Results 161 to 170 of about 4,251 (182)
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Cytoplasmic dynein in neurodegeneration
Pharmacology & Therapeutics, 2011Cytoplasmic dynein 1 (later referred to as dynein) is the major molecular motor moving cargoes such as mitochondria, organelles and proteins towards the minus end of microtubules. Dynein is involved in multiple basic cellular functions, such as mitosis, autophagy and structure of endoplasmic reticulum and Golgi, but also in neuron specific functions in
Judith, Eschbach, Luc, Dupuis
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Dynein‐like Cytoplasmic Microtubule Translocatorsa
Annals of the New York Academy of Sciences, 1986The eukaryotic flagellum presents an excellent predictive model of microtubule-mediated motility: movement is caused by microtubule translocators, called dyneins, which actively slide outer doublet microtubules against each other. Cytoplasmic movements, such as certain aspects of mitotic motion, may also be powered by dynein-like molecules.
D J, Asai, R J, Leslie, L, Wilson
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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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Cytoplasmic dynein binds to phospholipid vesicles
Cell Motility, 1994AbstractCytoplasmic dynein is the putative motor protein for retrograde organelle transport along microtubules in cells and, thus, must be capable of binding to organelle membranes. Such an attachment may occur via receptor proteins or through a direct interaction of dynein with the membrane phospholipids.
M L, Lacey, L T, Haimo
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Multiple modes of cytoplasmic dynein regulation
Nature Cell Biology, 2012In performing its multiple cellular functions, the cytoplasmic dynein motor is subject to complex regulation involving allosteric mechanisms within the dynein complex, as well as numerous extramolecular interactions controlling subcellular targeting and motor activity.
Richard B, Vallee +2 more
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1999
Abstract Cytoplasmic dynein is a large, two-headed ATPase which produces force along microtubules in the retrograde direction (toward the microtubufe minus end). It is involved in a wide range of functions, including retrograde axonal transport and mitosis, and it associates with numerous subcellular structures, including kinetochores ...
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Abstract Cytoplasmic dynein is a large, two-headed ATPase which produces force along microtubules in the retrograde direction (toward the microtubufe minus end). It is involved in a wide range of functions, including retrograde axonal transport and mitosis, and it associates with numerous subcellular structures, including kinetochores ...
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Substructure of sea urchin egg cytoplasmic dynein
Journal of Molecular Biology, 1987The substructure of the cytoplasmic dynein molecule was studied using the quick-freeze, deep-etch technique. Cytoplasmic dynein purified as a 12 S form from the eggs of the sea urchin Hemicentrotus pulcherrimus was composed of a single high molecular weight polypeptide.
S, Hisanaga, N, Hirokawa
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Axonal transport: beyond kinesin and cytoplasmic dynein
Current Opinion in Neurobiology, 1991In vitro and in vivo studies of specific neuronal fast and slow transport components are presently reshaping our understanding of how the processes of vesicular and cytoskeletal transport are regulated in axons and dendrites. Evidence suggests that vesicles possess an inherent directionality, possibly the result of their motor receptor proteins ...
M P, Sheetz, C H, Martenson
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An improved purification method for cytoplasmic dynein
Journal of Cellular Biochemistry, 1984AbstractAn improved method has been devised for the purification of cytoplasmic dynein from sea urchin eggs (Strongylocentrotus droebachiensis and S purpuratus). This protocol introduces three changes over a previously published procedure (Hisanaga and Sakai: J Biochem 93:87, 1983)—the substitution of diethylaminoethyl (DEAE)‐cellulose for ...
M M, Pratt, S, Hisanaga, D A, Begg
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Structural biology of cytoplasmic and axonemal dyneins
Journal of Structural Biology, 2012Dyneins are microtubule-based, ATP-driven motor proteins with six tandemly linked AAA+ domains, a long N-terminal tail and a coiled-coil stalk. Cytoplasmic dyneins function as individual homodimers and are responsible for minus-end-oriented transport along microtubules. Axonemal dyneins of flagella/cilia are anchored in arrays to peripheral microtubule
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