The Design, Synthesis and Potential Utility of Fluorescence Probes that Target DFG‐out Conformation of p38α for High Throughput Screening Binding Assay
Haile Tecle(Pfizer (United States)), Frédéric Féru(Pfizer (United States)), Hu Liu(Pfizer (United States)), Cyrille Kuhn(Pfizer (United States)), Glen R. Rennie(Pfizer (United States)), Mark J. Morris(Pfizer (United States)), Jiangxing Shao(Pfizer (United States)), Alan C. Cheng(Pfizer (United States)), Diana Gikunju(Pfizer (United States)), Juan J. Miret(Pfizer (United States)), Rocco Coli(Pfizer (United States)), Simon Xi(Pfizer (United States)), Susan L. Clugston(Pfizer (United States)), Simon Low(Pfizer (United States)), Steven L. Kazmirski(Pfizer (United States)), Yuanhua Ding(Pfizer (United States)), Qing Cao(Pfizer (United States)), Theresa Johnson(Pfizer (United States)), Gayatri D. Deshmukh(Pfizer (United States)), Jonathan P. DiNitto(Pfizer (United States)), Joe C. Wu(Pfizer (United States)), Jessie M. English(Pfizer (United States))
Cited by 11Open Access
Abstract
The design, synthesis and utility of fluorescence probes that bind to the DFG-out conformation of p38alpha kinase are described. Probes that demonstrate good affinity for p38alpha, have been identified and one of the probes, PF-04438255, has been successfully used in an high throughput screening (HTS) assay to identify two novel non-classical p38alpha inhibitors. In addition, a cascade activity assay was utilized to validate the selective binding of these non-classical kinase inhibitors to the unactive form of the enzyme.
Related Papers
No related papers found
Powered by citation graph analysis