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Transcriptional Adaptation of Mycobacterium tuberculosis within Macrophages
Open accessAbstract
Little is known about the biochemical environment in phagosomes harboring an infectious agent. To assess the state of this organelle we captured the transcriptional responses of Mycobacterium tuberculosis (MTB) in macrophages from wild-type and nitric oxide (NO) synthase 2–deficient mice before and after immunologic activation. The intraphagosomal transcriptome was compared with the transcriptome of MTB in standard broth culture and during growth in diverse conditions designed to simulate features of the phagosomal environment. Genes expressed differentially as a consequence of intraphagosomal residence included an interferon γ– and NO-induced response that intensifies an iron-scavenging program, converts the microbe from aerobic to anaerobic respiration, and induces a dormancy regulon. Induction of genes involved in the activation and β-oxidation of fatty acids indicated that fatty acids furnish carbon and energy. Induction of σE-dependent, sodium dodecyl sulfate–regulated genes and genes involved in mycolic acid modification pointed to damage and repair of the cell envelope. Sentinel genes within the intraphagosomal transcriptome were induced similarly by MTB in the lungs of mice. The microbial transcriptome thus served as a bioprobe of the MTB phagosomal environment, showing it to be nitrosative, oxidative, functionally hypoxic, carbohydrate poor, and capable of perturbing the pathogen's cell envelope.
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“Several studies have reported that nuo is down-regulated in M. tuberculosis during mouse lung infection (18), survival in macrophages (19), in both non-replicating persistence (NRP)-1 (1% oxygen saturation) and NRP-2 (0.06% oxygen saturation) relative to aerated mid-log growth (18), and upon starvation in vitro (20).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“In contrast, fumarate reductase, nitrate reductase and NDH-2 are all upregulated under these conditions (19).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“Transcriptional analysis of M. tuberculosis in the macrophage (phagosomal environment) has revealed that NDH-1, menaquinol-cytochrome c oxidoreductase and the ATP synthase are all down-regulated when compared to cells growing exponentially, suggesting that there is a reduced need for energy generation during bacteriostasis i.e., the growth state of intraphagosomal M. tuberculosis (19).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“In M. tuberculosis, the atp operon is downregulated during growth in macrophages (19), the mouse lung and in cells exposed to NO or hypoxia (18).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [19]
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“the fight of the host against the pathogen in M. tuberculosis infection involves several levels including containment of the microbe, generation of radicals and a hostile, acidic environment, deprivation from essential nutrients, formation of anti-mycobacterial peptides and cytokines which strengthen host responses by attracting other immune cells, down to cell damage and suicidal activities of MO”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [5]
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“Accordingly, transcriptional analysis of macrophages and M. tuberculosis has demonstrated that Mycobacteria regulate a myriad of genes to secure a sufficient supply of iron within the cell, whereas macrophages aim to restrict the availability of this metal by different mechanisms (5).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [5]
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Cites
In silico prediction of protein-protein interactions in human macrophages
Souiai, O., Guerfali, F. Z., Miled, S. B., Brun, C., & Benkahla, A. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-157 · Cited by 10,785
Significance analysis of microarrays applied to the ionizing radiation response
Tusher, V. G., Tibshirani, R., & Chu, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091062498 · Cited by 10,568
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Mechanisms of phagocytosis in macrophages
Aderem, A., & Underhill, D. M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.593 · Cited by 2,854
Escherichia coli and Salmonella.
Neidhart, F. C. (1996) · Cited by 1,577
Common themes in microbial pathogenicity revisited
Finlay, B. B., & Falkow, S. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.2.136-169.1997 · Cited by 1,474
Nathan, C., & Shiloh, M. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8841 · Cited by 1,469
Self-citationBetts, J. C., Lukey, P. T., Robb, L. C., McAdam, R. A., & Duncan, K. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02779.x · Cited by 1,395
McKinney, J. D., zu Bentrup, K. H., Muñoz‐Elías, E. J., Miczák, A., Chen, B., Chan, W.-T., Swenson, D. L., Sacchettini, J. C., Jacobs, W. R., & Russell, D. G. (2000) · Nature · doi:10.1038/35021074 · Cited by 1,361
Flynn, J., & Chan, J. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.19.1.93 · Cited by 1,144
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Research works printed but not linked: 1
- 1997, Microbiol. Mol. Biol. Rev., 61, 136
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Sorted by citations
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Bonde, B. K., Beste, D. J. V., Laing, E., Kierzek, A. M., & McFadden, J. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002060 · Cited by 22
Luo, X., Li, L., Xi, J., Liu, H., Liu, Z., Long, Y., & Tang, P. (2022) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14781 · Cited by 24
D’Halluin, A., Polgar, P., Kipkorir, T., Patel, Z., Cortes, T., & Arnvig, K. B. (2023) · iScience · doi:10.1016/j.isci.2023.106465 · Cited by 34
Tuberculosis: from genome to vaccine
de Jonge, M. I., Brosch, R., Brodin, P. M., Demangel, C., & Cole, S. T. (2005) · Expert Review of Vaccines · doi:10.1586/14760584.4.4.541 · Cited by 22
Pettersson, B. M. F., Das, S., Behra, P. R. K., Jordan, H. R., Ramesh, M., Mallick, A., Root, K. M., Cheramie, M. N., Melara, I. D. L. C., Small, P. L. C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139823 · Cited by 22
Lu, R., Schaefer, C. M., Nesbitt, N. M., Kuper, J., Kisker, C., & Sampson, N. S. (2017) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00072 · Cited by 22
Adams, K. N., Verma, A. K., Gopalaswamy, R., Adikesavalu, H., Singhal, D. K., Tripathy, S. P., Ranganathan, U. D., Sherman, D. R., Urdahl, K. B., Ramakrishnan, L., et al. (2019) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiy710 · Cited by 22
Functioning of Mycobacterial Heat Shock Repressors Requires the Master Virulence Regulator PhoP
Sevalkar, R. R., Arora, D., Singh, P. R., Singh, R. K., Nandicoori, V. K., Karthikeyan, S., & Sarkar, D. (2019) · Journal of Bacteriology · doi:10.1128/jb.00013-19 · Cited by 22
Introduction: Novel insights into TB research and drug discovery
Grüber, G. (2020) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2020.02.003 · Cited by 22
Shi, L., Sohaskey, C. D., North, R. J., & Gennaro, M. L. (2007) · Tuberculosis · doi:10.1016/j.tube.2007.08.007 · Cited by 22
Virulence insights from the Paracoccidioides brasiliensis transcriptome.
Tavares, A. H., Titze-de-Almeida, S. S., Bernardes, V. V., Maranhão, A. Q., Kyaw, C. M., Poças-Fonseca, M. J., & Silva-Pereira, I. (2005) · PubMed · Cited by 21
Fu, L., & Tai, S. C. (2009) · International Journal of Microbiology · doi:10.1155/2009/879621 · Cited by 22
Ewer, K., Cockle, P. J., Gordon, S., Mansoor, H., Govaerts, M., Walravens, K., Marché, S., Hewinson, R. G., & Vordermeier, M. H. (2006) · Clinical and Vaccine Immunology · doi:10.1128/cvi.13.1.90-97.2006 · Cited by 22
Yang, D., He, X., Li, S., Liu, J., Stabenow, J. M., Zalduondo, L., White, S. W., & Kong, Y. (2019) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiz169 · Cited by 19
Aulicino, A., Antanaviciute, A., Frost, J. N., Gerós, A. S., Mellado-Gomez, E., Attar, M., Jagielowicz, M., Hublitz, P., Sinz, J., Preciado‐Llanes, L., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03038-z · Cited by 21
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Nikitushkin, V. D., Shleeva, M. O., Loginov, D. S., Dyčka, F., Štěrba, J., & Kaprelyants, A. S. (2022) · PLoS ONE · doi:10.1371/journal.pone.0269847 · Cited by 20
Khan, H., Paul, P., Sevalkar, R. R., Kachhap, S., Singh, B., & Sarkar, D. (2022) · eLife · doi:10.7554/elife.80965 · Cited by 20
Mycobacterium avium subspecies paratuberculosis
Li, L.-L., Singh, S. V., Bannantine, J. P., Kanjilal, S., & Kapur, V. (2008) · Springer eBooks · doi:10.1007/978-3-540-74042-1_2 · Cited by 21
Cossu, A., Sechi, L. A., Bandino, E., Zanetti, S., & Rosu, V. (2013) · Microbial Pathogenesis · doi:10.1016/j.micpath.2013.10.004 · Cited by 21
Distribution and function of prophage phiRv1 and phiRv2 amongMycobacterium tuberculosiscomplex
Fan, X., Alla, A. A. E. A., & Xie, J. (2015) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2015.1022602 · Cited by 21
Nathan, C. (2008) · Science · doi:10.1126/science.1167452 · Cited by 21
Self-citationDrug targeting of heme proteins in Mycobacterium tuberculosis
McLean, K. J., & Munro, A. W. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.11.004 · Cited by 21
Li, F., Kang, H., Li, J., Zhang, D., Zhang, Y., Dannenberg, A. M., Liu, X., Niu, H., Ma, L., Tang, R., et al. (2017) · Scandinavian Journal of Immunology · doi:10.1111/sji.12556 · Cited by 21
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Islam, M. N., Hitchings, R., Kumar, S., Fontes, F. L., Lott, J. S., Kruh‐Garcia, N. A., & Crick, D. C. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.8b00092 · Cited by 21
SAR Analysis of Small Molecules Interfering with Energy-Metabolism in Mycobacterium tuberculosis
Appetecchia, F., Consalvi, S., Scarpecci, C., Biava, M., & Poce, G. (2020) · Pharmaceuticals · doi:10.3390/ph13090227 · Cited by 21
Mycobacterium tuberculosis lpdC, Rv0462, induces dendritic cell maturation and Th1 polarization
Heo, D. R., Shin, S. J., Kim, W. S., Noh, K. T., Park, J. W., Son, K. H., Park, W. S., Lee, M.-G., Kim, D., Shin, Y. K., et al. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.07.013 · Cited by 21
A case for passive immunoprophylaxis against tuberculosis
Reljić, R., & Iványi, J. (2006) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(06)70658-2 · Cited by 21
Bukka, A., Price, C. T. D., Kernodle, D. S., & Graham, J. E. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00266 · Cited by 21
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Yeware, A. M., Shurpali, K., Athalye, M. C., & Sarkar, D. M. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00105 · Cited by 21
van der Klugt, T. T., van den Biggelaar, R. H. G. A., & Saris, A. (2024) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2024.2370979 · Cited by 22
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Chiarelli, L. R., Salina, E. G., Mori, G., Azhikina, T. L., Riabova, O., Lepioshkin, A., Grigorov, A., Forbak, M., Madacki, J., Orena, B. S., et al. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00388 · Cited by 21
Growing and Handling of Mycobacterium tuberculosis for Macrophage Infection Assays
Nazarova, E. V., & Russell, D. G. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6581-6_22 · Cited by 20
Dual control of RegX3 transcriptional activity by SenX3 and PknB
Park, E., Kwon, Y. M., Lee, J., Kang, H.-Y., & Oh, J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008232 · Cited by 21
Dunlap, M. D., Prince, O. A., Rangel‐Moreno, J., Thomas, K. A., Scordo, J. M., Torrelles, J. B., Cox, J. S., Steyn, A. J. C., Zúñiga, J., Kaushal, D., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01325 · Cited by 20
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Kruh‐Garcia, N. A., Borgaro, J. G., Ruzsicska, B. P., Xu, H., & Tonge, P. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802169200 · Cited by 20
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McKinney, J. D., & Gomez, J. E. (2003) · Nature Medicine · doi:10.1038/nm1103-1356 · Cited by 20
Singh, D. K., Ahmed, M., Akter, S., Shivanna, V., Bucşan, A. N., Mishra, A., Golden, N., Didier, P. J., Doyle‐Meyers, L. A., Hall-Ursone, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57090-4 · Cited by 20
Kaku, T., Kawamura, I., Uchiyama, R., Kurenuma, T., & Mitsuyama, M. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00838.x · Cited by 19
Larsson, M., Lerm, M., Ängeby, K., Nordvall, M. J., Juréen, P., & Schön, T. (2014) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2014.08.015 · Cited by 19
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Ansari, M. Y., Batra, S. D., Ojha, H., Dhiman, K., Ganguly, A., Tyagi, J. S., & Mande, S. C. (2020) · FEBS Letters · doi:10.1002/1873-3468.13906 · Cited by 20
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Cornejo‐Granados, F., López-Leal, G., Mata‐Espinosa, D., Barrios‐Payán, J., Marquina‐Castillo, B., Equihua-Medina, E., Zatarain-Barrón, Z. L., Molina-Romero, C., Hernández‐Pando, R., & Ochoa‐Leyva, A. (2021) · Biology · doi:10.3390/biology10090848 · Cited by 21
López-Agudelo, V. A., Baena, A., Enriquez, V. P. B., Cabarcas, F., Álzate, J. F., Beste, D. J. V., Ríos‐Estepa, R., & Barrera, L. F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031803 · Cited by 20
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Birhanu, A. G., Gómez-Muñoz, M., Kalayou, S., Riaz, T., Lutter, T., Yimer, S. A., Abebe, M., & Tønjum, T. (2022) · ACS Omega · doi:10.1021/acsomega.1c05923 · Cited by 18
Mali, S. N., Thorat, B. R., Wagh, R. R., & Yamgar, R. (2022) · Current Computer - Aided Drug Design · doi:10.2174/1573409918666220610162158 · Cited by 19
Das, M., Sreedharan, S., Shee, S., Malhotra, N., Nandy, M., Banerjee, U., Kohli, S., Rajmani, R. S., Chandra, N. R., Seshasayee, A. S. N., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh2858 · Cited by 17
Roles of Lipolytic enzymes in Mycobacterium tuberculosis pathogenesis
Lin, H., Xing, J., Wang, H., Wang, S., Ren, F., Li, X., Li, Z., & Song, N. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1329715 · Cited by 19
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Buján, N., Hernández‐Haro, C., Monteoliva, L., Gil, C., & Magariños, B. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.05.008 · Cited by 19
Rudra, P., Prajapati, R. K., Banerjee, R., Sengupta, S., & Mukhopadhyay, J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv516 · Cited by 19
Haniu, A. E. C. J., Maricato, J. T., Mathias, P. P. M., Castilho, D. G., Miguel, R. B., Monteiro, H. P., Puccia, R., & Batista, W. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069590 · Cited by 19
Defelipe, L. A., Porto, D. F. D., Ramos, P. I. P., Nicolás, M., Sosa, E. J., Radusky, L., Lanzarotti, E., Turjanski, A. G., & Marti, M. A. (2015) · Tuberculosis · doi:10.1016/j.tube.2015.11.009 · Cited by 19
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Calder, B., Albeldas, C., Blackburn, J. M., & Soares, N. C. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00141 · Cited by 20
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Ganji, R., Dhali, S., Rizvi, A., Rapole, S., & Banerjee, S. (2016) · Scientific Reports · doi:10.1038/srep22060 · Cited by 19
Garcia, B. J., Loxton, A. G., Dolganov, G., Van, T. T., Davis, J. L., de Jong, B. C., Voskuil, M. I., Leach, S. M., Schoolnik, G. K., Walzl, G., et al. (2016) · Tuberculosis · doi:10.1016/j.tube.2016.07.004 · Cited by 19
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Walter, N. D., de Jong, B. C., Garcia, B. J., Dolganov, G., Worodria, W. O., Byanyima, P., Musisi, E., Huang, L., Chan, E. D., Vân, T. T. T., et al. (2016) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiw364 · Cited by 19
Self-citationBoot, M., Commandeur, S., Subudhi, A. K., Bahira, M., Smith, T. C., Abdallah, A. M., van Gemert, M., Lelièvre, J., Ballell, L., Aldridge, B. B., et al. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00083-18 · Cited by 19
Sun, X. L., Zhang, L., Jiang, J. H., Ng, M. C. W., Cui, Z., Mai, J., Ahn, S. K., Liu, J., Zhang, J., Liu, J., et al. (2018) · Virulence · doi:10.1080/21505594.2018.1514237 · Cited by 21
Clemmensen, H. S., Dubé, J.-Y., McIntosh, F. A., Rosenkrands, I., Jungersen, G., Aagaard, C., Andersen, P. L., Behr, M. A., & Mortensen, R. J. (2021) · mBio · doi:10.1128/mbio.00226-21 · Cited by 19
Verma, A., Kaur, M., Singh, L. V., Aggarwal, D., Verma, I., Radotra, B. D., & Sharma, S. (2021) · Scientific Reports · doi:10.1038/s41598-021-99257-1 · Cited by 19
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Gample, S. P., Agrawal, S., & Sarkar, D. M. (2019) · Scientific Reports · doi:10.1038/s41598-019-45652-8 · Cited by 19
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Li, Q., Ge, F., Tan, Y., Zhang, G., & Li, W. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050689 · Cited by 18
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Quezada, L. A. L., Smith, R. L., Lupoli, T. J., Edoo, Z., Li, X., Gold, B. S., Roberts, J., Ling, Y., Park, S. W., Nguyen, Q., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01248 · Cited by 18
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Immunology ofMycobacterium tuberculosisInfections
Sia, J. K., & Rengarajan, J. (2019) · ASM Press eBooks · doi:10.1128/9781683670131.ch64 · Cited by 22
Wang, Y., Kendall, J. J., Cavet, J. S., & Giedroc, D. P. (2010) · Biochemistry · doi:10.1021/bi100490u · Cited by 18
Sundaramurthi, J. C., Brindha, S., Shobitha, S. R., Swathi, A., Ramanandan, P., & Hanna, L. E. (2012) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2012.03.023 · Cited by 18
Arun, P. V. P. S., Miryala, S. K., Rana, A., Kurukuti, S., Akhter, Y., & Yellaboina, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-22884-8 · Cited by 18
A low-carb diet for a high-octane pathogen
Boshoff, H. I., & Barry, C. E. (2005) · Nature Medicine · doi:10.1038/nm0605-599 · Cited by 18
Vandal, O. H., Gelb, M. H., Ehrt, S., & Nathan, C. (2006) · Infection and Immunity · doi:10.1128/iai.74.3.1751-1756.2006 · Cited by 18
Self-citationKalam, H., Chou, C., Kadoki, M., Graham, D. B., Deguine, J., Hung, D. T., & Xavier, R. J. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.05.009 · Cited by 17
Ocampo, M., Patarroyo, M. A., Vanegas, M., Alba, M. P., & Patarroyo, M. E. (2013) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2013.763221 · Cited by 17
Isaza, J. P., Duque, C., Gomez, V., Robledo, J., Barrera, L. F., & Álzate, J. F. (2012) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2012.02540.x · Cited by 17
Systems biology approaches to understanding mycobacterial survival mechanisms
Boshoff, H. I., & Lun, D. S. (2010) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2010.09.008 · Cited by 17
Tiwari, P., Gosain, T. P., Singh, M., Sankhe, G. D., Arora, G., Kidwai, S., Agarwal, S., Chugh, S., Saini, D. K., & Singh, R. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008370 · Cited by 17
RetractedNienaber, L., Cave‐Freeman, E., Cross, M., Mason, L., Bailey, U., Amani, P., Davis, R. A., Taylor, P., & Hofmann, A. (2015) · FEBS Journal · doi:10.1111/febs.13313 · Cited by 17
Shleeva, M. O., Salina, E. G., & Kaprelyants, A. S. (2010) · Microbiology · doi:10.1134/s0026261710010017 · Cited by 18
The role of DNA repair in M. tuberculosis pathogenesis
Warner, D. F. (2010) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2010.08.002 · Cited by 17
Mukherjee, R., & Chatterji, D. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2007.08.009 · Cited by 17
Alanine dehydrogenases in mycobacteria
Jeong, J.-A., & Oh, J. (2019) · The Journal of Microbiology · doi:10.1007/s12275-019-8543-7 · Cited by 17
The many and varied niches occupied by Yersinia pestis as an arthropod-vectored zoonotic pathogen
Oyston, P. C. F., & Isherwood, K. E. (2005) · Antonie van Leeuwenhoek · doi:10.1007/s10482-004-4619-3 · Cited by 17
Parandhaman, D. K., Sharma, P., Bisht, D., & Narayanan, S. (2014) · Life Sciences · doi:10.1016/j.lfs.2014.06.013 · Cited by 16
Moopanar, K. R., Nyide, A. N. G., Senzani, S., & Mvubu, N. E. (2022) · Pathogens and Disease · doi:10.1093/femspd/ftac046 · Cited by 19
Tools to develop antibiotic combinations that target drug tolerance in Mycobacterium tuberculosis
Greenstein, T., & Aldridge, B. B. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1085946 · Cited by 17
Stealing Survival: Iron Acquisition Strategies of Mycobacterium tuberculosis.
Shankar, G., & Akhter, Y. (2024) · Biochimie · doi:10.1016/j.biochi.2024.06.006 · Cited by 12
Longo, B. M., Trunfio, M., & Calcagno, A. (2024) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkae288 · Cited by 16
Perrone, F., Siena, B. D., Muscariello, L., Kendall, S. L., Waddell, S. J., & Sacco, M. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02039 · Cited by 16
Metadata
- Authors
- Schnappinger, D., Ehrt, S., Voskuil, M. I., Liu, Y., Mangan, J. A., Monahan, I. M., Dolganov, G., Efron, B., Butcher, P. D., Nathan, C., & Schoolnik, G. K.
- Affiliations
- Cornell University (US)
- 3Department of Microbiology and Immunology, Weill Medical College and Graduate Programs in
- Stanford Medicine (US)
- St George's, University of London (GB)
- University of California, San Francisco (US)
- Stanford University (US)
- Corresponding author
- Schnappinger, Dirk
- ORCID
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2003-09-01
- Volume
- 198
- Issue
- 5
- Pages
- 693-704
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2194186
- OpenAlex
- W2007097682
- Cited by
- 1,420
- References
- 58
- Citations by year
- 2026: 26 · 2025: 35 · 2024: 46 · 2023: 32 · 2022: 55 · 2021: 41 · 2020: 37 · 2019: 68 · 2018: 63 · 2017: 65 · 2016: 61 · 2015: 96 · 2014: 90 · 2013: 75 · 2012: 96
- FWCI
- 31.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- St George's Online Research Archive (St George's University of London) (acceptedVersion)
- Funders
- Hearst Foundations
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Defense Advanced Research Projects Agency
- Advanced Research Projects Agency
- Medical Research Council
- National Heart, Lung, and Blood Institute (R01HL068525, HL 61241, HL68525, R01HL061241)
- National Institute of Allergy and Infectious Diseases (R01AI044826, AI-44826)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Mycobacterium tuberculosis, macrophages, nitric oxide synthase 2, interferon-gamma, iron scavenging, anaerobic respiration, fatty acid beta-oxidation, sigma E, cell envelope damage, hypoxia, nitrosative stress, tuberculosis pathogenesis
- MeSH terms
- Animals, Macrophages, Mycobacterium tuberculosis, Phagosomes, RNA, Bacterial, Transcription, Genetic, Gene Expression Regulation, Bacterial, Mice
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