A fluorescent probe for monitoring PTP-PEST enzymatic activity
Author:
Affiliation:
1. Department of Chemistry
2. University of Nebraska – Lincoln
3. Lincoln
4. USA
5. Department of Chemistry and Physics
Abstract
Design and optimization of a direct activity assay for PTP-PEST.
Funder
National Institute of General Medical Sciences
University of Virginia
Publisher
Royal Society of Chemistry (RSC)
Subject
Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/AN/D0AN00993H
Reference45 articles.
1. Inside the human cancer tyrosine phosphatome
2. Activation of Multiple Proto-oncogenic Tyrosine Kinases in Breast Cancer via Loss of the PTPN12 Phosphatase
3. Protein Tyrosine Phosphatase-PEST Regulates Focal Adhesion Disassembly, Migration, and Cytokinesis in Fibroblasts
4. Roles of protein tyrosine phosphatases in cell migration and adhesion
5. The Phosphatase PTP-PEST/PTPN12 Regulates Endothelial Cell Migration and Adhesion, but Not Permeability, and Controls Vascular Development and Embryonic Viability
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