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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
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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
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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.
H, NODA, S, 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.
H, NODA, S, EBASHI
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Journal of Neurocytology, 2000
The myosin super family is an extended family of actin-based motor proteins that can be divided into 15-18 structurally distinct classes (Sellers, J. R (2000) Biochemica et Biophysica Acta, 1496, 3-22; Hodge, T. & Cope, M. J. T. V. (2000) Journal of Cell Science, 113, 3353-3354; Berg, J. S., Powell, B. C. & Cheney, R. E. (2001) Molecular Biology of the
P C, Bridgman, L L, Elkin
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The myosin super family is an extended family of actin-based motor proteins that can be divided into 15-18 structurally distinct classes (Sellers, J. R (2000) Biochemica et Biophysica Acta, 1496, 3-22; Hodge, T. & Cope, M. J. T. V. (2000) Journal of Cell Science, 113, 3353-3354; Berg, J. S., Powell, B. C. & Cheney, R. E. (2001) Molecular Biology of the
P C, Bridgman, L L, Elkin
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2020
Although originally characterized as a cytoplasmic protein, myosin of various classes also performs key functions in the nucleus. We review the data concerning the nuclear localization, mechanism of entry, and functional interactions of myosin I, II, V, VI, X, XVI, and XVIII.
Ivan V, Maly, Wilma A, Hofmann
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Although originally characterized as a cytoplasmic protein, myosin of various classes also performs key functions in the nucleus. We review the data concerning the nuclear localization, mechanism of entry, and functional interactions of myosin I, II, V, VI, X, XVI, and XVIII.
Ivan V, Maly, Wilma A, Hofmann
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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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Nature, 1947
WE have been led to regard myosin as a rather involved system of substances, in spite of the fact that it readily crystallizes and behaves as a homogeneous substance on recrystallization. It consists of a skeleton to which are adsorbed a number of protein like substances. The skeleton, and also the adsorbed proteins, are, in themselves, inactive, their
I, BANGA, F, GUBA, A, SZENT-GYORGYI
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WE have been led to regard myosin as a rather involved system of substances, in spite of the fact that it readily crystallizes and behaves as a homogeneous substance on recrystallization. It consists of a skeleton to which are adsorbed a number of protein like substances. The skeleton, and also the adsorbed proteins, are, in themselves, inactive, their
I, BANGA, F, GUBA, A, SZENT-GYORGYI
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Essays in Biochemistry, 2000
Myosins constitute a large superfamily of F-actin-based motor proteins found in many organisms from yeast to humans. A phylogenetic comparison of their head sequences has allowed them to be grouped into 15 different classes. Unconventional myosins can be monomeric or dimeric, but are thought not to form filaments, unlike conventional myosin. The double-
G, Kalhammer, M, Bähler
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Myosins constitute a large superfamily of F-actin-based motor proteins found in many organisms from yeast to humans. A phylogenetic comparison of their head sequences has allowed them to be grouped into 15 different classes. Unconventional myosins can be monomeric or dimeric, but are thought not to form filaments, unlike conventional myosin. The double-
G, Kalhammer, M, Bähler
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Trends in Cell Biology, 1991
The traditional view of myosin, drawn from studies of myosins from striated muscles, is that of an elongated two-headed molecule that assembles into filaments. However, biochemical, molecular genetic and genetic studies have uncovered a host of ubiquitous single-headed nonfilamentous myosins known collectively as myosins I. All of the myosins I possess
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The traditional view of myosin, drawn from studies of myosins from striated muscles, is that of an elongated two-headed molecule that assembles into filaments. However, biochemical, molecular genetic and genetic studies have uncovered a host of ubiquitous single-headed nonfilamentous myosins known collectively as myosins I. All of the myosins I possess
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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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