Arylamine N‐acetyltransferases: from drug metabolism and pharmacogenetics to drug discovery
Arylamine N‐acetyltransferases (NAT s) are polymorphic drug‐metabolizing enzymes,
acetylating arylamine carcinogens and drugs including hydralazine and sulphonamides …
acetylating arylamine carcinogens and drugs including hydralazine and sulphonamides …
PharmGKB summary: very important pharmacogene information for: N:-acetyltransferase 2
EM McDonagh, S Boukouvala, E Aklillu… - Pharmacogenetics …, 2014 - journals.lww.com
Background Function and expression Arylamine N-acetyltransferases (NATs) are
xenobioticmetabolizing enzymes for which three distinct enzymatic activities have been …
xenobioticmetabolizing enzymes for which three distinct enzymatic activities have been …
Fluorescence umpolung enables light-up sensing of N-acetyltransferases and nerve agents
Intramolecular charge transfer (ICT) is a fundamental mechanism that enables the
development of numerous fluorophores and probes for bioimaging and sensing. However …
development of numerous fluorophores and probes for bioimaging and sensing. However …
Genetic Polymorphism in N-Acetyltransferase (NAT): Population Distribution of NAT1 and NAT2 Activity
K Walker, G Ginsberg, D Hattis, DO Johns… - Journal of Toxicology …, 2009 - Taylor & Francis
N-Acetyltransferases (NAT) are key enzymes in the conjugation of certain drugs and other
xenobiotics with an arylamine structure. Polymorphisms in NAT2 have long been recognized …
xenobiotics with an arylamine structure. Polymorphisms in NAT2 have long been recognized …
Arylamine N-acetyltransferases: from structure to function
Arylamine N-acetyltransferases (NATs) are cytosolic conjugating enzymes which transfer an
acetyl group from acetylCoenzyme A to a xenobiotic acceptor substrate. The enzyme has an …
acetyl group from acetylCoenzyme A to a xenobiotic acceptor substrate. The enzyme has an …
N-acetyltransferase SNPs: emerging concepts serve as a paradigm for understanding complexities of personalized medicine
DW Hein - Expert opinion on drug metabolism & toxicology, 2009 - Taylor & Francis
Arylamine N-acetyltransferase 1 and 2 exhibit single nucleotide polymorphisms in human
populations that modify drug and carcinogen metabolism. This paper updates the identity …
populations that modify drug and carcinogen metabolism. This paper updates the identity …
Extrahepatic metabolism at the body's internal–external interfaces
U Gundert-Remy, U Bernauer, B Blömeke… - Drug metabolism …, 2014 - Taylor & Francis
In general, xenobiotic metabolizing enzymes (XMEs) are expressed in lower levels in the
extrahepatic tissues than in the liver, making the former less relevant for the clearance of …
extrahepatic tissues than in the liver, making the former less relevant for the clearance of …
Arylamine N-acetyltransferase acetylation polymorphisms: paradigm for pharmacogenomic-guided therapy-a focused review
DW Hein, LM Millner - Expert opinion on drug metabolism & …, 2021 - Taylor & Francis
Introduction The N-acetylation polymorphism has been the subject of comprehensive
reviews describing the role of arylamine N-acetyltransferase 2 (NAT2) in the metabolism of …
reviews describing the role of arylamine N-acetyltransferase 2 (NAT2) in the metabolism of …
Pharmacogenetic association between NAT2 gene polymorphisms and isoniazid induced hepatotoxicity: trial sequence meta-analysis as evidence
Hepatotoxicity is a severe problem generally faced by tuberculosis (TB) patients. It is a well-
known adverse reaction due to anti-TB drugs in TB patients undergoing long-term treatment …
known adverse reaction due to anti-TB drugs in TB patients undergoing long-term treatment …
Arylamine N-acetyltransferases–from drug metabolism and pharmacogenetics to identification of novel targets for pharmacological intervention
E Sim, G Fakis, N Laurieri, S Boukouvala - Advances in pharmacology, 2012 - Elsevier
Arylamine N-acetyltransferases (NATs) are defined as xenobiotic metabolizing enzymes,
adding an acetyl group from acetyl coenzyme A (CoA) to arylamines and arylhydrazines …
adding an acetyl group from acetyl coenzyme A (CoA) to arylamines and arylhydrazines …