메뉴 건너뛰기




Volumn 90, Issue 4, 2006, Pages 1295-1307

Force generation in single conventional actomyosin complexes under high dynamic load

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN II; BIOTIN; MICROSPHERE; MOLECULAR MOTOR;

EID: 33645758327     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.068429     Document Type: Article
Times cited : (143)

References (71)
  • 1
    • 0034909695 scopus 로고    scopus 로고
    • Analysis of single-molecule mechanical recordings: Application to actomyosin interactions
    • Knight, A. E., C. Veigel, C. Chambers, and J. E. Molloy. 2001. Analysis of single-molecule mechanical recordings: application to actomyosin interactions. Prog. Biophys. Mol. Biol. 77:45-72.
    • (2001) Prog. Biophys. Mol. Biol. , vol.77 , pp. 45-72
    • Knight, A.E.1    Veigel, C.2    Chambers, C.3    Molloy, J.E.4
  • 3
    • 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. 386:113-119.
    • (1994) Nature , vol.386 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 5
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosins produce similar forces and displacements in the laser trap
    • Guilford, W. H., D. E. Dupuis, G. Kennedy, J. Wu, J. B. Patlak, and D. M. Warshaw. 1997. Smooth muscle and skeletal muscle myosins produce similar forces and displacements in the laser trap. Biophys. J. 72:1006-1021.
    • (1997) Biophys. J. , vol.72 , pp. 1006-1021
    • Guilford, W.H.1    Dupuis, D.E.2    Kennedy, G.3    Wu, J.4    Patlak, J.B.5    Warshaw, D.M.6
  • 6
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima, A., H. Kojima, T. Funatsu, M. Tokunaga, H. Higuchi, H. Tanaka, and T. Yanagida. 1998. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell. 92:161-171.
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 7
    • 0031668720 scopus 로고    scopus 로고
    • Orientation dependence of displacements by a single one-headed myosin relative to the actin filament
    • Tanaka, H., A. Ishijima, M. Honda, K. Saito, and T. Yanagida. 1998. Orientation dependence of displacements by a single one-headed myosin relative to the actin filament. Biophys. J. 75:1886-1894.
    • (1998) Biophys. J. , vol.75 , pp. 1886-1894
    • Tanaka, H.1    Ishijima, A.2    Honda, M.3    Saito, K.4    Yanagida, T.5
  • 8
    • 0036218298 scopus 로고    scopus 로고
    • The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules
    • Baker, J. E., C. Brosseau, P. B. Joel, and D. M. Warshaw. 2002. The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules. Biophys. J. 82:2134-2147.
    • (2002) Biophys. J. , vol.82 , pp. 2134-2147
    • Baker, J.E.1    Brosseau, C.2    Joel, P.B.3    Warshaw, D.M.4
  • 9
    • 0032411784 scopus 로고    scopus 로고
    • A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap
    • Lauzon, A.-M., M. J. Tyska, A. S. Rovner, Y. Freyzon, D. M. Warshaw, and K. M. Trybus. 1998. A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap. J. Muscle Res. Cell Motil. 19:825-837.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 825-837
    • Lauzon, A.-M.1    Tyska, M.J.2    Rovner, A.S.3    Freyzon, Y.4    Warshaw, D.M.5    Trybus, K.M.6
  • 11
    • 0034284538 scopus 로고    scopus 로고
    • An unexpectedly large working stroke from chymotryptic fragments of myosin II
    • Molloy, J. E., J. Kendrick-Jones, C. Veigel, and R. T. Tregear. 2000. An unexpectedly large working stroke from chymotryptic fragments of myosin II. FEBS Lett. 480:293-297.
    • (2000) FEBS Lett. , vol.480 , pp. 293-297
    • Molloy, J.E.1    Kendrick-Jones, J.2    Veigel, C.3    Tregear, R.T.4
  • 18
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • Veigel, C., J. E. Molloy, S. Schmitz, and J. Kendrick-Jones. 2003. Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers. Nat. Cell Biol. 5:980-986.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Schmitz, S.3    Kendrick-Jones, J.4
  • 19
    • 0028932523 scopus 로고
    • Characterization of single actin-myosin interactions
    • Finer, J. T., A. D. Mehta, and J. A. Spudich. 1995. Characterization of single actin-myosin interactions. Biophys. J. 68:291S-296S.
    • (1995) Biophys. J. , vol.68
    • Finer, J.T.1    Mehta, A.D.2    Spudich, J.A.3
  • 20
    • 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. 1995. Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers. Biophys. J. 68:298S-303S.
    • (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, D.C.S.6
  • 22
    • 0030791973 scopus 로고    scopus 로고
    • Actomyosin interaction in striated muscle
    • Cooke, R. 1997. Actomyosin interaction in striated muscle. Physiol. Rev. 77:671-697.
    • (1997) Physiol. Rev. , vol.77 , pp. 671-697
    • Cooke, R.1
  • 25
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • Veigel, C., M. L. Bartoo, D. C. S. White, J. C. Sparrow, and J. E. Molloy. 1998. The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer. Biophys. J. 75:1424-1438.
    • (1998) Biophys. J. , vol.75 , pp. 1424-1438
    • Veigel, C.1    Bartoo, M.L.2    White, D.C.S.3    Sparrow, J.C.4    Molloy, J.E.5
  • 26
    • 1842599025 scopus 로고
    • A quantitative comparison between the energy liberated and the work performed by the isolated sartorius muscle of the frog
    • Fenn, W. O. 1923. A quantitative comparison between the energy liberated and the work performed by the isolated sartorius muscle of the frog. J. Physiol. (Lond.). 58:175-203.
    • (1923) J. Physiol. (Lond.) , vol.58 , pp. 175-203
    • Fenn, W.O.1
  • 27
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. 1957. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:255-318.
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 30
    • 13444263735 scopus 로고    scopus 로고
    • Adenosine diphosphate and strain sensitivity in myosin motors
    • Nyitrai, M., and M. A. Geeves. 2004. Adenosine diphosphate and strain sensitivity in myosin motors. Philos. Trans. R. Soc. Lond. B Biol. Sci. 359:1867-1877.
    • (2004) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.359 , pp. 1867-1877
    • Nyitrai, M.1    Geeves, M.A.2
  • 31
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • Uyeda, T. Q. P., S. J. Kron, and J. A. Spudich. 1990. Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin. J. Mol. Biol. 214:699-710.
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 32
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • Harris, D. E., and D. M. Warshaw. 1993. Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro. J. Biol. Chem. 268:14764-14768.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 33
    • 0031806323 scopus 로고    scopus 로고
    • Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers
    • Hopkins, S. C., C. Sabido-David, J. E. T. Corrie, M. Irving, and Y. E. Goldman. 1998. Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers. Biophys. J. 74:3093-3110.
    • (1998) Biophys. J. , vol.74 , pp. 3093-3110
    • Hopkins, S.C.1    Sabido-David, C.2    Corrie, J.E.T.3    Irving, M.4    Goldman, Y.E.5
  • 34
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • De La Cruz, E. M., and E. M. Ostap. 2004. Relating biochemistry and function in the myosin superfamily. Curr. Opin. Cell Biol. 16:61-67.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 61-67
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 35
    • 0026067741 scopus 로고
    • Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres
    • Dantzig, J. A., M. G. Hibberd, D. R. Trentham, and Y. E. Goldman. 1991. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres. J. Physiol. 432:639-680.
    • (1991) J. Physiol. , vol.432 , pp. 639-680
    • Dantzig, J.A.1    Hibberd, M.G.2    Trentham, D.R.3    Goldman, Y.E.4
  • 36
    • 0029745362 scopus 로고    scopus 로고
    • ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin
    • Gollub, J., C. R. Cremo, and R. Cooke. 1996. ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin. Nat. Struct. Biol. 3:796-802.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 796-802
    • Gollub, J.1    Cremo, C.R.2    Cooke, R.3
  • 37
    • 1442339414 scopus 로고    scopus 로고
    • Single molecule force of myosin II measured with a novel optical trap system that eliminates linkage compliance
    • Abstr.
    • Takagi, Y., Y. E. Goldman, and H. Shuman. 2000. Single molecule force of myosin II measured with a novel optical trap system that eliminates linkage compliance. Biophys. J. 78:235a. (Abstr.).
    • (2000) Biophys. J. , vol.78
    • Takagi, Y.1    Goldman, Y.E.2    Shuman, H.3
  • 38
    • 85030608124 scopus 로고    scopus 로고
    • Analysis of isometric force measurements of myosin II using a modified mean-variance analysis
    • Abstr.
    • Takagi, Y., E. E. Homsher, Y. E. Goldman, and H. Shuman. 2001. Analysis of isometric force measurements of myosin II using a modified mean-variance analysis. Biophys. J. 80:78a. (Abstr.).
    • (2001) Biophys. J. , vol.80
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 39
    • 13444268730 scopus 로고    scopus 로고
    • Probing the transduction mechanism of rabbit skeletal myosin II underisometric condition using an optical trap
    • Abstr.
    • Takagi, Y., E. E. Homsher, Y. E. Goldman, and H. Shuman. 2002. Probing the transduction mechanism of rabbit skeletal myosin II underisometric condition using an optical trap. Biophys. J. 82:373a. (Abstr.).
    • (2002) Biophys. J. , vol.82
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 40
    • 85030604222 scopus 로고    scopus 로고
    • Mechanics of rabbit skeletal actomyosin in an isometric force clamp near rigor
    • Abstr.
    • Takagi, Y., Y. E. Goldman, and H. Shuman. 2003. Mechanics of rabbit skeletal actomyosin in an isometric force clamp near rigor. Biophys. J. 84:247a. (Abstr.).
    • (2003) Biophys. J. , vol.84
    • Takagi, Y.1    Goldman, Y.E.2    Shuman, H.3
  • 41
    • 13444302013 scopus 로고    scopus 로고
    • ATP and phosphate dependence of single rabbit skeletal actomyosin interactions under differing loads
    • Abstr.
    • Takagi, Y., E. E. Homsher, Y. E. Goldman, and H. Shuman. 2004. ATP and phosphate dependence of single rabbit skeletal actomyosin interactions under differing loads. Biophys. J. 86:54a. (Abstr.).
    • (2004) Biophys. J. , vol.86
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 42
    • 85030599844 scopus 로고    scopus 로고
    • A Markov process model to predict the mechanics and kinetics of single rabbit skeletal isometric actomyosin interactions
    • Abstr.
    • Takagi, Y., Y. E. Goldman, and H. Shuman. 2005. A Markov process model to predict the mechanics and kinetics of single rabbit skeletal isometric actomyosin interactions. Biophys. J. 88:634a. (Abstr.).
    • (2005) Biophys. J. , vol.88
    • Takagi, Y.1    Goldman, Y.E.2    Shuman, H.3
  • 43
    • 0030358936 scopus 로고    scopus 로고
    • Construction of multiple-beam optical traps with nanometer-resolution position sensing
    • Visscher, K., S. P. Gross, and S. M. Block. 1996. Construction of multiple-beam optical traps with nanometer-resolution position sensing. IEEE J. Select. Topics Quant. Electr. 2:1066-1076.
    • (1996) IEEE J. Select. Topics Quant. Electr. , vol.2 , pp. 1066-1076
    • Visscher, K.1    Gross, S.P.2    Block, S.M.3
  • 44
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and singlestranded DNA molecules
    • Smith, S. B., Y. Cui, and C. Bustamante. 1996. Overstretching B-DNA: the elastic response of individual double-stranded and singlestranded DNA molecules. Science. 271:795-799.
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.2    Bustamante, C.3
  • 45
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block, S. M., L. S. Goldstein, and B. J. Schnapp. 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.2    Schnapp, B.J.3
  • 46
    • 0031961707 scopus 로고    scopus 로고
    • Signals and noise in micromechanical measurements
    • Gittes, F., and C. F. Schmidt. 1998. Signals and noise in micromechanical measurements. Methods Cell Biol. 55:129-156.
    • (1998) Methods Cell Biol. , vol.55 , pp. 129-156
    • Gittes, F.1    Schmidt, C.F.2
  • 47
    • 0031904601 scopus 로고    scopus 로고
    • Two-dimensional tracking of ncd motility by back focal plane interferometry
    • Allersma, M. W., F. Gittes, M. J. deCastro, R. J. Stewart, and C. F. Schmidt. 1998. Two-dimensional tracking of ncd motility by back focal plane interferometry. Biophys. J. 74:1074-1085.
    • (1998) Biophys. J. , vol.74 , pp. 1074-1085
    • Allersma, M.W.1    Gittes, F.2    DeCastro, M.J.3    Stewart, R.J.4    Schmidt, C.F.5
  • 48
    • 0029976424 scopus 로고    scopus 로고
    • Quantitative measurements of forces and displacement using an optical trap
    • Simmons, R. M., J. T. Finer, S. Chu, and J. A. Spudich. 1996. Quantitative measurements of forces and displacement using an optical trap. Biophys. J. 70:1813-1822.
    • (1996) Biophys. J. , vol.70 , pp. 1813-1822
    • Simmons, R.M.1    Finer, J.T.2    Chu, S.3    Spudich, J.A.4
  • 49
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian, S. S., and S. Lowey. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85:55-71.
    • (1982) Methods Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 50
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Harada, Y., K. Sakurada, T. Aoki, D. D. Thomas, and T. Yanagida. 1990. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216:49-68.
    • (1990) J. Mol. Biol. , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 52
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • MacLean-Fletcher, S., and T. D. Pollard. 1980. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem. Biophys. Res. Commun. 96:18-27.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 53
    • 0034431113 scopus 로고    scopus 로고
    • In vitro assays of processive myosin motors
    • Rock, R. S., M. Rief, A. D. Mehta, and J. A. Spudich. 2000. In vitro assays of processive myosin motors. Methods. 22:373-381.
    • (2000) Methods , vol.22 , pp. 373-381
    • Rock, R.S.1    Rief, M.2    Mehta, A.D.3    Spudich, J.A.4
  • 55
    • 0030878880 scopus 로고    scopus 로고
    • Detection of singlemolecule interactions using correlated thermal diffusion
    • Mehta, A. D., J. T. Finer, and J. A. Spudich. 1997. Detection of singlemolecule interactions using correlated thermal diffusion. Proc. Natl. Acad. Sci. USA. 94:7927-7931.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7927-7931
    • Mehta, A.D.1    Finer, J.T.2    Spudich, J.A.3
  • 56
    • 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., L. Lucii, and V. Lombardi. 2002. The size and the speed of the working stroke of muscle myosin and its dependence on the force. J. Physiol. 545:145-151.
    • (2002) J. Physiol. , vol.545 , pp. 145-151
    • Piazzesi, G.1    Lucii, L.2    Lombardi, V.3
  • 57
    • 0029075829 scopus 로고
    • Unbinding force of a single motor molecule of muscle measured using optical tweezers
    • Nishizaka, T., H. Miyata, H. Yoshikawa, S. Ishiwata, and K. Kinosita Jr. 1995. Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature. 377:251-254.
    • (1995) Nature , vol.377 , pp. 251-254
    • Nishizaka, T.1    Miyata, H.2    Yoshikawa, H.3    Ishiwata, S.4    Kinosita Jr., K.5
  • 58
    • 0033884332 scopus 로고    scopus 로고
    • Characterization of single actomyosin rigor bonds: Load dependence of lifetime and mechanical properties
    • Nishizaka, T., R. Seo, H. Tadakuma, K. Kinosita Jr., and S. Ishiwata. 2000. Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties. Biophys. J. 79:962-974.
    • (2000) Biophys. J. , vol.79 , pp. 962-974
    • Nishizaka, T.1    Seo, R.2    Tadakuma, H.3    Kinosita Jr., K.4    Ishiwata, S.5
  • 59
    • 0029801074 scopus 로고    scopus 로고
    • Filament compliance and tension transients in muscle
    • Huxley, A. F., and S. Tideswell. 1996. Filament compliance and tension transients in muscle. J. Muscle Res. Cell Motil. 17:507-511.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 507-511
    • Huxley, A.F.1    Tideswell, S.2
  • 60
    • 0032425057 scopus 로고    scopus 로고
    • Estimation of cross-bridge stiffness from maximum thermodynamic efficiency
    • Barclay, C. J. 1998. Estimation of cross-bridge stiffness from maximum thermodynamic efficiency. J. Muscle Res. Cell Motil. 19:855-864.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 855-864
    • Barclay, C.J.1
  • 61
    • 0014688993 scopus 로고
    • The chemical energetics of muscle contraction. II. The chemistry, efficiency and power of maximally working sartorius muscles
    • Kushmerick, M. J., and R. E. Davies. 1969. The chemical energetics of muscle contraction. II. The chemistry, efficiency and power of maximally working sartorius muscles. Proc. R. Soc. Lond. B. Biol. Sci. 174:315-353.
    • (1969) Proc. R. Soc. Lond. B. Biol. Sci. , vol.174 , pp. 315-353
    • Kushmerick, M.J.1    Davies, R.E.2
  • 62
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd, M. G., J. A. Dantzig, D. R. Trentham, and Y. E. Goldman. 1985. Phosphate release and force generation in skeletal muscle fibers. Science. 228:1317-1319.
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Trentham, D.R.3    Goldman, Y.E.4
  • 63
    • 0015530342 scopus 로고
    • X-ray diffraction studies on skinned single fibres of frog skeletal muscle
    • Matsubara, I., and G. F. Elliott. 1972. X-ray diffraction studies on skinned single fibres of frog skeletal muscle. J. Mol. Biol. 72:657-669.
    • (1972) J. Mol. Biol. , vol.72 , pp. 657-669
    • Matsubara, I.1    Elliott, G.F.2
  • 64
    • 0020425131 scopus 로고
    • Orientation of spin labels attached to cross-bridges in contracting muscle fibres
    • Cooke, R., M. S. Crowder, and D. D. Thomas. 1982. Orientation of spin labels attached to cross-bridges in contracting muscle fibres. Nature. 300:776-778.
    • (1982) Nature , vol.300 , pp. 776-778
    • Cooke, R.1    Crowder, M.S.2    Thomas, D.D.3
  • 65
    • 0034308409 scopus 로고    scopus 로고
    • Cross-bridge action: Present views, prospects, and unknowns
    • Huxley, A. F. 2000. Cross-bridge action: present views, prospects, and unknowns. J. Biomech. 33:1189-1195.
    • (2000) J. Biomech. , vol.33 , pp. 1189-1195
    • Huxley, A.F.1
  • 66
    • 0017044811 scopus 로고
    • Energetics and mechanism of actomyosin adenosine triphosphatase
    • White, H. D., and E. W. Taylor. 1976. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry. 15:5818-5826.
    • (1976) Biochemistry , vol.15 , pp. 5818-5826
    • White, H.D.1    Taylor, E.W.2
  • 67
    • 0023161165 scopus 로고
    • Kinetics of the actomyosin ATPase in muscle fibers
    • Goldman, Y. E. 1987. Kinetics of the actomyosin ATPase in muscle fibers. Annu. Rev. Physiol. 49:637-654.
    • (1987) Annu. Rev. Physiol. , vol.49 , pp. 637-654
    • Goldman, Y.E.1
  • 68
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for the specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 69
    • 0018877621 scopus 로고
    • Cross-bridge model of muscle contraction. Quantitative analysis
    • Eisenberg, E., T. L. Hill, and Y. Chen. 1980. Cross-bridge model of muscle contraction. Quantitative analysis. Biophys. J. 29:195-227.
    • (1980) Biophys. J. , vol.29 , pp. 195-227
    • Eisenberg, E.1    Hill, T.L.2    Chen, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.