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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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Ap-2/eps15 interaction is required for receptor-mediated endocytosis

TL;DR: Results show that interaction of Eps15 with AP-2 is required for efficient receptor-mediated endocytosis and thus provide the first evidence that Eps15 is involved in the function of plasma membrane–coated pits.
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Advances in Analysis of Low Signal-to-Noise Images Link Dynamin and AP2 to the Functions of an Endocytic Checkpoint

TL;DR: A framework for unbiased measurement of EAP recruitment to CCPs and their direct effects on CCP dynamics is presented and dynamin and the EAP-binding α-adaptin appendage domain of the AP2 adaptor are identified as switches in a regulated, multistep maturation process and provide direct evidence for a molecular checkpoint in CME.
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Regulation of Clathrin-Mediated Endocytosis.

TL;DR: This review summarizes recent findings on the regulation of CME and the evolution of this complex process and describes the role of the GTPase dynamin in this process.
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Regulation of Macropinocytosis by p21-activated Kinase-1

TL;DR: The mechanisms by which PAK modulate macropinocytosis were examined in NIH3T3 cell lines expressing various PAK1 constructs under the control of a tetracycline-responsive transactivator, and data indicate that PAK 1 plays an important regulatory role in the process of macropInocyTosis.
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Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis

TL;DR: A novel member of the Prk/Ark family of serine/threonine kinases, adaptor-associated kinase (AAK)1 is identified and it is found that AAK1 copurifies with adaptor protein (AP)2 and that it directly binds the ear domain of α-adaptin in vivo and in vitro.