Chemical Biology & Drug Design

Chemical Biology Cover

We have developed competitive and direct binding methods to examine small-molecule inhibitors of protein tyrosine phosphatase activity. Focusing on the Yersinia pestis outer protein H, a potent bacterial protein tyrosine phosphatase, we describe how an understanding of the kinetic interactions involving Yersinia pestis outer protein H, peptide substrates, and small-molecule inhibitors of protein tyrosine phosphatase activity can be beneficial for inhibitor screening, and we further translate these results into a microarray assay for high-throughput screening

Citation: 

Hogan, M., Bahta, M., Cherry, S., Lountos, G.T., Tropea, J.E., Zhao, B., Burke Jr., T.R., Waugh, D.S., and Ulrich, R.G. (2013). Biomolecular interactions of small-molecule inhibitors affecting the YopH protein tyrosine phosphatase. Chem. Biol. Drug Des. 81:323-333

Published Date: 
March, 2013