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.
Papers
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Journal ArticleDOI
GTPase Cycle of Dynamin Is Coupled to Membrane Squeeze and Release, Leading to Spontaneous Fission
Pavel V. Bashkirov,Sergey A. Akimov,Sergey A. Akimov,Alexey I. Evseev,Sandra L. Schmid,Joshua Zimmerberg,Vadim A. Frolov +6 more
TL;DR: It is proposed that dynamin transmits GTP's energy to periodic assembling of a limited curvature scaffold that brings lipids to an unstable intermediate that is dependent on the curvature stress imposed by dynamin.
Journal ArticleDOI
Regulation of signal transduction by endocytosis.
Brian P. Ceresa,Sandra L. Schmid +1 more
TL;DR: There is a growing body of evidence suggesting that this process is much more sophisticated and that endocytic membrane trafficking regulates both the intensity of signaling and the co-localization of activated receptors with downstream signaling molecules.
Journal ArticleDOI
The emergence of clathrin-independent pinocytic pathways
TL;DR: The selective regulation of these alternate endocytic pathways and the identification of receptors targeted to them provide new tools for the functional and mechanistic characterization of clathrin-independent pinocytosis.
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SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation.
Fiona Simpson,Natasha K. Hussain,Britta Qualmann,Regis B. Kelly,Brian K. Kay,Peter S. McPherson,Sandra L. Schmid +6 more
TL;DR: The efficient reconstitution of ATP-, GTP-, cytosol- and dynamin-dependent formation of clathrin-coated vesicles in permeabilized 3T3-L1 cells is reported, suggesting that interactions between SH3 domains and their partners function sequentially in endocytic coated-vesicle formation.
Journal ArticleDOI
G domain dimerization controls dynamin's assembly-stimulated GTPase activity
TL;DR: The structure of the GTPase–GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission and key conformational changes that promote G domain dimerization and stimulated hydrolysis.