174678-80-9Relevant articles and documents
Rational design of selective organoruthenium inhibitors of protein tyrosine phosphatase 1B
Ong, Jun Xiang,Yap, Chun Wei,Ang, Wee Han
, p. 12483 - 12492 (2013/01/15)
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.
Structure of protein tyrosine phosphatase 1B in complex with inhibitors bearing two phosphotyrosine mimetics
Jia,Ye,Dinaut,Wang,Waddleton,Payette,Ramachandran,Kennedy,Hum,Taylor
, p. 4584 - 4594 (2007/10/03)
Protein tyrosine phosphatases (PTPases) are signal-transducing enzymes that dephosphorylate intracellular proteins that have phosphorylated tyrosine residues. It has been demonstrated that protein tyrosine phosphatase 1B (PTP1B) is an attractive therapeut
Synthesis of L-2,3,5,6-tetrafluoro-4-(phosphonomethyl)phenylalanine, a novel non-hydrolyzable phosphotyrosine mimetic and L-4-(phosphonodifluoromethyl)phenylalanine
Liu, Wang-Qing,Roques, Bernard P.,Garbay, Christiane
, p. 1389 - 1392 (2007/10/03)
A new non-hydrolyzable phosphotyrosine analogue, L-F4Pmp and its N-Fmoc protected derivative were prepared by using an enantioselective synthetic pathway with camphor sultam as chiral auxiliary. The side chain pKa2 (6.9) of L-F4
