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Mechanisms of mitral valve development and disease. [PDF]
Front Cardiovasc MedWang E, Zhou B.
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Editorial: Hypertrophic Cardiomyopathy and Precision Medicine in Cardiovascular Disease. [PDF]
Med Sci MonitParums DV.
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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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Myosin II independent contraction of actin filaments in membrane nanotubes
Ashraf MA +5 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
John A Hammer
exaly +3 more sources
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
John A Hammer
exaly +3 more sources
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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Current Opinion in Cell 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
exaly +4 more sources
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
exaly +4 more sources
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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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
openaire +2 more sources