PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15117974-2 2004 Mycolic acid biosynthesis is inhibited by isoniazid, a key frontline antitubercular drug that is inactivated by mycobacterial and human arylamine N-acetyltransferase (NAT). Isoniazid 42-51 bromodomain containing 2 Homo sapiens 167-170 11239577-3 2001 NAT has recently been identified within Mycobacterium tuberculosis itself and is an important candidate for modulating the response of mycobacteria to isoniazid. Isoniazid 151-160 bromodomain containing 2 Homo sapiens 0-3 11739761-1 2001 Arylamine N-acetyltransferase (NAT) in humans inactivates the anti-tubercular drug isoniazid (INH). Isoniazid 83-92 bromodomain containing 2 Homo sapiens 31-34 12668988-2 2003 Isoniazid is metabolized by hepatic N-acetyltransferase (NAT) and cytochrome P450 2E1 (CYP2E1) to form hepatotoxins. Isoniazid 0-9 bromodomain containing 2 Homo sapiens 57-60 11799105-2 2002 NAT was first identified as the enzyme responsible for the inactivation of the anti-tubercular drug isoniazid in humans. Isoniazid 100-109 bromodomain containing 2 Homo sapiens 0-3 11915035-3 2002 Isoniazid is mainly metabolized to hepatotoxic intermediates by N-acetyltransferase (NAT). Isoniazid 0-9 bromodomain containing 2 Homo sapiens 64-83 11915035-3 2002 Isoniazid is mainly metabolized to hepatotoxic intermediates by N-acetyltransferase (NAT). Isoniazid 0-9 bromodomain containing 2 Homo sapiens 85-88 11005799-1 2000 Arylamine N:-acetyltransferase (NAT) was first identified as the inactivator of the anti-tubercular drug isoniazid. Isoniazid 105-114 bromodomain containing 2 Homo sapiens 32-35 11005799-4 2000 NAT was identified recently in Mycobacterium tuberculosis and is a candidate for modulating the response to isoniazid. Isoniazid 108-117 bromodomain containing 2 Homo sapiens 0-3 8182542-4 1994 Arylamine N-acetyltransferase (NAT) catalyzes the acetyl CoA-dependent N-acetylation of primary arylamine and hydrazine substrates such as sulfamethazine, isoniazid, p-aminobenzoic acid as well as arylamine carcinogens such as 2-aminofluorene and benzidine. Isoniazid 155-164 bromodomain containing 2 Homo sapiens 31-34 1950579-1 1991 The effects of p-aminobenzoic acid (PABA), procainamide (PA), anisidine (AN) and isoniazid (INH) on N-acetyltransferase (NAT) activities in cultured human cells were determined. Isoniazid 81-90 bromodomain containing 2 Homo sapiens 100-119 1872889-4 1991 The second locus encodes an NAT which is termed polymorphic NAT (pNAT), has a distinct tissue distribution and is responsible for the difference in ability between individuals in acetylating certain arylamine (e.g. sulphamethazine) and hydrazine (e.g. isoniazid) drugs which are polymorphic substrates. Isoniazid 252-261 bromodomain containing 2 Homo sapiens 28-31 1950579-1 1991 The effects of p-aminobenzoic acid (PABA), procainamide (PA), anisidine (AN) and isoniazid (INH) on N-acetyltransferase (NAT) activities in cultured human cells were determined. Isoniazid 81-90 bromodomain containing 2 Homo sapiens 121-124 2344344-2 1990 The major route for dapsone metabolism leading to its inactivation and excretion is via acetylation by hepatic N-acetyl transferase (NAT), as is the case with isoniazid (INH) and sulfamethazine (SMZ). Isoniazid 159-168 bromodomain containing 2 Homo sapiens 111-131 2344344-2 1990 The major route for dapsone metabolism leading to its inactivation and excretion is via acetylation by hepatic N-acetyl transferase (NAT), as is the case with isoniazid (INH) and sulfamethazine (SMZ). Isoniazid 159-168 bromodomain containing 2 Homo sapiens 133-136 7225085-1 1980 Characterization of human lymphocyte N-acetyltransferase (NAT) for specific activity, substrate specificity, inhibition, pH optimum, apparent Km kinetic mechanism, trypsin stability, freezing stability, and heat stability was carried out in rapid and slow isoniazid (INH) acetylators. Isoniazid 256-265 bromodomain containing 2 Homo sapiens 58-61 28747958-1 2017 BACKGROUND: N-acetyl transferase (NAT) inactivates the pro-drug isoniazid (INH) to N-acetyl INH through a process of acetylation, and confers low-level resistance to INH in Mycobacterium tuberculosis (MTB). Isoniazid 64-73 bromodomain containing 2 Homo sapiens 34-37 18680474-7 2008 Arylamine N acetyltransferases (NAT) convert aromatic amines or hydrazines to aromatic amides and hydrazides. Isoniazid 98-108 bromodomain containing 2 Homo sapiens 10-30 24467436-12 2014 NAT in Salmonella typhimurium supports carcinogen activation and NAT in mycobacteria metabolizes isoniazid with polymorphism a minor factor in isoniazid resistance. Isoniazid 97-106 bromodomain containing 2 Homo sapiens 0-3 24467436-12 2014 NAT in Salmonella typhimurium supports carcinogen activation and NAT in mycobacteria metabolizes isoniazid with polymorphism a minor factor in isoniazid resistance. Isoniazid 97-106 bromodomain containing 2 Homo sapiens 65-68 24467436-12 2014 NAT in Salmonella typhimurium supports carcinogen activation and NAT in mycobacteria metabolizes isoniazid with polymorphism a minor factor in isoniazid resistance. Isoniazid 143-152 bromodomain containing 2 Homo sapiens 0-3 24467436-12 2014 NAT in Salmonella typhimurium supports carcinogen activation and NAT in mycobacteria metabolizes isoniazid with polymorphism a minor factor in isoniazid resistance. Isoniazid 143-152 bromodomain containing 2 Homo sapiens 65-68 24593909-3 2014 The major drug-metabolizing enzyme of isoniazid is N-acetyltransferase (NAT). Isoniazid 38-47 bromodomain containing 2 Homo sapiens 72-75 24467436-2 2014 The slow NAT phenotype increases susceptibility to hydralazine and isoniazid toxicity and to occupational bladder cancer. Isoniazid 67-76 bromodomain containing 2 Homo sapiens 9-12 18680474-7 2008 Arylamine N acetyltransferases (NAT) convert aromatic amines or hydrazines to aromatic amides and hydrazides. Isoniazid 98-108 bromodomain containing 2 Homo sapiens 32-35 18642144-10 2008 Genome analyses have identified NAT homologues in bacteria including Mycobacterium tuberculosis, in which the NAT enzyme metabolises inactivation of isoniazid. Isoniazid 149-158 bromodomain containing 2 Homo sapiens 32-35 18642144-10 2008 Genome analyses have identified NAT homologues in bacteria including Mycobacterium tuberculosis, in which the NAT enzyme metabolises inactivation of isoniazid. Isoniazid 149-158 bromodomain containing 2 Homo sapiens 110-113