메뉴 건너뛰기




Volumn 70, Issue 1, 1996, Pages 383-400

Multiple- and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: Unitary steps and forces

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 0030031120     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79582-6     Document Type: Article
Times cited : (196)

References (64)
  • 2
    • 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. Muscle Res. Cell Motil. 13:590-607.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 590-607
    • Burton, K.1
  • 3
    • 0000739073 scopus 로고
    • Optical measurement of picometer displacements of transparent microscopic objects
    • Denk, W., and W. W. Webb. 1990 Optical measurement of picometer displacements of transparent microscopic objects. Appl. Optics. 29. 2382-2391.
    • (1990) Appl. Optics , vol.29 , pp. 2382-2391
    • Denk, W.1    Webb, W.W.2
  • 4
    • 0018333803 scopus 로고
    • The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres
    • Edman, K. A. 1979. The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. J. Physiol. 291:143-159.
    • (1979) J. Physiol. , vol.291 , pp. 143-159
    • Edman, K.A.1
  • 5
    • 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-297s.
    • (1995) Biophys. J. , vol.68
    • Finer, J.T.1    Mehta, A.D.2    Spudich, J.A.3
  • 6
    • 0028261701 scopus 로고
    • Single myosin mechanics: Piconewton forces and nanometre steps
    • Finer, J. T., R. M. Simmons, and J. A. Spudich. 1994. Single myosin mechanics: piconewton forces and nanometre steps. Nature (Lond.). 368:113-119.
    • (1994) Nature (Lond.) , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 7
    • 0017385529 scopus 로고
    • Tension responses to sudden length change in stimulated frog muscle fibres near slack length
    • Ford, L. E., A. F. Huxley, and R. M. Simmons. 1977. Tension responses to sudden length change 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
  • 8
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu, T., Y Harada, M. Tokunaga, K. Saito, and T. Yanagida. 1995. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature (Lond.). 374: 555-559.
    • (1995) Nature (Lond.) , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 9
    • 0017508185 scopus 로고
    • Active and rigor muscle stiffness
    • Goldman, Y. E., and R. M. Simmons. 1977. Active and rigor muscle stiffness. J Physiol. 269:55-57
    • (1977) J Physiol. , vol.269 , pp. 55-57
    • Goldman, Y.E.1    Simmons, R.M.2
  • 10
    • 85010916780 scopus 로고
    • The structure of F-actin and of actin filaments isolated from muscle
    • Hanson, J., and J. Lowy. 1963. The structure of F-actin and of actin filaments isolated from muscle. J. Mol. Biol. 6:46-60.
    • (1963) J. Mol. Biol. , vol.6 , pp. 46-60
    • Hanson, J.1    Lowy, J.2
  • 11
    • 0023145911 scopus 로고
    • Sliding movement of single actin filaments on one-headed myosin filaments
    • Harada, Y., A. Noguchi A. Kishino, and T. Yanagida. 1987. Sliding movement of single actin filaments on one-headed myosin filaments. Nature (Lond.). 326:805-808.
    • (1987) Nature (Lond.) , vol.326 , pp. 805-808
    • Harada, Y.1    Noguchi, A.2    Kishino, A.3    Yanagida, T.4
  • 12
    • 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
  • 13
    • 0025817087 scopus 로고
    • Reconstitution of active movement in vitro based on the actin-myosin interaction
    • Higashi-Fujime, S. 1991. Reconstitution of active movement in vitro based on the actin-myosin interaction. Int. Rev. Cytol. 125:95-138.
    • (1991) Int. Rev. Cytol. , vol.125 , pp. 95-138
    • Higashi-Fujime, S.1
  • 14
    • 0025874034 scopus 로고
    • Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibers
    • Higuchi, H., and Y. E. Goldman. 1991. Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibers Nature (Lond.). 352:352-354.
    • (1991) Nature (Lond.) , vol.352 , pp. 352-354
    • Higuchi, H.1    Goldman, Y.E.2
  • 15
    • 0027238810 scopus 로고
    • Mechanical response to photolytic ATP pulsed of skinned muscle fibres pre-activated with a small pulse of ATP
    • Horiuti, K., T. Sakoda, and K. Yamada. 1993. Mechanical response to photolytic ATP pulsed of skinned muscle fibres pre-activated with a small pulse of ATP. J. Muscle Res. Cell Motil. 14:335-340.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 335-340
    • Horiuti, K.1    Sakoda, T.2    Yamada, K.3
  • 16
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard. J., A. J., Hudspeth, and R. D. Vale. 1987. Movement of microtubules by single kinesin molecules. Nature (Lond.). 342:154-158.
    • (1987) Nature (Lond.) , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 17
    • 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
  • 18
    • 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 (Lond.). 233:533-538.
    • (1971) Nature (Lond.) , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 19
    • 0025368569 scopus 로고
    • Sliding filaments and molecular motile systems
    • Huxley, H. E. 1990. Sliding filaments and molecular motile systems. J. Biol Chem. 265:8347-8350
    • (1990) J. Biol Chem. , vol.265 , pp. 8347-8350
    • Huxley, H.E.1
  • 20
    • 0025822885 scopus 로고
    • Sub-piconewton force fluctuations of actomyosin in vitro
    • Ishijima, A., T. Doi, K. Sakurada, and T. Yanagida. 1991. Sub-piconewton force fluctuations of actomyosin in vitro. Nature (Lond.). 352:301-306.
    • (1991) Nature (Lond.) , vol.352 , pp. 301-306
    • Ishijima, A.1    Doi, T.2    Sakurada, K.3    Yanagida, T.4
  • 22
    • 85031220368 scopus 로고
    • Force fluctuations on a single actin filament: Interaction with oriented myosin molecules
    • Ishijima, A., and T. Yanagida. 1991. Force fluctuations on a single actin filament: interaction with oriented myosin molecules (Japanese). Proc. 29th Japan Biophys. Sci. Meeting. S195.
    • (1991) Proc. 29th Japan Biophys. Sci. Meeting
    • Ishijima, A.1    Yanagida, T.2
  • 24
    • 0027522830 scopus 로고
    • Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion
    • Johara, M., Y. Y. Toyoshima, A. Ishijima, H. Kojima, T. Yanagida, and K. Sutoh. 1993. Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion. Proc. Natl. Acad. Sci. USA. 90:2127-2131.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2127-2131
    • Johara, M.1    Toyoshima, Y.Y.2    Ishijima, A.3    Kojima, H.4    Yanagida, T.5    Sutoh, K.6
  • 25
    • 0014934983 scopus 로고
    • Membrane noise produced by acetylcholine
    • Katz, B., and R. Miledi. 1971. Membrane noise produced by acetylcholine. Nature. 226:962-963.
    • (1971) Nature , vol.226 , pp. 962-963
    • Katz, B.1    Miledi, R.2
  • 26
    • 0019308296 scopus 로고
    • Sinusoidal analysis: A high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscle of rabbit, frog and crayfish
    • Kawai, M, and P. W. Brant. 1980. Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscle of rabbit, frog and crayfish. J. Muscle. Res. Cell Motil. 1:279-303.
    • (1980) J. Muscle. Res. Cell Motil. , vol.1 , pp. 279-303
    • Kawai, M.1    Brant, P.W.2
  • 27
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A., and T. Yanagida. 1988. Force measurements by micromanipulation of a single actin filament by glass needles. Nature (Lond.). 334:74-76.
    • (1988) Nature (Lond.) , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 29
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron, S. J., and J. A. Spudich. 1986. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. USA. 83: 6272-6276.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 30
    • 0027426228 scopus 로고
    • Skeletal muscle myosin light chains are essential for physiological speeds of shortening
    • Lowey, S., G. S. Waller, and M. K. Trybus. 1993. Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature (Lond.). 365:454-456.
    • (1993) Nature (Lond.) , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, M.K.3
  • 31
    • 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
  • 32
    • 0021358821 scopus 로고
    • Changes in the lateral filament spacing of skinned muscle fibers when cross-bridges attach
    • Matsubara, I., Y. E. Goldman, and R. M Simmons. 1984. Changes in the lateral filament spacing of skinned muscle fibers when cross-bridges attach. J. Mol. Biol. 173:15-33.
    • (1984) J. Mol. Biol. , vol.173 , pp. 15-33
    • Matsubara, I.1    Goldman, Y.E.2    Simmons, R.M.3
  • 33
    • 0016862443 scopus 로고
    • Use of an x-ray television for diffraction of the frog striated muscle
    • Matsubara, I., N. Yagi, and H. Hashizume. 1975. Use of an x-ray television for diffraction of the frog striated muscle. Nature (Lond.). 255:728-729.
    • (1975) Nature (Lond.) , vol.255 , pp. 728-729
    • Matsubara, I.1    Yagi, N.2    Hashizume, H.3
  • 34
    • 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., H. Hakozaki, H. Yoshikawa, N. Suzuki, K. Kinoshita, Jr., T. Nishizaka, and S. Ishiwata. 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    Kinoshita Jr., K.5    Nishizaka, T.6    Ishiwata, S.7
  • 36
    • 0028964579 scopus 로고
    • Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Droshophila actins using optical tweezers
    • Molloy, J. E., J. E. Burns, J. C. Sparrow, R. T. Tregear, J. K. Jones, and D. C. S. White. 1995a. Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Droshophila actins using optical tweezers. Biophys. J. 298s-305s.
    • (1995) Biophys. J.
    • Molloy, J.E.1    Burns, J.E.2    Sparrow, J.C.3    Tregear, R.T.4    Jones, J.K.5    White, D.C.S.6
  • 37
    • 9044229559 scopus 로고
    • Force and movement of myosin interacting with mutant actin, measured by optical tweezers
    • In press
    • Molloy, J. E., J. E. Burns, J. C. Sparrow, and D. C. S. White. 1995b. Force and movement of myosin interacting with mutant actin, measured by optical tweezers J. Physiol. In press.
    • (1995) J. Physiol.
    • Molloy, J.E.1    Burns, J.E.2    Sparrow, J.C.3    White, D.C.S.4
  • 38
    • 0017258698 scopus 로고
    • Single-channel currents recorded from membrane of denervated frog muscle fibres
    • Neher, E., and B. Sakmann. 1976. Single-channel currents recorded from membrane of denervated frog muscle fibres. Nature (Lond.). 260: 799-802.
    • (1976) Nature (Lond.) , vol.260 , pp. 799-802
    • Neher, E.1    Sakmann, B.2
  • 39
    • 0027390794 scopus 로고
    • Right-handed rotation of an actin filament in an in vitro motile system
    • Nishizaka. T., T. Yagi, Y. Tanaka, and S. Ishiwata. 1993. Right-handed rotation of an actin filament in an in vitro motile system. Nature (Lond.). 361:269-271.
    • (1993) Nature (Lond.) , vol.361 , pp. 269-271
    • Nishizaka, T.1    Yagi, T.2    Tanaka, Y.3    Ishiwata, S.4
  • 40
    • 0016292984 scopus 로고
    • Fine structure of the thick filament in molluscan catch muscle
    • Nonomura, Y. 1974. Fine structure of the thick filament in molluscan catch muscle. J. Mol. Biol. 88:445-455.
    • (1974) J. Mol. Biol. , vol.88 , pp. 445-455
    • Nonomura, Y.1
  • 41
    • 0025685506 scopus 로고
    • Inhibition of sliding movement of F-actin by cross-linking emphasizes the role of F-actin structure in the mechanism of motility
    • Prochniewicz, E., and T. Yanagida. 1990. Inhibition of sliding movement of F-actin by cross-linking emphasizes the role of F-actin structure in the mechanism of motility. J. Mol. Biol. 216:761-772.
    • (1990) J. Mol. Biol. , vol.216 , pp. 761-772
    • Prochniewicz, E.1    Yanagida, T.2
  • 43
    • 0028347113 scopus 로고
    • Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap
    • Saitoh, K., T. Aoki, T. Aoki, and T. Yanagida. 1994. Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap. Biophys. J. 66:769-777.
    • (1994) Biophys. J. , vol.66 , pp. 769-777
    • Saitoh, K.1    Aoki, T.2    Aoki, T.3    Yanagida, T.4
  • 44
    • 9044224243 scopus 로고
    • Movement of actin filaments by purified molluscan myosin and native thick filaments
    • Sellers, J. R., Y. J. Han, and B. Kachar. 1991. Movement of actin filaments by purified molluscan myosin and native thick filaments. Biophys. J. 59:187a.
    • (1991) Biophys. J. , vol.59
    • Sellers, J.R.1    Han, Y.J.2    Kachar, B.3
  • 45
    • 0025002994 scopus 로고
    • Polarity and velocity of sliding filaments: Control of direction by actin and of speed by myosin
    • Sellers, J. R., and B. Kachar, 1990. Polarity and velocity of sliding filaments: control of direction by actin and of speed by myosin. Science. 249:406-408.
    • (1990) Science , vol.249 , pp. 406-408
    • Sellers, J.R.1    Kachar, B.2
  • 47
    • 0015387225 scopus 로고
    • Inferences about membrane properties from electrical noise measurements
    • Stevens, C. F. 1972. Inferences about membrane properties from electrical noise measurements. Biophys. J. 12:1028-1047.
    • (1972) Biophys. J. , vol.12 , pp. 1028-1047
    • Stevens, C.F.1
  • 48
    • 0025858239 scopus 로고
    • Site-directed mutations of Dictyostelium actin: Disruption of a negative charge cluster at the N terminus
    • Sutoh, K., M. Ando, K. Sutoh, and Y. Y. Toyoshima. 1991. Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N terminus. Proc. Natl Acad. Sci. USA. 88 7711-7714
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7711-7714
    • Sutoh, K.1    Ando, M.2    Sutoh, K.3    Toyoshima, Y.Y.4
  • 49
    • 0028362896 scopus 로고
    • Forces and velocities measured for single kinesin molecules
    • Svoboda, K., and S. M. Block. 1993. Forces and velocities measured for single kinesin molecules Cell. 77:773-784.
    • (1993) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 50
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda, K., C. F. Schmidt, B. J. Schnapp, and S. M. Block 1994. Direct observation of kinesin stepping by optical trapping interferometry. Nature (Lond.). 365:721-727.
    • (1994) Nature (Lond.) , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 51
    • 0022761099 scopus 로고
    • Stiffness of carbodiimide-crosslinked glycerinated muscle fibres in rigor and relaxing solutions at high salt concentrations
    • Tawada, K., and M. Kimura. 1986. Stiffness of carbodiimide-crosslinked glycerinated muscle fibres in rigor and relaxing solutions at high salt concentrations. J. Muscle Res. Cell Motil. 7:339-350.
    • (1986) J. Muscle Res. Cell Motil. , vol.7 , pp. 339-350
    • Tawada, K.1    Kimura, M.2
  • 53
    • 0025076927 scopus 로고
    • The myosin step size: Measurement of the unit displacement per ATP hydrolyzed in an in vitro assay
    • Toyoshima, Y. Y , S. J. Kron, and J. A. Spudich. 1990. The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. Proc. Natl. Acad. Sci. USA. 87:7130-7134.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7130-7134
    • Toyoshima, Y.Y.1    Kron, S.J.2    Spudich, J.A.3
  • 54
    • 0015880246 scopus 로고
    • Myosin content and filament structure in smooth and striated muscle
    • Tregear R. T., and J. M. Squire. 1973. Myosin content and filament structure in smooth and striated muscle. J. Mol. Biol 77:279-290.
    • (1973) J. Mol. Biol , vol.77 , pp. 279-290
    • Tregear, R.T.1    Squire, J.M.2
  • 55
    • 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
  • 56
    • 0025900542 scopus 로고
    • Quantized velocities at low myosin densities in an in vitro motility assay
    • Uyeda, T. Q. P., H. M. Warrick, S. J. Kron, and J. A. Spudich. 1991. Quantized velocities at low myosin densities in an in vitro motility assay. Nature (Lond.). 352:307-311
    • (1991) Nature (Lond.) , vol.352 , pp. 307-311
    • Uyeda, T.Q.P.1    Warrick, H.M.2    Kron, S.J.3    Spudich, J.A.4
  • 57
    • 0026498425 scopus 로고
    • Small-angle Synchrotron x-ray scattering reveals distinct shape changes of the myosin head during hydrolysis of ATP
    • Wakabayasi, K., M. Tokunaga, I. Kohno, Y. Sugimoto, T. Hamanaka, Y. Takezawa, T. Wakabayashi, and Y. Amemiya. 1992. Small-angle Synchrotron x-ray scattering reveals distinct shape changes of the myosin head during hydrolysis of ATP. Science. 258:443-447.
    • (1992) Science , vol.258 , pp. 443-447
    • Wakabayasi, K.1    Tokunaga, M.2    Kohno, I.3    Sugimoto, Y.4    Hamanaka, T.5    Takezawa, Y.6    Wakabayashi, T.7    Amemiya, Y.8
  • 58
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin: Effects of divalent cations on proteolytic susceptibility
    • Weeds, A. G., and B. Pope. 1977. Studies on the chymotryptic digestion of myosin: effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 59
    • 0025102479 scopus 로고
    • Direction and speed of actin filaments moving along thick filaments isolated from molluscan smooth muscle
    • Yamada, A., N. Ishii, and K. Takahashi. 1990. Direction and speed of actin filaments moving along thick filaments isolated from molluscan smooth muscle. J. Biochem. 108:341-343.
    • (1990) J. Biochem. , vol.108 , pp. 341-343
    • Yamada, A.1    Ishii, N.2    Takahashi, K.3
  • 60
    • 0027475758 scopus 로고
    • Movement of actin away from the center of reconstituted rabbit myosin filament is slower than in the opposite direction
    • Yamada, A., and T. Wakabayashi. 1993. Movement of actin away from the center of reconstituted rabbit myosin filament is slower than in the opposite direction. Biopys. J. 64:565-569.
    • (1993) Biopys. J. , vol.64 , pp. 565-569
    • Yamada, A.1    Wakabayashi, T.2
  • 62
    • 0027296257 scopus 로고
    • Nano-manipulation of actomyosin molecular motors in vitro: A new working principle
    • Yanagida, T., Y. Harada, and A. Ishijima. 1993. Nano-manipulation of actomyosin molecular motors in vitro: a new working principle. Trends Biochem. Sci. 18:319-324.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 319-324
    • Yanagida, T.1    Harada, Y.2    Ishijima, A.3
  • 63
    • 0028914578 scopus 로고
    • Forces and steps generated by single myosin molecules
    • Yanagida, T., and Ishijima, A. 1995. Forces and steps generated by single myosin molecules. Biophys. J. 68:312s-320s.
    • (1995) Biophys. J. , vol.68
    • Yanagida, T.1    Ishijima, A.2
  • 64
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • Yanagida, T., M Nakase, K. Nishiyama, and F. Oosawa. 1984 Direct observation of motion of single F-actin filaments in the presence of myosin. Nature (Lond.). 307:58-60.
    • (1984) Nature (Lond.) , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.