Some Muscle References (2005)

 

Bagshaw, C. R. and D. R. Trentham (1974). The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction. Biochem J 141: 331-49.

Batra, R. and D. J. Manstein (1999). Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine. Biol Chem 380: 1017-23.

Bauer, C. B., H. M. Holden, J. B. Thoden, R. Smith and I. Rayment (2000). X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain. Journal of Biological Chemistry 275: 38494-9.

Bement, W. M. and M. S. Mooseker (1995). TEDS rule: a molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head. Cell Motil Cytoskeleton 31: 87-92.

Brzeska, H. and E. D. Korn (1996). Regulation of class I and class II myosins by heavy chain phosphorylation. J Biol Chem 271: 16983-6.

Coluccio, L. M. and M. A. Geeves (1999). Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension? J Biol Chem 274: 21575-80.

Cooke, R. (1986). The Mechanism of Muscle Contraction. CRC Crit Rev. Biochem 21: 53-118.

Coureux, P. D., H. L. Sweeney and A. Houdusse (2004). Three myosin V structures delineate essential features of chemo-mechanical transduction. Embo J 23: 4527-37.

Coureux, P. D., A. L. Wells, J. Menetrey, C. M. Yengo, C. A. Morris, H. L. Sweeney and A. Houdusse (2003). A structural state of the myosin V motor without bound nucleotide. Nature 425: 419-23.

Cremo, C. R. and M. A. Geeves (1998). Interaction of actin and ADP with the head domain of smooth muscle myosin: implications for strain-dependent ADP release in smooth muscle. Biochemistry 37: 1969-78.

Criddle, A. H., M. A. Geeves and T. Jeffries (1985). The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem J 232: 343-9.

Dantzig, J. A., Y. E. Goldman, N. C. Millar, J. Lacktis and E. Homsher (1992). Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J Physiol 451: 247-78.

De La Cruz, E. M., E. M. Ostap and H. L. Sweeney (2001). Kinetic mechanism and regulation of myosin VI. J Biol Chem 276: 32373-81.

Dominguez, R., Y. Freyzon, K. M. Trybus and C. Cohen (1998). Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre- power stroke state. Cell 94: 559-71.

Fenn, W. O. (1923). A quantitative comparison between the energy liberated and the work performed by the isolated sartorius muscle of the frog. J. Physiology 58: 175-203.

Fortune, N. S., M. A. Geeves and K. W. Ranatunga (1991). Tension responses to rapid pressure release in glycerinated rabbit muscle fibers. Proc Natl Acad Sci U S A 88: 7323-7.

Fujita-Becker, S., U. Durrwang, M. Erent, R. J. Clark, M. A. Geeves and D. J. Manstein (2004). Changes in Mg2+-Ion concentration and heavy chain phosphorylation regulate the motor activity of a class-I myosin. J Biol Chem 280, 6064-6071.

Furch, M., B. Remmel, M. A. Geeves and D. J. Manstein (2000). Stabilization of the actomyosin complex by negative charges on myosin. Biochemistry 39: 11602-8.

Geeves, M. A. and P. B. Conibear (1995). The role of three-state docking of myosin S1 with actin in force generation. Biophys J 68: 194S-199S; discussion 199S-201S.

Geeves, M. A. and K. C. Holmes (1999). Structural mechanism of muscle contraction. Annu Rev Biochem 68: 687-728.

Geeves, M. A. and K. C. Holmes (2005). The Molecular Mechanism of Muscle Contraction. Advances in Protein Chemistry 71, 161-193,

Geeves, M. A. and T. E. Jeffries (1988). The effect of nucleotide upon a specific isomerization of actomyosin subfragment 1. Biochem J 256: 41-6.

Geisterfer-Lowrance, A. A., S. Kass, G. Tanigawa, H. P. Vosberg, W. McKenna, C. E. Seidman and J. G. Seidman (1990). A molecular basis for familial hypertrophic cardiomyopathy: a beta cardiac myosin heavy chain gene missense mutation. Cell 62: 999-1006.

Holmes, K. C., I. Angert, F. J. Kull, W. Jahn and R. R. Schroder (2003). Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425: 423-7.

Holmes, K. C., R. R. Schršder, H. L. Sweeney and A. Houdusse (2004). The structure of the rigor complex and its implications for the power stroke. Phil. Trans. R. Soc. B 359: 1819-1828.

Houdusse, A., V. N. Kalabokis, D. Himmel, A. G. Szent-Gyorgyi and C. Cohen (1999). Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell 97: 459-70.

Jontes, J. D., E. M. Wilson-Kubalek and R. A. Milligan (1995). A 32 degree tail swing in brush border myosin I on ADP release. Nature 378: 751-3.

Kawai, M. and H. R. Halvorson (1991). Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle. Biophys J 59: 329-42.

Kovacs, M., A. Malnasi-Csizmadia, R. J. Woolley and C. R. Bagshaw (2002). Analysis of nucleotide binding to Dictyostelium myosin II motor domains containing a single tryptophan near the active site. J Biol Chem 277: 28459-67.

Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of proteins structures. J. Appl. Cryst. 24: 946-950.

Kurzawa, S. E. and M. A. Geeves (1996). A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein. J Muscle Res Cell Motil 17: 669-76.

Kurzawa, S. E., D. J. Manstein and M. A. Geeves (1997). Dictyostelium discoideum myosin II: characterization of functional myosin motor fragments. Biochemistry 36: 317-23.

Kurzawa-Goertz, S. E., C. L. Perreault-Micale, K. M. Trybus, A. G. Szent-Gyorgyi and M. A. Geeves (1998). Loop I can modulate ADP affinity, ATPase activity, and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms. Biochemistry 37: 7517-25.

Lymn, R. W. and E. W. Taylor (1971). Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10: 4617-24.

Malnasi-Csizmadia, A., M. Kovacs, R. J. Woolley, S. W. Botchway and C. R. Bagshaw (2001). The dynamics of the relay loop tryptophan residue in the Dictyostelium myosin motor domain and the origin of spectroscopic signals. J Biol Chem 276: 19483-90.

Malnasi-Csizmadia, A., D. S. Pearson, M. Kovacs, R. J. Woolley, M. A. Geeves and C. R. Bagshaw (2001). Kinetic resolution of a conformational transition and the atp hydrolysis step using relaxation methods with a dictyostelium myosin ii mutant containing a single tryptophan residue. Biochemistry 40: 12727-37.

Manstein, D. J., K. M. Ruppel and J. A. Spudich (1989). Expression and characterization of a functional myosin head fragment in Dictyostelium discoideum. Science 246: 656-8.

Margossian, S. S. and S. Lowey (1973a). Substructure of the myosin molecule: III Preparation of single- headed derivatives of myosin. J. Mol. Biol. 74: 301-311.

Margossian, S. S. and S. Lowey (1973b). Substructure of the myosin molecule; IV Interactions of myosin and its subfragments with adenosine triphosphate and actin. J. Mol. Biol. 74: 313-330.

Mehta, A. D., R. S. Rock, M. Rief, J. A. Spudich, M. S. Mooseker and R. E. Cheney (1999). Myosin-V is a processive actin-based motor. Nature 400: 590-3.

Merritt, E. A. and D. J. Bacon (1997). Raster3D Version 2: photorealistic molecular graphics. Methods of Enzymology 277: 505-524.

Millar, N. C. and M. A. Geeves (1983). The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1. FEBS Lett 160: 141-8.

Murphy, C. T. and J. A. Spudich (1998). Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates. Biochemistry 37: 6738-44.

Nyitrai, M. and M. Geeves (2004). ADP and Strain Sensitivity in Myosin Motors. Phil. Trans Roy. Soc. B 359: 1867-1877.

Onishi, H., K. Maeda, Y. Maeda, A. Inoue and K. Fujiwara (1995). Functional chicken gizzard heavy meromyosin expression in and purification from baculovirus-infected insect cells. Proc.  Natl. Acad. Sci.  USA 92: 704-8.

Ostap, E. M., V. A. Barnett and D. D. Thomas (1995). Resolution of three structural states of spin-labeled myosin in contracting muscle. Biophys J 69: 177-88.

Pato, M. D., J. R. Sellers, Y. A. Preston, E. V. Harvey and R. S. Adelstein (1996). Baculovirus expression of chicken nonmuscle heavy meromyosin II-B. Characterization of alternatively spliced isoforms. J  Biol Chem 271: 2689-95.

Pereira, J. S., D. Pavlov, M. Nili, M. Greaser, E. Homsher and R. L. Moss (2001). Kinetic differences in cardiac myosins with identical loop 1 sequences. J Biol Chem 276: 4409-15.

Purcell, T. J., C. Morris, J. A. Spudich and H. L. Sweeney (2002). Role of the lever arm in the processive stepping of myosin V. Proc Natl Acad Sci U S A 99: 14159-64.

Ranatunga, K. W., M. E. Coupland and G. Mutungi (2002). An asymmetry in the phosphate dependence of tension transients induced by length perturbation in mammalian (rabbit psoas) muscle fibres. J Physiol 542: 899-910.

Rayment, I., H. M. Holden, M. Whittaker, C. B. Yohn, M. Lorenz, K. C. Holmes and R. A. Milligan (1993b). Structure of the actin-myosin complex and its implications for muscle contraction. Science. 261: 58-65.

Rayment, I., W. R. Rypniewski, K. Schmidt-Base, R. Smith, D. R. Tomchick, M. M. Benning, D. A. Winkelmann, G. Wesenberg and H. M. Holden (1993a). Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261: 50-8.

Reubold, T. F., S. Eschenburg, A. Becker, F. J. Kull and D. J. Manstein (2003). A structural model for actin-induced nucleotide release in myosin. Nat Struct Biol 10: 826-30.

Rosenfeld, S. S., A. Houdusse and H. L. Sweeney (2004). Magnesium regulates ADP dissociation from myosin V. J Biol Chem. 280: 6072-6079

Siemankowski, R. F., M. O. Wiseman and H. D. White (1985). ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci U S A 82: 658-62.

Sleep, J. A. and R. L. Hutton (1980). Exchange between inorganic phosphate and adenosine 5'-triphosphate in the medium by actomyosin subfragment 1. Biochemistry 19: 1276-83.

Smith, C. A. and I. Rayment (1996). X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Biochemistry 35: 5404-17.

Smith, D. A. and J. Sleep (2004). Mechanokinetics of rapid tension recovery in muscle: the Myosin working stroke is followed by a slower release of phosphate. Biophys J 87: 442-56.

Sweeney, H. L. and A. Houdusse (2004). The motor mechanism of myosin V: insights for muscle contraction. Phil. Trans. R. Soc. B 359: 1829-1841.

Sweeney, H. L., S. S. Rosenfeld, F. Brown, L. Faust, J. Smith, J. Xing, L. A. Stein and J. R. Sellers (1998). Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket. J Biol Chem 273: 6262-70.

Tesi, C., F. Colomo, S. Nencini, N. Piroddi and C. Poggesi (2000). The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle. Biophys J 78: 3081-92.

Trentham, D. R., J. F. Eccleston and C. R. Bagshaw (1976). Kinetic analysis of ATPase mechanisms. Q Rev Biophys 9: 217-81.

Urbanke, C. and J. Wray (2001). A fluorescence temperature-jump study of conformational transitions in myosin subfragment 1. Biochem J 358: 165-73.

Uyeda, T. Q., P. D. Abramson and J. A. Spudich (1996). The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc Natl Acad Sci U S A 93: 4459-64.

Veigel, C., L. M. Coluccio, J. D. Jontes, J. C. Sparrow, R. A. Milligan and J. E. Molloy (1999). The motor protein myosin-I produces its working stroke in two steps. Nature 398: 530-3.

Veigel, C., J. E. Molloy, S. Schmitz and J. Kendrick-Jones (2003). Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers. Nat Cell Biol 5: 980-6.

Warshaw, D. M., W. H. Guilford, Y. Freyzon, E. Krementsova, K. A. Palmiter, M. J. Tyska, J. E. Baker and K. M. Trybus (2000). The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever. J Biol Chem 275: 37167-72.

Weiss, S., R. Rossi, M. A. Pellegrino, R. Bottinelli and M. A. Geeves (2001). Differing ADP release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers. J Biol Chem 276: 45902-8.

White, H. D., B. Belknap and M. R. Webb (1997). Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate. Biochemistry 36: 11828-36.

White, H. D. and E. W. Taylor (1976). Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15: 5818-26.

Whittaker, M., E. M. Wilson-Kubalek, J. E. Smith, L. Faust, R. A. Milligan and H. L. Sweeney (1995). A 35-A movement of smooth muscle myosin on ADP release. Nature 378: 748-51.

Woodward, S. K., J. F. Eccleston and M. A. Geeves (1991). Kinetics of the interaction of 2'(3')-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: characterization of two acto-S1-ADP complexes. Biochemistry 30: 422-30.

Zeng, W., P. B. Conibear, J. Dickens, R. Cowie, S. Wakelin, A. Malnasi-Csizmadia and C. Bagshaw (2004). Dynamics of actomyosin interactions in relation to the crossbridge cycle. Phil. Trans. R. Soc. B 359: 1843-1855.