000179646 001__ 179646
000179646 005__ 20181203022806.0
000179646 0247_ $$2doi$$a10.1002/cmdc.200700209
000179646 022__ $$a1860-7179
000179646 02470 $$2ISI$$a000251678000016
000179646 037__ $$aARTICLE
000179646 245__ $$aOrganometallic ruthenium inhibitors of glutathione-S-transferase P1-1 as anticancer drugs
000179646 260__ $$bWiley-Blackwell$$c2007
000179646 269__ $$a2007
000179646 336__ $$aJournal Articles
000179646 520__ $$aRuthenium-arene complexes conjugated to ethacrynic acid were prepared as part of a strategy to develop novel glutathione-S-transferase (GST) inhibitors with alternate modes of activity through the organometallic fragment, ultimately to provide targeted ruthenium-based anticancer drugs. Enzyme kinetics and electrospray mass spectrometry experiments using GST P1-1 and its cysteine-modified mutant forms revealed that the complexes ore effective enzyme inhibitors, but they also rapidly inactivate the enzyme by covalent binding at Cys 47 and, to a lesser extent, Cys 101. They ore highly effective against the GST Pi-positive A2780 and A2780cisR ovarian carcinoma cell lines, are among the most effective ruthenium complexes reported so for and target ubiquitous GST Pi overexpressed in many cancers.
000179646 6531_ $$aEthacrynic-Acid
000179646 6531_ $$aIn-Vitro
000179646 6531_ $$aComplexes
000179646 6531_ $$aResistance
000179646 6531_ $$aAdducts
000179646 700__ $$0240279$$g160772$$aAng, Wee Han
000179646 700__ $$aDe Luca, Anastasia
000179646 700__ $$aChapuis-Bernasconi, Catherine
000179646 700__ $$aJuillerat-Jeanneret, Lucienne
000179646 700__ $$aLo Bello, Mario
000179646 700__ $$aDyson, Paul J.$$g149418$$0240015
000179646 773__ $$j2$$tChemmedchem$$q1799-1806
000179646 909C0 $$xU9$$0252010$$pLCOM
000179646 909CO $$pSB$$particle$$ooai:infoscience.tind.io:179646
000179646 917Z8 $$x135992
000179646 937__ $$aEPFL-ARTICLE-179646
000179646 973__ $$rREVIEWED$$sPUBLISHED$$aEPFL
000179646 980__ $$aARTICLE