fibres. J. Physiol. 184:170-192.
    • (1966) J. Physiol. , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 15
    • 0025021116 scopus 로고
    • Cross-bridge cycling theories cannot explain high-speed lengthening behavior in frog muscle
    • Harry, J. D., A. W. Ward, N. C. Heglund, D. L. Morgan, and T. A. McMahon. 1990. Cross-bridge cycling theories cannot explain high-speed lengthening behavior in frog muscle. Biophys. J. 57:201-208.
    • (1990) Biophys. J. , vol.57 , pp. 201-208
    • Harry, J.D.1    Ward, A.W.2    Heglund, N.C.3    Morgan, D.L.4    McMahon, T.A.5
  • 16
    • 0029162081 scopus 로고
    • Compliance of thin filaments in skinned fibers of rabbit skeletal muscle
    • Higuchi, H., T. Yanagida, and Y. E. Goldman. 1995. Compliance of thin filaments in skinned fibers of rabbit skeletal muscle. Biophys. J. 69:1000-1010.
    • (1995) Biophys. J. , vol.69 , pp. 1000-1010
    • Higuchi, H.1    Yanagida, T.2    Goldman, Y.E.3
  • 17
    • 0343299432 scopus 로고
    • The effects of shortening on the phosphate release step of the actomyosin ATPase mechanism
    • Homsher, E., and J. Lacktis. 1988. The effects of shortening on the phosphate release step of the actomyosin ATPase mechanism. Biophys. J. 53:564a.
    • (1988) Biophys. J. , vol.53
    • Homsher, E.1    Lacktis, J.2
  • 18
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard, J. 1997. Molecular motors: structural adaptations to cellular functions. Nature. 389:561-567.
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 20
    • 0028145209 scopus 로고
    • The force exerted by a single kinesin molecule against a viscous load
    • Hunt, A. J., F. Gittes, and J. Howard. 1994. The force exerted by a single kinesin molecule against a viscous load. Biophys. J. 67:766-781.
    • (1994) Biophys. J. , vol.67 , pp. 766-781
    • Hunt, A.J.1    Gittes, F.2    Howard, J.3
  • 21
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and R. M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 22
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • Huxley, H. E., A. Stewart, H. Sosa, and T. Irving. 1994. X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys. J. 67:2411-2421.
    • (1994) Biophys. J. , vol.67 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 23
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations: Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert, H. P., A. C. Venier, A. Maggs, A. Fattoum, R. Kassab, D. Pantaloni, and M. R. Carlier. 1995. Flexibility of actin filaments derived from thermal fluctuations: effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 270:11437-11444.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11437-11444
    • Isambert, H.P.1    Venier, A.C.2    Maggs, A.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6    Carlier, M.R.7
  • 24
    • 0028607563 scopus 로고
    • Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima, H., A. Ishijima, and T. Yanagida. 1994. Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc. Natl. Acad. Sci. USA. 91:12962-12966.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 25
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers, H. A. 1940. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica. 7:284-304.
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 26
    • 0026732710 scopus 로고
    • Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi
    • Kushmerick, M. J., T. S. Moerland, and R. W. Wiseman. 1992. Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi. Proc. Natl. Acad Sci. USA. 89:7521-7525.
    • (1992) Proc. Natl. Acad Sci. USA , vol.89 , pp. 7521-7525
    • Kushmerick, M.J.1    Moerland, T.S.2    Wiseman, R.W.3
  • 27
    • 0029758343 scopus 로고    scopus 로고
    • On the theory of muscle contraction: Filament extensibility and the development of isometric force and stiffness
    • Mijailovich, S. M., J. J. Fredberg, and J. P. Butler. 1996. On the theory of muscle contraction: filament extensibility and the development of isometric force and stiffness. Biophys. J. 71:1475-1484.
    • (1996) Biophys. J. , vol.71 , pp. 1475-1484
    • Mijailovich, S.M.1    Fredberg, J.J.2    Butler, J.P.3
  • 29
    • 0028964579 scopus 로고
    • Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers
    • Molloy, J. E., J. E. Burns, J. C. Sparrow, R. T. Tregear, J. Kendrick-Jones, and D. C. S. White. 1995b. Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers. Biophys. J. 68:298-305.
    • (1995) Biophys. J. , vol.68 , pp. 298-305
    • Molloy, J.E.1    Burns, J.E.2    Sparrow, J.C.3    Tregear, R.T.4    Kendrick-Jones, J.5    White, D.C.S.6
  • 32
    • 0031028458 scopus 로고    scopus 로고
    • Cross-bridge detachment and attachment following a step stretch imposed on active single frog muscle fibers
    • Piazzesi, G., M. Linari, M. Reconditi, F. Vanzi, and V. Lombardi. 1997. Cross-bridge detachment and attachment following a step stretch imposed on active single frog muscle fibers. J. Physiol. (Lond.). 498:3-15.
    • (1997) J. Physiol. (Lond.) , vol.498 , pp. 3-15
    • Piazzesi, G.1    Linari, M.2    Reconditi, M.3    Vanzi, F.4    Lombardi, V.5
  • 33
    • 0028907268 scopus 로고
    • A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle
    • Piazzesi, G., and V. Lombardi. 1995. A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle. Biophys. J. 68:1966-1979.
    • (1995) Biophys. J. , vol.68 , pp. 1966-1979
    • Piazzesi, G.1    Lombardi, V.2
  • 35
    • 0030969084 scopus 로고    scopus 로고
    • Detachment of low-force bridges contributes to the rapid tension transients of skinned rabbit skeletal muscle fibres
    • Seow, C. Y., S. G. Shroff, and L. E. Ford. 1997. Detachment of low-force bridges contributes to the rapid tension transients of skinned rabbit skeletal muscle fibres. J. Physiol. (Lond.). 501:149-164.
    • (1997) J. Physiol. (Lond.) , vol.501 , pp. 149-164
    • Seow, C.Y.1    Shroff, S.G.2    Ford, L.E.3
  • 36
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin an myosin filaments during muscle contraction
    • Wakabayashi, K., Y. Sugimoto, H. Tanaka, Y. Ueno, Y. Takezawa, and Y. Amemiya. 1994. X-ray diffraction evidence for the extensibility of actin an myosin filaments during muscle contraction. Biophys. J. 67:2422-2435.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.