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Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet. [PDF]
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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.
George B Witman
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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.
George B Witman
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Axonemal dyneins: assembly, organization, and regulation
Current Opinion in Cell Biology, 1996Progress in the sequence determination of dynein subunits is providing new insights into the locations of functional domains in these microtubule motors. Combined structural and biochemical analyses of flagellar mutations are also yielding information on the three-dimensional organization of the dynein arms and on the different components that target ...
Mary E Porter
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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
Takashi Ishikawa
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Biochemical and Physiological Analysis of Axonemal Dyneins
Methods in Enzymology, 2013Axonemal dyneins are highly complex molecular motors that power the beating of cilia/flagella. In addition to the motor subunits, these enzymes contain components that allow for assembly at the correct axonemal location and also enable the motor to respond to a broad array of signals including phosphorylation, Ca(2+), redox changes, and mechanical ...
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Glycylation regulates axonemal dyneins
Science, 2021Cell Biology Physiological functions of the microtubule cytoskeleton are expected to be regulated by a variety of posttranslational tubulin modifications. For instance, tubulin glycylation is almost exclusively found in cilia and flagella, but its role in the function of these organelles remains unclear. Gadadhar et al.
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Axonemal dynein from Tetrahymena
Journal of Cell Science, 1991ABSTRACT Axonemal dynein from Tetrahymena cilia can be separated on a sucrose gradient into two fractions, at least one of which appears to be polymorphic. We have been using immuno-electron microscopy in order to try and locate the different types of dynein molecules within the axonemal structure.
E M, Crossley, S C, Hyman, C, Wells
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Biophysical Measurements on Axonemal Dyneins
2009In recent decades, the development of technologies such as optical trap nanometry and advanced fluorescence microscopy have provided tools for studying the dynamics of single protein molecules in vitro and in vivo with nanometer precision over timescales from milliseconds to seconds.
Hiroaki, Kojima +3 more
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