Lenaerts, A., Barry, C. E. 3rd & Dartois, V. Heterogeneity in tuberculosis pathology, microenvironments and therapeutic responses. Immunol. Rev. 264, 288–307 (2015).
Mishra, R., Yadav, V., Guha, M. & Singh, A. Heterogeneous host-pathogen encounters coordinate antibiotic resilience in mycobacterium tuberculosis. Trends Microbiol 29, 606–620 (2021).
Cadena, A. M., Fortune, S. M. & Flynn, J. L. Heterogeneity in tuberculosis. Nat. Rev. Immunol. 17, 691–702 (2017).
Liu, Y. et al. Immune activation of the host cell induces drug tolerance in Mycobacterium tuberculosis both in vitro and in vivo. J. Exp. Med 213, 809–825 (2016).
Huang, L., Nazarova, E. V., Tan, S., Liu, Y. & Russell, D. G. Growth of Mycobacterium tuberculosis in vivo segregates with host macrophage metabolism and ontogeny. J. Exp. Med 215, 1135–1152 (2018).
Pisu, D., Huang, L., Grenier, J. K. & Russell, D. G. Dual RNA-seq of Mtb-infected macrophages in vivo reveals ontologically distinct host-pathogen interactions. Cell Rep. 30, 335–350.e4 (2020).
Pisu, D. et al. Single cell analysis of M. tuberculosis phenotype and macrophage lineages in the infected lung. J. Exp. Med. 218,. e20210615 (2021).
Kalam, H. et al. Identification of host regulators of Mycobacterium tuberculosis phenotypes uncovers a role for the MMGT1-GPR156 lipid droplet axis in persistence. Cell Host Microbe 31, 978–992.e5 (2023).
Das, M. et al. Cysteine desulfurase (IscS)-mediated fine-tuning of bioenergetics and SUF expression prevents Mycobacterium tuberculosis hypervirulence. Sci. Adv. 9, eadh2858 (2023).
Anand, K. et al. Mycobacterium tuberculosis SufR responds to nitric oxide via its 4Fe-4S cluster and regulates Fe-S cluster biogenesis for persistence in mice. Redox Biol. 46, 102062 (2021).
Rutschmann, O., Toniolo, C. & McKinney, J. D. Preexisting heterogeneity of inducible nitric oxide synthase expression drives differential growth of Mycobacterium tuberculosis in macrophages. mBio 13, e0225122 (2022).
Sarathy, J. P. et al. Extreme drug tolerance of Mycobacterium tuberculosis in Caseum. Antimicrob. Agents Chemother. 62, e02266–e02317 (2018).
Hicks, N. D. et al. Clinically prevalent mutations in Mycobacterium tuberculosis alter propionate metabolism and mediate multidrug tolerance. Nat. Microbiol. 3, 1032–1042 (2018).
Muñoz-Elías, E. J. & McKinney, J. D. Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence. Nat. Med. 11, 638–644 (2005).
Safi, H. et al. Phase variation in Mycobacterium tuberculosis glpK produces transiently heritable drug tolerance. Proc. Natl Acad. Sci. 116, 19665–19674 (2019).
Sharma, A. et al. VapC21 Toxin contributes to drug-tolerance and interacts with non-cognate VapB32 antitoxin in Mycobacterium tuberculosis. Front. Microbiol. 11, 2037 (2020).
Singh, R., Barry, C. E. & Boshoff, H. I. M. The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 192, 1279–1291 (2010).
Tiwari, P. et al. MazF ribonucleases promote Mycobacterium tuberculosis drug tolerance and virulence in guinea pigs. Nat. Commun. 6, 6059 (2015).
Manina, G., Dhar, N. & McKinney, J. D. Stress and host immunity amplify Mycobacterium tuberculosis phenotypic heterogeneity and induce nongrowing metabolically active forms. Cell Host Microbe 17, 32–46 (2015).
Adams, K. N. et al. Drug tolerance in replicating mycobacteria mediated by a macrophage-induced efflux mechanism. Cell 145, 39–53 (2011).
Mishra, R. et al. Targeting redox heterogeneity to counteract drug tolerance in replicating Mycobacterium tuberculosis. Sci. Transl. Med. 11, eaaw6635 (2019).
Ufimtseva, E. G. & Eremeeva, N. I. Drug-tolerant Mycobacterium tuberculosis adopt different survival strategies in alveolar macrophages of patients with pulmonary tuberculosis. Int. J. Mol. Sci. 24, 14942 (2023).
Bhaskar, A. et al. Reengineering redox-sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection. PLoS Pathog. 10, e1003902 (2014).
Andreu, N. et al. Primary macrophages and J774 cells respond differently to infection with Mycobacterium tuberculosis. Sci. Rep. 7, 42225 (2017).
Rothchild, A. C. et al. Alveolar macrophages generate a noncanonical NRF2-driven transcriptional response to Mycobacterium tuberculosis in vivo. Sci. Immunol. 4, eaaw6693 (2019).
Ge, S. X., Jung, D. & Yao, R. ShinyGO: a graphical gene-set enrichment tool for animals and plants. Bioinformatics 36, 2628–2629 (2020).
Kuleshov, M. V. et al. Enrichr: a comprehensive gene set enrichment analysis web server 2016 update. Nucleic Acids Res. 44, W90–W97 (2016).
Keenan, A. B. et al. ChEA3: transcription factor enrichment analysis by orthogonal omics integration. Nucleic Acids Res. 47, W212–W224 (2019).
Waxman, E. A., Bach2 is a potent repressor of Nrf2-mediated antioxidant enzyme expression in dopaminergic neurons. Preprint at bioRxiv https://doi.org/10.1101/687590 (2019).
Tsukumo, S. et al. Bach2 maintains T cells in a naive state by suppressing effector memory-related genes. Proc. Natl Acad. Sci. USA 110, 10735–10740 (2013).
Mo, J. S. et al. Cellular energy stress induces AMPK-mediated regulation of YAP and the Hippo pathway. Nat. Cell Biol. 17, 500–510 (2015).
Wang, W. et al. AMPK modulates Hippo pathway activity to regulate energy homeostasis. Nat. Cell Biol. 17, 490–499 (2015).
Biswal, P., Sahu, M. R., Ahmad, M. H. & Mondal, A. C. The interplay between hippo signaling and mitochondrial metabolism: implications for cellular homeostasis and disease. Mitochondrion 76, 101885 (2024).
Dinkova-Kostova, A. T. & Abramov, A. Y. The emerging role of Nrf2 in mitochondrial function. Free Radic. Biol. Med. 88, 179–188 (2015).
Holmström, K. M. et al. Nrf2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration. Biol. Open 2, 761–770 (2013).
Kim, T. H. et al. NRF2 blockade suppresses colon tumor angiogenesis by inhibiting hypoxia-induced activation of HIF-1α. Cancer Res. 71, 2260–2275 (2011).
Cumming, B. M., Addicott, K. W., Adamson, J. H. & Steyn, A. J. Mycobacterium tuberculosis induces decelerated bioenergetic metabolism in human macrophages. Elife 7, e39169 (2018).
Chandra, P. et al. Inhibition of fatty acid oxidation promotes macrophage control of Mycobacterium tuberculosis. mBio 11, e01139–e01220 (2020).
Zotta, A. et al. Mitochondrial respiratory complex III sustains IL-10 production in activated macrophages and promotes tumor-mediated immune evasion. Sci. Adv. 11, eadq7307 (2025).
Murphy, M. ichaelP. How mitochondria produce reactive oxygen species. Biochem. J. 417, 1–13 (2008).
Roca, F. J., Whitworth, L. J., Prag, H. A., Murphy, M. P. & Ramakrishnan, L. Tumor necrosis factor induces pathogenic mitochondrial ROS in tuberculosis through reverse electron transport. Science 376, eabh2841 (2022).
Esteras, N. & Abramov, A. Y. Nrf2 as a regulator of mitochondrial function: Energy metabolism and beyond. Free Radic. Biol. Med. 189, 136–153 (2022).
Ryan, D. G. et al. Nrf2 activation reprograms macrophage intermediary metabolism and suppresses the type I interferon response. iScience 25, 103827 (2022).
Otsuki, A. et al. Unique cistrome defined as CsMBE is strictly required for Nrf2-sMaf heterodimer function in cytoprotection. Free Radic. Biol. Med. 91, 45–57 (2016).
Ren, X. et al. Overcoming the compensatory elevation of NRF2 renders hepatocellular carcinoma cells more vulnerable to disulfiram/copper-induced ferroptosis. Redox Biol. 46, 102122 (2021).
Li, Y. et al. Sorafenib induces mitochondrial dysfunction and exhibits synergistic effect with cysteine depletion by promoting HCC cells ferroptosis. Biochem Biophys. Res. Commun. 534, 877–884 (2021).
Dézsi, C. A. Trimetazidine in practice: review of the clinical and experimental evidence. Am. J. Ther. 23, e871–e879 (2016).
Shi, L., Jiang, Q., Bushkin, Y., Subbian, S. & Tyagi, S. Biphasic dynamics of macrophage immunometabolism during Mycobacterium tuberculosis infectionB. mBio 10, e02550–e02618 (2019).
Russell, D. G., Cardona, P. J., Kim, M. J., Allain, S. & Altare, F. Foamy macrophages and the progression of the human tuberculosis granuloma. Nat. Immunol. 10, 943–948 (2009).
Guerrini, V. et al. Storage lipid studies in tuberculosis reveal that foam cell biogenesis is disease-specific. PLoS Pathog. 14, e1007223 (2018).
McCommis, K. S. & Finck, B. N. Mitochondrial pyruvate transport: a historical perspective and future research directions. Biochem J. 466, 443–454 (2015).
Miyajima, H., Oda, T. & Ichiyama, A. Induction of mitochondrial serine: pyruvate aminotransferase of rat liver by glucagon and insulin through different mechanisms. J. Biochem 105, 500–504 (1989).
Martino, M. R. et al. Silencing alanine transaminase 2 in diabetic liver attenuates hyperglycemia by reducing gluconeogenesis from amino acids. Cell Rep. 39, 110733 (2022).
Höfler, S. et al. Dealing with the sulfur part of cysteine: four enzymatic steps degrade l-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria. Physiol. Plant. 157, 352–366 (2016).
Gohil, V. M. et al. Nutrient-sensitized screening for drugs that shift energy metabolism from mitochondrial respiration to glycolysis. Nat. Biotechnol. 28, 249–255 (2010).
Machado, C. M. et al. The galactose-induced decrease in phosphate levels leads to toxicity in yeast models of galactosemia. Biochim. Biophys. Acta (BBA) – Mol. Basis Dis. 1863, 1403–1409 (2017).
Gohil, V. M. et al. Meclizine inhibits mitochondrial respiration through direct targeting of cytosolic phosphoethanolamine metabolism. J. Biol. Chem. 288, 35387–35395 (2013).
Wai, T. & Langer, T. Mitochondrial dynamics and metabolic regulation. Trends Endocrinol. Metab. 27, 105–117 (2016).
Liesa, M. & Shirihai, O. S. Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure. Cell Metab. 17, 491–506 (2013).
Guido, C. Mitochondrial fission induces glycolytic reprogramming in cancer-associated myofibroblasts, driving stromal lactate production, and early tumor growth. Oncotarget 3, 798–810 (2012).
Suh, J. et al. Mitochondrial fragmentation and donut formation enhance mitochondrial secretion to promote osteogenesis. Cell Metab. 35, 345–360.e7 (2023).
Tan, S., Sukumar, N., Abramovitch, R. B., Parish, T. & Russell, D. G. Mycobacterium tuberculosis responds to chloride and pH as synergistic cues to the immune status of its host cell. PLoS Pathog. 9, e1003282 (2013).
Kramnik, I. & Beamer, G. Mouse models of human TB pathology: roles in the analysis of necrosis and the development of host-directed therapies. Semin. Immunopathol. 38, 221–237 (2016).
Singh, H., Sodhi, R. K., Chahal, S. K. & Madan, J. Meclizine ameliorates memory deficits in streptozotocin-induced experimental dementia in mice: role of nuclear pregnane X receptors. Can. J. Physiol. Pharmacol. 98, 383–390 (2020).
Wibble, T., Engstrom, J., Verrecchia, L. & Pansell, T. The effects of meclizine on motion sickness revisited. Br. J. Clin. Pharm. 86, 1510–1518 (2020).
Cohen, B. and J.M. DeJong, Meclizine and placebo in treating vertigo of vestibular origin. Relative efficacy in a double-blind study. Arch. Neurol. 27, 129–135 (1972).
Helaine, S., Conlon, B. P., Davis, K. M. & Russell, D. G. Host stress drives tolerance and persistence: the bane of anti-microbial therapeutics. Cell Host Microbe 32, 852–862 (2024).
Sakatos, A. et al. Posttranslational modification of a histone-like protein regulates phenotypic resistance to isoniazid in mycobacteria. Sci. Adv. 4, eaao1478 (2018).
Javid, B. et al. Mycobacterial mistranslation is necessary and sufficient for rifampicin phenotypic resistance. Proc. Natl Acad. Sci. USA 111, 1132–1137 (2014).
Rego, E. H., Audette, R. E. & Rubin, E. J. Deletion of a mycobacterial divisome factor collapses single-cell phenotypic heterogeneity. Nature 546, 153–157 (2017).
Aldridge, B. B. et al. Asymmetry and aging of mycobacterial cells lead to variable growth and antibiotic susceptibility. Science 335, 100–104 (2012).
Stapels, D. A. C. et al. Salmonella persisters undermine host immune defenses during antibiotic treatment. Science 362, 1156–1160 (2018).
Ronneau, S., Michaux, C. & Helaine, S. Decline in nitrosative stress drives antibiotic persister regrowth during infection. Cell Host Microbe 31, 993–1006.e6 (2023).
Bandyopadhyay, P. et al. S-Adenosylmethionine-responsive cystathionine beta-synthase modulates sulfur metabolism and redox balance in Mycobacterium tuberculosis. Sci. Adv. 8, eabo0097 (2022).
Shee, S. et al. Moxifloxacin-mediated killing of Mycobacterium tuberculosis involves respiratory downshift, reductive stress, and accumulation of reactive oxygen species. Antimicrob. Agents Chemother. 66, e0059222 (2022).
Ryu, K. W. et al. Cellular ATP demand creates metabolically distinct subpopulations of mitochondria. Nature 635, 746–754 (2024).
Chen, S., Ye, J. & Gu, Z. Mitochondrial heterogeneity: within and between cells. Mitochondrial Commun. 3, 52–53 (2025).
Dragotakes, Q. et al. Macrophages use a bet-hedging strategy for antimicrobial activity in phagolysosomal acidification. J. Clin. Invest. 130, 3805–3819 (2020).
Manina, G., Griego, A., Singh, L. K., McKinney, J. D. & Dhar, N. Preexisting variation in DNA damage response predicts the fate of single mycobacteria under stress. Embo J. 38, e101876 (2019).
Wakamoto, Y. et al. Dynamic persistence of antibiotic-stressed mycobacteria. Science 339, 91–95 (2013).
Gleeson, L. E. et al. Cutting edge: Mycobacterium tuberculosis induces aerobic glycolysis in human alveolar macrophages that is required for control of intracellular bacillary replication. J. Immunol. 196, 2444–2449 (2016).
Lachmandas, E. et al. Rewiring cellular metabolism via the AKT/mTOR pathway contributes to host defence against Mycobacterium tuberculosis in human and murine cells. Eur. J. Immunol. 46, 2574–2586 (2016).
Howard, N. C. & Khader, S. A. Immunometabolism during Mycobacterium tuberculosis Infection. Trends Microbiol. 28, 832–850 (2020).
Olson, G. S. et al. Type I interferon decreases macrophage energy metabolism during mycobacterial infection. Cell Rep. 35, 109195 (2021).
Tyagi, P. et al. Mycobacterium tuberculosis reactivates HIV-1 via exosome-mediated resetting of cellular redox potential and bioenergetics. mBio 11, e03293–e03319 (2020).
Kelly, D. M., ten Bokum, A. M., O’Leary, S. M., O’Sullivan, M. P. & Keane, J. Bystander macrophage apoptosis after Mycobacterium tuberculosis H37Ra infection. Infect. Immun. 76, 351–360 (2008).
Macdonald, S. H. F. et al. Networked T cell death following macrophage infection by Mycobacterium tuberculosis. PLOS ONE 7, e38488 (2012).
Haas, R. et al. Intermediates of metabolism: from bystanders to signalling molecules. Trends Biochem. Sci. 41, 460–471 (2016).
Leisching, G. & Keane, J. Bystander macrophage metabolic shift after Mycobacterium tuberculosis infection. Am. J. Respir. Cell Mol. Biol. 63, 863–865 (2020).
Shi, L. et al. Infection with Mycobacterium tuberculosis induces the Warburg effect in mouse lungs. Sci. Rep. 5, 18176 (2015).
Subbian, S. et al. Lesion-specific immune response in granulomas of patients with pulmonary tuberculosis: a pilot study. PLoS ONE 10, e0132249 (2015).
Braverman, J., Sogi, K. M., Benjamin, D., Nomura, D. K. & Stanley, S. A. HIF-1alpha Is an essential mediator of IFN-gamma-dependent immunity to mycobacterium tuberculosis. J. Immunol. 197, 1287–1297 (2016).
Marin Franco, J. L. et al. Host-derived lipids from tuberculous pleurisy impair macrophage microbicidal-associated metabolic activity. Cell Rep. 33, 108547 (2020).
Lastrucci, C. et al. Tuberculosis is associated with expansion of a motile, permissive and immunomodulatory CD16(+) monocyte population via the IL-10/STAT3 axis. Cell Res. 25, 1333–1351 (2015).
Garaude, J. et al. Mitochondrial respiratory-chain adaptations in macrophages contribute to antibacterial host defense. Nat. Immunol. 17, 1037–1045 (2016).
Geng, J. et al. Kinases Mst1 and Mst2 positively regulate phagocytic induction of reactive oxygen species and bactericidal activity. Nat. Immunol. 16, 1142–1152 (2015).
Wang, P. et al. Macrophage achieves self-protection against oxidative stress-induced ageing through the Mst-Nrf2 axis. Nat. Commun. 10, 755 (2019).
Qian, Z. et al. Expression of nuclear factor, erythroid 2-like 2-mediated genes differentiates tuberculosis. Tuberculosis 99, 56–62 (2016).
Gatbonton-Schwager, T. N., Sadhukhan, S., Zhang, G. F., Letterio, J. J. & Tochtrop, G. P. Identification of a negative feedback loop in biological oxidant formation fegulated by 4-hydroxy-2-(E)-nonenal. Redox Biol. 2, 755–763 (2014).
Ashino, T. et al. Negative feedback regulation of lipopolysaccharide-induced inducible nitric oxide synthase gene expression by heme oxygenase-1 induction in macrophages. Mol. Immunol. 45, 2106–2115 (2008).
Lewerenz, J. et al. The cystine/glutamate antiporter system x(c)(-) in health and disease: from molecular mechanisms to novel therapeutic opportunities. Antioxid. Redox Signal. 18, 522–555 (2013).
Vilcheze, C. & Jacobs, W. R. The promises and limitations of N-acetylcysteine as a potentiator of first-line and second-line tuberculosis drugs. Antimicrob Agents Chemother. 65, e01703–e01820 (2023).
Zhou, J. et al. Activation of Nrf2 modulates protective immunity against Mycobacterium tuberculosis infection in THP1-derived macrophages. Free Radic. Biol. Med. 193, 177–189 (2022).
Yabaji, S. M. et al. Peroxiredoxin-1 of macrophage is critical for mycobacterial infection and is controlled by early secretory antigenic target protein through the activation of p38 MAPK. Biochem. Biophys. Res. Commun. 494, 433–439 (2017).
Bates, T. A. et al. ESAT-6 undergoes self-association at phagosomal pH and an ESAT-6 specific nanobody restricts M. tuberculosis growth in macrophages. eLife (Sciences Publications, Ltd, 2019).
De Leon, J. et al. Mycobacterium tuberculosis ESAT-6 exhibits a unique membrane-interacting activity that is not found in its ortholog from non-pathogenic Mycobacterium smegmatis. J. Biol. Chem. 287, 44184–44191 (2012).
Beam, J. E. et al. The use of acute immunosuppressive therapy to improve antibiotic efficacy against intracellular staphylococcus aureus. Microbiol. Spectr. 10, e0085822 (2022).
Finkel, T. Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7–15 (2011).
Sinenko, S. A., Starkova, T. Y., Kuzmin, A. A. & Tomilin, A. N. Physiological signaling functions of reactive oxygen species in stem cells: from flies to man. Front. Cell Dev. Biol. 9, 714370 (2021).
Bonnet, S. et al. A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth. Cancer Cell 11, 37–51 (2007).
Chen, Q., Camara, A. K., Stowe, D. F., Hoppel, C. L. & Lesnefsky, E. J. Modulation of electron transport protects cardiac mitochondria and decreases myocardial injury during ischemia and reperfusion. Am. J. Physiol. Cell Physiol. 292, C137–C147 (2007).
Piantadosi, C. A. & Zhang, J. Mitochondrial generation of reactive oxygen species after brain ischemia in the rat. Stroke 27, 327–331 (1996).
Padmapriydarsini, C. et al. Randomized trial of metformin with anti-tuberculosis drugs for early sputum conversion in adults with pulmonary tuberculosis. Clin. Infect. Dis. 75, 425–434 (2022).
Hong, C. T., Chau, K. Y. & Schapira, A. H. Meclizine-induced enhanced glycolysis is neuroprotective in Parkinson disease cell models. Sci. Rep. 6, 25344 (2016).
Gohil, V. M. et al. Meclizine is neuroprotective in models of Huntington’s disease. Hum. Mol. Genet. 20, 294–300 (2011).
Lione, A. & Scialli, A. R. The developmental toxicity of the H1 histamine antagonists. Reprod. Toxicol. 10, 247–255 (1996).
Giurgea, M. & Puigdevall, J. Experimental teratology with Meclozine. Med. Pharm. Exp. Int J. Exp. Med. 15, 375–388 (1966).
Chandra, P., Grigsby, S. J. & Philips, J. A. Immune evasion and provocation by Mycobacterium tuberculosis. Nat. Rev. Microbiol. 20, 750–766 (2022).
Gern, B. H. et al. TGFbeta restricts the expansion, survival, and function of T cells within the tuberculous granuloma. Cell Host Microbe 29, 594–606.e6 (2021).
Gautam, U. S. et al. In vivo inhibition of tryptophan catabolism reorganizes the tuberculoma and augments immune-mediated control of Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 115, E62–E71 (2018).
Cronan, M. R. et al. Macrophage epithelial reprogramming underlies mycobacterial granuloma formation and promotes infection. Immunity 45, 861–876 (2016).
Guler, R. et al. Targeting molecular inflammatory pathways in granuloma as host-directed therapies for tuberculosis. Front. Immunol. 12, 733853 (2021).
Putri, G. H., Anders, S., Pyl, P. T., Pimanda, J. E. & Zanini, F. Analysing high-throughput sequencing data in Python with HTSeq 2.0. Bioinformatics 38, 2943–2945 (2022).
Love, M. I., Huber, W. & Anders, S. Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2. Genome Biol. 15, 550 (2014).
Liberzon, A. et al. Molecular signatures database (MSigDB) 3.0. Bioinformatics 27, 1739–1740 (2011).
Martinez, F. O., Gordon, S., Locati, M. & Mantovani, A. Transcriptional profiling of the human monocyte-to-macrophage differentiation and polarization: new molecules and patterns of gene expression. J. Immunol. 177, 7303–7311 (2006).
Fang, Z., Liu, X. & Peltz, G. GSEApy: a comprehensive package for performing gene set enrichment analysis in Python. Bioinformatics 39, btac757 (2023).
Walvekar, A., Rashida, Z., Maddali, H. & Laxman, S. A versatile LC-MS/MS approach for comprehensive, quantitative analysis of central metabolic pathways. Wellcome Open Res. 3, 122 (2018).
Robinson, M. D., McCarthy, D. J. & Smyth, G. K. edgeR: a Bioconductor package for differential expression analysis of digital gene expression data. Bioinformatics 26, 139–140 (2010).
Khan, M. Z. et al. Protein kinase G confers survival advantage to Mycobacterium tuberculosis during latency-like conditions. J. Biol. Chem. 292, 16093–16108 (2017).
Jain, R. et al. Enhanced and enduring protection against tuberculosis by recombinant BCG-Ag85C and its association with modulation of cytokine profile in lung. PLoS ONE 3, e3869 (2008).
Dutta, N. K., Pinn, M. L. & Karakousis, P. C. Reduced emergence of isoniazid resistance with concurrent use of thioridazine against acute murine tuberculosis. Antimicrob. Agents Chemother. 58, 4048–4053 (2014).