PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8587470-1	1995	The structure-activity relationships of phosphoramidon analogues for inhibition of endothelin-converting enzyme (ECE), neutral endopeptidase 24.11 (NEP), and angiotensin-converting enzyme (ACE) were compared.	phosphoramidon	40-54	endothelin converting enzyme 1	Homo sapiens	113-116	
8587470-2	1995	Phosphoramidon inhibited ECE, NEP, and ACE activities with IC50 values of 3.5, 0.034, and 78 microM, respectively.	phosphoramidon	0-14	endothelin converting enzyme 1	Homo sapiens	25-28	
8587470-3	1995	Removal of the rhamnose moiety of phosphoramidon (dipeptide 3) reduced the potency for ECE (IC50 = 70 microM), whereas the potencies for NEP (0.003 microM) and ACE (0.20 microM) were increased.	phosphoramidon	34-48	endothelin converting enzyme 1	Homo sapiens	87-90	
8587470-6	1995	These results suggest that a hydrophobic group in the P1 position of phosphoramidon analogues increases the potency for ECE significantly, whereas compounds containing a free phosphonic acid are optimal for inhibition of NEP and ACE.	phosphoramidon	69-83	endothelin converting enzyme 1	Homo sapiens	120-123