ArticleACS medicinal chemistry letters2025
Targeted Histone Deacetylase Degradation via Chemical Induced Proximity by Direct Recruitment of the CUL4 Complex Adaptor Protein DDB1.
Article in ACS medicinal chemistry letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- DNA-Encoded Library (DEL) Selection Identifies a Distinct DDB1 Ligand Binding Site.ACS medicinal chemistry letters · 2026Article
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Authors and funding
7 authors.
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Abstract
Targeted protein degradation using proteolysis-targeting chimeras (PROTACs) has emerged as a powerful strategy for disease treatment. By recruiting E3 ligases, these molecules enable selective degradation of pathogenic proteins. Cereblon (CRBN), a key component of the CUL4-DDB1-CRBN E3 ligase complex, is the most commonly recruited E3 ligase in PROTACs, including those targeting histone deacetylases (HDACs). In this study, we designed
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Registered trials
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