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NAT2 encodes an enzyme that functions to both activate and deactivate arylamine and hydrazine drugs and carcinogens. Zusätzlich bieten wir Ihnen NAT2 Antikörper (67) und NAT2 Kits (1) und viele weitere Produktgruppen zu diesem Protein an.
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NAT2 (zeige SLC38A1 Proteine) polymorphism is not associated with passive smoking associated breast cancer risk.
NAT2 (zeige SLC38A1 Proteine) role in the metabolic detoxification of heterocyclic aromatic amines
hydralazine efficacy and safety could be improved by NAT2 (zeige SLC38A1 Proteine) genotype-dependent dosing strategies
Studied the association between N-acetyl transferase 2 (NAT2)genetic polymorphisms, environmental factors and risk factors in colon or rectal cancer.
There were significant differences in NAT2 (zeige SLC38A1 Proteine)(rs1799929, rs1799930) genotype or allele frequencies between the infertile and fertile groups and synergy effects of GSTP1 (zeige GSTP1 Proteine) and NAT2 (zeige SLC38A1 Proteine) polymorphisms might lead to significant increase of infertility risk.
The increased risk of prostate cancer was observed among individuals with the NAT2 (zeige SLC38A1 Proteine) slow acetylator phenotype
Genotyping of TB patients from south India for NAT2 gene polymorphism revealed that 58 per cent of the study population comprised slow acetylators. Two-hour INH concentrations differed significantly among the three genotypes.
Slow NAT2 (zeige SLC38A1 Proteine) acetylators demonstrated a significant association with risk of anti-tuberculosis drug-induced liver injury in Thai patients.
The present study demonstrated no association between NAT2 (zeige SLC38A1 Proteine) genotype and drug-induced hepatotoxicity in the north Indian patients with tuberculosis.
CYP3A4 (zeige CYP3A4 Proteine) expression and N-acetyl transferase 2 acetylator phenotype can better identify the patients with higher risk of adverse reactions and can facilitate the improvement of personalized clonazepam therapy and withdrawal regimen.
This study illustrated that deficiency of NAT1/2 decreases isoniazid (INH) acetylation, but increases the interactions of INH with endobiotics in the liver.
It was concluded that an acute colonic inflammation impairs the expression and function of NAT2 enzyme, thereby diminishing the capacity for 5-aminosalisylic acid metabolism by colonic mucosa.
Hyperhomocysteinemia-induced decrease of peroxynitrite level is associated with an increase of hepatic Nat2 isoform activity with a reversal effect of wine polyphenol extract supplementation.
Mouse NAT2 is likely to influence epigenetic gene control, particularly of its own locus, and this is consistent with recent evidence associating aberrant mouse Nat2/human NAT1 (zeige EIF4G2 Proteine) gene expression with certain developmental malformations and cancers.
Nat2 knockout mouse line demonstrates that different Nat2 isoforms have distinct functions with no compensatory expression, in Nat2 knockout animals, of the other isoforms.
Variation in capacity for acetylation of 4ABP and PABA resulting from endogenous murine NAT2 alleles is insufficient to affect 4ABP genotoxicity in liver.
Results suggest that peroxynitrite-dependent inactivation of NAT1 (zeige EIF4G2 Proteine) and 2 may contribute to muscle dysfunction by impairing the biotransformation activity of this key cellular defense enzyme system.
These ocular phenotypes and their association with Nat2 genotype indicate that the Nat2 locus may be responsible for the previously described microphthalmic Cat4 (zeige SLC7A4 Proteine) phenotype.
study reports the detailed expression of the Nat2 gene and encoded protein in mouse embryos
Mouse N-acetyltransferase-2 was produced as a recombinant protein and found to have a substrate specificity profile similar to human N-acetyltransferase type 1 (zeige NAT1 Proteine).
The study is the first to thoroughly characterize the properties of a polymorphic NAT isoenzyme in a non-human primate model.
This gene encodes an enzyme that functions to both activate and deactivate arylamine and hydrazine drugs and carcinogens. Polymorphisms in this gene are responsible for the N-acetylation polymorphism in which human populations segregate into rapid, intermediate, and slow acetylator phenotypes. Polymorphisms in this gene are also associated with higher incidences of cancer and drug toxicity. A second arylamine N-acetyltransferase gene (NAT1) is located near this gene (NAT2).
N-acetyltransferase type 2
, arylamide acetylase 2
, arylamine N-acetyltransferase 2
, lambda R-1
, polymorphic arylamine N-acetyltransferase
, N-acetyl transferase 2
, N-Acetyltransferase-2 (arylamine N-acetyltransferase)
, N-acetyltransferase 2 (arylamine N-acetyltransferase)
, Arylamide acetylase 2
, NAT2 15
, Polymorphic arylamine N-acetyltransferase
, arylamine N-acetyltransferase-2