PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18324760-2	2008	Here we report the discovery of potent and selective inhibitors of ACE2, which have been identified by evaluating a series of phosphinic di- and tripeptides of the general formula: Z-Xaa(PO 2-CH 2)YaaOH and Ac-Zaa-Xaa(PO 2-CH 2)YaaOH.	di- and tripeptides	137-156	angiotensin converting enzyme 2	Homo sapiens	67-71	
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.	tripeptide K-26	46-56	angiotensin converting enzyme 2	Homo sapiens	100-104	
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	
18324760-4	2008	A model of interaction between one inhibitor of this series and ACE2 suggests that the critical role played by a proline in inhibitors, but also for substrates hydrolysis, may rely on the presence of Tyr (510) in the ACE2 active site.	Proline	113-120	angiotensin converting enzyme 2	Homo sapiens	64-68	
18324760-4	2008	A model of interaction between one inhibitor of this series and ACE2 suggests that the critical role played by a proline in inhibitors, but also for substrates hydrolysis, may rely on the presence of Tyr (510) in the ACE2 active site.	Proline	113-120	angiotensin converting enzyme 2	Homo sapiens	217-221	
18324760-4	2008	A model of interaction between one inhibitor of this series and ACE2 suggests that the critical role played by a proline in inhibitors, but also for substrates hydrolysis, may rely on the presence of Tyr (510) in the ACE2 active site.	Tyrosine	200-203	angiotensin converting enzyme 2	Homo sapiens	64-68	
18324760-4	2008	A model of interaction between one inhibitor of this series and ACE2 suggests that the critical role played by a proline in inhibitors, but also for substrates hydrolysis, may rely on the presence of Tyr (510) in the ACE2 active site.	Tyrosine	200-203	angiotensin converting enzyme 2	Homo sapiens	217-221