PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11574417-15	2001	IR substrate-1-associated phosphatidylinositol (PI) 3-kinase activation by insulin was also lower in the HiIMCL group than in the LoIMCL group (49 +/- 23 vs. 84 +/- 27% above basal, P < 0.05 between HiIMCL and LoIMCL).	Phosphatidylinositols	26-46	insulin receptor	Homo sapiens	0-2	
8628319-2	1996	This extension is absent from the human insulin receptor but resembles a region in insulin receptor substrate (IRS) proteins which binds to the phosphatidylinositol (PI) 3-kinase and mediates mitogenesis.	Phosphatidylinositols	144-164	insulin receptor	Homo sapiens	40-56	
11423472-5	2001	By using inhibitors of the different signaling pathways evoked by insulin-receptor binding, it has been shown that the biosynthesis of PAI-1 is due to phosphatidylinositol (PI) 3-kinase activation, followed by protein kinase C and ultimately by mitogen-activated protein (MAP) kinase activation and extracellular signal-regulated kinase 2 phosphorylation.	Phosphatidylinositols	151-171	insulin receptor	Homo sapiens	66-82	
3038645-0	1987	Phospholipid activation of the insulin receptor kinase: regulation by phosphatidylinositol.	Phosphatidylinositols	70-90	insulin receptor	Homo sapiens	31-47	
1385401-1	1992	After adding insulin to cells overexpressing the insulin receptor, the activity of phosphatidylinositol (PI) 3-kinase in the anti-phosphotyrosine immunoprecipitates was rapidly and greatly increased.	Phosphatidylinositols	83-103	insulin receptor	Homo sapiens	49-65	
1332046-1	1992	IRS-1 is an insulin receptor substrate that undergoes tyrosine phosphorylation and associates with the phosphatidylinositol (PtdIns) 3"-kinase immediately after insulin stimulation.	Phosphatidylinositols	103-123	insulin receptor	Homo sapiens	12-28	
3038645-5	1987	Phosphorylation of PtdIns occurred with these purified insulin receptor preparations, but this activity was insulin-independent, and the turnover number for PtdIns phosphorylation in the presence of soybean phospholipid was 1/220th as small as the turnover number for the autophosphorylating activity.	Phosphatidylinositols	19-25	insulin receptor	Homo sapiens	55-71	
3038645-5	1987	Phosphorylation of PtdIns occurred with these purified insulin receptor preparations, but this activity was insulin-independent, and the turnover number for PtdIns phosphorylation in the presence of soybean phospholipid was 1/220th as small as the turnover number for the autophosphorylating activity.	Phosphatidylinositols	157-163	insulin receptor	Homo sapiens	55-71	
3038645-6	1987	These results suggest that although PtdIns can modulate the activity of the insulin receptor kinase, PtdIns phosphorylation itself is not directly involved in this regulation.	Phosphatidylinositols	36-42	insulin receptor	Homo sapiens	76-92	
3007126-2	1986	Phosphatidylinositol was phosphorylated to phosphatidylinositol 4-phosphate by the partially purified insulin receptor.	Phosphatidylinositols	0-20	insulin receptor	Homo sapiens	102-118	
6090205-1	1984	Insulin receptor preparations from human placenta at various states of purity were shown to catalyze insulin-stimulated phosphate incorporation from [gamma-32P]ATP into endogenous (membrane) and exogenous phosphatidylinositol.	Phosphatidylinositols	205-225	insulin receptor	Homo sapiens	0-16	
31969308-3	2019	Moreover, treatment with SES promoted the gene and protein expression levels of insulin receptor (InsR) and the post-receptor associated proteins, such as insulin receptor substrate 1 (IRS1), insulin receptor substrate 2 (IRS2), PI3K (phosphatidylinositol 3-kinase), GLUT4 (glucose transporter 4) significantly, which were determined by RT-PCR and immunoblot analysis.	Phosphatidylinositols	235-255	insulin receptor	Homo sapiens	80-96	
16702775-5	2006	This results from at least two independent insulin receptor signals, one leading to the activation of phosphatidylinositol (PI) 3-kinase and the other to the activation of the Rho family small GTP-binding protein TC10.	Phosphatidylinositols	102-122	insulin receptor	Homo sapiens	43-59	
31872693-2	2019	Insulin stimulation causes autophosphorylation of the insulin receptor( IR),which then activates tyrosine phosphorylation of insulin receptor substrate( IRS).Phosphorylation of IRS can induce and activate phosphatidylinositol 3-kinase( PI3 K),subsequently activate downstream 3-phosphoinositide-dependent protease 1( PDK1) and Akt/PKB,and finally promote expression and translocation of glucose transporter 4 to increase glucose uptake of insulin-sensitive tissues and alleviate insulin resistance.	Phosphatidylinositols	205-225	insulin receptor	Homo sapiens	54-70	
31872693-2	2019	Insulin stimulation causes autophosphorylation of the insulin receptor( IR),which then activates tyrosine phosphorylation of insulin receptor substrate( IRS).Phosphorylation of IRS can induce and activate phosphatidylinositol 3-kinase( PI3 K),subsequently activate downstream 3-phosphoinositide-dependent protease 1( PDK1) and Akt/PKB,and finally promote expression and translocation of glucose transporter 4 to increase glucose uptake of insulin-sensitive tissues and alleviate insulin resistance.	Phosphatidylinositols	276-294	insulin receptor	Homo sapiens	54-70