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Volumn 75, Issue 3, 1998, Pages 1424-1438

The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN MYOSIN INTERACTION; ANIMAL TISSUE; ARTICLE; CELL MOTILITY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUSCLE CONTRACTION; MUSCLE TONE; NONHUMAN; PROTEIN CONFORMATION;

EID: 0031656226     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)74061-5     Document Type: Article
Times cited : (195)

References (34)
  • 1
    • 0030791973 scopus 로고    scopus 로고
    • Actomyosin interaction in striated muscle
    • Cooke, R. 1998. Actomyosin interaction in striated muscle. Physiol. Rev. 77:671-697.
    • (1998) Physiol. Rev. , vol.77 , pp. 671-697
    • Cooke, R.1
  • 3
    • 0021891073 scopus 로고
    • Power and efficiency of insect flight muscle
    • Ellington, C. P. 1985. Power and efficiency of insect flight muscle. J. Exp. Biol. 115:293-304.
    • (1985) J. Exp. Biol. , vol.115 , pp. 293-304
    • Ellington, C.P.1
  • 4
    • 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 and skeletal muscle myosin produce similar forces and displacements in the laser trap
    • Guilford, W. H., D. H. Dupuis, G. Kennedy, J. Wu, J. B. Patlak, and D. M. Warshaw. 1997. Smooth and skeletal muscle myosin 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.H.2    Kennedy, G.3    Wu, J.4    Patlak, J.B.5    Warshaw, D.M.6
  • 6
    • 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
  • 7
    • 0029801074 scopus 로고    scopus 로고
    • Filament compliance and tension transients in muscle
    • Huxley, A. F., and S. Tideswell. 1997. Filament compliance and tension transients in muscle. J. Muscle Res. Cell Motil. 17:507-511.
    • (1997) J. Muscle Res. Cell Motil. , vol.17 , pp. 507-511
    • Huxley, A.F.1    Tideswell, S.2
  • 8
    • 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
  • 10
    • 0030031120 scopus 로고    scopus 로고
    • Multiple and single molecule analysis of the actomyosin motor by nanometer piconewton manipulation with a microneedle: Unitary steps and force
    • Ishijima, A., H. Kojima, H. Higuchi, Y. Harada, T. Funatsu, and T. Yanagida. 1996. Multiple and single molecule analysis of the actomyosin motor by nanometer piconewton manipulation with a microneedle: unitary steps and force. 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
  • 11
    • 0028607563 scopus 로고
    • Direct measurements of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima, H., A. Ishijima, and T. Yanagida. 1994. Direct measurements 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
  • 12
  • 13
    • 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. Biol. 174:315-353.
    • (1969) Proc. R. Soc. Lond. Biol. , vol.174 , pp. 315-353
    • Kushmerick, M.J.1    Davies, R.E.2
  • 14
    • 0031958205 scopus 로고    scopus 로고
    • The stiffness of skeletal muscle in isometric contraction and rigor: The fraction of myosin heads bound to actin
    • Linari, M., I. Dobbie, M. Reconditi, N. Koubassova, M. Irving, G. Piazzesi, and V. Lombardi. 1998. The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin. Biophys. J. 74:2459-2473.
    • (1998) Biophys. J. , vol.74 , pp. 2459-2473
    • Linari, M.1    Dobbie, I.2    Reconditi, M.3    Koubassova, N.4    Irving, M.5    Piazzesi, G.6    Lombardi, V.7
  • 15
    • 0028959884 scopus 로고
    • Elastic distortion of myosin heads and repriming of the working stroke in muscle
    • Lombardi, V., G. Piazzesi, M. A. Ferenczi, H. Thirlwell, I. Dobie, and M. Irving. 1995. Elastic distortion of myosin heads and repriming of the working stroke in muscle. Nature. 374:553-555.
    • (1995) Nature , vol.374 , pp. 553-555
    • Lombardi, V.1    Piazzesi, G.2    Ferenczi, M.A.3    Thirlwell, H.4    Dobie, I.5    Irving, M.6
  • 16
    • 0004366104 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn, R. W., and E. W. Taylor. 1971. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 21:1925-1928.
    • (1971) Biochemistry , vol.21 , pp. 1925-1928
    • Lymn, R.W.1    Taylor, E.W.2
  • 17
    • 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
  • 18
    • 0018427133 scopus 로고
    • N-Ethylmaleimide-modified heavy meromyosin, a probe for actomyosin interactions
    • Meeusen, R., and Z. Cande. 1979. N-Ethylmaleimide-modified heavy meromyosin, a probe for actomyosin interactions. J. Cell Biol. 82: 57-65.
    • (1979) J. Cell Biol. , vol.82 , pp. 57-65
    • Meeusen, R.1    Cande, Z.2
  • 19
    • 0030878880 scopus 로고    scopus 로고
    • Detection of single molecule interactions using correlated thermal diffusion
    • Mehta, A. D., J. T. Finer, and J. A. Spudich. 1997. Detection of single molecule 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
  • 20
    • 34250314531 scopus 로고    scopus 로고
    • Optical chopsticks: Digital synthesis of multiple optical traps
    • Molloy, J. E. 1997. Optical chopsticks: digital synthesis of multiple optical traps. Methods Cell Biol. 55:205-216.
    • (1997) Methods Cell Biol. , vol.55 , pp. 205-216
    • Molloy, J.E.1
  • 22
    • 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 K., Jr.5
  • 23
    • 0017805583 scopus 로고
    • Can a myosin molecule bind to two actin filaments?
    • Offer, G., and A. Elliott. 1978. Can a myosin molecule bind to two actin filaments? Nature. 271:325-329.
    • (1978) Nature , vol.271 , pp. 325-329
    • Offer, G.1    Elliott, A.2
  • 26
    • 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
  • 28
    • 0028347113 scopus 로고
    • Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap
    • Saito, K., 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
    • Saito, K.1    Aoki, T.2    Yanagida, T.3
  • 29
    • 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
  • 32
    • 0014316853 scopus 로고
    • The energetics of tortoise muscle
    • Woledge, R. C. 1968. The energetics of tortoise muscle. J. Physiol. (Lond.). 197:685-707.
    • (1968) J. Physiol. (Lond.) , vol.197 , pp. 685-707
    • Woledge, R.C.1
  • 34
    • 0024044377 scopus 로고
    • Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells
    • Woledge, R. C., and P. C. Reilly. 1988. Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells. Biophys. J. 54:97-104.
    • (1988) Biophys. J. , vol.54 , pp. 97-104
    • Woledge, R.C.1    Reilly, P.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.