PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25152299-4	2014	In this study, synthetic peptides corresponding to the predicted binding sites of DGAT1 enzyme were examined using synchrotron radiation circular dichroism spectroscopy, fluorescence emission and adsorption onto lipid monolayers to determine their interactions with substrates associated with triacylglyceride synthesis (oleoyl-CoA and dioleoylglycerol).	oleoyl-coenzyme A	321-331	diacylglycerol O-acyltransferase 1	Homo sapiens	82-87	
32433610-5	2020	Here we present the cryo-electron microscopy structure of human DGAT1 in complex with an oleoyl-CoA substrate.	oleoyl-coenzyme A	89-99	diacylglycerol O-acyltransferase 1	Homo sapiens	64-69	
32433611-6	2020	A structure obtained with oleoyl-CoA substrate resolved at approximately 3.2 A shows that the CoA moiety binds DGAT1 on the cytosolic side and the acyl group lies deep within a hydrophobic channel, positioning the acyl-CoA thioester bond near an invariant catalytic histidine residue.	oleoyl-coenzyme A	26-36	diacylglycerol O-acyltransferase 1	Homo sapiens	111-116