Results 211 to 220 of about 20,285 (238)
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Archives of Biochemistry and Biophysics, 1967
Abstract The reaction of succinic anhydride with the free amino groups of myosin introduced a high negative charge density and thus greatly altered the properties of this protein. Succinylated myosin was water-soluble and remained so even after prolonged heating.
K. Bárány+3 more
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Abstract The reaction of succinic anhydride with the free amino groups of myosin introduced a high negative charge density and thus greatly altered the properties of this protein. Succinylated myosin was water-soluble and remained so even after prolonged heating.
K. Bárány+3 more
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Current Opinion in Cell Biology, 1993
The number and variety of myosins that have been identified has increased greatly over the past few years, and is still growing. Myosins have been classified into at least six distinct classes. Research during the last year has concentrated on identifying the roles of various myosins.
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The number and variety of myosins that have been identified has increased greatly over the past few years, and is still growing. Myosins have been classified into at least six distinct classes. Research during the last year has concentrated on identifying the roles of various myosins.
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Biochimica et Biophysica Acta, 1960
Abstract Myosin A molecules aggregate and form polymers of about 1 μ in length, when the ionic strength of pH of their solution is lowered. In 0.2 M KCl, myosin A is fulully dissociated at pH 7.3 and higher, but fully polymerized at pH 6.5 and lower.
Haruhiko Noda, Setsuro Ebashi
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Abstract Myosin A molecules aggregate and form polymers of about 1 μ in length, when the ionic strength of pH of their solution is lowered. In 0.2 M KCl, myosin A is fulully dissociated at pH 7.3 and higher, but fully polymerized at pH 6.5 and lower.
Haruhiko Noda, Setsuro Ebashi
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Rigidity of myosin and myosin rod by electric birefringence [PDF]
AbstractThe 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.
Søren Hvidt, Hyuk Yu, Taihyun Chang
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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.
Richard J. Harrison+2 more
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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.
Richard J. Harrison+2 more
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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.
Inna A. Belyantseva+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.
Inna A. Belyantseva+2 more
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Myosine and Adenosinetriphosphatase [PDF]
ORDINARY aqueous or potassium chloride extracts of muscle exhibit but a slight capacity to mineralize adenosinetriphosphate. Even this slight liberation of phosphate is mainly due, not to direct hydrolysis of adenosinetriphosphate, but to a process of secondary, indirect mineralization, accompanying the transfer of phosphate from the adenylic system to
M. N. Ljubimowa, W. A. Engelhardt
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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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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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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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