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.