PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8603747-6	1996	Second, the activation by diacylglycerol is not stereospecific, in marked contrast to the specificity for 1,2-diacyl-sn-glycerol in the activation of protein kinase C. Because circulating levels of insulin are below the Kd of the insulin receptor for insulin, the ability of diacylglycerol to modulate the affinity of the receptor for ligand suggests that increases in cellular levels of diacylglycerol directly sensitize the receptor to insulin.	1,2-diacyl-sn-glycerol	106-128	insulin	Homo sapiens	198-205	
8603747-6	1996	Second, the activation by diacylglycerol is not stereospecific, in marked contrast to the specificity for 1,2-diacyl-sn-glycerol in the activation of protein kinase C. Because circulating levels of insulin are below the Kd of the insulin receptor for insulin, the ability of diacylglycerol to modulate the affinity of the receptor for ligand suggests that increases in cellular levels of diacylglycerol directly sensitize the receptor to insulin.	1,2-diacyl-sn-glycerol	106-128	insulin	Homo sapiens	230-237	
8603747-6	1996	Second, the activation by diacylglycerol is not stereospecific, in marked contrast to the specificity for 1,2-diacyl-sn-glycerol in the activation of protein kinase C. Because circulating levels of insulin are below the Kd of the insulin receptor for insulin, the ability of diacylglycerol to modulate the affinity of the receptor for ligand suggests that increases in cellular levels of diacylglycerol directly sensitize the receptor to insulin.	1,2-diacyl-sn-glycerol	106-128	insulin	Homo sapiens	230-237	
2405021-1	1990	Recent evidence has suggested that pancreatic islets isolated from rats synthesize 1,2-diacyl-sn-glycerol (DAG) de novo from glucose and that this process may constitute the long-sought link between the metabolism of glucose and the induction of insulin secretion.	1,2-diacyl-sn-glycerol	83-105	insulin	Homo sapiens	246-253