PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11108798-0	2000	Inactivation of human arylamine N-acetyltransferase 1 by the hydroxylamine of p-aminobenzoic acid.	Hydroxylamine	61-74	N-acetyltransferase 1	Homo sapiens	22-53	
15723621-6	2005	Recent advances on the regulation of human NAT1 activity has shown that hydroxylamine and/or nitroso intermediates of NAT1 substrates inhibit the enzyme through direct irreversible interaction with its catalytic cysteine residue.	Hydroxylamine	72-85	N-acetyltransferase 1	Homo sapiens	43-47	
15723621-6	2005	Recent advances on the regulation of human NAT1 activity has shown that hydroxylamine and/or nitroso intermediates of NAT1 substrates inhibit the enzyme through direct irreversible interaction with its catalytic cysteine residue.	Hydroxylamine	72-85	N-acetyltransferase 1	Homo sapiens	118-122	
9131488-11	1996	Both NATs, particularly NAT1, also can further metabolize hydroxylamine metabolites to N-acetoxy derivatives.	Hydroxylamine	58-71	N-acetyltransferase 1	Homo sapiens	24-28