Synthesis and Biological Activity of a Focused Library of Mitogen‐activated Protein Kinase Phosphatase Inhibitors

Mitogen‐activated protein kinase phosphatase 1 is a tyrosine phosphatase superfamily member that dephosphorylates and inactivates mitogen‐activated protein kinase substrates, such as p38, c‐Jun‐N‐terminal kinase, and extracellular signal‐related kinase. These mitogen‐activated protein kinase substrates regulate many cellular processes associated with human diseases. In spite of this potential as a molecular target for chemotherapy, however, pharmacologically tractable inhibitors of mitogen‐activated protein kinase phosphatase‐1 have yet to be developed. Based on the results from a high‐throughput screen for small molecule inhibitors of mitogen‐activated protein kinase phosphatase‐1, we designed, synthesized, and evaluated a focused library in an effort to further understand the structural requirements for mitogen‐activated protein kinase phosphatase‐1 inhibitory activity.

Synthesis and Biological Activity of a Focused Library of Mitogen‐activated Protein Kinase Phosphatase Inhibitors Journal Articles