PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21783632-9	2005	An addition of acetylsalicylic acid, known, non-specific inhibitor of prolidase to the cells treated with 100muM NiCl(II), significantly reduced both collagen biosynthesis and prolidase activity.	Aspirin	15-35	peptidase D	Homo sapiens	70-79	
16991207-2	2006	Effects of four nonsteroidal anti-inflammatory drugs including aspirin, paracetamol, sodium salicylate and phenacetin on prolidase (PLD) activity in erythrocytes were investigated.	Aspirin	63-70	peptidase D	Homo sapiens	132-135	
16991207-3	2006	Aspirin enhanced PLD activity whereas the other three had inhibiting effects.	Aspirin	0-7	peptidase D	Homo sapiens	17-20	
21783632-9	2005	An addition of acetylsalicylic acid, known, non-specific inhibitor of prolidase to the cells treated with 100muM NiCl(II), significantly reduced both collagen biosynthesis and prolidase activity.	Aspirin	15-35	peptidase D	Homo sapiens	176-185	
21783632-10	2005	It suggests that acetylsalicylic acid prevents nickel-induced increase in collagen biosynthesis through inhibition of prolidase activity in human fibroblasts.	Aspirin	17-37	peptidase D	Homo sapiens	118-127	
15173663-6	2004	RESULTS: In cells treated with acetylsalicylic acid, a concomitant decrease in prolidase activity, prolidase phosphorylation (at the threonine residue), and collagen biosynthesis were observed.	Aspirin	31-51	peptidase D	Homo sapiens	79-88	
15173663-6	2004	RESULTS: In cells treated with acetylsalicylic acid, a concomitant decrease in prolidase activity, prolidase phosphorylation (at the threonine residue), and collagen biosynthesis were observed.	Aspirin	31-51	peptidase D	Homo sapiens	99-108	
15173663-10	2004	CONCLUSIONS: The inhibitory effect of acetylsalicylic acid on collagen biosynthesis in fibroblasts is coupled to the inhibition of prolidase phosphorylation (but not expression) and down-regulation of the intracellular signal transmitted by the b1-integrin receptor.	Aspirin	38-58	peptidase D	Homo sapiens	131-140	
9112701-4	1996	Prolidase activity was measured in cultured human skin fibroblasts, treated with some non-steroid antiinflammatory drugs (acetyl-salicylic acid, sodium salicylate, phenylbutazone, indometacin).	Aspirin	122-143	peptidase D	Homo sapiens	0-9	
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	118-121	peptidase D	Homo sapiens	75-84	
15337432-0	2004	Acetylsalicylic acid as a potential regulator of prolidase-convertible pro-drugs in control and neoplastic cells.	Aspirin	0-20	peptidase D	Homo sapiens	49-58	
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	96-116	peptidase D	Homo sapiens	75-84	
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	96-116	peptidase D	Homo sapiens	75-84	
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	118-121	peptidase D	Homo sapiens	75-84	
15337432-6	2004	It suggests that ASA may serve as an inhibitor of prolidase-convertible pro-drugs in normal cells.	Aspirin	17-20	peptidase D	Homo sapiens	50-59