Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance

• Main Authors: Phelan, J, Coll, F, McNerney, R, Ascher, D.B, Pires, D.E, Furnham, N, Coeck, N, Hill-Cawthorne, G.A, Nair, M.B, Mallard, K, Ramsay, A, Campino, S, Hibberd, M.L, Pain, A, Rigouts, L, Clark, T.G
• Other Authors: MICROBIOLOGY AND IMMUNOLOGY
• Format: Article
• Published: 2020
• Subjects: aminosalicylic acid; capreomycin; ethambutol; ethionamide; isoniazid; ofloxacin; rifampicin; streptomycin; tuberculostatic agent; bacterial protein; Article; bacterial gene; bacterial genome; bacterium isolate; binding site; controlled study; convergent evolution; drug efficacy; drug resistant tuberculosis; gene mutation; genetic association study; genetic polymorphism; minimum inhibitory concentration; Mycobacterium tuberculosis; nonhuman; patient care; protein stability; protein structure; tuberculosis control; whole genome sequencing; chemistry; DNA sequence; genetics; genome-wide association study; human; isolation and purification; metabolism; microbial sensitivity test; microbiology; molecular model; multidrug resistance; mutation; protein conformation; Tuberculosis, Multidrug-Resistant; Antitubercular Agents; Bacterial Proteins; Drug Resistance, Multiple, Bacterial; Genome, Bacterial; Genome-Wide Association Study; Humans; Isoniazid; Microbial Sensitivity Tests; Models, Molecular; Mutation; Protein Conformation; Sequence Analysis, DNA
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/179956
• Institution: National University of Singapore

10.1186/s12916-016-0575-9