ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin

[1]  J. Spudich,et al.  The neck region of the myosin motor domain acts as a lever arm to generate movement. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[2]  M. Irving,et al.  Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle. , 1996, Biophysical journal.

[3]  M. Irving,et al.  Orientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers. , 1996, Biophysical journal.

[4]  James D. Jontes,et al.  A 32° tail swing in brush border myosin I on ADP release , 1995, Nature.

[5]  Michael Whittaker,et al.  A 35-Å movement of smooth muscle myosin on ADP release , 1995, Nature.

[6]  A. Baker,et al.  The myosin catalytic domain does not rotate during the working power stroke. , 1995, Biophysical journal.

[7]  Malcolm Irving,et al.  Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle , 1995, Nature.

[8]  D. D. Thomas,et al.  Orientational dynamics of indane dione spin-labeled myosin heads in relaxed and contracting skeletal muscle fibers. , 1995, Biophysical journal.

[9]  G. Radda,et al.  The creatine kinase equilibrium, free [ADP] and myosin ATPase in vascular smooth muscle cross-bridges. , 1995, Journal of theoretical biology.

[10]  J. Sellers,et al.  Two Heads Are Required for Phosphorylation-dependent Regulation of Smooth Muscle Myosin (*) , 1995, The Journal of Biological Chemistry.

[11]  K. Trybus.  Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length. , 1994, The Journal of biological chemistry.

[12]  Kathleen M. Trybuss.  Regulation of Expressed Truncated Smooth Muscle Myosins , 1994 .

[13]  K C Holmes,et al.  Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. , 1993, Journal of molecular biology.

[14]  K. Trybus,et al.  Skeletal muscle myosin light chains are essential for physiological speeds of shortening , 1993, Nature.

[15]  Ivan Rayment,et al.  Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1 , 1993, Nature.

[16]  R A Milligan,et al.  Structure of the actin-myosin complex and its implications for muscle contraction. , 1993, Science.

[17]  D A Winkelmann,et al.  Three-dimensional structure of myosin subfragment-1: a molecular motor. , 1993, Science.

[18]  K. Trybus,et al.  Chimeric regulatory light chains as probes of smooth muscle myosin function. , 1993, The Journal of biological chemistry.

[19]  K. Török,et al.  The effects of MgADP on cross‐bridge kinetics: a laser flash photolysis study of guinea‐pig smooth muscle. , 1993, The Journal of physiology.

[20]  R. Cooke,et al.  Paramagnetic probes attached to a light chain on the myosin head are highly disordered in active muscle fibers. , 1992, Biophysical journal.

[21]  C. Cremo,et al.  A new method to specifically label thiophosphorylatable proteins with extrinsic probes. Labeling of serine-19 of the regulatory light chain of smooth muscle myosin. , 1992, Bioconjugate chemistry.

[22]  D. D. Thomas,et al.  Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibres. , 1992, Journal of molecular biology.

[23]  M. Ikebe,et al.  Exchange of the fluorescence-labeled 20,000-dalton light chain of smooth muscle myosin. , 1991, Biochemistry.

[24]  M. Geeves.  The dynamics of actin and myosin association and the crossbridge model of muscle contraction. , 1991, The Biochemical journal.

[25]  W. Kabsch,et al.  Atomic model of the actin filament , 1990, Nature.

[26]  W. Kabsch,et al.  Atomic structure of the actin: DNase I complex , 1990, Nature.

[27]  P. Fajer,et al.  General method for multiparameter fitting of high-resolution EPR spectra using a simplex algorithm☆ , 1990 .

[28]  J. Sellers,et al.  Effect of phosphorylation on the binding of smooth muscle heavy meromyosin X ADP to actin. , 1987, The Journal of biological chemistry.

[29]  Y. Goldman,et al.  Kinetics of the actomyosin ATPase in muscle fibers. , 1987, Annual review of physiology.

[30]  D. D. Thomas,et al.  Spectroscopic probes of muscle cross-bridge rotation. , 1987, Annual review of physiology.

[31]  V. Barnett,et al.  High-Resolution Detection of muscle Crossbridge Orientation by Electron Paramagnetic Resonance. , 1986, Biophysical journal.

[32]  R. Cooke,et al.  The mechanism of muscle contraction. , 1986, CRC critical reviews in biochemistry.

[33]  D. Hartshorne,et al.  Effects of Ca2+ on the conformation and enzymatic activity of smooth muscle myosin. , 1985, The Journal of biological chemistry.

[34]  D. Hartshorne,et al.  Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: preparation of heavy meromyosin and subfragment 1 with intact 20 000-dalton light chains. , 1985, Biochemistry.

[35]  R. Cooke,et al.  Orientation of spin labels attached to cross-bridges in contracting muscle fibres , 1982, Nature.

[36]  D. Labuda,et al.  Codon-induced tRNA association: quantitative analysis by sedimentation equilibrium , 1982 .

[37]  R. Cooke,et al.  Orientation of spin-labeled myosin heads in glycerinated muscle fibers. , 1980, Biophysical journal.

[38]  R. Cooke.  A new method for producing myosin subfragment-1. , 1972, Biochemical and biophysical research communications.

[39]  J. Freed,et al.  Estimating slow-motional rotational correlation times for nitroxides by electron spin resonance , 1972 .