The Use of Plasmapheresis in Treatment of Patients with Infertility, Peritoneal Endometriosis and Nat2 Gene Polymorphism [PDF]
It is known that 30–40 % of patients with peritoneal endometriosis suffer from infertility. Half of the patients with endometriosis are identified point mutation in NAT2 – gene, which plays an important role in the acetylation of aromatic and ...
Dubinskaya, E. (Ekaterina)+2 more
core +2 more sources
Alcohol consumption, tobacco smoking, and subsequent risk of renal cell carcinoma: The JPHC study
Abstract The effects of alcohol consumption and tobacco smoking on renal cell carcinoma (RCC) incidence have not been well‐investigated in Asian populations. Here, we evaluated these effects in a large Japanese prospective cohort. We collected data on eligible participants in the Japan Public Health Center‐based Prospective Study, and undertook ...
Tetsuji Minami+5 more
wiley +1 more source
Abstract The oral cavity is an entry path into the body, enabling the intake of nutrients but also leading to the ingestion of harmful substances. Thus, saliva and oral tissues contain enzyme systems that enable the early neutralization of xenobiotics as soon as they enter the body.
Mathieu Schwartz+6 more
wiley +1 more source
N-acetyltransferase 2 polymorphism in Parkinson's disease. The Rotterdam study [PDF]
The N-acetyltransferase-2 gene (NAT-2) has been associated with Parkinson's disease. The genotype associated with slow acetylation has been reported to be increased in patients with Parkinson's disease.
Breteler, M.M.B. (Monique)+5 more
core +5 more sources
Arylamine N-acetyltransferase 2 (NAT2) genetic diversity and traditional subsistence: a worldwide population survey. [PDF]
Arylamine N-acetyltransferase 2 (NAT2) is involved in human physiological responses to a variety of xenobiotic compounds, including common therapeutic drugs and exogenous chemicals present in the diet and the environment.
Audrey Sabbagh+3 more
doaj +1 more source
The role of lysine100 in the binding of acetylcoenzyme A to human arylamine N-acetyltransferase 1: Implications for other acetyltransferases [PDF]
The arylamine N-acetyltransferases (NATs) catalyze the acetylation of aromatic and heterocyclic amines as well as hydrazines. All proteins in this family of enzymes utilize acetyl coenzyme A (AcCoA) as an acetyl donor, which initially binds to the enzyme
Butcher, Neville J, Minchin, Rodney F
core +1 more source
The expression pattern of N‐acetyltransferase 1 in healthy human skin
Abstract Background N‐acetyltransferase 1 (NAT1) is an enzyme expressed among others in keratinocytes in human skin. NAT1 is important in the biotransformation of aromatic amines, an important example being p‐phenylenediamine (PPD), a hair dye molecule. Unoxidized PPD penetrates the skin and is N‐acetylated by NAT1.
Cynthia C. A. van Amerongen+3 more
wiley +1 more source
Biochemical Characterization of Arylamine N-acetyltransferases From Vibrio vulnificus [PDF]
Vibrio vulnificus is a zoonotic bacterium that is capable of causing highly lethal diseases in humans; this pathogen is responsible for 95% of all seafood-related deaths in the United States. Arylamine N-acetyltransferases (NAT, E.C. 2.3.1.5) is a major family of xenobiotic-metabolizing enzymes that can biotransform aromatic amine chemicals.
Xinning Liu+15 more
openaire +4 more sources
Comparative analysis of xenobiotic metabolising N-acetyltransferases from ten non-human primates as in vitro models of human homologues [PDF]
Xenobiotic metabolising N-acetyltransferases (NATs) perform biotransformation of drugs and carcinogens. Human NAT1 is associated with endogenous metabolic pathways of cells and is a candidate drug target for cancer.
Boukouvala, Sotiria+7 more
core +2 more sources
The Bacillus anthracis arylamine N-acetyltransferase ((BACAN)NAT1) that inactivates sulfamethoxazole, reveals unusual structural features compared with the other NAT isoenzymes [PDF]
Arylamine N-acetyltransferases (NATs) are xenobiotic-metabolizing enzymes that biotransform arylamine drugs. The Bacillus anthracis (BACAN)NAT1 enzyme affords increased resistance to the antibiotic sulfamethoxazole through its acetylation.
Dairou, Julien+6 more
core +1 more source