ArticleCell chemical biology2026
Assessing the suitability of deubiquitylases as substrates for targeted protein degradation.
Article in Cell chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Targeted degradation of USP7 in solid cancer cells reveals distinct effects of deubiquitinase degraders and inhibitors.Nature communications · 2026Article
- Targeted protein degradation dismantles undruggable targets to reverse immune evasion and therapy resistance in cancer.Frontiers in immunology · 2026Review
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4 authors.
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Abstract
The development of selective inhibitors of deubiquitylase enzymes (DUBs) is difficult due to a high level of homology in the active sites of the ≈100 such enzymes in the human proteome. A potential way to achieve this in a more facile manner would be to develop proteolysis-targeting chimera (PROTAC) or molecular glues that engage the target DUB in a less conserved region outside of the catalytic domain. However, this raises the concern that auto-deubiquitylation would make DUBs poor substrates for this modality. Here, we describe a chemical genetics system to evaluate this issue. We find that some DUBs are readily degradable via the Ubiquitin-proteasome pathway, and some are not. Of the latter category, some resist turnover through auto-deubiquitylation, and some are simply poor proteasome substrates.
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