PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15563471-2	2005	Using purified recombinant IRK fragments and the isolated intact insulin receptor, we show here that autophosphorylation is inhibited by ADP and that this effect is essentially reversed by hydrogen peroxide.	Adenosine Diphosphate	137-140	insulin receptor	Homo sapiens	65-81	
8200911-9	1994	However, a monoclonal antibody to the insulin receptor (MA-20) at equimolar concentrations with insulin equally inhibits pertussis toxin-catalyzed ADP ribosylation of Gi without activating tyrosine kinase or insulin receptor autophosphorylation.	Adenosine Diphosphate	147-150	insulin receptor	Homo sapiens	38-54	
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.	Adenosine Diphosphate	129-132	insulin receptor	Homo sapiens	62-78	
1385393-2	1992	This observation suggests the existence of two distinct classes of phosphotyrosyl residues of the phosphorylated insulin receptor: one in which the phosphoryl groups undergo reversible transfer to ADP and one in which they do not.	Adenosine Diphosphate	197-200	insulin receptor	Homo sapiens	113-129	
1385393-8	1992	The dependence of the degree of phosphorylation of insulin receptor on the ATP:ADP ratio may provide a mechanism for modulating the cellular response to insulin.	Adenosine Diphosphate	79-82	insulin receptor	Homo sapiens	51-67