PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10617622-6	2000	By taking these data into account, computer-assisted modeling techniques were used to build a tridimensional model of the neurotensin-(8-13)-binding site in which the N-terminal tetrapeptide of neurotensin-(8-13) fits in the third extracellular loop and the C-terminal dipeptide binds to residues at the junction between the extracellular and transmembrane domains of the receptor.	Dipeptides	269-278	neurotensin	Rattus norvegicus	122-133	
10617622-6	2000	By taking these data into account, computer-assisted modeling techniques were used to build a tridimensional model of the neurotensin-(8-13)-binding site in which the N-terminal tetrapeptide of neurotensin-(8-13) fits in the third extracellular loop and the C-terminal dipeptide binds to residues at the junction between the extracellular and transmembrane domains of the receptor.	Dipeptides	269-278	neurotensin	Rattus norvegicus	194-205	
3409880-12	1988	(d) Pro-Xaa dipeptides (where Xaa represented aromatic or hydrophobic residues) were the most potent inhibitors of tritiated neurotensin degradation while all the Xaa-Pro dipeptides tested were totally ineffective.	Dipeptides	12-22	neurotensin	Rattus norvegicus	125-136	
1761032-1	1991	The inhibitory effect of various dipeptides on the neurotensin-degrading metallopeptidase, endopeptidase 24.16, was examined.	Dipeptides	33-43	neurotensin	Rattus norvegicus	51-62	
1761032-2	1991	These dipeptides mimick the Pro10-Tyr11 bond of neurotensin that is hydrolyzed by endopeptidase 24.16.	Dipeptides	6-16	neurotensin	Rattus norvegicus	48-59