PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1628144-9	1992	The inhibition of brain COMT activity was estimated by decreases of hypothalamic and striatal homovanillic acid (HVA) and 3-methoxytyramine (3-MT; after pargyline) levels.	Pargyline	153-162	catechol-O-methyltransferase	Rattus norvegicus	24-28	
8821542-4	1996	COMT activity, evaluated by the ability to methylate adrenaline to metanephrine, was determined in liver and kidney homogenates prepared in 0.5 mM phosphate buffer (pH = 7.8) containing pargyline (0.1 mM), MgCl2 (0.1 mM), EGTA (1 mM) and S-adenosyl-L-methionine (0.1 mM).	Pargyline	186-195	catechol-O-methyltransferase	Rattus norvegicus	0-4	
7990969-2	1994	Monoamine oxidase and catechol-O-methyl transferase were inhibited with pargyline (500 mumol/l) and Ro 01-2812 (3,5-dinitropyrocatechol; 2 mumol/l), respectively.	Pargyline	72-81	catechol-O-methyltransferase	Rattus norvegicus	22-51	
1766471-10	1991	In pargyline-treated rats, COMT inhibitors did not alter dopamine, DOPAC or HVA levels but all of them decreased significantly 3-MT levels, particularly Ro 41-0960.	Pargyline	3-12	catechol-O-methyltransferase	Rattus norvegicus	27-31	
1766471-13	1991	COMT inhibitors suppressed 3-OMD formation also in clorgyline and pargyline (+ levodopa/carbidopa) treated rats.	Pargyline	66-75	catechol-O-methyltransferase	Rattus norvegicus	0-4	
6104592-1	1980	The administration of pargyline to normal rats enhanced the adrenal catecholamines noradrenaline + adrenaline content, tyrosine hydroxylase (TH) and catechol -0-methyl transferase (COMT) activity together with a reduction in monoamine oxidase (MAO) activity.	Pargyline	22-31	catechol-O-methyltransferase	Rattus norvegicus	181-185	
3010139-1	1986	The adrenergic nerve endings of vasa deferentia of either untreated or reserpine (R) and/or pargyline (P) pretreated rats were loaded with 3H-noradrenaline; COMT was inhibited by U-0521 (U).	Pargyline	92-101	catechol-O-methyltransferase	Rattus norvegicus	157-161	
6514013-2	1984	Inhibition of monoamine oxidase (MAO) (by pretreatment of the animals with pargyline) increased the formation of O-methylated metabolites by nearly that amount by which the formation of deaminated metabolites declined; hence, catechol-O-methyl transferase (COMT) seemed to be able to nearly fully compensate for the loss of MAO activity.	Pargyline	75-84	catechol-O-methyltransferase	Rattus norvegicus	226-255	
6514013-2	1984	Inhibition of monoamine oxidase (MAO) (by pretreatment of the animals with pargyline) increased the formation of O-methylated metabolites by nearly that amount by which the formation of deaminated metabolites declined; hence, catechol-O-methyl transferase (COMT) seemed to be able to nearly fully compensate for the loss of MAO activity.	Pargyline	75-84	catechol-O-methyltransferase	Rattus norvegicus	257-261	
3683592-3	1987	The extraneuronal COMT activity was determined under conditions of inhibition of both neuronal uptake and MAO (pretreatment with pargyline).	Pargyline	129-138	catechol-O-methyltransferase	Rattus norvegicus	18-22