Results 271 to 280 of about 196,791 (307)
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Rigidity of myosin and myosin rod by electric birefringence
Biopolymers, 1984AbstractThe rotational relaxation times of rabbit myosin and myosin rod have been determined by electric birefringence measurement. The relaxation time of myosin measured in 10 mM pyrophosphate buffers in a pH range of 7.6–9.5 was found to have substantial concentration and pH dependences.
S, Hvidt, T, Chang, H, Yu
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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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Journal of Muscle Research & Cell Motility, 1999
The discovery in the past few years of a huge diversity within the myosin superfamily has been coupled with an understanding of the role of these motor proteins in various cellular functions. Extensive studies have revealed that myosin isoforms are not only involved in muscle contraction but also in crucial functions of many specialized mammalian cells
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The discovery in the past few years of a huge diversity within the myosin superfamily has been coupled with an understanding of the role of these motor proteins in various cellular functions. Extensive studies have revealed that myosin isoforms are not only involved in muscle contraction but also in crucial functions of many specialized mammalian cells
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2001
This review focuses on selected papers that illustrate an historical perspective and the current knowledge of myosin structure and function in protists. The review contains a general description of myosin structure, a phylogenetic tree of the myosin classes, and descriptions of myosin isoforms identified in protists. Each myosin is discussed within the
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This review focuses on selected papers that illustrate an historical perspective and the current knowledge of myosin structure and function in protists. The review contains a general description of myosin structure, a phylogenetic tree of the myosin classes, and descriptions of myosin isoforms identified in protists. Each myosin is discussed within the
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Myosin VI assists in fork protection
Nature Reviews Molecular Cell Biology, 2023Paulina Strzyz
exaly
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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