PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3709569-5	1986	The reduced activities of two manganese-dependent enzymes, prolidase and arginase in erythrocytes in combination with an increased manganese content cannot be explained at the moment and leads to the speculation that manganese is inaccessible for enzyme activation.	Manganese	30-39	peptidase D	Homo sapiens	59-68	
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Manganese	45-54	peptidase D	Homo sapiens	6-15	
10965990-12	2000	The strong ability of DNR to chelate manganese may explain the potential mechanism for inhibition of prolidase activity, subsequently collagen biosynthesis and poor wound healing in patients administered DNR.	Manganese	37-46	peptidase D	Homo sapiens	101-110	
3148067-2	1988	With pro-val as substrate and manganese in the reaction buffer, prolinase activity was higher in prolidase-deficient cells than in control cells (mean (SEM) 917 (67) nmol min-1 mg-1, n = 3, control mean (SEM) 294, (50), n = 11).	Manganese	30-39	peptidase D	Homo sapiens	97-106	
11137854-10	2001	Since prolidase is metalloprotease, requiring manganese for catalytic activity, and anthracyclines are known as chelators of divalent cations, we considered that the chelating ability of anthracyclines might be an underlying mechanism for the anthracyclines-induced inhibition of prolidase activity.	Manganese	46-55	peptidase D	Homo sapiens	6-15	
3436060-1	1987	The effect of prolonged preincubation for 24 h at 37 degrees C in the presence of 1 mmol/l manganese at pH 7.8 was investigated on the two forms of human erythrocyte prolidase after their separation by DEAE-Sephadex chromatography.	Manganese	91-100	peptidase D	Homo sapiens	166-175	
6408304-0	1983	In-vitro responses to ascorbate and manganese in fibroblasts from a patient with prolidase deficiency and iminodipeptiduria: cell growth, prolidase activity and collagen metabolism.	Manganese	36-45	peptidase D	Homo sapiens	81-90	
6408304-2	1983	Since in vivo, ascorbate and manganese seemed to be responsible for both biochemical and clinical improvement, they were also expected to activate prolidase activity in vitro.	Manganese	29-38	peptidase D	Homo sapiens	147-156