ArticleJournal of computational chemistry2025
Substrates (Acyl-CoA and Diacylglycerol) Entry and Products (CoA and Triacylglycerol) Egress Pathways in DGAT1.
Article in Journal of computational chemistry, 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.
- Case Report: DGAT1 deficiency in three infants including a novel missense variant: structural insights and comparison with reported cases.Frontiers in pediatrics · 2026Article
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Authors and funding
2 authors.
Funding
Abstract
Diacylglycerol O-acyltransferase 1 (DGAT1) is an integral membrane protein that uses acyl-coenzyme A (acyl-CoA) and diacylglycerol (DAG) to catalyze the formation of triacylglycerides (TAGs). The acyl transfer reaction occurs between the activated carboxylate group of the fatty acid and the free hydroxyl group on the glycerol backbone of DAG. However, how the two substrates enter DGAT1's catalytic reaction chamber and interact with DGAT1 remains elusive. This study aims to explore the structural basis of DGAT1's substrate recognition by investigating each substrate's pathway to the reaction chamber. Using a human DGAT1 cryo-EM structure in complex with an oleoyl-CoA substrate, we designed two different all-atom molecular dynamics (MD) simulation systems: DGAT1
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Registered trials
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