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internal business plan Et al. 2003. A widely applicable, high-throughput TR-FRET assay for the measurement of kinase autophosphorylation: VEGFR-2 as a prototype. J. Biomol. Screen. 8, 447–452. Newman, M. and S. Josiah. 2004. Utilization of fluorescence polarization and time resolved fluorescence resonance energy transfer assay formats for SAR studies: Src kinase as a model system. J. Biomol. Screen. 9, 525–532. Nickischer, D. et al. 2006. Development and implementation of three mitogen-activated protein kinase (MAPK) signaling pathway imaging assays to provide MAPK module selectivity profiling for kinase inhibitors.
Et al. 1998. Synthesis of fluorescent substrates for protein tyrosine phosphatase assays. Bioorg. Med. Chem. Lett. 8, 1301–1302. , Y. N. Hodge. 2003. Determining appropriate substrate conversion for enzymatic assays in high-throughput screening. J. Biomol. Screen. 8, 694–700. D. R. Oldenburg. 1999. A simple statistical parameter for use in evaluation and validation of high-throughput screening assays. J. Biomol. Screen. 4, 67–73. L. et al. 2007. An enzyme-linked immunosorbent assay to measure insulin receptor dephosphorylation by PTP1B.
The presence of “promiscuous” inhibitors or “aggregating” compounds in a chemical library has become a recent area of research. These compounds can cause false positives that can be reduced with certain detergents and can frequently be recognized by steep concentration response curves or enzyme concentration-dependent shifts in the IC50 (Feng and Shoichet, 2006; Shoichet, 2006). The exact mechanism of these false positives is not known but it is possible that these compounds induce the formation of compound–enzyme clusters that reduce enzyme activity.