PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2413806-2	1985	Purification of tyrosyl-phosphorylated insulin receptor was effected by adsorption on and elution (with a hapten) from a column of O-phosphotyrosyl-binding antibody immobilized on protein A-Sepharose (Ab-protein A).	cyclo(tyrosyl-tyrosyl)	16-23	insulin receptor	Homo sapiens	39-55	
10751417-7	2000	Compared with control cells, cells expressing high levels of PTP1B showed a 50-60% decrease in maximally insulin-stimulated tyrosyl phosphorylation of IR and insulin receptor substrate-1 (IRS-1) and phosphoinositide 3-kinase (PI3K) activity associated with IRS-1 or with phosphotyrosine.	cyclo(tyrosyl-tyrosyl)	124-131	insulin receptor	Homo sapiens	151-153	
10751417-11	2000	Our results suggest that: 1) insulin stimulation of glucose transport in adipocytes requires </=45% of maximal tyrosyl phosphorylation of IR or IRS-1 and <50% of maximal activation of PI3K, 2) a novel PI3K-independent pathway may play a role in insulin-induced glucose transport in adipocytes, and 3) overexpression of PTP1B alone in adipocytes does not impair glucose transport.	cyclo(tyrosyl-tyrosyl)	114-121	insulin receptor	Homo sapiens	141-143	
9884156-2	1998	Previous studies demonstrated that the adverse effects of ethanol are mediated by inhibition of tyrosyl phosphorylation of the insulin receptor and the insulin receptor substrate-type 1 (IRS-1).	cyclo(tyrosyl-tyrosyl)	96-103	insulin receptor	Homo sapiens	127-143	
8567177-1	1995	The insulin receptor, as a consequence of ligand binding, undergoes autophosphorylation of critical tyrosyl residues within the cytoplasmic portion of its beta-subunit.	cyclo(tyrosyl-tyrosyl)	100-107	insulin receptor	Homo sapiens	4-20	
8276809-8	1994	These data support the hypothesis that binding of tyrosyl-phosphorylated receptors to p85 SH2 domains is a general mechanism for PtdIns 3"-kinase activation, and they suggest that direct interactions between the insulin receptor and PtdIns 3"-kinase may provide an alternative pathway for the activation of this enzyme by insulin.	cyclo(tyrosyl-tyrosyl)	50-57	insulin receptor	Homo sapiens	212-228	
2155093-2	1990	The autophosphorylation of the insulin receptor on tyrosyl residues activates the intrinsic tyrosine kinase of the receptor, rendering its ligand independent.	cyclo(tyrosyl-tyrosyl)	51-58	insulin receptor	Homo sapiens	31-47	
2465763-1	1989	Insulin increased dramatically the tyrosyl phosphorylation of the insulin receptor beta-subunit in mouse NIH-3T3 fibroblasts transfected with the human insulin receptor.	cyclo(tyrosyl-tyrosyl)	35-42	insulin receptor	Homo sapiens	152-168	
19251044-4	2009	IRS-proteins are insulin receptor substrates that mediate insulin signaling via multiple tyrosyl phosphorylations.	cyclo(tyrosyl-tyrosyl)	89-96	insulin receptor	Homo sapiens	17-33	
7782332-2	1995	In the present study, GH is shown to stimulate tyrosyl phosphorylation of insulin receptor substrate 1 (IRS-1), the principle substrate of the insulin receptor.	cyclo(tyrosyl-tyrosyl)	47-54	insulin receptor	Homo sapiens	74-90	
8130075-0	1993	The role of polybasic compounds in determining the tyrosyl phosphorylation of calmodulin by the human insulin receptor.	cyclo(tyrosyl-tyrosyl)	51-58	insulin receptor	Homo sapiens	102-118	
1385393-1	1992	When the catalytically active, tyrosyl-phosphorylated form of insulin receptor was isolated from human placenta and treated with ADP, only partial dephosphorylation was observed.	cyclo(tyrosyl-tyrosyl)	31-38	insulin receptor	Homo sapiens	62-78	
1385393-7	1992	Phosphorylation of the irreversible phosphorylation sites then renders the insulin receptor relatively insensitive to the continued presence of insulin and facilitates rapid reversible phosphorylation of a second group of tyrosyl residues.	cyclo(tyrosyl-tyrosyl)	222-229	insulin receptor	Homo sapiens	75-91