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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A Highly Efficient Method for Site-Specific Modification of Unprotected Peptides after Chemical Synthesis
TL;DR: This methodology takes advantage of the selective reactivity of an N-methylaminooxy amino acid that is appropriately protected for direct incorporation during solid-phase peptide synthesis to develop a highly efficient method for the site-specific attachment of biophysical probes to unprotected peptides after chemical synthesis.
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Domain requirements for an endocytosis-independent, isoform-specific function of dynamin-2.
TL;DR: The structural requirements for a readily quantifiable, isoform-specific function of dynamin-2, the activation of caspase-3 to trigger apoptosis are explored using Dyn2/Dyn1 chimeras and it is found that swapping the highly homologous GTPase domain of dynamIn-2 into Dynamin-1 was sufficient to confer caspases-3 activation.
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Stage-specific assays for coated pit formation and coated vesicle budding in vitro
TL;DR: In this article, the internalization of transferrin receptors into semi-intact A431 cells was assessed by two different criteria which have allowed us to distinguish partial reactions in the complex overall process of receptor-mediated endocytosis.
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Dynamin-catalyzed membrane fission requires coordinated GTP hydrolysis.
TL;DR: It is established that efficient fission from supported bilayers with excess membrane reservoir (SUPER) templates requires coordinated GTP hydrolysis across two rungs of an assembled dynamin collar.
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DASC, a sensitive classifier for measuring discrete early stages in clathrin-mediated endocytosis.
TL;DR: A thermodynamics-inspired method is developed that resolves ACs from CCPs based on single channel fluorescent movies and shows that DASC is a sensitive detector of phenotypic variation in CCP dynamics that is uncorrelated to the variation in biochemical measurements of CME.