Results 201 to 210 of about 12,142 (258)
Myosin IXb is involved in multiple pathological conditions. [PDF]
PeerJDong S, Wang K, Yi FS, Hu Y, Zhang X.
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Structure and Functions of Actin and Actin-Binding Proteins in <i>Leishmania</i>. [PDF]
PathogensGupta CM, Thiyagarajan S.
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MYO1F interactome reveals the SH3-domain linked CASS complex at podosomes and the phagocytic cup
Arden SD +5 more
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Annual Review of Cell and Developmental Biology, 1992
Myosins are molecular motors that upon interaction with actin filaments convert energy from ATP hydrolysis into mechanical force. Evidence has emerged for the existence of a large, widely expressed and evolutionarily ancient superfamily of myosin genes.
R E, Cheney, M S, Mooseker
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Myosins are molecular motors that upon interaction with actin filaments convert energy from ATP hydrolysis into mechanical force. Evidence has emerged for the existence of a large, widely expressed and evolutionarily ancient superfamily of myosin genes.
R E, Cheney, M S, Mooseker
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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 ...
Verl B, Siththanandan, James R, Sellers
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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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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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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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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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