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• W2044522424 abstract "The complexity of the human proteome is greatly expanded by post-translational modifications. New tools capable of recognizing these modifications in a sequence-specific fashion provide a route to purify these modified proteins, to alter protein trafficking, and to visualize signal transduction in real time. Here, we have evolved novel, modification-specific ligands that target phosphorylated IκBα. To do this, we employed mRNA display-based in vitro selection using a 30-trillion-member protein library based on the fibronectin type III domain. The selection yielded one fibronectin molecule, 10C17C25, that binds a phospho-IκBα peptide with Kd = 18 nM and is over 1000-fold specific compared to the nonphosphorylated peptide. 10C17C25 specifically recognizes endogenous phosphorylated IκBα from mammalian cell extract and stabilizes phospho-IκBα in vivo. We also incorporated 10C17C25 into a FRET indicator that detects IκB kinase (IKK) activity in vitro, demonstrating the utility of selecting designed adaptors for kinase activity sensors." @default.
• W2044522424 created "2016-06-24" @default.
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• W2044522424 date "2008-07-01" @default.
• W2044522424 modified "2023-09-30" @default.
• W2044522424 title "mRNA Display Selection of a High-Affinity, Modification-Specific Phospho-IκBα-Binding Fibronectin" @default.
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• W2044522424 doi "https://doi.org/10.1021/cb800069c" @default.
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