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Eleonora Barone

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Inhibitors supercharge kinase turnover through native proteolytic circuits - Nature

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By Natalie S. Scholes, Arnau Comajuncosa-Creus, Xuefei Guo, Fabian Frommelt, Matthias Hinterndorfer, Hlib Razumkov, Martin P. Schwalm, Hana Imrichova, Andrea Rukavina, Miriam Abele, Anna Koren, Stefan Kubicek, Stefan Knapp, Nathanael S. Gray, Giulio Superti-Furga, Bernhard Kuster, Yigong Shi, Patrick Aloy, Sandra Roehm, Eleonora Barone
| Nature Verified
Abstract Targeted protein degradation is a pharmacological strategy that relies on small molecules such as proteolysis-targeting chimeras (PROTACs) or molecular glues, which induce proximity between a target protein and an E3 ubiquitin ligase to prompt target ubiquitination and proteasomal degradation1. Sporadic reports indicated that ligands designed to inhibit a target can also induce its destabilization2,3,4. Among others, this has repeatedly been observed for kinase inhibitors5,6,7.
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