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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 ...
T, Hasson, R E, Cheney
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2007
Motor proteins are molecular machines that convert the chemical energy derived from the hydrolysis of ATP into mechanical work used to power cellular motility. In addition to specialized motile cells like muscle fibers and cellular processes like cilia, all eukaryotic cells contain motor proteins (Fig. 1).
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Motor proteins are molecular machines that convert the chemical energy derived from the hydrolysis of ATP into mechanical work used to power cellular motility. In addition to specialized motile cells like muscle fibers and cellular processes like cilia, all eukaryotic cells contain motor proteins (Fig. 1).
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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, Holzbaur
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Chromatin folding through nonuniform motorization by responsive motor proteins
The Journal of Chemical PhysicsChromatin is partially structured through the effects of biological motors. “Swimming motors” such as RNA polymerases and chromatin remodelers are thought to act differentially on the active parts of the genome and the stored inactive part. By systematically expanding the many-body master equation for chromosomes driven by swimming motors, we show that
Zhiyu Cao, Peter G. Wolynes
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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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Non-motor microtubule-associated proteins
Current Opinion in Cell Biology, 1993This past year, the structure and function of microtubule-associated proteins (MAPs) have been investigated in studies probing their phosphorylation, patterns of expression, and the function of the microtubule-binding domain. Cellular studies have also contributed new insights into the roles of these proteins in process outgrowth.
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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.
A R, Reilein +3 more
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Mechanics of Motor Proteins and the Cytoskeleton
, 2001J. Howard, R. Clark
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Non-motor microtubule-associated proteins
Current Opinion in Cell Biology, 1991Cloning of primary sequences has generated information on the structures of the non-motor microtubule-associated proteins and their relationship to one another. Questions about how classes of microtubule-associated proteins interact are starting to be addressed in vitro and, in vivo, tests of function are being pursued using a variety of cellular and ...
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