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Possibly of even greater importance, and of major scientific elegance, is his work from more recent years: the design of chemical tools to study the enzymes that transfer ubiquitin onto proteins: ubiquitin ligases. Next to the fact that the design and development of these tools represented challenges even surpassing those for creating the ubiquitin hydrolase probes, the biomedical potential of the ligase tools is potentially enormous. Protein ubiquitylation is at least as complex as protein phosphorylation, and the corresponding ubiquitin ligase family at least as diverse as the corresponding family of phosphorylating enzymes: the kinases. The past decades have witnessed the clinical development of numerous kinase inhibitors for the treatment of various cancers. In contrast, no ubiquitin ligase inhibitors have made it to the clinic yet. Thanks to the groundbreaking work of Huib, the discovery and development of such inhibitors is now a realistic goal and in that sense the future in terms of new anticancer agents, even though too late for Huib, is bright.
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Proceedings of the National Academy of Sciences of the United States of Americano. 50 (2023)
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bioRxiv (Cold Spring Harbor Laboratory) (2023)
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The EMBO Journalno. 16 (2022)
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