메뉴 건너뛰기




Volumn 91, Issue 11, 2006, Pages 4102-4109

Filament compliance effects can explain tension overshoots during force development

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN;

EID: 33845357154     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.087312     Document Type: Article
Times cited : (41)

References (21)
  • 1
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. USA. 85:3265-3269.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 2
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., E. Homsher, and M. Regnier. 2000. Regulation of contraction in striated muscle. Physiol. Rev. 80:853-924.
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 3
    • 33645766813 scopus 로고    scopus 로고
    • Tension recovery in permeabilized rat soleus muscle fibers after rapid shortening and restretch
    • Campbell, K. S. 2006. Tension recovery in permeabilized rat soleus muscle fibers after rapid shortening and restretch. Biophys. J. 90:1288-1294.
    • (2006) Biophys. J. , vol.90 , pp. 1288-1294
    • Campbell, K.S.1
  • 4
    • 15844429778 scopus 로고    scopus 로고
    • The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle
    • Sleep, J., M. Irving, and K. Burton. 2005. The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle. J. Physiol. (Lond.). 563:671-687.
    • (2005) J. Physiol. (Lond.) , vol.563 , pp. 671-687
    • Sleep, J.1    Irving, M.2    Burton, K.3
  • 5
    • 0031953771 scopus 로고    scopus 로고
    • Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning
    • Daniel, T. L., A. C. Trimble, and P. B. Chase. 1998. Compliant realignment of binding sites in muscle: transient behavior and mechanical tuning. Biophys. J. 74:1611-1621.
    • (1998) Biophys. J. , vol.74 , pp. 1611-1621
    • Daniel, T.L.1    Trimble, A.C.2    Chase, P.B.3
  • 6
    • 33845356158 scopus 로고    scopus 로고
    • Random numbers
    • C. B. Moler, editor. Society for Industrial and Applied Mathematics, Philadelphia
    • Moler, C. B. 2004. Random numbers. In Numerical Computing with MATLAB. C. B. Moler, editor. Society for Industrial and Applied Mathematics, Philadelphia. 257-268.
    • (2004) Numerical Computing with MATLAB , pp. 257-268
    • Moler, C.B.1
  • 9
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and 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 and 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
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0031038445 scopus 로고    scopus 로고
    • Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics
    • Campbell, K. 1997. Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics. Biophys. J. 72:254-262.
    • (1997) Biophys. J. , vol.72 , pp. 254-262
    • Campbell, K.1
  • 14
    • 0028005290 scopus 로고
    • Coupling calcium binding to troponin C and cross-bridge cycling in skinned cardiac cells
    • Landesberg, A., and S. Sideman. 1994. Coupling calcium binding to troponin C and cross-bridge cycling in skinned cardiac cells. Am. J. Physiol. 266:H1260-H1271.
    • (1994) Am. J. Physiol. , vol.266
    • Landesberg, A.1    Sideman, S.2
  • 15
    • 0033555870 scopus 로고    scopus 로고
    • Changes in conformation of myosin heads during the development of isometric contraction and rapid shortening in single frog muscle fibres
    • Piazzesi, G., M. Reconditi, I. Dobbie, M. Linari, P. Boesecke, O. Diat, M. Irving, and V. Lombardi. 1999. Changes in conformation of myosin heads during the development of isometric contraction and rapid shortening in single frog muscle fibres. J. Physiol. (Lond.). 514:305-312.
    • (1999) J. Physiol. (Lond.) , vol.514 , pp. 305-312
    • Piazzesi, G.1    Reconditi, M.2    Dobbie, I.3    Linari, M.4    Boesecke, P.5    Diat, O.6    Irving, M.7    Lombardi, V.8
  • 16
    • 0027234246 scopus 로고
    • A model of stress relaxation in cross-bridge systems: Effect of a series elastic element
    • Luo, Y., R. Cooke, and E. Pate. 1993. A model of stress relaxation in cross-bridge systems: effect of a series elastic element. Am. J. Physiol. 265:C279-C288.
    • (1993) Am. J. Physiol. , vol.265
    • Luo, Y.1    Cooke, R.2    Pate, E.3
  • 17
    • 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
  • 18
    • 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
  • 20
    • 33746238508 scopus 로고    scopus 로고
    • Residual force enhancement in skeletal muscle
    • Herzog, W., E. J. Lee, and D. E. Rassier. 2006. Residual force enhancement in skeletal muscle. J. Physiol. (Lond.). 574:635-642.
    • (2006) J. Physiol. (Lond.) , vol.574 , pp. 635-642
    • Herzog, W.1    Lee, E.J.2    Rassier, D.E.3
  • 21
    • 1842339908 scopus 로고    scopus 로고
    • The biphasic force-velocity relationship in frog muscle fibres and its evaluation in terms of cross-bridge function
    • Edman, K. A., A. Mansson, and C. Caputo. 1997. The biphasic force-velocity relationship in frog muscle fibres and its evaluation in terms of cross-bridge function. J. Physiol. (Lond.). 503:141-156.
    • (1997) J. Physiol. (Lond.) , vol.503 , pp. 141-156
    • Edman, K.A.1    Mansson, A.2    Caputo, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.