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Volumn 5, Issue 1, 1998, Pages 73-86

Modelling and simulation of motility in actomyosin systems

Author keywords

Actomyosin interaction; Langevin dynamics

Indexed keywords

ACTIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 0031901545     PISSN: 10665277     EISSN: None     Source Type: Journal    
DOI: 10.1089/cmb.1998.5.73     Document Type: Article
Times cited : (4)

References (51)
  • 1
    • 0028811467 scopus 로고
    • One small step for myosin
    • Block, S.M. 1995. One small step for myosin. Nature 378, 132-133.
    • (1995) Nature , vol.378 , pp. 132-133
    • Block, S.M.1
  • 2
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block, S.M., Goldstein, L.S.B., and Schnapp, B.J. 1990. Bead movement by single kinesin molecules studied with optical tweezers. Nature 348, 348-352.
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.B.2    Schnapp, B.J.3
  • 3
    • 0016684015 scopus 로고
    • Structural dynamics of frog muscle during isometric contraction
    • Bonner, F.R., and Carlson, F.D. 1975. Structural dynamics of frog muscle during isometric contraction. J. Gen. Physiol. 65, 555-581.
    • (1975) J. Gen. Physiol. , vol.65 , pp. 555-581
    • Bonner, F.R.1    Carlson, F.D.2
  • 4
    • 0017729576 scopus 로고
    • Fluctuations in tension during contraction of single muscle fibers
    • Borejdo, J., and Morales, M.F. 1977. Fluctuations in tension during contraction of single muscle fibers. Biophys. J. 20, 315-334.
    • (1977) Biophys. J. , vol.20 , pp. 315-334
    • Borejdo, J.1    Morales, M.F.2
  • 5
    • 0017172336 scopus 로고
    • Computer simulation of movement-generating cross-bridges
    • Brokaw, C.J. 1976. Computer simulation of movement-generating cross-bridges. Biophys. J. 16, 1013-1027.
    • (1976) Biophys. J. , vol.16 , pp. 1013-1027
    • Brokaw, C.J.1
  • 6
    • 0027103829 scopus 로고
    • Myosin step size: Estimates from motility assays and shortening muscle
    • Burton, K. 1992. Myosin step size: Estimates from motility assays and shortening muscle. J. Musl. Res. Cell Motil. 13, 590-607.
    • (1992) J. Musl. Res. Cell Motil. , vol.13 , pp. 590-607
    • Burton, K.1
  • 7
    • 0016805847 scopus 로고
    • Structural fluctuations in the steady state of muscular contraction
    • Carlson, F.D. 1975. Structural fluctuations in the steady state of muscular contraction. Biophys. J. 15, 633-649.
    • (1975) Biophys. J. , vol.15 , pp. 633-649
    • Carlson, F.D.1
  • 8
    • 0002121327 scopus 로고
    • Stochastic problems in physics and astronomy
    • Chandrasekhar, S. 1943. Stochastic problems in physics and astronomy. Rev. Mod. Phys. 15, 1-89.
    • (1943) Rev. Mod. Phys. , vol.15 , pp. 1-89
    • Chandrasekhar, S.1
  • 9
    • 0026513219 scopus 로고
    • Dynamics of single-motor molecules: The thermal ratchet model
    • Cordova, N.J., Ermentrout, B., and Oster, G.F. 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
    • Cordova, N.J.1    Ermentrout, B.2    Oster, G.F.3
  • 11
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • Finer, J.T., Simmons, R.M., and Spudich, J.A. 1994. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature 368, 113-118.
    • (1994) Nature , vol.368 , pp. 113-118
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 12
    • 0028932523 scopus 로고
    • Characterization of single actin-myosin interactions
    • Finer, J.T., Mehta, A.D., and Spudich, J.A. 1995. Characterization of single actin-myosin interactions. Biophys J. 68, 291s-297s.
    • (1995) Biophys J. , vol.68
    • Finer, J.T.1    Mehta, A.D.2    Spudich, J.A.3
  • 13
    • 0017385529 scopus 로고
    • Tension responses to sudden length change in simulated frog muscle fibres near slack length
    • Ford, L.E., Huxley, A.F., and Simmons, R.M. 1977. Tension responses to sudden length change in simulated frog muscle fibres near slack length. J. Physiol 269, 441-515.
    • (1977) J. Physiol , vol.269 , pp. 441-515
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 14
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in vertebrate muscle fibers
    • Gordon, A.M., Huxley, A.F., and Julian, F.J. 1966. The variation in isometric tension with sarcomere length in vertebrate muscle fibers. 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
    • 0031041817 scopus 로고    scopus 로고
    • Smooth-muscle and skeletal-muscle myosins produce similar unitary forces and displacements in laser trap
    • Guilford, W.H., Dupuis, D.E., Kennedy, G., Wu, J., Patlak, J.B., and Warshaw, D.M. 1997. Smooth-muscle and skeletal-muscle myosins produce similar unitary forces and displacements in laser trap. Biophys. J. 72, 1-16.
    • (1997) Biophys. J. , vol.72 , pp. 1-16
    • Guilford, W.H.1    Dupuis, D.E.2    Kennedy, G.3    Wu, J.4    Patlak, J.B.5    Warshaw, D.M.6
  • 16
    • 0016180488 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle: Part I
    • Hill, T.L. 1974. Theoretical formalism for the sliding filament model of contraction of striated muscle: Part I. Prog. Biophys. Mol. Biol. 28, 269-341.
    • (1974) Prog. Biophys. Mol. Biol. , vol.28 , pp. 269-341
    • Hill, T.L.1
  • 17
    • 0028314288 scopus 로고
    • Clamping down on myosin
    • Howard, J. 1994. Clamping down on myosin. Nature 368, 98-99.
    • (1994) Nature , vol.368 , pp. 98-99
    • Howard, J.1
  • 18
    • 36949093311 scopus 로고
    • Changes in the cross-striation of muscle during contraction and stretch and their structural interpretation
    • Huxley, H.E., and Hanson, J. 1954. Changes in the cross-striation of muscle during contraction and stretch and their structural interpretation. Nature 173, 973-976.
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.E.1    Hanson, J.2
  • 19
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A.F. 1957. Muscle structure and theories of contraction. Prog. Biophys. Chem. 7, 255-318.
    • (1957) Prog. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 20
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley, H.E. 1969. The mechanism of muscular contraction. Science 164, 1356-1366.
    • (1969) Science , vol.164 , pp. 1356-1366
    • Huxley, H.E.1
  • 21
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A.F., and Simmons, R.M. 1971. Proposed mechanism of force generation in striated muscle. Nature 233, 533-540.
    • (1971) Nature , vol.233 , pp. 533-540
    • Huxley, A.F.1    Simmons, R.M.2
  • 23
    • 0030031120 scopus 로고    scopus 로고
    • Multiple- and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: Unitary steps and forces
    • Ishijima, A., Kojima, H., Higuchi, H., Harada, Y., Funatsu, T., and Yanagida, T. 1996. Multiple- and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: Unitary steps and forces. Biophys. J. 70, 383-400.
    • (1996) Biophys. J. , vol.70 , pp. 383-400
    • Ishijima, A.1    Kojima, H.2    Higuchi, H.3    Harada, Y.4    Funatsu, T.5    Yanagida, T.6
  • 24
    • 0014495551 scopus 로고
    • Activation in a skeletal muscle contraction model with a modification for insect fibrilar muscle
    • Julian, F.J. 1969. Activation in a skeletal muscle contraction model with a modification for insect fibrilar muscle. Biophys. J. 14, 547-570.
    • (1969) Biophys. J. , vol.14 , pp. 547-570
    • Julian, F.J.1
  • 25
    • 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. 1994. Effect of series elasticity on delay in development of tension relative to stiffness during muscle activation. Am. J. Physiol. 267, C1598-C1606.
    • (1994) Am. J. Physiol. , vol.267
    • Luo, Y.1    Cooke, R.2    Pate, E.3
  • 27
    • 0028408334 scopus 로고
    • Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay
    • Miyata, H., Hakozaki, H., Yoshikawa, H., Suzuki, N., Kinosita, K., Nishizaka, T., and Ishiwata, S. 1994. Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay. J. Biochem. 115, 644-647.
    • (1994) J. Biochem. , vol.115 , pp. 644-647
    • Miyata, H.1    Hakozaki, H.2    Yoshikawa, H.3    Suzuki, N.4    Kinosita, K.5    Nishizaka, T.6    Ishiwata, S.7
  • 29
    • 0028964579 scopus 로고
    • Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or drosophila actin using optical tweezers
    • Molloy, J.E., Burns, J.E., Sparrow, J.C., Tregear, R.T., Kendrick-Jones, J., and White, C.S. 1995b. Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or drosophila actin using optical tweezers. Biophys. J. 68, 298s-350s.
    • (1995) Biophys. J. , vol.68
    • Molloy, J.E.1    Burns, J.E.2    Sparrow, J.C.3    Tregear, R.T.4    Kendrick-Jones, J.5    White, C.S.6
  • 30
    • 0031091777 scopus 로고    scopus 로고
    • Smooth and skeletal muscle single-molecule mechanical experiments
    • Molloy, J.E., and White, C.S. 1997. Smooth and skeletal muscle single-molecule mechanical experiments. Biophys. J. 72, 984-986.
    • (1997) Biophys. J. , vol.72 , pp. 984-986
    • Molloy, J.E.1    White, C.S.2
  • 31
    • 0019166529 scopus 로고
    • A model of cardiac muscle mechanics and energetics
    • Panerai, R.B. 1980. A model of cardiac muscle mechanics and energetics. J. Biomech. 13, 929-940.
    • (1980) J. Biomech. , vol.13 , pp. 929-940
    • Panerai, R.B.1
  • 32
    • 0025775887 scopus 로고
    • Simulation of stochastic processes in motile cross-bridge systems
    • Pate, E., and Cooke, R. 1991. Simulation of stochastic processes in motile cross-bridge systems. J. Musl. Res. Cell Motil. 12, 376-393.
    • (1991) J. Musl. Res. Cell Motil. , vol.12 , pp. 376-393
    • Pate, E.1    Cooke, R.2
  • 33
    • 0027194750 scopus 로고
    • Measuring kinetics of complex single ion channel data using mean-variance histograms
    • Patlak, J.B. 1993. Measuring kinetics of complex single ion channel data using mean-variance histograms. Biophys. J. 65, 29-42.
    • (1993) Biophys. J. , vol.65 , pp. 29-42
    • Patlak, J.B.1
  • 34
    • 0000380208 scopus 로고
    • Muscle contraction transients, crossbridge kinetics, and the Fenn effect
    • Podolsky, R.J., and Nolan, A.C. 1973. Muscle contraction transients, crossbridge kinetics, and the Fenn effect. Cold Spring Harbor Symp. Quant. Biol. 37, 661.
    • (1973) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 661
    • Podolsky, R.J.1    Nolan, A.C.2
  • 35
    • 84890506631 scopus 로고
    • Life at low Reynolds number
    • Purcell, E.M. 1977. Life at low Reynolds number. Am. J. Phys. 45, 3-11.
    • (1977) Am. J. Phys. , vol.45 , pp. 3-11
    • Purcell, E.M.1
  • 36
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment, I., Holden, H.M., Whittaker, M., Yohn, C.B., and Lorenz, M. 1993. Structure of the actin-myosin complex and its implications for muscle contraction. Science 26, 58-65.
    • (1993) Science , vol.26 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3    Yohn, C.B.4    Lorenz, M.5
  • 37
    • 0013850715 scopus 로고
    • Induced changes in orientation of the crossbridges of glycerinated insect flight muscle
    • Reedy, M.K., Holmes, K.C., and Tregear, R.T. 1965. Induced changes in orientation of the crossbridges of glycerinated insect flight muscle. Nature 207, 1276-1280.
    • (1965) Nature , vol.207 , pp. 1276-1280
    • Reedy, M.K.1    Holmes, K.C.2    Tregear, R.T.3
  • 40
    • 4243114736 scopus 로고
    • Molecular-dynamics study of a three-dimensional one-component model for distortive phase transitions
    • Schneider, T., and Stoll, E. 1978. Molecular-dynamics study of a three-dimensional one-component model for distortive phase transitions. Phys. Rev. B 17, 1302-1322.
    • (1978) Phys. Rev. B , vol.17 , pp. 1302-1322
    • Schneider, T.1    Stoll, E.2
  • 42
    • 0022117773 scopus 로고
    • Equilibrium muscle crossbridge behavior: Theoretical considerations
    • Schoenberg, M. 1985. Equilibrium muscle crossbridge behavior: Theoretical considerations. Biophys. J. 48, 467-475.
    • (1985) Biophys. J. , vol.48 , pp. 467-475
    • Schoenberg, M.1
  • 43
    • 0026527497 scopus 로고
    • Actin as the generator of tension during muscle contraction
    • Schutt, C.E., and Lindberg, V. 1992. Actin as the generator of tension during muscle contraction. Proc. Natl., Acad. Sci. USA 89, 319-323.
    • (1992) Proc. Natl., Acad. Sci. USA , vol.89 , pp. 319-323
    • Schutt, C.E.1    Lindberg, V.2
  • 44
    • 0028933051 scopus 로고
    • Structural studies on the ribbon-to-helix transitions in profilin: Actin crystals
    • Schutt, C.E., Rozycki, M.D., Chik, J.K., and Lindberg, V. 1995. Structural studies on the ribbon-to-helix transitions in profilin: Actin crystals. Biophys. J. 68, 12s-18s.
    • (1995) Biophys. J. , vol.68
    • Schutt, C.E.1    Rozycki, M.D.2    Chik, J.K.3    Lindberg, V.4
  • 45
    • 0017366025 scopus 로고
    • Studies on isolated smooth muscle cells: The contractile apparatus
    • Small, J.V. 1977. Studies on isolated smooth muscle cells: The contractile apparatus. J. Cell Sci. 24, 327.
    • (1977) J. Cell Sci. , vol.24 , pp. 327
    • Small, J.V.1
  • 47
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda, K., Schmidt, C.F., Schnapp, B.J., and Block, S.M. 1993. Direct observation of kinesin stepping by optical trapping interferometry. Nature 365, 721-727.
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 48
    • 0028956597 scopus 로고
    • A theory of tension fluctuations due to muscle cross-bridges
    • Thomas, N., and Thornhill, R.A. 1995. A theory of tension fluctuations due to muscle cross-bridges. Proc. R. Soc. Lond. B 259, 235-242.
    • (1995) Proc. R. Soc. Lond. B , vol.259 , pp. 235-242
    • Thomas, N.1    Thornhill, R.A.2
  • 49
    • 0025222740 scopus 로고
    • Protein motors and Maxwell's demons: Does mechano-chemical transduction involve a thermal ratchet?
    • Vale, R.D., and Oosawa, F. 1990. Protein motors and Maxwell's demons: Does mechano-chemical transduction involve a thermal ratchet? Adv. Biophys. 26, 97-134.
    • (1990) Adv. Biophys. , vol.26 , pp. 97-134
    • Vale, R.D.1    Oosawa, F.2
  • 50
    • 0025335344 scopus 로고
    • Smooth muscle myosin crossbridge interactions modulate actin filament sliding velocity in vitro
    • Warshaw, D.M., Desrosiers, J.M., Work, S.S., and Trybus, K.M. 1990. Smooth muscle myosin crossbridge interactions modulate actin filament sliding velocity in vitro. J. Cell Biol. 111, 453-463.
    • (1990) J. Cell Biol. , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Trybus, K.M.4
  • 51
    • 0039470294 scopus 로고    scopus 로고
    • The in vitro motility assay: A window into the myosin molecular motor
    • Warshaw, D.M. 1996. The in vitro motility assay: a window into the myosin molecular motor. News Physiol. Sc. 11, 1-7.
    • (1996) News Physiol. Sc. , vol.11 , pp. 1-7
    • Warshaw, D.M.1


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