Results 291 to 300 of about 159,767 (320)
Some of the next articles are maybe not open access.
2020
Directed movements on actin filaments within the cell are powered by molecular motors of the myosin superfamily. On actin filaments, myosin motors convert the energy from ATP into force and movement. Myosin motors power such diverse cellular functions as cytokinesis, membrane trafficking, organelle movements, and cellular migration.
Sweeney, H Lee +3 more
openaire +2 more sources
Directed movements on actin filaments within the cell are powered by molecular motors of the myosin superfamily. On actin filaments, myosin motors convert the energy from ATP into force and movement. Myosin motors power such diverse cellular functions as cytokinesis, membrane trafficking, organelle movements, and cellular migration.
Sweeney, H Lee +3 more
openaire +2 more sources
Regulation of myosin 5a and myosin 7a
Biochemical Society Transactions, 2011The myosin superfamily is diverse in its structure, kinetic mechanisms and cellular function. The enzymatic activities of most myosins are regulated by some means such as Ca2+ ion binding, phosphorylation or binding of other proteins. In the present review, we discuss the structural basis for the regulation of mammalian myosin 5a and Drosophila myosin ...
James R. Sellers, Verl Siththanandan
openaire +3 more sources
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
openaire +3 more sources
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
openaire +3 more sources
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.
openaire +2 more sources
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.
openaire +2 more sources
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
openaire +3 more sources
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
openaire +3 more sources
Rigidity of myosin and myosin rod by electric birefringence [PDF]
Biopolymers, 1984 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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +3 more sources
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
openaire +3 more sources
Myosine and Adenosinetriphosphatase [PDF]
Nature, 1939 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
openaire +1 more source
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.
openaire +2 more sources
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.
openaire +2 more sources