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- W4254976913 abstract "Abstract N‐Terminal myristoylation facilitates membrane binding and activity of proteins, in particular of Src family kinases, but the underlying mechanisms are only beginning to be understood. The chaperones UNC119A/B regulate the cellular distribution and signaling of N‐myristoylated proteins. Selective small‐molecule modulators of the UNC119–cargo interaction would be invaluable tools, but have not been reported yet. We herein report the development of the first UNC119–cargo interaction inhibitor, squarunkin A. Squarunkin A selectively inhibits the binding of a myristoylated peptide representing the N‐terminus of Src kinase to UNC119A with an IC 50 value of 10 n m . It binds to UNC119 proteins in cell lysate and interferes with the activation of Src kinase. Our results demonstrate that small‐molecule inhibition of the UNC119–cargo interaction might provide new opportunities for modulating the activity of Src kinases that are independent of direct inhibition of the enzymatic kinase activity." @default.
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- W4254976913 date "2017-05-04" @default.
- W4254976913 modified "2023-10-16" @default.
- W4254976913 title "Small‐Molecule Inhibition of the UNC119–Cargo Interaction" @default.
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- W4254976913 doi "https://doi.org/10.1002/ange.201701905" @default.
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