PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9202751-4	1997	The further activation of N-hydroxyarylamines by phase-II metabolism can involve both N, O-acetylation and N, O-sulfonation catalyzed by N-acetyltransferases (NAT1 and NAT2) and sulfotransferases, respectively.	n-hydroxyarylamines	26-45	N-acetyltransferase 2	Homo sapiens	168-172	
7627960-8	1995	NAT2 alleles with nucleic acid substitution T341C (NAT2*5A,*5B,*5C) expressed recombinant NAT2 allozymes, with the greatest reductions in metabolic activation of N-hydroxyarylamines and N-hydroxyarylamides by O- and N,O-acetylation, respectively.	n-hydroxyarylamines	162-181	N-acetyltransferase 2	Homo sapiens	0-4	
7627960-8	1995	NAT2 alleles with nucleic acid substitution T341C (NAT2*5A,*5B,*5C) expressed recombinant NAT2 allozymes, with the greatest reductions in metabolic activation of N-hydroxyarylamines and N-hydroxyarylamides by O- and N,O-acetylation, respectively.	n-hydroxyarylamines	162-181	N-acetyltransferase 2	Homo sapiens	51-55	
7627960-8	1995	NAT2 alleles with nucleic acid substitution T341C (NAT2*5A,*5B,*5C) expressed recombinant NAT2 allozymes, with the greatest reductions in metabolic activation of N-hydroxyarylamines and N-hydroxyarylamides by O- and N,O-acetylation, respectively.	n-hydroxyarylamines	162-181	N-acetyltransferase 2	Homo sapiens	51-55	
7627960-11	1995	NAT2 alleles with nucleic acid substitutions C282T (silent), C481T (silent), and A803G (Lys268-->Arg) expressed recombinant NAT2 allozymes that did not have significant reductions in the metabolic activations of N-hydroxyarylamines and N-hydroxyarylamides.	n-hydroxyarylamines	215-234	N-acetyltransferase 2	Homo sapiens	0-4	
7627960-11	1995	NAT2 alleles with nucleic acid substitutions C282T (silent), C481T (silent), and A803G (Lys268-->Arg) expressed recombinant NAT2 allozymes that did not have significant reductions in the metabolic activations of N-hydroxyarylamines and N-hydroxyarylamides.	n-hydroxyarylamines	215-234	N-acetyltransferase 2	Homo sapiens	127-131	
7627960-12	1995	The differential capacity for the metabolic activation of N-hydroxyarylamines and N-hydroxyarylamides by recombinant human NAT2 allozymes encoded by polymorphic NAT2 alleles supports the hypothesis that acetylator phenotype may predispose to cancers related to activation of N-hydroxy-arylamine and N-hydroxyarylamide carcinogens.	n-hydroxyarylamines	58-77	N-acetyltransferase 2	Homo sapiens	123-127	
7627960-12	1995	The differential capacity for the metabolic activation of N-hydroxyarylamines and N-hydroxyarylamides by recombinant human NAT2 allozymes encoded by polymorphic NAT2 alleles supports the hypothesis that acetylator phenotype may predispose to cancers related to activation of N-hydroxy-arylamine and N-hydroxyarylamide carcinogens.	n-hydroxyarylamines	58-77	N-acetyltransferase 2	Homo sapiens	161-165	
7581492-3	1995	In this study, we established cell lines which carried cDNAs coding for human CYP1A2 and N-acetyltransferase (NAT); the latter functions as O-acetyltransferase for N-hydroxyarylamines formed by CYP1A2.	n-hydroxyarylamines	164-183	N-acetyltransferase 2	Homo sapiens	110-113	
7627960-0	1995	Metabolic activation of N-hydroxyarylamines and N-hydroxyarylamides by 16 recombinant human NAT2 allozymes: effects of 7 specific NAT2 nucleic acid substitutions.	n-hydroxyarylamines	24-43	N-acetyltransferase 2	Homo sapiens	92-96	
8179482-0	1994	Metabolic activation of aromatic and heterocyclic N-hydroxyarylamines by wild-type and mutant recombinant human NAT1 and NAT2 acetyltransferases.	n-hydroxyarylamines	50-69	N-acetyltransferase 2	Homo sapiens	121-125	
8179482-2	1994	Both NAT1 and NAT2 (including all mutant human NAT2s tested) catalyzed the metabolic activation of each of the N-hydroxyarylamines to products that bound to DNA.	n-hydroxyarylamines	111-130	N-acetyltransferase 2	Homo sapiens	14-18