The DOI matches its Crossref record; 71 of the 72 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
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
Reactive oxygen species and mitochondria: A nexus of cellular homeostasis
Dunn, J. D., Álvarez, L., Zhang, X., & Soldati, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.005 · Cited by 1,233
Linkermann, A., & Green, D. R. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1310050 · Cited by 1,103
Necroptosis in development, inflammation and disease
Weinlich, R., Oberst, A., Beere, H. M., & Green, D. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.149 · Cited by 1,016
Macrophage defense mechanisms against intracellular bacteria
Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989
TNF and ROS crosstalk in inflammation
Blaser, H., Dostert, C., Mak, T. W., & Brenner, D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.002 · Cited by 1,008
Host-directed therapies for bacterial and viral infections
Kaufmann, S. H. E., Dorhoi, A., Hotchkiss, R. S., & Bartenschlager, R. F. W. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.162 · Cited by 869
Necroptosis: a regulated inflammatory mode of cell death
Dhuriya, Y. K., & Sharma, D. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1235-0 · Cited by 752
The Function of Fish Cytokines
Zou, J., & Secombes, C. J. (2016) · Biology · doi:10.3390/biology5020023 · Cited by 722
ROS and diseases: role in metabolism and energy supply
Yang, S., & Lian, G. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03667-9 · Cited by 689
Functions of ROS in Macrophages and Antimicrobial Immunity
Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633
Immune evasion and provocation by Mycobacterium tuberculosis
Chandra, P., Grigsby, S. J., & Philips, J. A. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00763-4 · Cited by 652
Zhang, Y., Su, S. S., Zhao, S., Yang, Z., Zhong, C., Chen, X., Cai, Q., Yang, Z.-H., Huang, D., Wu, R., et al. (2017) · Nature Communications · doi:10.1038/ncomms14329 · Cited by 609
Are Reactive Oxygen Species Always Detrimental to Pathogens?
Paiva, C. N., & Bozza, M. T. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5447 · Cited by 577
Tuberculosis and lung damage: from epidemiology to pathophysiology
Ravimohan, S., Kornfeld, H., Weissman, D., & Bisson, G. P. (2018) · European Respiratory Review · doi:10.1183/16000617.0077-2017 · Cited by 580
Turning 21: Induction of miR-21 as a Key Switch in the Inflammatory Response
Sheedy, F. J. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00019 · Cited by 496
Tuberculous meningitis: more questions, still too few answers
Thwaites, G. E., van Toorn, R., & Schoeman, J. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70168-6 · Cited by 482
Glover, H. L., Schreiner, A., Dewson, G., & Tait, S. W. G. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01429-4 · Cited by 515
The Formation and Function of Granulomas
Pagán, A. J., & Ramakrishnan, L. (2018) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-100022 · Cited by 450
Self-citationHost Evasion and Exploitation Schemes of Mycobacterium tuberculosis
Cambier, C. J., Falkow, S., & Ramakrishnan, L. (2014) · Cell · doi:10.1016/j.cell.2014.11.024 · Cited by 454
Self-citationMacrophages and Iron Metabolism
Soares, M. P., & Hamza, I. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.016 · Cited by 401
Necroptosis Drives Motor Neuron Death in Models of Both Sporadic and Familial ALS
Ré, D. B., Verche, V. L., Yu, C., Amoroso, M. W., Politi, K. A., Phani, S., Ikiz, B., Hoffmann, L., Koolen, M., Nagata, T., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.011 · Cited by 421
Mitochondrial ROS promotes susceptibility to infection via gasdermin D-mediated necroptosis
Weindel, C. G., Martinez, E. L., Zhao, X. L., Mabry, C. J., Bell, S. L., Vail, K. J., Coleman, A. K., VanPortfliet, J. J., Zhao, B., Wagner, A. R., et al. (2022) · Cell · doi:10.1016/j.cell.2022.06.038 · Cited by 404
TNFR1 and TNFR2 in the Control of the Life and Death Balance of Macrophages
Wajant, H., & Siegmund, D. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00091 · Cited by 415
Pathogenesis of HIV-1 and Mycobacterium tuberculosis co-infection
Bell, L. C. K., & Noursadeghi, M. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.128 · Cited by 416
Tuberculosis and HIV Coinfection: Table 1.Preprint
Bruchfeld, J., Correia‐Neves, M., & Källenius, G. (2015) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a017871 · Cited by 379
Programmed necrotic cell death of macrophages: Focus on pyroptosis, necroptosis, and parthanatos
Robinson, N., Ganesan, R., Hegedűs, C., Kovács, K. É., Kufer, T. A., & Virág, L. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101239 · Cited by 375
Hodgson, K., Morris, J. L., Bridson, T. L., Govan, B., Rush, C. M., & Ketheesan, N. (2014) · Immunology · doi:10.1111/imm.12394 · Cited by 375
Programmed Necrosis in the Cross Talk of Cell Death and Inflammation
Chan, F. K.-M., Luz, N. F., & Moriwaki, K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112248 · Cited by 359
Sakai, S., Kauffman, K. D., Sallin, M. A., Sharpe, A. H., Young, H. A., Ganusov, V. V., & Barber, D. L. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005667 · Cited by 349
New insights into the evasion of host innate immunity by Mycobacterium tuberculosis
Chai, Q., Wang, L., Liu, C. H., & Ge, B. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0502-z · Cited by 347
Inflammatory signaling in human tuberculosis granulomas is spatially organized
Marakalala, M. J., Raju, R. M., Sharma, K., Zhang, Y. J., Eugenín, E. A., Prideaux, B., Daudelin, I. B., Chen, P., Booty, M. G., Kim, J. H., et al. (2016) · Nature Medicine · doi:10.1038/nm.4073 · Cited by 315
Khan, N., Downey, J., Sanz, J., Kaufmann, E., Blankenhaus, B., Pacis, A., Pernet, E., Ahmed, E. A., Cardoso, S., Nijnik, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.062 · Cited by 306
Regulated Cell Death: Signaling and Mechanisms
Ashkenazi, A., & Salvesen, G. S. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013226 · Cited by 289
Hall, C. J., Boyle, R. H., Astin, J. W., Flores, M. V., Oehlers, S. H., Sanderson, L. E., Ellett, F., Lieschke, G. J., Crosier, K. E., & Crosier, P. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.06.018 · Cited by 266
Stanley, S. A., Barczak, A. K., Silvis, M. R., Luo, S. S., Sogi, K., Vokes, M., Bray, M.-A., Carpenter, A. E., Moore, C. B., Siddiqi, N., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003946 · Cited by 251
Kumar, M., Sahu, S. K., Kumar, R., Subuddhi, A., Maji, R. K., Jana, K., Gupta, P., Raffetseder, J., Lerm, M., Ghosh, Z., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.01.007 · Cited by 259
Reactive oxygen species regulate Smac mimetic/TNFα-induced necroptotic signaling and cell death
Schenk, B., & Fulda, S. (2015) · Oncogene · doi:10.1038/onc.2015.35 · Cited by 235
Roca, F. J., Whitworth, L. J., Redmond, S., Jones, A. A., & Ramakrishnan, L. (2019) · Cell · doi:10.1016/j.cell.2019.08.004 · Cited by 233
Self-citationThe Iron age of host–microbe interactions
Soares, M. P., & Weiss, G. (2015) · The EMBO Reports · doi:10.15252/embr.201540558 · Cited by 227
Dorhoi, A., Yeremeev, V., Nouailles, G., Weiner, J. M., Jörg, S., Heinemann, E., Oberbeck‐Müller, D., Knaul, J. K., Vogelzang, A., Reece, S. T., et al. (2014) · European Journal of Immunology · doi:10.1002/eji.201344219 · Cited by 239
Progress in tuberculosis vaccine development and host-directed therapies—a state of the art review
Kaufmann, S. H. E., Lange, C. G., Rao, M., Balaji, K. N., Lotze, M. T., Schito, M. L., Zumla, A. I., & Maeurer, M. J. (2014) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(14)70033-5 · Cited by 219
The double-edged functions of necroptosis
Ye, K., Chen, Z., & Xu, Y. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05691-6 · Cited by 239
Kim, S. R., Kim, D. I., Kim, S. H., Lee, H. J., Lee, K. S., Cho, S., & Lee, Y. C. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.460 · Cited by 209
Therapeutic host-directed strategies to improve outcome in tuberculosis
Young, C., Walzl, G., & du Plessis, N. (2019) · Mucosal Immunology · doi:10.1038/s41385-019-0226-5 · Cited by 202
The Innate Immune Response to Mycobacterium tuberculosis Infection
Ravesloot-Chávez, M. M., Dis, E. S. V., & Stanley, S. A. (2021) · Annual Review of Immunology · doi:10.1146/annurev-immunol-093019-010426 · Cited by 213
B cells and antibodies in the defense against M ycobacterium tuberculosis infection
Achkar, J. M., Chan, J., & Casadevall, A. (2015) · Immunological Reviews · doi:10.1111/imr.12276 · Cited by 207
Zebrafish models in translational research: tipping the scales toward advancements in human health
Phillips, J. B., & Westerfield, M. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.015545 · Cited by 206
Pajuelo, D., González-Juarbe, N., Tak, U., Sun, J., Orihuela, C. J., & Niederweis, M. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.042 · Cited by 191
Flipping the dogma – phosphatidylserine in non-apoptotic cell death
Shlomovitz, I., Speir, M., & Gerlic, M. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0437-0 · Cited by 189
Molecular Determinants in Phagocyte-Bacteria Interactions
Kaufmann, S. H. E., & Dorhoi, A. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.014 · Cited by 196
Feedback regulation via AMPK and HIF-1 mediates ROS-dependent longevity in Caenorhabditis elegans
Hwang, A. B., Ryu, E.-A., Artan, M., Chang, H., Kabir, M. H., Nam, H.-J., Lee, D.-Y., Yang, J., Kim, S., Mair, W. B., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411199111 · Cited by 196
Sirt3 promotes antimycobacterial defenses by coordinating mitochondrial and autophagic functions
Kim, T. S., Jin, Y. B., Kim, Y. S., Kim, S., Kim, J. K., Lee, H.-M., Suh, H.-W., Choe, J. H., Kim, Y. J., Koo, B.-S., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1582743 · Cited by 172
Immunity and Immunopathology in the Tuberculous GranulomaPreprint
Pagán, A. J., & Ramakrishnan, L. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a018499 · Cited by 189
Self-citationZebrafish Infection: From Pathogenesis to Cell Biology
Torraca, V., & Mostowy, S. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.10.002 · Cited by 175
Tuberculosis drug discovery in the post‐post‐genomic era
Lechartier, B., Rybniker, J., Zumla, A. I., & Cole, S. T. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201201772 · Cited by 169
Roca, F. J., Whitworth, L. J., Prag, H. A., Murphy, M. P., & Ramakrishnan, L. (2022) · Science · doi:10.1126/science.abh2841 · Cited by 177
Self-citationKramnik, I., & Beamer, G. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-015-0538-9 · Cited by 169
Kim, J. K., Kim, Y. S., Lee, H., Jin, H. S., Neupane, C., Kim, S., Lee, S., Min, J., Sasai, M., Jeong, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06487-5 · Cited by 175
Necroptosis, in vivo detection in experimental disease models
Jouan-Lanhouet, S., Riquet, F. B., Duprez, L., Berghe, T. V., Takahashi, N., & Vandenabeele, P. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.08.010 · Cited by 166
Tumor necrosis factor alpha in mycobacterial infection
Dorhoi, A., & Kaufmann, S. H. E. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.04.003 · Cited by 171
Phenolic Glycolipid Facilitates Mycobacterial Escape from Microbicidal Tissue-Resident Macrophages
Cambier, C. J., O’Leary, S. M., O’Sullivan, M. P., Keane, J., & Ramakrishnan, L. (2017) · Immunity · doi:10.1016/j.immuni.2017.08.003 · Cited by 158
Self-citationHost-Directed Therapeutic Strategies for Tuberculosis
Kolloli, A., & Subbian, S. (2017) · Frontiers in Medicine · doi:10.3389/fmed.2017.00171 · Cited by 164
Jia, Y., Wang, F., Guo, Q., Li, M., Wang, L., Zhang, Z., Jiang, S., Jin, H., Chen, A., Tan, S., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.007 · Cited by 158
Immune cell interactions in tuberculosis
Flynn, J. L., & Chan, J. (2022) · Cell · doi:10.1016/j.cell.2022.10.025 · Cited by 161
Torraca, V., Masud, S., Spaink, H. P., & Meijer, A. H. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.015594 · Cited by 163
Human Immunology of Tuberculosis
Scriba, T. J., Coussens, A. K., & Fletcher, H. A. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.tbtb2-0016-2016 · Cited by 168
Coupling Heme and Iron Metabolism via Ferritin H Chain
Gozzelino, R., & Soares, M. P. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5666 · Cited by 151
Host-Directed Therapeutics for Tuberculosis: Can We Harness the Host?
Hawn, T. R., Matheson, A. I., Maley, S. N., & Vandal, O. H. (2013) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00032-13 · Cited by 152
Mycobacterial Dormancy Systems and Host Responses in Tuberculosis
Peddireddy, V., Doddam, S. N., & Ahmed, N. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00084 · Cited by 157
Origin and Evolution of Adaptive Immunity
Boehm, T. L. J., & Swann, J. B. (2013) · Annual Review of Animal Biosciences · doi:10.1146/annurev-animal-022513-114201 · Cited by 161
Host‐directed therapy to combat mycobacterial infections*
Kilinç, G., Saris, A., Ottenhoff, T. H. M., & Haks, M. C. (2021) · Immunological Reviews · doi:10.1111/imr.12951 · Cited by 148
Arsenault, R. J., Määttänen, P., Daigle, J., Potter, A. A., Griebel, P. J., & Napper, S. (2014) · Veterinary Research · doi:10.1186/1297-9716-45-54 · Cited by 136
Granulomas and Inflammation: Host-Directed Therapies for Tuberculosis
Ndlovu, H., & Marakalala, M. J. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00434 · Cited by 142
Mechanisms of M. tuberculosis Immune Evasion as Challenges to TB Vaccine Design
Ernst, J. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.06.004 · Cited by 137
McBee, M. E., Chionh, Y. H., Sharaf, M. L., Ho, P., Cai, M. W. L., & Dedon, P. C. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00459 · Cited by 141
Inflammation in tuberculosis: interactions, imbalances and interventions
Kaufmann, S. H. E., & Dorhoi, A. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.05.005 · Cited by 138
Anti-PD-1 immunotherapy leads to tuberculosis reactivation via dysregulation of TNF-α
Tezera, L. B., Bielecka, M. K., Ogongo, P., Walker, N. F., Ellis, M. J., Garay‐Baquero, D. J., Thomas, K., Reichmann, M. T., Johnston, D. A., Wilkinson, K. A., et al. (2020) · eLife · doi:10.7554/elife.52668 · Cited by 135
Lysosomal Disorders Drive Susceptibility to Tuberculosis by Compromising Macrophage Migration
Berg, R. D., Levitte, S., O’Sullivan, M. P., O’Leary, S. M., Cambier, C. J., Cameron, J. R., Takaki, K. K., Moens, C. B., Tobin, D. M., Keane, J., et al. (2016) · Cell · doi:10.1016/j.cell.2016.02.034 · Cited by 133
Self-citationSilwal, P., Kim, J. K., Kim, Y. J., & Jo, E. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01649 · Cited by 129
Necroptosis: is there a role for mitochondria?
Marshall, K. D., & Baines, C. P. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00323 · Cited by 131
Torraca, V., Cui, C., Boland, R., Bebelman, J., van der Sar, A. M., Smit, M. J., Siderius, M. H., Spaink, H. P., & Meijer, A. H. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.017756 · Cited by 129
Cronan, M. R., Hughes, E. J., Brewer, W. J., Viswanathan, G., Hunt, E. G., Singh, B., Mehra, S., Oehlers, S. H., Gregory, S. G., Kaushal, D., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.046 · Cited by 123
A Macrophage Response to Mycobacterium leprae Phenolic Glycolipid Initiates Nerve Damage in Leprosy
Madigan, C. A., Cambier, C. J., Kelly‐Scumpia, K. M., Scumpia, P. O., Cheng, T., Zailaa, J., Bloom, B. R., Moody, D. B., Smale, S. T., Sagasti, A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.030 · Cited by 126
Self-citationNeutrophils in host defense: new insights from zebrafish
Harvie, E. A., & Huttenlocher, A. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr1114-524r · Cited by 136
Mitochondrial reactive oxygen species as major effectors of antimicrobial immunity
Shekhova, E. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008470 · Cited by 124
Host-Directed Therapies for Tuberculosis: Figure 1.Preprint
Tobin, D. M. (2015) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a021196 · Cited by 123
RIPK 3 in cell death and inflammation: the good, the bad, and the ugly
Orozco, S. L., & Oberst, A. (2017) · Immunological Reviews · doi:10.1111/imr.12536 · Cited by 122
Primary macrophages and J774 cells respond differently to infection with Mycobacterium tuberculosis
Andreu, N., Phelan, J. E., de Sessions, P. F., Cliff, J. M., Clark, T. G., & Hibberd, M. L. (2017) · Scientific Reports · doi:10.1038/srep42225 · Cited by 125
Mitochondria: A target for bacteria
Lobet, E., Letesson, J., & Arnould, T. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.02.007 · Cited by 117
Fit for consumption: zebrafish as a model for tuberculosis
Cronan, M. R., & Tobin, D. M. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.016089 · Cited by 114
Paradoxical reactions and immune reconstitution inflammatory syndrome in tuberculosis
Bell, L. C. K., Breen, R. A. M., Miller, R. F., Noursadeghi, M., & Lipman, M. C. I. (2015) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2014.12.030 · Cited by 120
Mechanisms of Control of Mycobacterium tuberculosis by NK Cells: Role of Glutathione
Allen, M., Bailey, C., Cahatol, I., Dodge, L., Yim, J., Kassissa, C., Luong, J., Kasko, S., Pandya, S., & Venketaraman, V. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00508 · Cited by 119
Insights into battles between Mycobacterium tuberculosis and macrophages
Xu, G., Wang, J., Gao, G. F., & Liu, C. H. (2014) · Protein & Cell · doi:10.1007/s13238-014-0077-5 · Cited by 118
Towards efficient immunotherapy for bacterial infection
McCulloch, T. R., Wells, T. J., & Souza-Fonseca-Guimarães, F. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2021.05.005 · Cited by 116
Thương, N. T. T., Heemskerk, D., Tram, T. T. B., Thảo, L. T. P., Ramakrishnan, L., Ha, V. T. N., Bang, N. D., Chau, T. T. H., Lân, N. H., Caws, M., et al. (2017) · The Journal of Infectious Diseases · doi:10.1093/infdis/jix050 · Cited by 111
Self-citationRedox biology of regulated cell death in cancer: A focus on necroptosis and ferroptosis
Florean, C., Song, S., Dicato, M. A., & Diederich, M. F. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.01.008 · Cited by 110
Investigating the Causes for Decreased Levels of Glutathione in Individuals with Type II Diabetes
Lagman, M., Ly, J., Saing, T., Singh, M., Tudela, E. V., Morris, D., Chi, P.-T., Ochoa, C., Sathananthan, A., & Venketaraman, V. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118436 · Cited by 108
Gold, M. C., Napier, R. J., & Lewinsohn, D. M. (2015) · Immunological Reviews · doi:10.1111/imr.12271 · Cited by 110
Pagán, A. J., Yang, C.-T., Cameron, J. R., Swaim, L. E., Ellett, F. E., Lieschke, G. J., & Ramakrishnan, L. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.06.008 · Cited by 107
Self-citationThe role of mitochondrial ROS in antibacterial immunity
Pinegin, B. V., Vorobjeva, N. V., Pashenkov, M. V., & Chernyak, B. V. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26117 · Cited by 108
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review