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• W2517093136 abstract "The efficacious practice of precision personalized medicine requires a more exact understanding of the molecular mechanisms of drug, hence then it is necessary to identify the binding site of the drugs derived from natural sources. In the study, we investigated the suppressive effect and underlying mechanism of isoliquiritigenin (2',4',4-trihydroxychalcone; ILG), a phyto-flavonoid, on human T lymphocyte activation in vitro and in vivo. The results showed that ILG dose-dependently suppressed human T cell activation via suppressing IκBα phosphorylation and degradation, NF-κB nuclear translocation and IKKβ activity. Molecular docking results predicted that cysteine 46 (Cys-46) is probably the binding site of ILG on IKKβ, and this prediction has been validated by competition assay and kinase assay. To further verify the binding site of this compound in vivo, IKKβC46A transgenic (IKKβC46A) mice were generated. We found that ILG had a less potent immune-suppressive effect in homozygous IKKβC46A mice than IKKβ wild type (IKKβ wt) littermates with the delay-type hypersensitivity (DTH), suggesting that ILG cannot significantly suppress the inflammation due to the mutation of Cys-46 in the transgenic mice. Collectively, our findings indicate that the ILG inhibited T cell activation in vivo and in vitro via directly binding to IKKβ Cys46." @default.
• W2517093136 created "2016-09-16" @default.
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• W2517093136 date "2016-09-10" @default.
• W2517093136 modified "2023-10-16" @default.
• W2517093136 title "Isoliquiritigenin suppresses human T Lymphocyte activation <i>via</i> covalently binding cysteine 46 of IκB kinase" @default.
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• W2517093136 doi "https://doi.org/10.18632/oncotarget.11934" @default.
• W2517093136 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5470962" @default.
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