Synthesis and Biological Activity of a Focused Library of Mitogen-activated Protein Kinase Phosphatase Inhibitors Academic Article uri icon

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abstract

  • 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.

authors

  • Arnold, Donald
  • Foster, Caleb
  • Huryn, Donna M
  • Lazo, John S
  • Johnston, Paul A
  • Wipf, Peter

publication date

  • January 2007

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