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Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme.
Nature
58
2020
CoA, DGAT, DGAT1, MBOAT, N, O, Triacylglycerol, Triacylglycerols, acyl, acyl-CoA, acyl-CoA diacylglycerol acyltransferase, acyl-CoA thioester, diacylglycerol, dimeric human DGAT1, histidine, human, human triacylglycerol-synthesis enzyme, humans, membrane-bound O-acyltransferase, metabolic diseases1, obesity, oleoyl-CoA, triacylglycerol, triacylglycerols
Author NameAffiliation
Maofu LiaoHarvard Medical School
Tobias C WaltherHarvard T. H. Chan School of Public Health
Tobias C WaltherHoward Hughes Medical Institute
Tobias C WaltherBroad Institute of MIT and Harvard
Tobias C WaltherHarvard Medical School
Tobias C WaltherHarvard T. H. Chan School of Public Health
Tobias C WaltherHarvard Medical School
Tobias C WaltherBroad Institute of MIT and Harvard
Tobias C WaltherHoward Hughes Medical Institute
Robert V FareseHarvard T. H. Chan School of Public Health
Robert V FareseHarvard Medical School
Robert V FareseBroad Institute of MIT and Harvard
Robert V FareseHarvard T. H. Chan School of Public Health
Robert V FareseHarvard Medical School
Robert V FareseBroad Institute of MIT and Harvard
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