Mechanism of myofilament sliding in muscle contraction /

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Bibliographic Details
Imprint:New York : Plenum Press, c1993.
Description:xvi, 866 p. : ill. ; 27 cm.
Language:English
Series:Advances in experimental medicine and biology v. 332
Subject:
Format: Print Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/1556611
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Other authors / contributors:Sugi, Haruo, 1933-
Pollack, Gerald H.
ISBN:0306444525
Notes:Proceedings of a symposium on Mechanism of myofilament sliding in muscle contraction, held Nov. 11-15, 1991, in Hakone, Japan.
Includes bibliographical references and indexes.
Table of Contents:
  • Introductory lecture on muscle contraction / A. F. Huxley
  • A comparison of the atomic model of F-actin with cryo-electron micrographs of actin and decorated actin / K. C. Holmes, M. Tirion, D. Popp, M. Lorenz, W. Kabsch and R. A. Milligan
  • A new crystal form of tropomyosin / A. Miegel, L. Lee, Z. Dauter and Y. Maeda
  • Experiments on rigor crossbridge actin and filament sliding in insect flight muscle / M. K. Reedy, C. Lucaveche, M. C. Reedy and B. Somasundaram
  • Gross structural features of myosin head during sliding movement of actin as studied by quick-freeze deep-etch electron microscopy / E. Katayama
  • Cross-bridge angle distribution and thin filament stiffness in frog skeletal muscle fibers as studied by quick-freeze deep-etch electron microscopy / S. Suzuki, Y. Oshimi and H. Sugi
  • Elastic properties of connecting filaments along the sarcomere / K. Trombitas and G. H. Pollack
  • Structural studies on the conformations of myosin / A. R. Faruqi, R. A. Cross and J. Kendrick-Jones
  • Activation and relaxation mechanisms in single muscle fibres / C. C. Ashley, T. J. Lea, I. P. Milligan, R. E. Palmer and S. J. Simnett
  • The molecular switch in troponin C / J. Gergely, Z. Grabareck and T. Tao
  • The mechanism of Ca[superscript 2+]-coordination in the EF-hand of TnC, by cassette mutagenesis / A. Babu, H. Su and J. Gulati
  • The strength of binding of the weakly-binding crossbridge created by sulfhydryl modification has very low calcium sensitivity / V. A. Barnett and M. Schoenberg
  • Role of parvalbumin in relaxation in relaxation of frog skeletal muscle / T. Hou, J. D. Johnson and J. A. Rall
  • Evidence for the existence of endothelial factors regulating contractility in rat heart / S. Winegrad
  • Effects of tropomyosin deficiency in flight muscle of Drosophila melanogaster / J. Molloy, A. Kreuz, R. Miller, T. Tansey and D. Maughan
  • Effect of myosin heavy chain peptides on contractile activation of skinned cardiac muscle fibres / J. C. Ruegg, J. D. Strauss, C. Zeugner and I. Trayer
  • Cross-bridges affect both TnC structure and calcium affinity in muscle fibers / A. M. Gordon and E. B. Ridgway
  • Phosphorylation-contraction coupling in smooth muscle: Role of caldesmon / G. Pfitzer, W. Fischer and J. M. Chalovich
  • Influence of Ca-activated brevin on the mechanical properties of skinned smooth muscle / Ph. Gailly, J. M. Gillis and J. P. Capony
  • Obituary: Ken Hotta
  • Interaction between two myosin heads in acto-smooth muscle heavy meromyosin rigor complex / H. Onishi
  • Luminescent/paramagnetic probes of order and orientation in biological assemblies: The transformation of luminescent probes into p-radicals by photochemical reduction within the contractile apparatus / T. P. Burghardt and K. Ajtai
  • The region in myosin S-1 that may be involved in energy transduction / M. F. Morales, K. Ue and D. B. Bivin
  • Identification of actin surface interacting with myosin during the actin myosin sliding / K. Sutoh
  • Photochemical cleavage of myosin heavy chain and the effect on the interaction with actin / Y. Okamoto and C. Cremo
  • How are myosin fragments bound to nitrocellulose film? / Y. Y. Toyoshima
  • In vitro studies of determinants of smooth muscle mechanics / J. R. Sellers, S. Umemoto and G. Cuda
  • Factors affecting filament velocity in in vitro motility assays and their relation to unloaded shortening velocity in muscle fibers / E. Homsher, F. Wang and J. Sellers
  • Dynamical role of "protein friction" in the sliding movement of protein motors in vitro / K. Tawada
  • Dependence of the work done by ATP-induced actin-myosin sliding on the initial baseline force: Its implications for kinetic properties of myosin heads in muscle contraction / H. Sugi, K. Oiwa and S. Chaen
  • Unitary distance of ATP-induced actin-myosin sliding studied with an in vitro force-movement assay system / K. Oiwa, T. Kawakami and H. Sugi
  • Orientations of actin monomers in moving actin filaments / K. Kinosita, Jr., N. Suzuki, S. Ishiwata, T. Nishizuka, H. Itoh, H. Hakozaki, G. Marriott and H. Miyata
  • Force on single actin filaments in a motility assay measured with an optical trap / R. M. Simmons, J. T. Finer, H. M. Warrick, B. Kralik and J. A. Spudich
  • Coupling between ATPase and force-generating attachment-detachment cycles of actomyosin in vitro / T. Yanagida, A. Ishijima, K. Saito and Y. Harada
  • Kinetic properties of the ATP-dependent actin-myosin sliding as revealed by the force-movement assay system with a centrifuge microscope / S. Chaen, K. Oiwa, T. Kobayashi, T. Gross, E. Kamitsubo, T. Shimmen and H. Sugi
  • Electrostatic potential around actin / T. Ando, N. Kobayashi and E. Muneoka
  • Further studies of the self-induced translation model of myosin head motion along the actin filament / T. Mitsui and H. Oshima
  • Discussion on the myosin step size
  • Crossbridge rotation in EDC-crosslinked striated muscle fibers / H. Iwamoto and R. J. Podolsky
  • Time-resolved equatorial X-ray diffraction measurements in single intact muscle fibres / P. J. Griffiths, C. C. Ashley, M. A. Bagni, G. Cecchi and Y. Maeda
  • Current X-ray diffraction experiments using a synchrotron radiation source / N. Yagi, S. Takemori and M. Watanabe
  • Time-resolved studies of crossbridge movement: Why use fish muscle? / J. Squire and J. Harford
  • The first thin filament layer line decreases in intensity during an isometric contraction of frog skeletal muscle / K. Wakabayashi, H. Saito, N. Moriwaki, T. Kobayashi and H. Tanaka
  • Evidence for structural changes in crossbridges during force generation / B. Brenner and L. C. Yu
  • Mechanics and structure of cross-bridges during contractions initiated by photolysis of caged Ca[superscript 2+] / T. D. Lenart, T. S. Allen, R. J. Barsotti, G. C. R. Ellis-Davies, J. H. Kaplan, C. Franzini-Armstrong and Y. E. Goldman
  • Effects of ionic strength on force transients induced by flash photolysis of caged ATP in covalently crosslinked rabbit psoas muscle fibers / K. Yamada, Y. Emoto, K. Horiuti and K. Tawada
  • Kinetics of force generation and Pi release in rabbit soleus muscle fibers / E. Homsher and N. Millar
  • Distance of myofilament sliding per ATP molecule in skeletal muscle fibers studied using laser flash photolysis of caged ATP / T. Yamada, O. Abe, T. Kobayashi and H. Sugi
  • Kinetic and physical characterization of force generation in muscle: A laser temperature-jump and length-jump study on activated and contracting rigor fibers / J. S. Davis and W. F. Harrington
  • Dynamic actin interaction of cross-bridges during force generation: Implications for cross-bridge action in muscle / B. Brenner
  • Spontaneous tension oscillation (SPOC) of muscle fibers and myofibrils. Minimum requirements for SPOC / S. Ishiwata, T. Anazawa, T. Fujita, N. Fukuda, H. Shimizu and K. Yasuda
  • Inferences concerning crossbridges from work on insect muscle / R. T. Tregear, E. Townes, J. Gabriel and C. Ellington
  • Elementary steps of contraction probed by sinusoidal analysis technique in rabbit psoas fibers / M. Kawai, Y. Zhao and H. R. Halvorson
  • The effect of lattice spacing changes on cross-bridge kinetics in rabbit psoas fibers / Y. Zhao, M. Kawai and J. Wray
  • Molecular biology of the length-tension relation in cardiac muscle / J. Gulati
  • Effect of cross-linking on the contractile behavior of myofibrils / W. F. Harrington, T. Karr and W. B. Busa
  • Essential role of myosin S-2 region in muscle contraction / T. Kobayashi, K. Noguchi, T. Gross and H. Sugi
  • Taking the first steps in contraction mechanics of single myocytes from frog heart / P. W. Brandt, F. Colomo, C. Poggesi and C. Tesi
  • Tension and intracellular calcium transients of activated ferret ventricular muscle in response to step length changes / Y. Saeki, S. Kurihara, K. Hongo and E. Tanaka
  • Determinants of velocity of sarcomere shortening in mammalian myocardium / H. E. D. J. ter Keurs and P. P. de Tombe
  • Mechanism underlying double hyperbolic force-velocity relation in vertebrate skeletal muscle / K. A. P. Edman
  • Shortening-induced tension enhancement: Implication for length-tension relations / G. H. Pollack, A. Horowitz, M. Wussling and K. Trombitas
  • Kinetics of regeneration of cross-bridge power stroke in shortening muscle / G. Piazzesi, M. Linari and V. Lombardi
  • Force response of unstimulated intact frog muscle fibres to ramp stretches / M. A. Bagni, C. Cecchi, F. Colomo and P. Garzella
  • Measurement of transverse stiffness change during contraction in frog skeletal muscle by scanning laser acoustic microscope / T. Tsuchiya, H. Iwamoto, Y. Tamura and H. Sugi
  • Power and efficiency: How to get the most out of striated muscle / N. A. Curtin and R. C. Woledge
  • The efficiency of energy conversion by swimming muscle of fish / R. C. Woledge and N. A. Curtin
  • Two classes of mammalian skeletal muscle fibers distinguished by metabolite content / M. J. Kushmerick, T. S. Moerland and R. W. Wiseman
  • Influence of ionic strength on contractile force and energy consumption of skinned fibers from mammalian and crustacean striated muscle / R. E. Godt, R. T. H. Fogaca, M. A. W. Andrewa and T. M. Nosek
  • Variable crossbridge cycling-ATP coupling accounts for cardiac mechanoenergetics / T. W. Taylor and H. Suga
  • Structural changes during contraction
  • Muscle contraction mechanisms as studied with in vitro assay systems
  • Regulatory mechanisms of muscle contraction
  • The cross-bridge cycle in muscle contraction
  • How much work from one cross-bridge cycle?
  • Summary and Conclusion / A. F. Huxley.