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Kevin Schooler

Researcher at University of Utah

Publications -  5
Citations -  624

Kevin Schooler is an academic researcher from University of Utah. The author has contributed to research in topics: Tyrosine phosphorylation & Endosome. The author has an hindex of 5, co-authored 5 publications receiving 606 citations. Previous affiliations of Kevin Schooler include University of Florida & Pacific Northwest National Laboratory.

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Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking.

TL;DR: It is concluded that the association of the EGFR with different proteins is compartment specific and ligand loss is the proximal cause of EGFR inactivation, and regulated trafficking could potentially influence the pattern as well as the duration of signal transduction.
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Effect of Epidermal Growth Factor Receptor Internalization on Regulation of the Phospholipase C-γ1 Signaling Pathway

TL;DR: It is concluded that EGFR signaling through the PLC pathway is spatially restricted at a point between PLC-γ1 phosphorylation and PIP2 hydrolysis, perhaps because of limited access of EGFR-bound PLC -γ1 to its substrate in endocytic trafficking organelles.
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The nucleophosmin-anaplastic lymphoma kinase fusion protein induces c-Myc expression in pediatric anaplastic large cell lymphomas.

TL;DR: C-Myc may be a downstream target of ALK signaling and its expression a defining characteristic ofALK-positive ALCLs, and to assess the clinical relevance of this observation, c- myc expression was determined in pediatric ALK- positive and -negative lymphomas.
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The transglutaminase 2 gene is aberrantly hypermethylated in glioma

TL;DR: Transglutaminase 2 expression in gliomas was found to vary widely, with many tumors showing overexpression or underexpression of this gene, and in primary brain tumors it was observed that the TGM2 promoter is commonly hypermethylated and that this feature is a cancer-associated phenomenon.
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Ratiometric assay of epidermal growth factor receptor tyrosine kinase activation.

TL;DR: A ratiometric enzyme-linked immunosorbent assay (ELISA) using epidermal growth factor receptors (EGFR) as a model provided a rapid and sensitive method of determining EGFR activation status and could be easily modified to evaluate any tyrosine-phosphorylated protein.