Results 261 to 270 of about 181,791 (317)
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Nature of Myosin

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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Unconventional myosins

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

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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Aggregation of myosin A

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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Myosin XVIII

2020
Class XVIII myosins represent a branch of the myosin family tree characterized by the presence of large N- and C-terminal extensions flanking a generic myosin core. These myosins display the highest sequence similarity to conventional class II muscle myosins and are compatible with but not restricted to myosin-2 contractile structures.
Manuel H, Taft, Sharissa L, Latham
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Succinylation of myosin

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.
H, Oppenheimer   +3 more
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Myosin Structures

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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Myosins in Cytokinesis

2020
Nearly five decades of research have established myosin as the main motor responsible for cytokinesis in organisms on the branch of the phylogenetic tree that includes amoebas, fungi and animals. This research has grown to be more mechanistic over the past decade, so we now have computer simulations of physically reasonable models that explain how ...
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Myosins in the Nucleus

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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Axonal myosins

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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