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Regularity and Synchrony in Motor Proteins
Bulletin of Mathematical Biology, 2007We investigate the origin of the regularity and synchrony which have been observed in numerical experiments of two realistic models of molecular motors, namely Fisher-Kolomeisky's model of myosin V for vesicle transport in cells and Duke's model of myosin II for sarcomere shortening in muscle contraction.
R. E. Lee DeVille, Eric Vanden-Eijnden
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Motor proteins in cell division
Trends in Cell Biology, 1991The movements of eukaryotic cell division depend upon the conversion of chemical energy into mechanical work, which in turn involves the actions of motor proteins, molecular transducers that generate force and motion relative cytoskeletal elements. In animal cells, microtubule-based motor proteins of the mitotic apparatus are involved in segregating ...
Kenneth E. Sawin, Jonathan M. Scholey
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Mechanisms of motor protein reversal
Current Opinion in Cell Biology, 2001Members of the kinesin superfamily of microtubule-based motors and the myosin superfamily of actin-based motors that move 'backwards' have been identified. As the core catalytic domains of myosins and kinesins are similar in structure, this raises the intriguing questions of how direction reversal is accomplished and whether kinesins and myosins share ...
Richard E. Cheney, Tama Hasson
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Motor proteins for cytoplasmic microtubules
Current Opinion in Cell Biology, 1992It has been thought that motile structures within the cell are driven toward the plus and minus ends of microtubules by the ATPases, kinesin and dynein, respectively. Recently obtained data indicate that this model is far too simplistic. Kinesin is now understood to be one representative of a family of proteins. Another member of the kinesin family has
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2007
The cell skeleton forms a scaffold, along which motor proteins can move. These proteins convert the chemical energy of ATP-hydrolysis into mechanical energy. Movement is unidirectional, either from minus to plus or vice versa. The most important systems are microfilament /myosin and microtubule /kinesin and -dynamin .
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The cell skeleton forms a scaffold, along which motor proteins can move. These proteins convert the chemical energy of ATP-hydrolysis into mechanical energy. Movement is unidirectional, either from minus to plus or vice versa. The most important systems are microfilament /myosin and microtubule /kinesin and -dynamin .
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Mutational Analysis of Motor Proteins
Annual Review of Physiology, 1996Mutations in motor proteins, which can arise by design or randomly, provide powerful insights into the normal function of the protein. This review organizes the available data on mutations of members of the myosin, kinesin, and dynein superfamilies of motor proteins.
H. L. Sweeney, E. L. F. Holzbaur
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The structure of microtubule motor proteins
2005Microtubules are the intracellular tracks for two classes of motor proteins: kinesins and dyneins. During the past few years, the motor domain structures of several kinesins from different organisms have been determined by X-ray crystallography. Compared with kinesins, dyneins are much larger proteins and attempts to crystallize them have failed so far.
E. Mandelkow, Jens Müller, A. Marx
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Association of motor proteins with membranes
Current Opinion in Cell Biology, 1991The motility of intracellular components, and of the cell as a whole, is mediated by cytoplasmic motor proteins. This review discusses what is known about the binding of cytoplasmic motors to membranes. Mechanisms by which these interactions may result in observed motile phenomena are proposed.
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Regulation of molecular motor proteins
2001Motor proteins in the kinesin, dynein, and myosin superfamilies are tightly regulated to perform multiple functions in the cell requiring force generation. Although motor proteins within families are diverse in sequence and structure, there are general mechanisms by which they are regulated.
Amy Reilein +6 more
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Coupling between motor proteins determines dynamic behaviors of motor protein assemblies
Physical Chemistry Chemical Physics, 2010Transport of intracellular cargos by multiple microtubule motor proteins is believed to be a common and significant phenomenon in vivo, yet signatures of the microscopic dynamics of multiple motor systems are only now beginning to be resolved. Understanding these mechanisms largely depends on determining how grouping motors affect their association ...
Rahul K. Das +5 more
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