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-Reference-Cited by-同舟云学术

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

Published:2018-07-18 Issue:11 Volume:57 Page:1458-1466
ISSN:0899-1987
Container-title:Molecular Carcinogenesis
language:en
Short-container-title:Molecular Carcinogenesis

Author:

Carlisle Samantha M.¹^ORCID,Trainor Patrick J.²,Doll Mark A.¹,Stepp Marcus W.¹,Klinge Carolyn M.³,Hein David W.¹^ORCID

Affiliation:

1. Department of Pharmacology and ToxicologyUniversity of Louisville School of MedicineLouisvilleKentucky

2. Division of Cardiovascular MedicineUniversity of Louisville School of MedicineLouisvilleKentucky

3. Department of Biochemistry and Molecular GeneticsUniversity of Louisville School of MedicineLouisvilleKentucky

Funder

U.S. Public Health Service

Publisher

Wiley

Subject

Cancer Research,Molecular Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/mc.22869

Reference35 articles.

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3. Metabolic activation and deactivation of arylamine carcinogens by recombinant human NAT1 and polymorphic NAT2 acetyltransferases

4. Folate-dependent hydrolysis of acetyl-coenzyme A by recombinant human and rodent arylamine N-acetyltransferases

5. From Arylamine N-Acetyltransferase to Folate-Dependent Acetyl CoA Hydrolase: Impact of Folic Acid on the Activity of (HUMAN)NAT1 and Its Homologue (MOUSE)NAT2

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