| Literature DB >> 22705189 |
Lok Hang Mak1, Jessica Knott, Katherine A Scott, Claire Scott, Gillian F Whyte, Yu Ye, David J Mann, Oscar Ces, James Stivers, Rudiger Woscholski.
Abstract
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-ß. 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.Entities:
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Year: 2012 PMID: 22705189 PMCID: PMC3389297 DOI: 10.1016/j.bmc.2012.05.040
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641