How molecular motors work
暂无分享,去创建一个
[1] W. Kabsch,et al. A comparison of the atomic model of F-actin with cryo-electron micrographs of actin and decorated actin. , 1993, Advances in experimental medicine and biology.
[2] E. Taylor,et al. Kinetic mechanism of myofibril ATPase. , 1994, Biophysical journal.
[3] K. Johnson,et al. Pre-steady-state kinetics of the microtubule-kinesin ATPase. , 1994, Biochemistry.
[4] R. Vallee,et al. Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein , 1988, Nature.
[5] Michael P. Sheetz,et al. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility , 1985, Cell.
[6] M. Riley,et al. Phylogenetic analysis of the myosin superfamily. , 1993, Cell motility and the cytoskeleton.
[7] H. Higuchi,et al. Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres , 1991, Nature.
[8] Toshio Yanagida,et al. Force measurements by micromanipulation of a single actin filament by glass needles , 1988, Nature.
[9] L. Goldstein,et al. Identification of the gene for fly non‐muscle myosin heavy chain: Drosophila myosin heavy chains are encoded by a gene family. , 1989, The EMBO journal.
[10] T. Yanagida,et al. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. , 1990, Journal of molecular biology.
[11] J. Spudich,et al. Fluorescent actin filaments move on myosin fixed to a glass surface. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[12] W. Kabsch,et al. Atomic structure of the actin: DNase I complex , 1990, Nature.
[13] E. Taylor,et al. A kinetic study of the kinesin ATPase. , 1992, The Journal of biological chemistry.
[14] R. Vale. Microtubule motors: many new models off the assembly line. , 1992, Trends in biochemical sciences.
[15] Ivan Rayment,et al. Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1 , 1993, Nature.
[16] J. Spudich,et al. Single myosin molecule mechanics: piconewton forces and nanometre steps , 1994, Nature.
[17] S. Kawamoto,et al. Evidence for inserted sequences in the head region of nonmuscle myosin specific to the nervous system. Cloning of the cDNA encoding the myosin heavy chain-B isoform of vertebrate nonmuscle myosin. , 1992, The Journal of biological chemistry.
[18] Toshio Yanagida,et al. Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle , 1985, Nature.
[19] J. Spudich,et al. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin , 1994, Nature.
[20] Force generation in muscle. , 1990, Current opinion in cell biology.
[21] Stephen J Kron,et al. Quantized velocities at low myosin densities in an in vitro motility , 1991, Nature.
[22] I. Mabuchi,et al. The effect of myosin antibody on the division of starfish blastomeres , 1977, The Journal of cell biology.
[23] A. Huxley,et al. Proposed Mechanism of Force Generation in Striated Muscle , 1971, Nature.
[24] L. Goldstein,et al. With apologies to scheherazade: tails of 1001 kinesin motors. , 1993, Annual review of genetics.
[25] D. Hackney. The rate-limiting step in microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains occurs while bound to the microtubule. , 1994, The Journal of biological chemistry.
[26] A. Huxley. Muscular contraction. Review lecture , 1974 .
[27] D. Trentham,et al. Relationships between chemical and mechanical events during muscular contraction. , 1986, Annual review of biophysics and biophysical chemistry.
[28] Huxley He. The fine structure of striated muscle and its functional significance. , 1966 .
[29] R. Adelstein,et al. An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. , 1993, The Journal of biological chemistry.
[30] J. Spudich,et al. In pursuit of myosin function. , 1989, Cell regulation.
[31] J. Spudich,et al. Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin. , 1990, Journal of molecular biology.
[32] E. Taylor,et al. Mechanism of adenosine triphosphate hydrolysis by actomyosin. , 1971, Biochemistry.
[33] T. Yanagida,et al. Single-molecule analysis of the actomyosin motor using nano-manipulation. , 1994, Biochemical and biophysical research communications.
[34] Michael P. Sheetz,et al. Movement of myosin-coated beads on oriented filaments reconstituted from purified actin , 1985, Nature.
[35] James A. Spudich,et al. Myosin subfragment-1 is sufficient to move actin filaments in vitro , 1987, Nature.
[36] D A Knecht,et al. Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. , 1987, Science.
[37] J. Spudich,et al. Myosin structure and function in cell motility. , 1987, Annual review of cell biology.
[38] J. Spudich,et al. Molecular evolution of the myosin family: relationships derived from comparisons of amino acid sequences. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[39] Christoph F. Schmidt,et al. Direct observation of kinesin stepping by optical trapping interferometry , 1993, Nature.
[40] T. Yanagida,et al. Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap. , 1994, Biophysical journal.
[41] T. Yanagida,et al. Force-generating domain of myosin motor. , 1993, Biochemical and biophysical research communications.
[42] R. F. Siemankowski,et al. Kinetics of the interaction between actin, ADP, and cardiac myosin-S1. , 1984, The Journal of biological chemistry.
[43] J. Spudich,et al. The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[44] J. Spudich,et al. A functional recombinant myosin II lacking a regulatory light chain-binding site. , 1993, Science.
[45] W. Kabsch,et al. Atomic model of the actin filament , 1990, Nature.
[46] H E Huxley,et al. The Mechanism of Muscular Contraction , 1965, Scientific American.
[47] I. Schlichting,et al. Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution , 1994, Nature.
[48] E. Taylor,et al. Mechanism of actomyosin ATPase and the problem of muscle contraction. , 1979, CRC critical reviews in biochemistry.
[49] J. Spudich,et al. Movement of myosin-coated fluorescent beads on actin cables in vitro , 1983, Nature.
[50] R A Milligan,et al. Structure of the actin-myosin complex and its implications for muscle contraction. , 1993, Science.
[51] D A Winkelmann,et al. Three-dimensional structure of myosin subfragment-1: a molecular motor. , 1993, Science.
[52] J. Spudich,et al. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. , 1987, Science.
[53] J. Spudich,et al. Role of highly conserved lysine 130 of myosin motor domain. In vivo and in vitro characterization of site specifically mutated myosin. , 1994, The Journal of biological chemistry.
[54] K. Trybus,et al. Skeletal muscle myosin light chains are essential for physiological speeds of shortening , 1993, Nature.
[55] G. Piazzesi,et al. Myosin head movements are synchronous with the elementary force-generating process in muscle , 1992, Nature.
[56] M. Bárány,et al. ATPase Activity of Myosin Correlated with Speed of Muscle Shortening , 1967, The Journal of general physiology.