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

10.1186/s12916-016-0575-9

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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
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1799562024-03-27T08:18:50Z Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance 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 MICROBIOLOGY AND IMMUNOLOGY aminosalicylic acid capreomycin ethambutol ethionamide isoniazid ofloxacin rifampicin streptomycin tuberculostatic agent bacterial protein isoniazid tuberculostatic agent 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 bacterial genome chemistry DNA sequence genetics genome-wide association study human isolation and purification metabolism microbial sensitivity test microbiology molecular model multidrug resistance mutation Mycobacterium tuberculosis 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 Mycobacterium tuberculosis Protein Conformation Sequence Analysis, DNA Tuberculosis, Multidrug-Resistant 10.1186/s12916-016-0575-9 BMC Medicine 14 1 31 2020-10-26T05:15:53Z 2020-10-26T05:15:53Z 2016 Article 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 (2016). Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance. BMC Medicine 14 (1) : 31. ScholarBank@NUS Repository. https://doi.org/10.1186/s12916-016-0575-9 17417015 https://scholarbank.nus.edu.sg/handle/10635/179956 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Unpaywall 20201031
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	aminosalicylic acid capreomycin ethambutol ethionamide isoniazid ofloxacin rifampicin streptomycin tuberculostatic agent bacterial protein isoniazid tuberculostatic agent 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 bacterial genome chemistry DNA sequence genetics genome-wide association study human isolation and purification metabolism microbial sensitivity test microbiology molecular model multidrug resistance mutation Mycobacterium tuberculosis 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 Mycobacterium tuberculosis Protein Conformation Sequence Analysis, DNA Tuberculosis, Multidrug-Resistant
spellingShingle	aminosalicylic acid capreomycin ethambutol ethionamide isoniazid ofloxacin rifampicin streptomycin tuberculostatic agent bacterial protein isoniazid tuberculostatic agent 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 bacterial genome chemistry DNA sequence genetics genome-wide association study human isolation and purification metabolism microbial sensitivity test microbiology molecular model multidrug resistance mutation Mycobacterium tuberculosis 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 Mycobacterium tuberculosis Protein Conformation Sequence Analysis, DNA Tuberculosis, Multidrug-Resistant 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 Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance
description	10.1186/s12916-016-0575-9
author2	MICROBIOLOGY AND IMMUNOLOGY
author_facet	MICROBIOLOGY AND IMMUNOLOGY 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
format	Article
author	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
author_sort	Phelan, J
title	Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance
title_short	Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance
title_full	Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance
title_fullStr	Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance
title_full_unstemmed	Mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance
title_sort	mycobacterium tuberculosis whole genome sequencing and protein structure modelling provides insights into anti-tuberculosis drug resistance
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/179956
_version_	1795301271625793536

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

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