ReviewXenobiotica; the fate of foreign compounds in biological systems2012
Understanding substrate selectivity of human UDP-glucuronosyltransferases through QSAR modeling and analysis of homologous enzymes.
Review in Xenobiotica; the fate of foreign compounds in biological systems, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Human variability in isoform-specific UDP-glucuronosyltransferases: markers of acute and chronic exposure, polymorphisms and uncertainty factors.Archives of toxicology · 2020Pooled it
- Glycosylated cannabinoids inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification of novel FRedox biology · 2024Article
- Enzymatic properties of UDP-glycosyltransferase 89B1 from radish and modulation of enzyme catalytic activity via loop region mutation.PloS one · 2024Article
- Repurposing degradation pathways for modular metabolite biosynthesis in nematodes.Nature chemical biology · 2023Review
- Discovery of an Orally Bioavailable and Selective PKMYT1 Inhibitor, RP-6306.Journal of medicinal chemistry · 2022Article
- Article
- Article
- The Fusarium metabolite culmorin suppresses the in vitro glucuronidation of deoxynivalenol.Archives of toxicology · 2019Article
- Overcoming Drug Resistance through the Development of Selective Inhibitors of UDP-Glucuronosyltransferase Enzymes.Journal of molecular biology · 2019Article
- Functional and informatics analysis enables glycosyltransferase activity prediction.Nature chemical biology · 2018Article
- Differences in the glucuronidation of resveratrol and pterostilbene: altered enzyme specificity and potential gender differences.Drug metabolism and pharmacokinetics · 2014Article
- Enzymatic detoxication, conformational selection, and the role of molten globule active sites.The Journal of biological chemistry · 2013Article
- Identification of flavone glucuronide isomers by metal complexation and tandem mass spectrometry: regioselectivity of uridine 5'-diphosphate-glucuronosyltransferase isozymes in the biotransformation of flavones.Journal of agricultural and food chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The UDP-glucuronosyltransferase (UGT) enzyme catalyzes the glucuronidation reaction which is a major metabolic and detoxification pathway in humans. Understanding the mechanisms for substrate recognition by UGT assumes great importance in an attempt to predict its contribution to xenobiotic/drug disposition in vivo. Spurred on by this interest, 2D/3D-quantitative structure activity relationships and pharmacophore models have been established in the absence of a complete mammalian UGT crystal structure. This review discusses the recent progress in modeling human UGT substrates including those with multiple sites of glucuronidation. A better understanding of UGT active site contributing to substrate selectivity (and regioselectivity) from the homologous enzymes (i.e. plant and bacterial UGTs, all belong to family 1 of glycosyltransferase (GT1)) is also highlighted, as these enzymes share a common catalytic mechanism and/or overlapping substrate selectivity.
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