PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18024134-4	2008	A hypothesis for the reduced hPNMT inhibitory potency of these compounds has been formed on the basis of molecular modeling and docking studies using the X-ray crystal structures of hPNMT co-crystallized with THIQ-type inhibitors and S-adenosyl-L-homocysteine as a template.	S-Adenosylhomocysteine	234-259	phenylethanolamine N-methyltransferase	Homo sapiens	29-34	
24018397-1	2013	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the conversion of norepinephrine (noradrenaline) to epinephrine (adrenaline) while, concomitantly, S-adenosyl-L-methionine (AdoMet) is converted to S-adenosyl-L-homocysteine.	S-Adenosylhomocysteine	204-229	phenylethanolamine N-methyltransferase	Homo sapiens	0-38	
24018397-1	2013	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the conversion of norepinephrine (noradrenaline) to epinephrine (adrenaline) while, concomitantly, S-adenosyl-L-methionine (AdoMet) is converted to S-adenosyl-L-homocysteine.	S-Adenosylhomocysteine	204-229	phenylethanolamine N-methyltransferase	Homo sapiens	40-44	
18024134-4	2008	A hypothesis for the reduced hPNMT inhibitory potency of these compounds has been formed on the basis of molecular modeling and docking studies using the X-ray crystal structures of hPNMT co-crystallized with THIQ-type inhibitors and S-adenosyl-L-homocysteine as a template.	S-Adenosylhomocysteine	234-259	phenylethanolamine N-methyltransferase	Homo sapiens	182-187	
16279783-1	2005	The X-ray structure of human phenylethanolamine N-methyltransferase (hPNMT) complexed with its product, S-adenosyl-L-homocysteine (4), and the most potent inhibitor reported to date, SK&F 64139 (7), was used to identify the residues involved in inhibitor binding.	S-Adenosylhomocysteine	104-129	phenylethanolamine N-methyltransferase	Homo sapiens	29-67	
16279783-1	2005	The X-ray structure of human phenylethanolamine N-methyltransferase (hPNMT) complexed with its product, S-adenosyl-L-homocysteine (4), and the most potent inhibitor reported to date, SK&F 64139 (7), was used to identify the residues involved in inhibitor binding.	S-Adenosylhomocysteine	104-129	phenylethanolamine N-methyltransferase	Homo sapiens	69-74	
11807261-2	2002	Human PNMT has been crystallized in complex with an inhibitor and the cofactor product S-adenosyl-L-homocysteine using the hanging-drop technique with PEG 6000 and lithium chloride as precipitant.	S-Adenosylhomocysteine	89-112	phenylethanolamine N-methyltransferase	Homo sapiens	6-10	
6838886-4	1983	Phenylethanolamine-N-methyltransferase inhibitors S-adenosyl-homocysteine and SK & F 64139 can block this photoactivated cross-linkage.	S-Adenosylhomocysteine	52-73	phenylethanolamine N-methyltransferase	Homo sapiens	0-38