PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19232015-5	2009	Activities of ACE1 and ACE2 and their inhibition by bioactive tripeptides (Ile-Pro-Pro, Val-Pro-Pro, Leu-Pro-Pro) as well as by a standard ACE-inhibitor captopril were assayed in the vitreous body, the retina and the ciliary body using fluorometric detection methods.	tripeptides	62-73	angiotensin converting enzyme 2	Homo sapiens	23-27	
19232015-9	2009	The tripeptides inhibited ACE1 at one-thousandth of the concentration needed to inhibit ACE2.	tripeptides	4-15	angiotensin converting enzyme 2	Homo sapiens	88-92	
18324760-3	2008	The most potent inhibitor in this series is a tripeptide that displays a K i value of 0.4 nM toward ACE2 and is 3 orders of magnitude less potent toward carboxypeptidase A. Phosphinic tripeptides exhibit high potency exclusively when the Xaa position is occupied by a pseudoproline.	tripeptides	184-195	angiotensin converting enzyme 2	Homo sapiens	100-104