Associated Papers
Human N-acetyltransferase 2 (NAT2) gene variability in Brazilian populations from different geographical areas.
Lopes MQP et al.
Frontiers in Pharmacology, 2023
Humans and Chimpanzees Display Opposite Patterns of Diversity in Arylamine N-Acetyltransferase Genes.
Vangenot C et al.
G3 (bethesda, Md.), 2019
NAT2 polymorphisms and risk for Parkinson's disease: a systematic review and meta-analysis.
Jiménez-Jiménez FJ et al.
Expert Opinion on Drug Metabolism & Toxicology, 2016
Genetic variability in N-acetyltransferase 2 gene determines susceptibility to childhood lymphoid or myeloid leukemia in Brazil.
Zanrosso CW et al.
Leukemia & Lymphoma, 2012
Accuracy of various human NAT2 SNP genotyping panels to infer rapid, intermediate and slow acetylator phenotypes.
Hein DW et al.
Pharmacogenomics, 2012
Effects of single nucleotide polymorphisms on human N-acetyltransferase 2 structure and dynamics by molecular dynamics simulation.
Rajasekaran M et al.
Plos One, 2011
Interethnic diversity of NAT2 polymorphisms in Brazilian admixed populations.
Talbot J et al.
Bmc Genetics, 2010
Well-done meat consumption, NAT1 and NAT2 acetylator genotypes and prostate cancer risk: the multiethnic cohort study.
Sharma S et al.
Cancer Epidemiology, Biomarkers & Prevention : a Publication of the American Association for Cancer Research, Cosponsored by the American Society of Preventive Oncology, 2010
Sequence analysis of NAT2 gene in Brazilians: identification of undescribed single nucleotide polymorphisms and molecular modeling of the N-acetyltransferase 2 protein structure.
Teixeira RL et al.
Mutation Research, 2010
Comparison of genetic polymorphisms of the NAT2 gene between Korean and four other ethnic groups.
Kang TS et al.
Journal of Clinical Pharmacy and Therapeutics, 2009
N-acetyltransferase SNPs: emerging concepts serve as a paradigm for understanding complexities of personalized medicine.
Hein DW
Expert Opinion on Drug Metabolism & Toxicology, 2009
Genetic polymorphism in N-Acetyltransferase (NAT): Population distribution of NAT1 and NAT2 activity.
Walker K et al.
Journal of Toxicology and Environmental Health. Part B, Critical Reviews, 2009
Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2.
Walraven JM et al.
Current Drug Metabolism, 2008
Worldwide distribution of NAT2 diversity: implications for NAT2 evolutionary history.
Sabbagh A et al.
Bmc Genetics, 2008
Functional characterization of single-nucleotide polymorphisms and haplotypes of human N-acetyltransferase 2.
Zang Y et al.
Carcinogenesis, 2007
[Detection of mutation in NAT II gene as a method of determination of izoniazyd (INH) acetylation type in human population].
Augustynowicz-Kopeć E et al.
Pneumonologia I Alergologia Polska, 2007
Effects of single nucleotide polymorphisms in human N-acetyltransferase 2 on metabolic activation (O-acetylation) of heterocyclic amine carcinogens.
Hein DW et al.
International Journal of Cancer, 2006
Genetic basis of toxic reactions to drugs and chemicals.
Cascorbi I
Toxicology Letters, 2006
N-acetyltransferase 2 genetic polymorphism: effects of carcinogen and haplotype on urinary bladder cancer risk.
Hein DW
Oncogene, 2006
Restriction fragments length polymorphism in the NAT1 gene of Europeans in West Siberia.
Nikishina MV et al.
Bulletin of Experimental Biology and Medicine, 2003
NAT2 slow acetylation and GSTM1 null genotypes may increase postmenopausal breast cancer risk in long-term smoking women.
van der Hel OL et al.
Pharmacogenetics, 2003
N-acetyltransferase 1 and 2 genotypes do not predict response or toxicity to treatment with mesalamine and sulfasalazine in patients with ulcerative colitis.
Ricart E et al.
The American Journal of Gastroenterology, 2002
Analysis of six SNPs of NAT2 in Ngawbe and Embera Amerindians of Panama and determination of the Embera acetylation phenotype using caffeine.
Jorge-Nebert LF et al.
Pharmacogenetics, 2002
N-acetyltransferase polymorphisms and colorectal cancer: a HuGE review.
Brockton N et al.
American Journal of Epidemiology, 2000
Study of the role of the highly conserved residues Arg9 and Arg64 in the catalytic function of human N-acetyltransferases NAT1 and NAT2 by site-directed mutagenesis.
Deloménie C et al.
The Biochemical Journal, 1997
[Use of restriction endonucleases Bst2U I and Acc65 I to detect Kpn I polymorphism of NAT2 gene].
Nikishina MV et al.
Biomeditsinskaia Khimiia, 0