Results 221 to 230 of about 12,173 (260)
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American Journal of Physiology-Cell Physiology, 1997
The class I myosins are single-headed, actin-binding, mechanochemical “motor” proteins with heavy chains in the molecular mass range of 110-130 kDa; they do not form filaments. Each myosin I heavy chain is associated with one to six light chains that bind to specific motifs known as IQ domains.
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The class I myosins are single-headed, actin-binding, mechanochemical “motor” proteins with heavy chains in the molecular mass range of 110-130 kDa; they do not form filaments. Each myosin I heavy chain is associated with one to six light chains that bind to specific motifs known as IQ domains.
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Journal of Molecular Biology, 1971
Abstract Myosin and its helical subfragments form bipolar “segment” aggregates which may be related to the bare zone of the thick filament. Two distinct modes of aggregation have now been observed: one with an overlap of 1300 A and another with an overlap of about 900 A. Both are consistent with a value of 1450 A for the length of the rod.
R G, Harrison, S, Lowey, C, Cohen
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Abstract Myosin and its helical subfragments form bipolar “segment” aggregates which may be related to the bare zone of the thick filament. Two distinct modes of aggregation have now been observed: one with an overlap of 1300 A and another with an overlap of about 900 A. Both are consistent with a value of 1450 A for the length of the rod.
R G, Harrison, S, Lowey, C, Cohen
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2012
Myosin X (Myo10), an actin-based molecular motor, induces filopodia formation and controls cell migration in vitro. In the 25 years since Myo10 was first identified, it has been implicated in several different functions in different cell types including phagocytosis in macrophages, axon outgrowth in neurons, cell-cell adhesion in epithelial and ...
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Myosin X (Myo10), an actin-based molecular motor, induces filopodia formation and controls cell migration in vitro. In the 25 years since Myo10 was first identified, it has been implicated in several different functions in different cell types including phagocytosis in macrophages, axon outgrowth in neurons, cell-cell adhesion in epithelial and ...
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2020
Hearing loss is both genetically and clinically heterogeneous, and pathogenic variants of over a hundred different genes are associated with this common neurosensory disorder. A relatively large number of these "deafness genes" encode myosin super family members.
Thomas B, Friedman +2 more
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Hearing loss is both genetically and clinically heterogeneous, and pathogenic variants of over a hundred different genes are associated with this common neurosensory disorder. A relatively large number of these "deafness genes" encode myosin super family members.
Thomas B, Friedman +2 more
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Myosin and myosin phosphorylation in pheochromocytoma (PC12) cells
Biochimica et Biophysica Acta (BBA) - General Subjects, 1984Myosin was isolated from extracts of a clonal cell line of pheochromocytoma (PC12) cells by ammonium sulfate fractionation and gel filtration. This myosin consisted of heavy chains and two light chains (20 and 17 kDa). The 20 kDa light chain could be phosphorylated by a protein kinase which was also present in the extracts and which eluted after myosin
D F, Englert, R L, Perlman
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Rigidity of myosin and myosin rod by electric birefringence
Biopolymers, 1984AbstractThe rotational relaxation times of rabbit myosin and myosin rod have been determined by electric birefringence measurement. The relaxation time of myosin measured in 10 mM pyrophosphate buffers in a pH range of 7.6–9.5 was found to have substantial concentration and pH dependences.
S, Hvidt, T, Chang, H, Yu
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Current Opinion in Cell Biology, 1997
It has been a banner year for the study of yeast myosins. Thanks to the completion of the Saccharomyces cerevisiae genome project, it is now known that budding yeast contains a total of five myosins. Furthermore, functions have been newly ascribed to several of them: two have been implicated in endocytosis, and another has been implicated in generating
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It has been a banner year for the study of yeast myosins. Thanks to the completion of the Saccharomyces cerevisiae genome project, it is now known that budding yeast contains a total of five myosins. Furthermore, functions have been newly ascribed to several of them: two have been implicated in endocytosis, and another has been implicated in generating
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Cooperativity and Regulation of Scallop Myosin and Myosin Fragments
Biochemistry, 1997Scallop heavy meromyosin (HMM) preparation obtained by a new improved method showed a Mg-ATPase activity that was activated 15-fold by calcium. The ATPase activity depended on ionic strength and reached maximum at 0.1 M without altering calcium sensitivity.
V N, Kalabokis, A G, Szent-Györgyi
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2007
Myosin II, the myosin which has provided the most biochemical and structural data, is dimeric consisting of a long coiled-coil region with the motor domain flexibly attached to the N-terminal end of the coiled-coil. The motor domain (subfragment 1, S1, or cross-bridge) is obtained by proteolytic cleavage of myosin.
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Myosin II, the myosin which has provided the most biochemical and structural data, is dimeric consisting of a long coiled-coil region with the motor domain flexibly attached to the N-terminal end of the coiled-coil. The motor domain (subfragment 1, S1, or cross-bridge) is obtained by proteolytic cleavage of myosin.
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2020
Myosins constitute a superfamily of actin-based molecular motor proteins that mediates a variety of cellular activities including muscle contraction, cell migration, intracellular transport, the formation of membrane projections, cell adhesion, and cell signaling. The 12 myosin classes that are expressed in humans share sequence similarities especially
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Myosins constitute a superfamily of actin-based molecular motor proteins that mediates a variety of cellular activities including muscle contraction, cell migration, intracellular transport, the formation of membrane projections, cell adhesion, and cell signaling. The 12 myosin classes that are expressed in humans share sequence similarities especially
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