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|Title:||Rational design of selective organoruthenium inhibitors of protein tyrosine phosphatase 1B|
|Citation:||Ong, J.X., Yap, C.W., Ang, W.H. (2012-11-19). Rational design of selective organoruthenium inhibitors of protein tyrosine phosphatase 1B. Inorganic Chemistry 51 (22) : 12483-12492. ScholarBank@NUS Repository. https://doi.org/10.1021/ic301884j|
|Abstract:||Protein tyrosine phosphatases (PTPs) belong to a large family of important regulatory enzymes involved in vital mammalian signaling pathways. Selective inhibitors of PTPs are highly valuable from a therapeutic standpoint given their association with various pathological conditions. One such target is PTP-1B which has previously been linked to diabetes and cancer. However, developing a selective inhibitor against PTP-1B has proven to be daunting because the enzyme shares a high degree of structural homology with TC-PTP, an essential PTP involved in modulating immune functions. To address this challenge, a series of organoruthenium complexes was developed to bind at the PTP substrate-binding site while simultaneously target the peripheral structural space. By capitalizing on the potential difference in the structural environment proximal to the active site between different PTPs, selectivity toward PTP-1B over TC-PTP was improved, paving the way for organoruthenium complexes as selective PTP-1B metalloinhibitors. © 2012 American Chemical Society.|
|Source Title:||Inorganic Chemistry|
|Appears in Collections:||Staff Publications|
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