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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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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 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
Luc Dupuis, Luc Dupuis, Judith Eschbach
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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 ...
Erika L. F. Holzbaur +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 ...
Erika L. F. Holzbaur +4 more
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Trends in Cell Biology, 1998
Three classes of cytoskeletal motor protein have been identified--myosins, kinesins and dyneins. Together, these proteins are now thought to be responsible for the remarkable variety of movements that occur in eukaryotic cells and that are essential for reproduction and survival.
Richard B. Vallee, Melissa Gee
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Three classes of cytoskeletal motor protein have been identified--myosins, kinesins and dyneins. Together, these proteins are now thought to be responsible for the remarkable variety of movements that occur in eukaryotic cells and that are essential for reproduction and survival.
Richard B. Vallee, Melissa Gee
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Cell Motility, 1995
Axonemal dyneins and cytoplasmic dynein have evolved separate strategies to perform their tasks. The multi-dynein hypothesis accurately describes the highly specialized axonemal isoforms; each isoform is encoded by a separate gene, is located in a precise place, produces specific forces which contribute to the overall generation of propagated bending ...
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Axonemal dyneins and cytoplasmic dynein have evolved separate strategies to perform their tasks. The multi-dynein hypothesis accurately describes the highly specialized axonemal isoforms; each isoform is encoded by a separate gene, is located in a precise place, produces specific forces which contribute to the overall generation of propagated bending ...
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Reconstitution of Dynein/Dynactin Transport Using Recombinant Dynein
2023Cytoplasmic dynein-1 is activated by dynactin and a cargo adaptor for processive transport along microtubules. Dynein's motility can be visualized at the single-molecule level using total internal reflection fluorescence microscopy. Our understanding of the motile behavior of the dynein/dynactin complex has been aided by advances in recombinant ...
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The molecular anatomy of dynein
Essays in Biochemistry, 2000Recent molecular, genetic and functional studies have led to an unparalleled growth in our understanding of dynein and the roles played by the various polypeptides of these massive macromolecular assemblies. Dyneins are highly complex 1-2MDa complexes that function as molecular motor and move the cargo to which they are attached towards the minus-end ...
Stephen M. King, Alistair Harrison
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2012
Dyneins: Ancient Protein Complexes Gradually Reveal Their Secrets, L. A. Amos and K. Hirose Two Decades of Cytoplasmic Dynein: From Fast to Forceful, R. J. McKenney and R. B. Vallee Functional Analysis of the Dynein Motor Domain, T. Shima, K. Sutoh, and T. Kon Structural Studies on the Dynein Heavy Chain, A. J. Roberts and S. A.
Linda A. Amos, Keiko Hirose
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Dyneins: Ancient Protein Complexes Gradually Reveal Their Secrets, L. A. Amos and K. Hirose Two Decades of Cytoplasmic Dynein: From Fast to Forceful, R. J. McKenney and R. B. Vallee Functional Analysis of the Dynein Motor Domain, T. Shima, K. Sutoh, and T. Kon Structural Studies on the Dynein Heavy Chain, A. J. Roberts and S. A.
Linda A. Amos, Keiko Hirose
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Structural comparison of purified dynein proteins with in situ dynein arms
Journal of Molecular Biology, 1984Using the quick-freeze deep-etch technique, we describe the structure of outerarm dynein proteins from Chlamydomonas and Tetrahymena after adsorption to a mica surface, after high-salt dissociation, and after glutaraldehyde fixation, and compare these images to the configuration of outer arms bound to microtubules.
John E. Heuser, Ursula Goodenough
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