S
Sandra L. Schmid
Researcher at University of Texas Southwestern Medical Center
Publications - 209
Citations - 32222
Sandra L. Schmid is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Endocytosis & Dynamin. The author has an hindex of 89, co-authored 209 publications receiving 30096 citations. Previous affiliations of Sandra L. Schmid include University of British Columbia & Stanford University.
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Endocytic pathways and endosomal trafficking: a primer
TL;DR: This brief overview of endocytic trafficking is written in honor of Renate Fuchs, who retires this year, and describes other sorting machinery and mechanisms, as well as the rab proteins and phosphatidylinositol lipids that serve to dynamically define membrane compartments along the endocytical pathway.
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Dynamin GTpase domain mutants block endocytic vesicle formation at morphologically distinct stages
TL;DR: It is found that overexpression of dynamin mutants with subtle differences in their GTPase properties can lead to the accumulation of distinct intermediates in endocytic coated vesicle formation.
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Dissecting dynamin’s role in clathrin-mediated endocytosis
TL;DR: Findings that have led to the current models for dynamin function are reviewed, suggesting that dynamin plays a dual role in CME, functioning at early stages as a fidelity monitor to regulate clathrin-coated pit maturation and at later stages to directly catalyse membrane fission and clathin- coated vesicle formation.
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Conserved Functions of Membrane Active GTPases in Coated Vesicle Formation
TL;DR: Recent evidence suggests that, although structurally diverse, Arf family GTPases and dynamin may play mechanistically similar roles as fidelity monitors that govern cargo packaging and coated vesicle maturation and as components of the fission machinery to mediate vesicles release.
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The dynamin middle domain is critical for tetramerization and higher-order self-assembly
Rajesh Ramachandran,Mark C. Surka,Joshua S. Chappie,Douglas M. Fowler,Ted R. Foss,Byeong Doo Song,Sandra L. Schmid +6 more
TL;DR: It is demonstrated that two mutations in this domain, R361S and R399A, disrupt the tetrameric structure of dynamin in the unassembled state and impair its ability to stably bind to and nucleate higher‐order self‐assembly on membranes.