Access provided by Autonomous University of Puebla. Download to read the full chapter text
Chapter PDF
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
Bagshaw CR, Eccleston JF, Trentham DR, and Yates DW. Transient kinetic studies of the Mg++-dependent ATPase of myosin and its proteolytic fragments. Cold Spring Harb Symp Quant Biol 37: 127–135, 1973.
Brenner B, Schoenberg M, Chalovich JM, Greene LC, and Eisenberg E. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proc Natl Acad Sci USA 79: 7288–7291, 1982.
Brenner B, Yu LC, and Podolsky R.J. X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. Biophys J 46: 299–306, 1984.
Brenner B, and Yu LC. Equatorial X-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Changes in intensities and lattice spacing. Biophys J 48:829–834, 1985.
Brenner B, Chalovich JM, Greene LC, Eisenberg E, and Schoenberg M. Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solutions. Biophys J 50: 685–691, 1986.
Brenner B, Yu LC, Greene LC, Eisenberg E, and Schoenberg M. Ca2+-sensitive cross-bridge dissociation in the presence of MgPPi in skinned rabbit psoas fibers. Biophys J 50: 1101–1108, 1986(b).
Brenner B. Muscle mechanics and biochemical kinetics, in: Molecular Mechanism of Muscular Contraction, John Squire, ed, Macmillan Press Ltd., London, pp. 77–149, 1990.
Brenner B, Yu LC, and Chalovich JM. Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon. Implications for the pathway to force generation. Proc Natl Acad Sci USA 88: 5739–5743, 1991.
Brenner B, Chalovich JM, and Yu LC. Distinct molecular processes associated with isometric force generation and with rapid tension recovery after quick release. Biophys J 68:106s–111s, 1995.
Brenner B, Kraft T, and Chalovich JM. Fluorescence of NBD-labeled troponin-I as a probe for the kinetics of thin filament activation. Adv Exp Med Mol Biol 453:177–185, 1998.
Brenner B, and Chalovich JM. Kinetics of thin filament activation probed by fluorescence of N-((2-Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-l,3-diazole-labelled troponin I incorporated in skinned fibers of rabbit psoas muscle. Implications for regulation of muscle contraction. Biophys J 77:2692–2708, 1999.
Brenner B, Kraft T, Yu LC, and Chalovich JM. Thin filament activation probed by fluorescence of N-((2-Iodoacetoxy)ethyi)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labelled troponin I incorporated in skinned fibers of rabbit psoas muscle. Biophys J 77:2677–2691, 1999.
Chase PB, Martyn DA, Kushmerick MJ, and Gordon AM. Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit. J Physiol Lond 460:231–46, 1993.
Dantzig JA, Goldman YE, Millar NC, Lacktis J, and Homsher E. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J Physiol Lond 451:247–278, 1992.
Frisbie SM, Chalovich JM, Brenner B, and Yu LC Modulation of cross-bridge affinity for MgGTP by Ca++ in skinned fibers of rabbit psoas muscle. Biophys J 72:2255–2261, 1997.
Geeves MA, Goody RS, and Gutfreund H. Kinetics of acto.Sl interaction. J Muscle Res Cell Motil 5:351–361, 1984.
Geeves MA, and Conibear PB. The role of three state docking of myosin S1 with actin in force generation. Biophys J 68:l94s–201s, 1995.
Goody RS, and Hofmann F. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides J Muscle Res Cell Motil 1:101–115, 1980.
Greene LE, and Eisenberg E. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc Natl Acad Sci USA: 77:2616–2620, 1980.
Greene LE, Sellers JR, Eisenberg E, and Adelstein RS. Binding of gizzard smooth muscle myosin subfragment-one to actin in the presence and absence of ATP. Biochemistry 22:530–535, 1983.
Gu J, Xu S, and Yu LC. A model of cross-bridge attachment to actin in the A*M*ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle. Biophys J 82:2123–33, 2002.
Head JG, Ritchie MD, and Geeves MA. Characterization of the equilibrium between blocked and closed states of muscle thin filaments. Eur J Biochem 227:694–699, 1995.
Holmes KC. The actomyosin interaction and its control by tropomyosin. Biophys J 68:2s–5s, 1995.
Kraft T, Yu LC, Kuhn HJ, and Brenner B. Effect of Ca++ on weak cross-bridge interaction with actin in the presence of the nucleotide analog ATPyS. Proc Natl Acad Sci USA 89: 11362–11366, 1992.
Kraft T, Chalovich JM, Yu LC, and Brenner B. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological temperature and ionic strength conditions. Additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. Biophys J 68:2404–2418, 1995.
Kraft T, Xu S, Brenner B, and Yu LC. The effect of thin filament activation on the attachment of weak binding cross-bridges: A 2D-Xray-diffraction study on single muscle fibers. Biophys J 76:1494–1513, 1999.
Kraft T, Mattel T, Radocaj A, Piep B, Nocula Ch, Furch M, and Brenner B. Structural features of cross-bridges in isometrically contracting skeletal muscle Biophys J 82:2536–2547, 2002.
Kraft T, Mählmann E, Mattei T, and Brenner B. Effects of myosin binding to actin on structural and functional properties of the myosin head domain. Biophys J 86:266a, 2004
Lehman W, Craig R, and Vibert P. Ca2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368:65–67, 1994.
Lehman W, Vibert P, Uman P, and Craig R. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J Mol Biol 251:191–196, 1995.
Mattel T, Mählmann E, Piep B, Kraft T, and Brenner B. MgADP.AlF4-binding to cross-bridges under rigor conditions: mechanical and structural properties of the resulting cross-bridge state. Biophys J 86:266a, 2004.
McKillop DFA, and Geeves MA. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 65:693–701, 1993.
Millar NC, and Homsher E. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady state and transient kinetic study. J Biol Chem 265:20234–20240, 1990.
Schoenberg M. Equilibrium muscle cross-bridge behavior. Theoretical considerations. Biophys J 48:467–475, 1985.
Stein LA, Schwartz RP, Chock PB, and Eisenberg E. Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5′-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. Biochemistry 18, 3895–3909, 1979.
Stein LE, Chock PB, and Eisenberg E. The rate-limiting step in the actomyosin adenosintriphosphatase cycle. Biochemistry 23:1555–1563, 1984.
White HD, and Taylor EW. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15:5818–5826, 1976.
Xu S, Malinchik S, Gllroy D, Kraft T, Brenner B, and Yu LC. X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle. Biophys J 72:2292–2303, 1997.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2005 Springer Science+Business Media, Inc.
About this paper
Cite this paper
Brenner, B., Mählmann, E., Mattei, T., Kraft, T. (2005). Driving Filament Sliding: Weak binding cross-bridge states, strong binding cross-bridge states, and the power stroke. In: Sugi, H. (eds) Sliding Filament Mechanism in Muscle Contraction. Advances in Experimental Medicine and Biology, vol 565. Springer, Boston, MA. https://doi.org/10.1007/0-387-24990-7_7
Download citation
DOI: https://doi.org/10.1007/0-387-24990-7_7
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-387-24989-6
Online ISBN: 978-0-387-24990-2
eBook Packages: MedicineMedicine (R0)