Results 211 to 220 of about 12,173 (260)
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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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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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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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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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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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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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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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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
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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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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