PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17884087-3	2007	Compared with the lisinopril-MMP-9 model in our previous study, imidapril was stabilized effectively on the active site with less of molecular distortions.	Lisinopril	18-28	matrix metallopeptidase 9	Homo sapiens	29-34	
17884087-4	2007	We also measured ACE and MMP-9 inhibitory activities of imidapril and lisinopril after myocardial infarction.	Lisinopril	70-80	matrix metallopeptidase 9	Homo sapiens	25-30	
17884087-6	2007	These findings show that imidapril inhibits MMP-9 directly like lisinopril and its hydrophobic interactions with the S1 site of MMP-9 would be important for enhancing inhibitory activity.	Lisinopril	64-74	matrix metallopeptidase 9	Homo sapiens	44-49	
17512521-0	2007	Inhibition of matrix metalloproteinase-9 activity by lisinopril after myocardial infarction in hamsters.	Lisinopril	53-63	matrix metallopeptidase 9	Homo sapiens	14-40	
17512521-4	2007	Lisinopril significantly inhibited both angiotensin-converting enzyme and matrix metalloproteinase-9 activities, but candesartan cilexetil did not.	Lisinopril	0-10	matrix metallopeptidase 9	Homo sapiens	74-100	
12381651-8	2002	Lisinopril inhibited MMP-9 significantly but did not inhibit MMP-2 in vitro (IC50 MMP-2: 7.4 (0.88); MMP-9: 7.86 (2.23)).	Lisinopril	0-10	matrix metallopeptidase 9	Homo sapiens	21-26	
17275782-1	2007	To characterize the inhibitory specificity of angiotensin converting enzyme (ACE) inhibitors for matrix metalloproteinase 9 (MMP-9) activity, molecular modeling of these complex was performed referring the recent X-ray structure analyses using lisinopril as an ACE inhibitor.	Lisinopril	244-254	matrix metallopeptidase 9	Homo sapiens	97-123	
17275782-1	2007	To characterize the inhibitory specificity of angiotensin converting enzyme (ACE) inhibitors for matrix metalloproteinase 9 (MMP-9) activity, molecular modeling of these complex was performed referring the recent X-ray structure analyses using lisinopril as an ACE inhibitor.	Lisinopril	244-254	matrix metallopeptidase 9	Homo sapiens	125-130	
17275782-3	2007	Lisinopril was effectively stabilized by specific hydrogen bonds and hydrophobic interactions in the active site of MMP-9, and its hydrophobic group appeared to interact preferentially with the S1 site compared with the S1" site.	Lisinopril	0-10	matrix metallopeptidase 9	Homo sapiens	116-121