PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1909177-4	1991	The amine-phosphate interaction also served to confirm that a quinazolin-4(3H)-one binds in the PNPase active sites like a purine substrate.	amine-phosphate	4-19	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	96-102	
1909177-4	1991	The amine-phosphate interaction also served to confirm that a quinazolin-4(3H)-one binds in the PNPase active sites like a purine substrate.	4-hydroxyquinazoline	62-82	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	96-102	
1909177-4	1991	The amine-phosphate interaction also served to confirm that a quinazolin-4(3H)-one binds in the PNPase active sites like a purine substrate.	purine	123-129	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	96-102	
1909177-5	1991	From models of the PNPase active site it was possible to design quinazoline-based quinones that undergo a reductive-addition reaction with an active-site glutamate residue.	quinazoline-based quinones	64-90	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	19-25	
1909177-5	1991	From models of the PNPase active site it was possible to design quinazoline-based quinones that undergo a reductive-addition reaction with an active-site glutamate residue.	Glutamic Acid	154-163	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	19-25	
1909177-6	1991	The best inhibitor studied, 2-(chloromethyl)quinazoline-4,5,8(3H)-trione, rapidly inactivates PNPase by a first-order process with an inhibitor to enzyme stoichiometry of 150.	2-(chloromethyl)quinazoline-4,5,8(3h)-trione	28-72	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	94-100	
1909177-8	1991	Thus, this inhibitor is designed to cross-link the PNPase active site by reductive addition followed by the generation of an alkylating quinone methide species.	quinone	136-143	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	51-57