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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Journal ArticleDOI
Discovery of antivirals against smallpox
Stephen C. Harrison,Bruce Alberts,Ellie Ehrenfeld,Lynn W. Enquist,Harvey V. Fineberg,Steven L. McKnight,Bernard Moss,Mike O'Donnell,Hidde L. Ploegh,Sandra L. Schmid,K. Peter Walter,Julie A. Theriot +11 more
TL;DR: The concern that undeclared stocks of variola virus might exist and that they might be used as a bioterrorist weapon was heightened in late 2001 by the deliberate release of Bacillus anthracis, the agent of anthrax, in the weeks after the September 11, 2001, attacks as discussed by the authors.
Journal ArticleDOI
ATP- and Cytosol-dependent Release of Adaptor Proteins from Clathrin-coated Vesicles: A Dual Role for Hsc70
TL;DR: A novel quantitative assay for the ATP- and cytosol- dependent release of APs from CCV shows that hsc70 is not sufficient for AP release; however, immunodepletion and reconstitution experiments establish that it is necessary.
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Cytosol- and clathrin-dependent stimulation of endocytosis in vitro by purified adaptors.
TL;DR: Using stage-specific assays for receptor-mediated endocytosis of transferrin (Tfn) into perforated A431 cells it is shown that purified adaptors stimulate coated pit assembly and ligand sequestration into deeply invaginated coated pits.
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An Intramolecular Signaling Element that Modulates Dynamin Function In Vitro and In Vivo
Joshua S. Chappie,Sharmistha Acharya,Ya-Wen Liu,Marilyn Leonard,Thomas J. Pucadyil,Sandra L. Schmid +5 more
TL;DR: The components of the GTPase-GED interface act as an intramolecular signaling module, which the authors term the bundle signaling element, that can modulate dynamin function in vitro and in vivo.
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AAK1-mediated μ2 phosphorylation is stimulated by assembled clathrin
TL;DR: It is reported that Aak1 is an atypical kinase that is rate limited by its stable association with AP2 and that clathrin stimulates μ2 phosphorylation by AAK1, and a model in which AAK 1 is specifically activated in coated pits to enhance cargo recruitment and efficient internalization is suggested.