Role of Mutations in Dihydrofolate Reductase DfrA (Rv2763c) and Thymidylate Synthase ThyA (Rv2764c) in Mycobacterium tuberculosis Drug Resistance
Author:
Affiliation:
1. Department of Genetics University of Cambridge Cambridge, United Kingdom
2. Computational Bioscience Research Center King Abdullah University of Science and Technology Thuwal, Kingdom of Saudi Arabia
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Link
https://journals.asm.org/doi/pdf/10.1128/AAC.00422-10
Reference35 articles.
1. Argyrou, A., M. Vetting, B. Aladegbami, and J. Blanchard. 2006. Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid. Nat. Struct. Mol. Biol.13:408-413.
2. Baca, A., R. Sirawaraporn, S. Turley, W. Sirawaraporn, and W. Hol. 2000. Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action. J. Mol. Biol.302:1193-1212.
3. Besier, S., A. Ludwig, K. Ohlsen, V. Brade, and T. Wichelhaus. 2007. Molecular analysis of the thymidine-auxotrophic small colony variant phenotype of Staphylococcus aureus. Int. J. Med. Microbiol.297:217-225.
4. The Thymidine-Dependent Small-Colony-Variant Phenotype Is Associated with Hypermutability and Antibiotic Resistance in Clinical Staphylococcus aureus Isolates
5. In Vivo Mutations of Thymidylate Synthase (Encoded by thyA ) Are Responsible for Thymidine Dependency in Clinical Small-Colony Variants of Staphylococcus aureus
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