D
Dixie-Lee Shurland
Researcher at University of California, Los Angeles
Publications - 6
Citations - 2689
Dixie-Lee Shurland is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Dynamin & GTPase. The author has an hindex of 5, co-authored 6 publications receiving 2458 citations.
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Journal ArticleDOI
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
TL;DR: It is shown that mutations in the human dynamin-related protein Drp1 cause mitochondria to form perinuclear clusters that consist of highly interconnected mitochondrial tubules, which indicates that the balance between mitochondrial division and fusion is shifted toward fusion.
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A Human Dynamin-related Protein Controls the Distribution of Mitochondria
TL;DR: It is proposed that Drp1 is important for distributing mitochondrial tubules throughout the cell and represents a novel role for a member of the dynamin family of proteins.
Journal ArticleDOI
A model for dynamin self-assembly based on binding between three different protein domains.
Elena Smirnova,Dixie-Lee Shurland,Erin D. Newman-Smith,Babak Pishvaee,Alexander M. van der Bliek +4 more
TL;DR: Three different intramolecular binding interactions that may account for the process of dynamin self-assembly are described, suggesting a model in which dynamin molecules first dimerize and are then linked into a chain by a second binding reaction.
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A dynamin GTPase mutation causes a rapid and reversible temperature-inducible locomotion defect in C. elegans
Scott G. Clark,Dixie-Lee Shurland,Elliot M. Meyerowitz,Cornelia I. Bargmann,Alexander M. van der Bliek +4 more
TL;DR: The results suggest that dyn-1 function is required during development and for normal locomotion in Drosophila shibire and mammalian dynamins.
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Contribution of the GTPase Domain to the Subcellular Localization of Dynamin in the Nematode Caenorhabditis elegans
TL;DR: Dynamin domains contribute to axonal transport and the sequestration of a pool of dynamin molecules in synaptic cytosol, and the GFP-GTPase chimera was most strongly localized, although the GTPase domain has no known interactions with proteins other than with dynamin itself.