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DynAPs and cytoplasmic assembly of axonemal dyneins. [PDF]
J Cell SciWallingford JB +4 more
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Axonemal dynein contributions to flagellar beat types and waveforms
Fochler S +8 more
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Current Biology, 2023
Dyneins are a family of motor proteins that carry out motility and force generation functions towards the minus end of microtubule filaments. Cytoplasmic dynein (dynein-1) is responsible for transporting intracellular cargos in the retrograde direction in the cytoplasm, anchoring several organelles to the microtubule network, driving nuclear migration ...
Ahmet, Yildiz, Yuanchang, Zhao
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Dyneins are a family of motor proteins that carry out motility and force generation functions towards the minus end of microtubule filaments. Cytoplasmic dynein (dynein-1) is responsible for transporting intracellular cargos in the retrograde direction in the cytoplasm, anchoring several organelles to the microtubule network, driving nuclear migration ...
Ahmet, Yildiz, Yuanchang, Zhao
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Journal of Cell Science, 2023
ABSTRACT The microtubule minus-end-directed motility of cytoplasmic dynein 1 (dynein), arguably the most complex and versatile cytoskeletal motor, is harnessed for diverse functions, such as long-range organelle transport in neuronal axons and spindle assembly in dividing cells.
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ABSTRACT The microtubule minus-end-directed motility of cytoplasmic dynein 1 (dynein), arguably the most complex and versatile cytoskeletal motor, is harnessed for diverse functions, such as long-range organelle transport in neuronal axons and spindle assembly in dividing cells.
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Nature Structural & Molecular Biology, 2012
Dyneins are the largest of the cytoskeletal motor proteins, and their mechanochemical behavior is complex. Recent high-resolution crystallographic structures have revealed new surprises regarding motor domain organization and new insights into how force and movement are achieved.
Peter, Höök, Richard, Vallee
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Dyneins are the largest of the cytoskeletal motor proteins, and their mechanochemical behavior is complex. Recent high-resolution crystallographic structures have revealed new surprises regarding motor domain organization and new insights into how force and movement are achieved.
Peter, Höök, Richard, Vallee
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Current Opinion in Cell Biology, 2002
Cytoplasmic dynein is a minus end directed microtubule motor protein with numerous functions during interphase and mitosis. Recent evidence has identified several roles mediated by a fraction of cytoplasmic dynein associated with the cell cortex. So far, these include nuclear migration, mitotic spindle orientation, and cytoskeletal reorientation during
Denis L, Dujardin, Richard B, Vallee
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Cytoplasmic dynein is a minus end directed microtubule motor protein with numerous functions during interphase and mitosis. Recent evidence has identified several roles mediated by a fraction of cytoplasmic dynein associated with the cell cortex. So far, these include nuclear migration, mitotic spindle orientation, and cytoskeletal reorientation during
Denis L, Dujardin, Richard B, Vallee
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Biochemical Society Transactions, 2011
The organization and function of eukaryotic cells rely on the action of many different molecular motor proteins. Cytoplasmic dynein drives the movement of a wide range of cargoes towards the minus ends of microtubules, and these events are needed, not just at the single-cell level, but are vital for correct development.
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The organization and function of eukaryotic cells rely on the action of many different molecular motor proteins. Cytoplasmic dynein drives the movement of a wide range of cargoes towards the minus ends of microtubules, and these events are needed, not just at the single-cell level, but are vital for correct development.
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Current Opinion in Cell Biology, 1992
Recent advances in our understanding of the axonemal dyneins reveal them to be much more complex than previously believed. A combination of genetic, molecular genetic, ultrastructural and biochemical approaches is now aiding the elucidation of the organization and function of these important mechanochemical transducers.
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Recent advances in our understanding of the axonemal dyneins reveal them to be much more complex than previously believed. A combination of genetic, molecular genetic, ultrastructural and biochemical approaches is now aiding the elucidation of the organization and function of these important mechanochemical transducers.
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Journal of Cell Science, 1986
ABSTRACT The structure of dynein isolated from several sources follows the pattern first observed with Tetrahymena 22 S dynein, which has three globular heads attached by three flexible strands to a root-like base. Recent biochemical data indicate that there is one ATPase site on each dynein head and that all three heads interact with ...
K A, Johnson +4 more
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ABSTRACT The structure of dynein isolated from several sources follows the pattern first observed with Tetrahymena 22 S dynein, which has three globular heads attached by three flexible strands to a root-like base. Recent biochemical data indicate that there is one ATPase site on each dynein head and that all three heads interact with ...
K A, Johnson +4 more
openaire +2 more sources