Results 271 to 280 of about 43,287 (283)
Some of the next articles are maybe not open access.
Current Opinion in Structural Biology, 2004
Dyneins are the largest and most complex of the three classes of linear motor proteins in eukaryotic cells. The mass of the dynein motor domain is about ten times that of the other microtubule motor, kinesin. Dynein's homology with the AAA+ superfamily of mechanoenzymes distinguishes it from both kinesin and myosin, which share a common fold and ...
Stan A. Burgess, Peter J. Knight
openaire +3 more sources
Dyneins are the largest and most complex of the three classes of linear motor proteins in eukaryotic cells. The mass of the dynein motor domain is about ten times that of the other microtubule motor, kinesin. Dynein's homology with the AAA+ superfamily of mechanoenzymes distinguishes it from both kinesin and myosin, which share a common fold and ...
Stan A. Burgess, Peter J. Knight
openaire +3 more sources
Nature Cell Biology, 2008
Individual neurons form specific elaborate dendritic structures that receive presynaptic information. The pattern of dendritic branching is regulated by the microtubule-associated motor protein dynein, which is responsible for the transport of essential endosomes and other organelles into the dendrites.
openaire +3 more sources
Individual neurons form specific elaborate dendritic structures that receive presynaptic information. The pattern of dendritic branching is regulated by the microtubule-associated motor protein dynein, which is responsible for the transport of essential endosomes and other organelles into the dendrites.
openaire +3 more sources
Pathway of the Microtubule-Dynein ATPase and the Structure of Dynein: A Comparison with Actomyosin
Annual Review of Biophysics and Biomolecular Structure, 1985Dynein and myosin show several important similarities in design as well as some interesting differences in detail. Both ATPases function as crossbridges that undergo microscopic movements to drive the sliding of filaments, which results in macroscopic movements. They share a common design employing globular heads attached to flexible strands. Each head
openaire +2 more sources
Chapter 23 Preparation and Purification of Dynein
1982Publisher Summary This chapter describes the preparation, storage, use, and properties of dynein ATPase from sea urchin sperm flagella, which is probably one of the best available sources for providing relatively large quantities of this enzyme. Selective extraction and recombination followed by electron microscopy indicate that dynein comprises part
Winfield S. Sale +4 more
openaire +4 more sources
Purification of Axonemal Dyneins and Dynein-Associated Components from Chlamydomonas
2009Axonemal dyneins are responsible for generating the force required to power ciliary and flagellar motility. These highly complex enzymes form the inner and outer arms associated with the outer doublet microtubules. They are built around one or more ~520kD heavy chains that exhibit motor activity and also include additional components that are required ...
openaire +3 more sources
Kinesin and dynein superfamily proteins and the mechanism of organelle transport.
Science, 1998N. Hirokawa
semanticscholar +1 more source