Results 21 to 30 of about 17,361 (234)

CRISPR/Cas9 knockout of human arylamine N-acetyltransferase 1 in MDA-MB-231 breast cancer cells suggests a role in cellular metabolism. [PDF]

Sci Rep, 2020
Human arylamine N-acetyltransferase 1 (NAT1), present in all tissues, is classically described as a phase-II xenobiotic metabolizing enzyme but can also catalyze the hydrolysis of acetyl-Coenzyme A (acetyl-CoA) in the absence of an arylamine substrate ...
Carlisle SM, Trainor PJ, Hong KU, Doll MA, Hein DW.   +4 more
europepmc   +2 more sources

Small Molecule Inhibitors of Arylamine N-Acetyltransferase 1 Attenuate Cellular Respiration. [PDF]

ACS Pharmacol Transl Sci
Arylamine N-acetyltransferase 1 (NAT1) expression has been shown to attenuate mitochondrial function, suggesting it is a promising drug target in diseases of mitochondrial dysfunction.
Choudhury C, Egleton JE, Butcher NJ, Russell AJ, Minchin RF.   +4 more
europepmc   +2 more sources

Transcriptional Regulation of Human Arylamine N-Acetyltransferase 2 Gene by Glucose and Insulin in Liver Cancer Cell Lines. [PDF]

Toxicol Sci, 2022
Hong KU, Salazar-González RA, Walls KM, Hein DW.   +3 more
europepmc   +2 more sources

Identification and characterization of potent, selective, and efficacious inhibitors of human arylamine N-acetyltransferase 1. [PDF]

Arch Toxicol, 2022
Leggett CS, Doll MA, Salazar-González RA, Habil MR, Trent JO, Hein DW.   +5 more
europepmc   +2 more sources

Functional expression of human arylamine N-acetyltransferase NAT1*10 and NAT1*11 alleles: a mini review. [PDF]

Pharmacogenet Genomics, 2018
The arylamine N-acetyltransferase (NAT) nomenclature committee assigns functional phenotypes for human arylamine N-acetyltransferase 1 (NAT1) alleles in those instances in which the committee determined a consensus has been achieved in the scientific ...
Hein DW, Fakis G, Boukouvala S.
europepmc   +2 more sources

A pilot study of the modulation of sirtuins on arylamine N-acetyltransferase 1 and 2 enzymatic activity [PDF]

Acta Pharmaceutica Sinica B, 2018
Arylamine N-acetyltransferase (NAT; E.C. 2.3.1.5) enzymes are responsible for the biotransformation of several arylamine and hydrazine drugs by acetylation.
Eneida Turiján-Espinoza, Rául Alejandro Salazar-González, Edith Elena Uresti-Rivera, Gloria Estela Hernández-Hernández, Montserrat Ortega-Juárez, Rosa Milán, Diana Portales-Pérez   +6 more
doaj   +2 more sources

Mechanism by which arylamine N-acetyltransferase 1 ablation causes insulin resistance in mice. [PDF]

Proc Natl Acad Sci U S A, 2017
Significance Insulin resistance in liver and skeletal muscle are major factors in the pathogenesis of type 2 diabetes; however, the molecular mechanism or mechanisms responsible for this phenomenon have not been established. Recently, an association of a
Camporez JP, Wang Y, Faarkrog K, Chukijrungroat N, Petersen KF, Shulman GI.   +5 more
europepmc   +2 more sources

Arylamine N-acetyltransferase 2 (NAT2) genetic diversity and traditional subsistence: a worldwide population survey. [PDF]

PLoS ONE, 2011
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, Pierre Darlu, Brigitte Crouau-Roy, Estella S Poloni   +3 more
doaj   +2 more sources

Deletion of arylamine N-acetyltransferase 1 in MDA-MB-231 human breast cancer cells reduces primary and secondary tumor growth in vivo with no significant effects on metastasis. [PDF]

Mol Carcinog, 2022
Doll MA, Ray AR, Salazar-González RA, Shah PP, Vega AA, Sears SM, Krueger AM, Hong KU, Beverly LJ, Hein DW.   +9 more
europepmc   +2 more sources

Knockout of human arylamine N-acetyltransferase 1 (NAT1) in MDA-MB-231 breast cancer cells leads to increased reserve capacity, maximum mitochondrial capacity, and glycolytic reserve capacity. [PDF]

Mol Carcinog, 2018
Human arylamine N‐acetyltransferase 1 (NAT1) is a phase II xenobiotic metabolizing enzyme found in almost all tissues. NAT1 can also hydrolyze acetyl‐coenzyme A (acetyl‐CoA) in the absence of an arylamine substrate.
Carlisle SM, Trainor PJ, Doll MA, Stepp MW, Klinge CM, Hein DW.   +5 more
europepmc   +2 more sources