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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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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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2020
Myosin XVI (Myo16), a vertebrate-specific motor protein, is a recently discovered member of the myosin superfamily. The detailed functionality regarding myosin XVI requires elucidating or clarification; however, it appears to portray an important role in neural development and in the proper functioning of the nervous system.
Beáta, Bugyi, András, Kengyel
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Myosin XVI (Myo16), a vertebrate-specific motor protein, is a recently discovered member of the myosin superfamily. The detailed functionality regarding myosin XVI requires elucidating or clarification; however, it appears to portray an important role in neural development and in the proper functioning of the nervous system.
Beáta, Bugyi, András, Kengyel
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2020
The birth of widely available genomic databases at the turn of the millennium led to the identification of many previously unknown myosin genes and identification of novel classes of myosin, including MYO19. Further sequence analysis has revealed the unique evolutionary history of class XIX myosins. MYO19 is found in species ranging from vertebrates to
Jennifer L, Bocanegra +2 more
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The birth of widely available genomic databases at the turn of the millennium led to the identification of many previously unknown myosin genes and identification of novel classes of myosin, including MYO19. Further sequence analysis has revealed the unique evolutionary history of class XIX myosins. MYO19 is found in species ranging from vertebrates to
Jennifer L, Bocanegra +2 more
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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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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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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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2007
Myosin II, the myosin which has provided the most biochemical and structural data, is dimeric consisting of a long coiled-coil region with the motor domain flexibly attached to the N-terminal end of the coiled-coil. The motor domain (subfragment 1, S1, or cross-bridge) is obtained by proteolytic cleavage of myosin.
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Myosin II, the myosin which has provided the most biochemical and structural data, is dimeric consisting of a long coiled-coil region with the motor domain flexibly attached to the N-terminal end of the coiled-coil. The motor domain (subfragment 1, S1, or cross-bridge) is obtained by proteolytic cleavage of myosin.
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