ArticleChemical science2025
A method to identify small molecule/protein pairs susceptible to protein ubiquitination by the CRBN E3 ligase.
Article in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- A Versatile DNA-Encoded Library Platform for the Discovery of Highly Cooperative Chemical Inducers of Proximity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- From Serendipity to Strategy: Rationalizing Molecular Glue Discovery and Proximity-Induced Pharmacology through Chemical Biology.Journal of the American Chemical Society · 2026Review
- Exploring Novel E3 Ligases and Neosubstrates for Molecular Glue Degraders and Therapeutic Applications in Cancer.Oncology research · 2026Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although using DNA-encoded libraries (DELs) to find small molecule binders of target proteins is well-established, identifying molecules with functions beyond binding remains challenging in pooled screens. Here, we develop an approach for multiplexing functional screens that simultaneously evaluates encoded small molecules and encoded collections of protein targets in functional selections. We focus on ubiquitin (Ub) transfer with the cereblon-bound CRL4 E3 ligase because of its proven versatility in drug discovery. The functional selections recover small molecule/G-hairpin loop pairs based on their ability to promote Ub-transfer onto the G-hairpin loop. As Ub-transfer is the first step in tagging proteins for proteasomal destruction, finding small molecules capable of selectively reprogramming it is a significant challenge in contemporary drug development. Our work lays the foundation for functional DEL selections that match small molecule Ub-transfer catalysts with their optimal protein substrates.
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Registered trials
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