ArticleProceedings of the National Academy of Sciences of the United States of America1998
Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 396 papers.
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Who cites it
396 citing papers in PubMed, 1,103 citations in OpenAlex.
- DGAT1-associated lipid-retinoid dysregulation correlates with metabolic impairment in the RPE of Stargardt disease.iScience · 2026Article
- A membrane homeostatic response to lipid overload coordinates fatty acid metabolism.bioRxiv : the preprint server for biology · 2026Article
- Activity-dependent lipid droplet biogenesis and turnover regulate synaptic integrity.bioRxiv : the preprint server for biology · 2026Article
- Protein lactylation in metabolic dysfunction-associated steatotic liver disease: a mechanistic review.Diabetology & metabolic syndrome · 2026Review
- Functional diversity of sunflower DGAT1 and DGAT2 enzymes underlying seed triacylglycerol biosynthesis.Frontiers in plant science · 2026Article
- Metabolic Engineering of Microalgae for Biofuel Production.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Ribosomal protein control of hematopoietic stem cell transformation through regulation of metabolism.Cell reports · 2025Article
- IL33-induced lipid droplet formation in mature low-density neutrophils drives colorectal cancer liver metastasis.Cellular & molecular immunology · 2025Article
- Longitudinal multimodal characterization of radiation dermatitis in the C57BL/6J mouse model.bioRxiv : the preprint server for biology · 2025Article
- Quantitative proteomic analysis of Arabidopsis thaliana with different levels of phospholipid:diacylglycerol acyltransferase1 expression.BMC genomics · 2025Article
- Mechanism for oil-phase separation by the lipid droplet assembly complex.bioRxiv : the preprint server for biology · 2025Article
- Combined Genetic and Transcriptional Study Unveils the Role ofBiomedicines · 2025Article
- A Conserved N-Terminal Di-Arginine Motif Stabilizes Plant DGAT1 and Modulates Lipid Droplet Organization.International journal of molecular sciences · 2025Article
- Inhibition of diacylglycerol O-acyltransferase 1 provides neuroprotection by inhibiting ferroptosis in ischemic stroke.Molecular medicine (Cambridge, Mass.) · 2025Article
- Milk traits characterization and association studies with DGAT1 polymorphisms in Bagnolese sheep.Animal bioscience · 2025Article
- Substrates (Acyl-CoA and Diacylglycerol) Entry and Products (CoA and Triacylglycerol) Egress Pathways in DGAT1.Journal of computational chemistry · 2025Article
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- Phosphatidic acid phosphatase LPIN1 in phospholipid metabolism and stemness in hematopoiesis and AML.HemaSphere · 2025Article
- The protective effect of higher serum TAG (51:4) levels against Parkinson's disease.The British journal of nutrition · 2025Article
- The Diacylglycerol Acyltransferase 3 ofBiomolecules · 2025Article
336 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
Triacylglycerols are quantitatively the most important storage form of energy for eukaryotic cells. Acyl CoA:diacylglycerol acyltransferase (DGAT, EC 2.3.1.20) catalyzes the terminal and only committed step in triacylglycerol synthesis, by using diacylglycerol and fatty acyl CoA as substrates. DGAT plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, and lactation. DGAT is an integral membrane protein that has never been purified to homogeneity, nor has its gene been cloned. We identified an expressed sequence tag clone that shared regions of similarity with acyl CoA:cholesterol acyltransferase, an enzyme that also uses fatty acyl CoA as a substrate. Expression of a mouse cDNA for this expressed sequence tag in insect cells resulted in high levels of DGAT activity in cell membranes. No other acyltransferase activity was detected when a variety of substrates, including cholesterol, were used as acyl acceptors. The gene was expressed in all tissues examined; during differentiation of NIH 3T3-L1 cells into adipocytes, its expression increased markedly in parallel with increases in DGAT activity. The identification of this cDNA encoding a DGAT will greatly facilitate studies of cellular glycerolipid metabolism and its regulation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.