Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 20, Issue 14, Pages 4371-4376Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2012.05.040
Keywords
Arylstibonic acids; Protein tyrosine phosphatase; Cdc25 inhibitor
Funding
- EPSRC Centre for Doctoral Training Studentship from the Institute of Chemical Biology (Imperial College London)
- Cancer research UK
- NIH [GM068626, GM056834]
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Arylstibonates structurally resemble phosphotyrosine side chains in proteins and here we addressed the ability of such compounds to act as inhibitors of a panel of mammalian tyrosine and dual-specificity phosphatases. Two arylstibonates both possessing a carboxylate side chain were identified as potent inhibitors of the protein tyrosine phosphatase PTP-beta. In addition, they inhibited the dual-specificity, cell cycle regulatory phosphatases Cdc25a and Cdc25b with sub-micromolar potency. However, the Cdc25c phosphatase was not affected demonstrating that arylstibonates may be viable leads from which to develop isoform specific Cdc25 inhibitors. (C) 2012 Elsevier Ltd. All rights reserved.
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