Results 151 to 160 of about 7,885 (177)
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Cytoplasmic dynein/dynactin mediates the assembly of aggresomes
Cell Motility, 2002AbstractAggresomes are pericentrosomal cytoplasmic structures into which aggregated, ubiquitinated, misfolded proteins are sequestered. Misfolded proteins accumulate in aggresomes when the capacity of the intracellular protein degradation machinery is exceeded.
Jennifer A, Johnston +2 more
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1999
Abstract The dynactin molecule as a unit appears to be unique, though it is structurally similar to the short actin filaments that comprise the erythrocyte membrane cytoskeleton. This has led to speculation that the dynactin Arp1 filament might bind membranes via a spectrin network.
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Abstract The dynactin molecule as a unit appears to be unique, though it is structurally similar to the short actin filaments that comprise the erythrocyte membrane cytoskeleton. This has led to speculation that the dynactin Arp1 filament might bind membranes via a spectrin network.
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Dynactin mutations and promises for neurodegenerative pathology
Clinical Genetics, 2009DCTN1 mutations in Perry syndromeFarrer et al.
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Dynein and dynactin as organizers of the system of cell microtubules
Russian Journal of Developmental Biology, 2006A review of the role of the microtubule motor dynein and its cofactor dynactin in the formation of a radial system of microtubules in the interphase cells and of mitotic spindle. Deciphering of the structure, functions, and regulation of activity of dynein and dynactin promoted the understanding of mechanisms of cell and tissue morphogenesis, since it ...
A V, Burakov, E S, Nadezhdina
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Dynactin increases the processivity of the cytoplasmic dynein motor
Nature Cell Biology, 1999Cytoplasmic dynein supports long-range intracellular movements of cargo in vivo but does not appear to be a processive motor protein by itself. We show here that the dynein activator, dynactin, binds microtubules and increases the average length of cytoplasmic-dynein-driven movements without affecting the velocity or microtubule-stimulated ATPase ...
S J, King, T A, Schroer
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Organelle Movement: Dynactin: portrait of a dynein regulator
Current Biology, 1994Recent studies of dynactin, a protein complex implicated in regulating the cytoplasmic motor protein dynein, reveal that the complex contains a specialized actin filament and may also interact with microtubules.
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Microsporidian Spore/Sporoplasm Dynactin in Spraguea
The Biological Bulletin, 2001440. 7. Brown, A., and R. J. Lasek. 1990. Pp. 235–302 in Squid as Experimental Animals. D. L. Gilbert, W. J. Adelman, Jr., and J. M. Arnold, eds., Plenum Press, New York. 8. Grant, P., D. Tseng, R. M. Gould, H. Gainer, and H. C. Pant. 1995. J. Comp. Neurol. 356: 311–326. 9. Tsai, M.-Y., G. Morfini, G. Szebenyi, and S. T. Brady. 2000. Mol. Biol. Cell 11:
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Assay and Properties of Rab6 Interaction with Dynein–Dynactin Complexes
2005RAB GTPases help to maintain the fidelity of membrane trafficking events by recruiting cytosolic tethering and motility factors to vesicle and organelle membranes. In the case of Rab6, it recruits the dynein-dynaction complex to Golgi-associated vesicles via an adaptor protein of the Bicaudal-D family. Here we describe methods for the identification of
Fuchs, E., Short, B., Barr, F.
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1998
Dynactin is a multi-subunit complex which was initially identified in 1991 as an activator of cytoplasmic dynein-driven microtubule-based organelle motility in vitro . Although genetic studies also supported the involvement of both complexes in the same functional pathways in yeast, filamentous fungi, and Drosophila , none of these findings yielded ...
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Dynactin is a multi-subunit complex which was initially identified in 1991 as an activator of cytoplasmic dynein-driven microtubule-based organelle motility in vitro . Although genetic studies also supported the involvement of both complexes in the same functional pathways in yeast, filamentous fungi, and Drosophila , none of these findings yielded ...
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