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• W1962364135 startingPage "4809" @default.
• W1962364135 abstract "11 Note: web pages available at http://www.sbg.ac.at/che/ and http://www.biozentrum.uni-wuerzburg.de/ The transcription factor Stat6 (signal transducer and activator of transcription 6) is activated following stimulation with interleukin (IL)-4 or IL-13. Stat6 binds via a single SH2 domain first to tyrosine-phosphorylated motifs in the IL-4Rα chain, and then to another Stat6 molecule, which results in the formation of active dimers. We show here that a peptide derived from the Stat6-binding region of IL-4Rα (Stat6BP) is an effective inhibitor when it is delivered into cells by coupling with a membrane-permeable peptide. Stat6BP completely inhibited IL-4 dependent phosphorylation of Stat6, as well as basal and IL-4 stimulated transcription from a reporter gene construct with a Stat6-dependent promoter, while IL-3 and IL-4 dependent phosphorylation of Stat5 was not affected. The inhibitory effect of Stat6BP was transient, but could be prolonged by treating the cells with the phosphatase inhibitor pervanadate." @default.
• W1962364135 created "2016-06-24" @default.
• W1962364135 creator A5054444035 @default.
• W1962364135 creator A5056876135 @default.
• W1962364135 creator A5090042687 @default.
• W1962364135 date "2001-09-01" @default.
• W1962364135 modified "2023-10-16" @default.
• W1962364135 title "Specific inhibition of interleukin-4-dependent Stat6 activation by an intracellularly delivered peptide" @default.
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• W1962364135 doi "https://doi.org/10.1046/j.1432-1327.2001.02417.x" @default.
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