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TNF Dually Mediates Resistance and Susceptibility to Mycobacteria via Mitochondrial Reactive Oxygen Species
Open accessAbstract
Tumor necrosis factor (TNF) constitutes a critical host defense against tuberculosis, but its excess is also implicated in tuberculosis pathogenesis in zebrafish and humans. Using the zebrafish, we elucidate the pathways by which TNF mediates tuberculosis pathogenesis. TNF excess induces mitochondrial reactive oxygen species (ROS) in infected macrophages through RIP1-RIP3-dependent pathways. While initially increasing macrophage microbicidal activity, ROS rapidly induce programmed necrosis (necroptosis) and release mycobacteria into the growth-permissive extracellular milieu. TNF-induced necroptosis occurs through two pathways: modulation of mitochondrial cyclophilin D, implicated in mitochondrial permeability transition pore formation, and acid sphingomyelinase-mediated ceramide production. Combined genetic blockade of cyclophilin D and acid sphingomyelinase renders the high TNF state hyperresistant by preventing macrophage necrosis while preserving increased microbicidal activity. Similarly, the cyclophilin D-inhibiting drug alisporivir and the acid sphingomyelinase-inactivating drug, desipramine, synergize to reverse susceptibility, suggesting the therapeutic potential of these orally active drugs against tuberculosis and possibly other TNF-mediated diseases.
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“Membrane-disrupting damage of mitochondria or opening of the mitochondrial permeability transition pore (mPTP) is necessary for matrix mtROS release into the cytosol [127,128,129,130,131].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [129]
In the citing paper
“matrix mtROS cannot escape from intact mitochondria, which was confirmed for isolated mitochondria as well as in cells [127,128,129].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [129]
In the citing paper
“The early effect of cytosolic mtROS released by the opened mPTP led to killing of Mtb, but later on it resulted in necroptosis of macrophages [129].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [129]
In the citing paper
“Priming with TNF, however, induced production of antibacterial matrix mtROS by two converging signaling pathways. Firstly, TNF mediated induction of matrix mtROS production by ryanoid-receptor-receptor-interacting serine/threonine-protein kinase 1 (RIPK1)-RIPK3-mediated calcium overload of mitochondria [257]. Secondly, since matrix mtROS cannot escape the matrix of intact mitochondria [127,128,129”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [129]
In the citing paper
“Mtb infection alone was not sufficient to increase total cellular ROS levels or to induce matrix mtROS production in zebrafish macrophages.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [129]
In the citing paper
“Moreover, from intact mitochondria matrix mtROS cannot reach the cytosol or other compartments [38,122,127,129,131,310].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [129]
In the citing paper
“The recent finding that Mø necroptosis impairs granuloma formation and compromises resistance to Mycobacteria infection in zebrafish supports this notion [174].”
From The Iron age of host–microbe interactions (2015) · cites this paper as [174]
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Citations
Cites
Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,131
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
Pyroptosis: host cell death and inflammation
Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,288
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Wang, L., Yan, J., Liu, W., Lei, X., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.031 · Cited by 2,698
Cho, Y., Challa, S., Moquin, D., Genga, R., Ray, T. D., Guildford, M., & Chan, F. K.-M. (2009) · Cell · doi:10.1016/j.cell.2009.05.037 · Cited by 2,435
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280
Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059
Holler, N., Zaru, R., Micheau, O., Thome, M., Attinger, A., Valitutti, S., Bodmer, J.-L., Schneider, P., Seed, B., & Tschopp, J. (2000) · Nature Immunology · doi:10.1038/82732 · Cited by 1,987
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1 of the 72 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Kim, 2010, NecroX as a novel class of mitochondrial reactive oxygen species and ONOO− scavenger, Arch. Pharm. Res., 33, 1813, 10.1007/s12272-010-1114-4 · DOI
Cited by
Sorted by citations
Items 101–200 of 592
Current translational potential and underlying molecular mechanisms of necroptosis
Molnár, T., Mázló, A., Tslaf, V., Szöllősi, A. G., Emri, G., & Koncz, G. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2094-z · Cited by 110
The role of lysosome in regulated necrosis
Alu, A., Han, X., Ma, X., Wu, M., Wei, Y., & Wei, X. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.07.003 · Cited by 109
Negatu, D. A., Gengenbacher, M., Dartois, V. A., & Dick, T. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.575586 · Cited by 108
The Tuberculous Granuloma and Preexisting Immunity
Cohen, S. B., Gern, B. H., & Urdahl, K. B. (2022) · Annual Review of Immunology · doi:10.1146/annurev-immunol-093019-125148 · Cited by 105
Programmed necrosis in microbial pathogenesis
Sridharan, H., & Upton, J. W. (2014) · Trends in Microbiology · doi:10.1016/j.tim.2014.01.005 · Cited by 103
Zhang, H., Ran, C., Teame, T., Ding, Q., Hoseinifar, S. H., Xie, M., Zhang, Z., Yang, Y., Olsen, R. E., Gatlin, D. M., et al. (2020) · Reviews in Fish Biology and Fisheries · doi:10.1007/s11160-020-09614-y · Cited by 102
Protection and pathology in TB: learning from the zebrafish model
Meijer, A. H. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-015-0522-4 · Cited by 103
Cell death at the cross roads of host-pathogen interaction in Mycobacterium tuberculosis infection
Mohareer, K., Asalla, S., & Banerjee, S. (2018) · Tuberculosis · doi:10.1016/j.tube.2018.09.007 · Cited by 99
CFTR Protects against Mycobacterium abscessus Infection by Fine-Tuning Host Oxidative Defenses
Bernut, A., Dupont, C., Ogryzko, N. V., Neyret, A., Herrmann, J., Floto, R. A., Renshaw, S. A., & Kremer, L. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.071 · Cited by 98
Deciphering the landscape of host barriers to Listeria monocytogenes infection
Zhang, T., Abel, S., Wiesch, P. A. Z., Sasabe, J., Davis, B. M., Higgins, D. E., & Waldor, M. K. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702077114 · Cited by 97
Regulation of necroptosis signaling and cell death by reactive oxygen species
Fulda, S. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0102 · Cited by 95
Liang, S., Song, Z., Wu, Y., Gao, Y., Gao, M., Liu, F., Wang, F., & Zhang, Y. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1701448 · Cited by 95
Comparative studies of Toll-like receptor signalling using zebrafish
Kanwal, Z., Wiegertjes, G. F., Veneman, W. J., Meijer, A. H., & Spaink, H. P. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.02.003 · Cited by 95
Khan, N. R., Lawlor, K. E., Murphy, J. M., & Vince, J. E. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.10.017 · Cited by 93
Singh, A. K., & Gupta, U. D. (2018) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_554_18 · Cited by 91
Grayfer, L., Hodgkinson, J. W., & Belosevic, M. (2013) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2013.08.003 · Cited by 98
Wu, Q., Kroon, P. A., Shao, H., Needs, P. W., & Yang, X. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b02420 · Cited by 91
Hoseinifar, S. H., Shakouri, M., Doan, H. V., Shafiei, S., Yousefi, M., Raeisi, M., Yousefi, S., Harikrishnan, R., & Reverter, M. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.02.006 · Cited by 90
Hattori, Y., Morita, D., Fujiwara, N., Mori, D., Nakamura, T., Harashima, H., Yamasaki, S., & Sugita, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.566489 · Cited by 87
Interaction of Mycobacterium tuberculosis with Host Cell Death PathwaysPreprint
Srinivasan, L., Ahlbrand, S. E., & Briken, V. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a022459 · Cited by 90
Reactive Oxygen Species: Not Omnipresent but Important in Many Locations
Herb, M., Gluschko, A., & Schramm, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.716406 · Cited by 93
Mitochondrial Reactive Oxygen Species in Infection and Immunity
Mukherjee, A., Ghosh, K. K., Chakrabortty, S., Gulyás, B. Z., Padmanabhan, P., & Ball, W. B. (2024) · Biomolecules · doi:10.3390/biom14060670 · Cited by 99
Dorhoi, A., & Kaufmann, S. H. E. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.10.002 · Cited by 90
Stutz, M. D., Ojaimi, S., Allison, C. C., Preston, S., Arandjelovic, P., Hildebrand, J. M., Sandow, J. J., Webb, A. I., Silke, J., Alexander, W. S., et al. (2017) · Cell Death and Differentiation · doi:10.1038/s41418-017-0031-1 · Cited by 85
Mycobacterium tuberculosis : Pathogenesis and therapeutic targets
Yang, J., Zhang, L., Qiao, W., & Luo, Y. (2023) · MedComm · doi:10.1002/mco2.353 · Cited by 91
Bcl-xL mediates RIPK3-dependent necrosis in M. tuberculosis-infected macrophages
Zhao, X., Khan, N., Gan, H. T., Tzelepis, F., Nishimura, T., Park, S.-Y., Divangahi, M., & Remold, H. G. (2017) · Mucosal Immunology · doi:10.1038/mi.2017.12 · Cited by 80
Metabolic tricks of cancer cells
Hönigová, K., Navrátil, J., Peltanová, B., Polanska, H. H., Raudenská, M., & Masařík, M. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188705 · Cited by 84
Carbon monoxide negatively regulates NLRP3 inflammasome activation in macrophages
Jung, S. S., Moon, J., Xu, J., Ifedigbo, E., Ryter, S. W., Choi, A. M. K., & Nakahira, K. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00400.2014 · Cited by 84
mTOR-regulated mitochondrial metabolism limits mycobacterium-induced cytotoxicity
Pagán, A. J., Lee, L. J., Edwards-Hicks, J., Moens, C. B., Tobin, D. M., Busch‐Nentwich, E. M., Pearce, E. L., & Ramakrishnan, L. (2022) · Cell · doi:10.1016/j.cell.2022.08.018 · Cited by 84
Self-citationImmune mechanisms of granuloma formation in sarcoidosis and tuberculosis
Weeratunga, P. N., Möller, D. R., & Ho, L. (2024) · Journal of Clinical Investigation · doi:10.1172/jci175264 · Cited by 78
Gaiha, G. D., McKim, K. J., Woods, M. W., Pertel, T., Rohrbach, J., Barteneva, N. S., Chin, C. R., Liu, D., Soghoian, D. Z., Cesa, K. T., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.12.011 · Cited by 76
Immune Vulnerability of Infants to Tuberculosis
Driessche, K. V., Persson, A., Marais, B. J., Fink, P. J., & Urdahl, K. B. (2013) · Clinical and Developmental Immunology · doi:10.1155/2013/781320 · Cited by 83
Lin, Z., Altaf, N., Li, C., Chen, M., Pan, L., Wang, D., Xie, L., Zheng, Y., Fu, H., Han, Y., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.05.023 · Cited by 73
Regulated necrosis, a proinflammatory cell death, potentially counteracts pathogenic infections
Zhang, G., Wang, J., Zhao, Z., Xin, T., Fan, X., Shen, Q., Raheem, A., Lee, C. R., Jiang, H., & Ding, J. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05066-3 · Cited by 75
Zumla, A. I., Rao, M., Dodoo, E., & Maeurer, M. J. (2016) · BMC Medicine · doi:10.1186/s12916-016-0635-1 · Cited by 73
Perspective for Precision Medicine for Tuberculosis
Lange, C. G., Aarnoutse, R. E., Chesov, D., van Crevel, R., Gillespie, S. H., Grobbel, H.-P., Kalsdorf, B., Kontsevaya, I., van Laarhoven, A., Nishiguchi, T., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.566608 · Cited by 70
Defining a Research Agenda to Address the Converging Epidemics of Tuberculosis and Diabetes
Ronacher, K., van Crevel, R., Critchley, J., Bremer, A. A., Schlesinger, L. S., Kapur, A., Basaraba, R. J., Kornfeld, H., & Restrepo, B. I. (2017) · CHEST Journal · doi:10.1016/j.chest.2017.02.032 · Cited by 72
The Zebrafish Guide to Tuberculosis Immunity and TreatmentPreprint
Ramakrishnan, L. (2013) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2013.78.023283 · Cited by 73
Self-citationUnderstanding and overcoming the barriers to T cell-mediated immunity against tuberculosis
Urdahl, K. B. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.10.003 · Cited by 70
Mitochondrial Mechanisms of Necroptosis in Liver Diseases
Xue, C., Gu, X., Li, G., Bao, Z., & Li, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010066 · Cited by 70
Host-Directed Therapies for Tuberculosis
Jeong, E.-K., Lee, H.-J., & Jung, Y. (2022) · Pathogens · doi:10.3390/pathogens11111291 · Cited by 74
Versatile myeloid cell subsets contribute to tuberculosis‐associated inflammation
Dorhoi, A., & Kaufmann, S. H. E. (2015) · European Journal of Immunology · doi:10.1002/eji.201545493 · Cited by 71
Cilfone, N. A., Ford, C. B., Marino, S., Mattila, J. T., Gideon, H. P., Flynn, J. L., Kirschner, D. E., & Linderman, J. J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400734 · Cited by 68
Mechanistic connections between mitochondrial biology and regulated cell death
Chipuk, J. E., Mohammed, J. N., Gelles, J. D., & Chen, Y. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.03.033 · Cited by 69
Redox signaling in innate immunity and inflammation: focus on macrophages and neutrophils
Braunstein, I., Motohashi, H., Dallenga, T. K., Schaible, U. E., & Benhar, M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.006 · Cited by 75
Gräb, J., Suárez, I., van Gumpel, E., Winter, S., Schreiber, F., Esser, A., Hölscher, C., Fritsch, M., Herb, M., Schramm, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08405-9 · Cited by 69
The potential role of necroptosis in clinical diseases (Review)
Dai, W., Cheng, J. Q., Leng, X., Hu, X., & Ao, Y. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.4922 · Cited by 70
Perspectives on antigen presenting cells in zebrafish
Lewis, K. L. T., Cid, N. D., & Traver, D. J. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.03.010 · Cited by 65
Lee, K. S., Jeong, J. S., Kim, S. R., Cho, S., Kolliputi, N., Ko, Y. H., Lee, K.-B., Park, S. C., Park, H. J., & Lee, Y. C. (2015) · Thorax · doi:10.1136/thoraxjnl-2015-207096 · Cited by 66
Tzelepis, F., Blagih, J., Khan, N., Gillard, J., Mendonca, L., Roy, D. G., Ma, E. H., Joubert, P., Jones, R. G., & Divangahi, M. (2018) · Science Immunology · doi:10.1126/sciimmunol.aar4135 · Cited by 65
Hawn, T. R., Shah, J. A., & Kalman, D. (2015) · Immunological Reviews · doi:10.1111/imr.12255 · Cited by 66
Amaral, E. P., Lasunskaia, E., & Lima, M. R. D. (2015) · Microbes and Infection · doi:10.1016/j.micinf.2015.09.005 · Cited by 70
Macrophage Heterogeneity in the Immunopathogenesis of Tuberculosis
Marakalala, M. J., Martínez, F. O., Plüddemann, A., & Gordon, S. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01028 · Cited by 68
In Vivo Imaging with Genetically Encoded Redox Biosensors
Kostyuk, A. I., Panova, A. S., Kokova, A. D., Kotova, D. A., Maltsev, D. I., Podgorny, O. V., Belousov, V. V., & Bilan, D. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218164 · Cited by 66
Virulence Factors of Mycobacterium tuberculosis as Modulators of Cell Death Mechanisms
Ramón‐Luing, L. A., Palacios, Y., Ruíz, A., Téllez-Navarrete, N. A., & Chávez‐Galán, L. (2023) · Pathogens · doi:10.3390/pathogens12060839 · Cited by 71
Hartig, E. I., Zhu, S., King, B. L., & Coffman, J. A. (2016) · Biology Open · doi:10.1242/bio.020065 · Cited by 66
Transmembrane TNF and Its Receptors TNFR1 and TNFR2 in Mycobacterial Infections
Ruíz, A., Palacios, Y., Garcia, I., & Chávez‐Galán, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115461 · Cited by 61
Lyu, J., Narum, D. E., Baldwin, S. L., Larsen, S. E., Bai, X., Griffith, D. E., Dartois, V. A., Naidoo, T., Steyn, A. J. C., Coler, R. N., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1427559 · Cited by 76
The Zebrafish Breathes New Life into the Study of Tuberculosis
Myllymäki, H., Bäuerlein, C. A., & Rämet, M. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00196 · Cited by 64
Interaction of Mycobacteria With Host Cell Inflammasomes
Rastogi, S., & Briken, V. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.791136 · Cited by 64
Wang, F., Zhou, F., Peng, J., Chen, H., Xie, J., Liu, C., Xiong, H., Chen, S., Xue, G., Zhou, X., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103072 · Cited by 62
Protein Thiol Redox Signaling in Monocytes and Macrophages
Short, J. D., Downs, K. P., Tavakoli, S., & Asmis, R. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6697 · Cited by 58
Modeling Infectious Diseases in the Context of a Developing Immune System
Masud, S., Torraca, V., & Meijer, A. H. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.10.006 · Cited by 59
A Common Variant in the Adaptor Mal Regulates Interferon Gamma Signaling
Cheallaigh, C. N., Sheedy, F. J., Harris, J., Muñoz‐Wolf, N., Lee, J., West, K., Pålsson‐McDermott, E. M., Smyth, A., Gleeson, L. E., Coleman, M. M., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.019 · Cited by 58
Srivastava, S., Battu, M. B., Khan, M. Z., Nandicoori, V. K., & Mukhopadhyay, S. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801143 · Cited by 58
Sullivan, C., Soos, B.-L., Millard, P. J., Kim, C. H., & King, B. L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.636623 · Cited by 57
Washington, M. N., Suh, G. K., Orozco, A. F., Sutton, M. N., Yang, H., Wang, Y., Mao, W., Millward, S. W., Ornelas, A., Atkinson, N., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.208 · Cited by 59
Hudock, T. A., Foreman, T. W., Bandyopadhyay, N., Gautam, U. S., Veatch, A. V., LoBato, D. N., Gentry, K. M., Golden, N., Cavigli, A., Mueller, M., et al. (2017) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2016-0239oc · Cited by 57
Jaisinghani, N., Dawa, S., Singh, K., Nandy, A., Menon, D., Bhandari, P. D., Khare, G., Tyagi, A. K., & Gandotra, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01490 · Cited by 58
Potentiation of P2RX7 as a host-directed strategy for control of mycobacterial infection
Matty, M. A., Knudsen-Palmer, D. R., Walton, E. M., Beerman, R. W., Cronan, M. R., Pyle, C. J., Hernandez, R. E., & Tobin, D. M. (2019) · eLife · doi:10.7554/elife.39123 · Cited by 59
Complex regulation of neutrophil-derived MMP-9 secretion in central nervous system tuberculosis
Ong, C. W. M., Pabisiak, P. J., Brilha, S., Singh, P., Roncaroli, F., Elkington, P. T., & Friedland, J. S. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0801-1 · Cited by 58
Septins restrict inflammation and protect zebrafish larvae from Shigella infection
Mazón, M. J., Willis, A. R., Torraca, V., Boucontet, L., Shenoy, A. R., Colucci‐Guyon, E., & Mostowy, S. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006467 · Cited by 58
Targeting immunometabolism in host defence against Mycobacterium tuberculosis
Sheedy, F. J., & Divangahi, M. (2020) · Immunology · doi:10.1111/imm.13276 · Cited by 62
Chen, L., Zhang, G., Li, G., Wang, W., Ge, Z., Yang, Y., He, X., Liu, Z., Zhang, Z., Mai, Q., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00547-3 · Cited by 60
Immunopathology in human tuberculosis
Scriba, T. J., Maseeme, M., Young, C., Taylor, L. J., & Leslie, A. J. (2024) · Science Immunology · doi:10.1126/sciimmunol.ado5951 · Cited by 57
TB: the Yin and Yang of lipid mediators
Tobin, D. M., & Ramakrishnan, L. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.06.007 · Cited by 57
Self-citationCLARITY and PACT-based imaging of adult zebrafish and mouse for whole-animal analysis of infections
Cronan, M. R., Rosenberg, A. F., Oehlers, S. H., Saelens, J. W., Sisk, D. M., Smith, K. L. J., Lee, S., & Tobin, D. M. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.021394 · Cited by 58
Stocks, C. J., Schembri, M. A., Sweet, M. J., & Kapétanovic, R. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.4ri0917-358r · Cited by 58
Proteomic analysis of necroptotic extracellular vesicles
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Metadata
- Authors
- Roca, F. J., & Ramakrishnan, L.
- Affiliations
- University of Washington (US)
- Corresponding author
- Ramakrishnan, Lalita
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2013-04
- Volume
- 153
- Issue
- 3
- Pages
- 521-534
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3790588
- OpenAlex
- W2129443010
- Cited by
- 592
- References
- 72
- Citations by year
- 2026: 26 · 2025: 38 · 2024: 47 · 2023: 32 · 2022: 45 · 2021: 54 · 2020: 59 · 2019: 36 · 2018: 37 · 2017: 43 · 2016: 45 · 2015: 48 · 2014: 60 · 2013: 22
- FWCI
- 42.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Hispana (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (DP1OD006782)
- National Institute of Allergy and Infectious Diseases (R01AI036396, R37AI054503)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- TNF-α, tuberculosis, mycobacteria, mitochondrial reactive oxygen species, necroptosis, cyclophilin D, mitochondrial permeability transition pore, acid sphingomyelinase, ceramide, macrophage microbicidal activity, alisporivir, desipramine, drug synergy, host-pathogen interaction, zebrafish model
- MeSH terms
- Peptidyl-Prolyl Isomerase F, Animals, Disease Models, Animal, Disease Susceptibility, Humans, Macrophages, Mitochondria, Mycobacterium, Necrosis, Tuberculosis, Zebrafish, Reactive Oxygen Species, Cyclophilins, Tumor Necrosis Factors, Receptor-Interacting Protein Serine-Threonine Kinases, Metabolic Networks and Pathways
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