ArticleRSC chemical biology2026
Development of a spectrophotometric assay for high-throughput screening and mechanistic characterization of glucose-1-phosphate thymidylyltransferase inhibitors.
Article in RSC chemical biology, 2026. 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.
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1 citing paper in PubMed.
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4 authors.
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Abstract
The sugar β-l-rhamnose is often a conserved component of bacterial polysaccharide capsules, an extracellular structure featured in many drug-resistant, pathogenic bacteria. The β-l-rhamnose biosynthetic enzymes (RmlA-D) have therefore become key targets in antibiotic development. However, inhibitor discovery for these enzymes, particularly α-d-glucose-1-phosphate thymidylyltransferase, has been hindered by a lack of robust activity assays. To address this challenge, we report a continuous, coupled-enzyme assay for screening α-d-glucose-1-phosphate thymidylyltransferase inhibitors, using
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