ArticleeLife2022
SDR enzymes oxidize specific lipidic alkynylcarbinols into cytotoxic protein-reactive species.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- HSD17B11 maintains FSP1 localization on lipid droplets to support ferroptosis defense.bioRxiv : the preprint server for biology · 2026Article
- A plug and play approach to structural variations of bio-inspired anticancer lipidic phenyl dialkynylcarbinols.RSC advances · 2025Article
- InteracTor: Feature engineering and explainable AI for profiling protein structure-interaction-function relationships.PLoS computational biology · 2025Article
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Authors and funding
26 authors at 5 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hundreds of cytotoxic natural or synthetic lipidic compounds contain chiral alkynylcarbinol motifs, but the mechanism of action of those potential therapeutic agents remains unknown. Using a genetic screen in haploid human cells, we discovered that the enantiospecific cytotoxicity of numerous terminal alkynylcarbinols, including the highly cytotoxic dialkynylcarbinols, involves a bioactivation by HSD17B11, a short-chain dehydrogenase/reductase (SDR) known to oxidize the C-17 carbinol center of androstan-3-alpha,17-beta-diol to the corresponding ketone. A similar oxidation of dialkynylcarbinols generates dialkynylketones, that we characterize as highly protein-reactive electrophiles. We established that, once bioactivated in cells, the dialkynylcarbinols covalently modify several proteins involved in protein-quality control mechanisms, resulting in their lipoxidation on cysteines and lysines through
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Registered trials
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