Philip D. Stahl
Washington University in St. Louis
226 Papers
3.5K Citations
Philip D. Stahl is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Endosome & Endocytosis. The author has an hindex of 78, co-authored 198 publications.
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Papers
Clearance of lysosomal hydrolases following intravenous infusion: The role of liver in the clearance of β-glucuronidase and N-acetyl-β-d-glucosaminidase
TL;DR: Results indicate that β-glucuronidase, N -acetyl-β- d -glucosaminidases, and probably other glycosidases are rapidly incorporated into the lysosomal compartment of liver.
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The hominoid-specific oncogene TBC1D3 activates Ras and modulates epidermal growth factor receptor signaling and trafficking.
Marisa J. Wainszelbaum,Audra J. Charron,Chen Kong,Donald S. Kirkpatrick,Priya Srikanth,M. Alejandro Barbieri,Steven P. Gygi,Philip D. Stahl +7 more
TL;DR: The expression of TBC1D3 generates a delay in EGFR degradation, a decrease in ubiquitination, and a failure to recruit adapter proteins that ultimately dysregulate EGFR signal transduction and enhance cell proliferation.
63
•Journal Article
Morphological analysis of ligand uptake and processing: the role of multivesicular endosomes and CURL in receptor-ligand processing.
TL;DR: The receptor-mediated endocytosis and intracellular processing of transferrin and mannose receptor ligands were investigated in bone marrow-derived macrophages, fibroblasts and reticulocytes and suggest a model for differential receptor-ligand and ligand-ligands sorting.
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Biosynthesis and processing of the mannose receptor in human macrophages.
TL;DR: Newly synthesized mannose receptor exhibits a half-life of 33 h as determined by pulse-chase studies, which indicates that on the average, each molecule of receptor recycles between the cell surface and endosomes hundreds of times before degradation.
61
Human β-GIucuronidase. II. Fate of Infused Human Placental β-Glucuronidase in the Rat
TL;DR: The experiments presented suggest that placental β-glucuronidase is cleared predominantly by organs with significant reticuloendothelial components, and the clearance mechanism appears to recognize the carbohydrate structure of the enzyme, but may recognize carbohydrate components different from those responsible for enzyme uptake by fibroblasts.