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.
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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
RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
Zhang, D.-W., Shao, J., Lin, J., Zhang, N., Lu, B.-J., Lin, S.-C., Dong, M.-Q., & Han, J. (2009) · Science · doi:10.1126/science.1172308 · Cited by 1,931
Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635
Molecular mechanisms of N-acetylcysteine actions
Zafarullah, M., Li, W. Q., Sylvester, J., & Ahmad, M. (2003) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s000180300001 · Cited by 1,343
Mitochondrial Oxidative Stress: Implications for Cell Death
Orrenius, S., Gogvadze, V. G., & Zhivotovsky, B. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105122 · Cited by 1,294
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
Optimal alignments in linear space
Myers, E. W., & Miller, W. (1988) · Computer applications in the biosciences · doi:10.1093/bioinformatics/4.1.11 · Cited by 1,241
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200
Identification of nitric oxide synthase as a protective locus against tuberculosis
MacMicking, J. D., North, R. J., LaCourse, R., Mudgett, J. S., Shah, S. K., & Nathan, C. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5243 · Cited by 1,180
Population genomics of human gene expression
Stranger, B. E., Nica, A. C., Forrest, M. S., Dimas, A. S., Bird, C., Beazley, C., Ingle, C., Dunning, M., Flicek, P., Koller, D., et al. (2007) · Nature Genetics · doi:10.1038/ng2142 · Cited by 1,151
mpeg1 promoter transgenes direct macrophage-lineage expression in zebrafish
Ellett, F. E., Pase, L. B., Hayman, J. W., Andrianopoulos, A., & Lieschke, G. J. (2010) · Blood · doi:10.1182/blood-2010-10-314120 · Cited by 1,085
Chan, J., Xing, Y., Magliozzo, R. S., & Bloom, B. R. (1992) · The Journal of Experimental Medicine · doi:10.1084/jem.175.4.1111 · Cited by 1,062
Dexamethasone for the Treatment of Tuberculous Meningitis in Adolescents and Adults
Thwaites, G. E., Bang, N. D., Dung, N. H., Quy, H. T., Oanh, D. T. T., Thoa, N. T. C., Hien, N. Q., Thuc, N. T., Nh, N., Lan, N. T. N., et al. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040573 · Cited by 1,052
Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949
Revisiting the role of the granuloma in tuberculosis
Ramakrishnan, L. (2012) · Nature reviews. Immunology · doi:10.1038/nri3211 · Cited by 943
Self-citationSchulze‐Osthoff, K., Bakker, A. C., Vanhaesebroeck, B., Beyaert, R., Jacob, W. A., & Fiers, W. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42768-8 · Cited by 941
Tumor necrosis factor can induce both apoptic and necrotic forms of cell lysis.
Laster, S. M., Wood, J. G., & Gooding, L. R. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.141.8.2629 · Cited by 909
The Role of the Granuloma in Expansion and Dissemination of Early Tuberculous Infection
Davis, J. M., & Ramakrishnan, L. (2009) · Cell · doi:10.1016/j.cell.2008.11.014 · Cited by 907
Self-citationMore than one way to die: apoptosis, necrosis and reactive oxygen damage
Fiers, W. C., Beyaert, R., Declercq, W., & Vandenabeele, P. (1999) · Oncogene · doi:10.1038/sj.onc.1203249 · Cited by 871
Crompton, M., Ellinger, H., & COSTI, A. (1988) · PubMed Central · Cited by 841
Dexamethasone for treatment of tuberculous meningitis in adolescents and adults
Tunkel, A. R. (2005) · Current Infectious Disease Reports · doi:10.1007/s11908-005-0059-0 · Cited by 668
RIP Kinase-Dependent Necrosis Drives Lethal Systemic Inflammatory Response Syndrome
Duprez, L., Takahashi, N., Hauwermeiren, F. V., Vandendriessche, B., Goossens, V., Berghe, T. V., Declercq, W., Libert, C., Cauwels, A., & Vandenabeele, P. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.020 · Cited by 607
Host Genotype-Specific Therapies Can Optimize the Inflammatory Response to Mycobacterial Infections
Tobin, D. M., Roca, F. J., Oh, S. F., McFarland, R., Vickery, T. W., Ray, J. P., Ko, D. C., Zou, Y., Bang, N. D., Chau, T. T. H., et al. (2012) · Cell · doi:10.1016/j.cell.2011.12.023 · Cited by 583
Self-citationKim, Y., Morgan, M. J., Choksi, S., & Liu, Z.-G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.021 · Cited by 523
The lta4h Locus Modulates Susceptibility to Mycobacterial Infection in Zebrafish and Humans
Tobin, D. M., Vary, J. C., Ray, J. P., Walsh, G. S., Dunstan, S. J., Bang, N. D., Hagge, D. A., Khadge, S., King, M., Hawn, T. R., et al. (2010) · Cell · doi:10.1016/j.cell.2010.02.013 · Cited by 520
Self-citationCaseation of human tuberculosis granulomas correlates with elevated host lipid metabolism
Kim, M., Wainwright, H. C., Locketz, M., Bekker, L., Walther, G. B., Dittrich, C., Visser, A., Wang, W., Hsu, F., Wiehart, U., et al. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000079 · Cited by 489
Effects of tempol and redox-cycling nitroxides in models of oxidative stress
Wilcox, C. S. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.01.003 · Cited by 478
Amifostine: The First Selective-Target and Broad-Spectrum Radioprotector
Kouvaris, J., Kouloulias, V., & Vlahos, L. J. (2007) · The Oncologist · doi:10.1634/theoncologist.12-6-738 · Cited by 457
Mycobacterial survival strategies in the phagosome: defence against host stresses
Ehrt, S., & Schnappinger, D. (2009) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01335.x · Cited by 448
Robinson, N., McComb, S., Mulligan, R., Dudani, R., Krishnan, L., & Sad, S. (2012) · Nature Immunology · doi:10.1038/ni.2397 · Cited by 438
Q-VD-OPh, a broad spectrum caspase inhibitor with potent antiapoptotic properties
Caserta, T. M., Smith, A. N., Gultice, A. D., Reedy, M., & Brown, T. L. (2003) · APOPTOSIS · doi:10.1023/a:1024116916932 · Cited by 408
Schoeman, J. F., Zyl, L. E. V., Laubscher, J. A., & Donald, P. R. (1997) · PEDIATRICS · doi:10.1542/peds.99.2.226 · Cited by 300
Yang, C.-T., Cambier, C. J., Davis, J. M., Hall, C. J., Crosier, P. S., & Ramakrishnan, L. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.07.009 · Cited by 293
Self-citationDichotomous Role of the Macrophage in Early Mycobacterium marinum Infection of the Zebrafish
Clay, H., Davis, J. M., Beery, D., Anna Huttenlocher, A., Lyons, S. E., & Ramakrishnan, L. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.06.004 · Cited by 243
Self-citationLee, J., Remold, H. G., Ieong, M. H., & Kornfeld, H. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.7.4267 · Cited by 238
Cyclic AMP intoxication of macrophages by a Mycobacterium tuberculosis adenylate cyclase
Agarwal, N., Lamichhane, G., Gupta, R., Nolan, S. T., & Bishai, W. R. (2009) · Nature · doi:10.1038/nature08123 · Cited by 230
Lee, S. B., Bae, I. H., Bae, Y. S., & Um, H.-D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606702200 · Cited by 187
Loss of PINK1 Function Affects Development and Results in Neurodegeneration in Zebrafish
Anichtchik, O. V., Diekmann, H., Fleming, A., Roach, A. G., Goldsmith, P., & Rubinsztein, D. C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0979-08.2008 · Cited by 184
He, S., Lamers, G. E. M., Beenakker, J. M., Cui, C., Ghotra, V. P. S., Danen, E. H. J., Meijer, A. H., Spaink, H. P., & Snaar-Jagalska, E. B. (2012) · The Journal of Pathology · doi:10.1002/path.4013 · Cited by 183
Dumitru, C. A., & Gulbins, E. (2006) · Oncogene · doi:10.1038/sj.onc.1209568 · Cited by 166
Dewas, C., Dang, P. M., Gougerot‐Pocidalo, M., & Benna, J. E. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.8.4392 · Cited by 163
Zunino, F., Pratesi, G., Micheloni, A., Cavalletti, E., Sala, F., & Tofanetti, O. (1989) · Chemico-Biological Interactions · doi:10.1016/0009-2797(89)90065-3 · Cited by 156
Galluzzi, L., Berghe, T. V., Vanlangenakker, N., Büttner, S., Eisenberg, T., Vandenabeele, P., Madeo, F., & Kroemer, G. (2011) · International review of cytology · doi:10.1016/b978-0-12-386039-2.00001-8 · Cited by 152
A Phase I Study of Topical Tempol for the Prevention of Alopecia Induced by Whole Brain Radiotherapy
Metz, J. M., Smith, D., Mick, R., Lustig, R. A., Mitchell, J. B., Cherakuri, M., GLATSTEIN, E. J., & Hahn, S. M. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-0658 · Cited by 150
Ceramide mediates caspase‐independent programmed cell death
Thon, L., Möhlig, H., Mathieu, S., Lange, A., Bulanova, E., Winoto‐Morbach, S., Schütze, S., Bulfone‐Paus, S., & Adam, D. (2005) · The FASEB Journal · doi:10.1096/fj.05-3726com · Cited by 123
Tiepolo, T., Angelin, A., Palma, E., Sabatelli, P., Merlini, L., Nicolosi, L., Finetti, F., Braghetta, P., Vuagniaux, G., Dumont, J., et al. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00316.x · Cited by 121
Mycobacterium tuberculosis Induces an Atypical Cell Death Mode to Escape from Infected Macrophages
Lee, J., Repasy, T., Papavinasasundaram, K. G., Sassetti, C. M., & Kornfeld, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018367 · Cited by 121
Reconsidering Adjuvant Immunotherapy for Tuberculosis
Wallis, R. S. (2005) · Clinical Infectious Diseases · doi:10.1086/430914 · Cited by 121
Nitration of the mitochondrial complex I subunit NDUFB8 elicits RIP1- and RIP3-mediated necrosis
Davis, C. W., Hawkins, B. J., Ramasamy, S., Irrinki, K. M., Cameron, B. A., Islam, K., Daswani, V. P., Doonan, P. J., Manevich, Y., & Madesh, M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.11.001 · Cited by 113
New insights on the use of desipramine as an inhibitor for acid ceramidase
Elojeimy, S. N., Holman, D. H., Liu, X., El-Zawahry, A. M., Villani, M., Cheng, J., Mahdy, A. E. M., Zeidan, Y. H., Bielwaska, A., Hannun, Y. A., et al. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.071 · Cited by 110
An In Vivo Platform for Rapid High-Throughput Antitubercular Drug Discovery
Takaki, K. K., Cosma, C. L., Troll, M. A., & Ramakrishnan, L. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.06.008 · Cited by 105
Self-citationCadieux, N., Parra, M., Cohen, H., Maric, D., Morris, S. L., & Brennan, M. J. (2010) · Microbiology · doi:10.1099/mic.0.041996-0 · Cited by 84
NecroX as a novel class of mitochondrial reactive oxygen species and ONOO− scavenger
Kim, H. J., Koo, S. Y., Ahn, B., Park, O., Park, D. H., Seo, D. O., Won, J. H., Yim, H. J., Kwak, H.-S., Park, H. S., et al. (2010) · Archives of Pharmacal Research · doi:10.1007/s12272-010-1114-4 · Cited by 82
Tumor Necrosis Factor and Anti-Tumor Necrosis Factor Therapies
Keystone, E., & Ware, C. F. (2010) · Journal of Rheumatology Supplement · doi:10.3899/jrheum.091463 · Cited by 76
Targeting of Mycobacterium tuberculosis Heparin-Binding Hemagglutinin to Mitochondria in Macrophages
Sohn, H., Kim, J.-S., Shin, S. J., Kim, K., Won, C.-J., Kim, W. S., Min, K.-N., Choi, H., Lee, J. C., Park, J., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002435 · Cited by 67
Cirillo, S. L. G., Subbian, S., Chen, B., Weisbrod, T. R., Jacobs, W. R., & Cirillo, J. D. (2009) · Infection and Immunity · doi:10.1128/iai.01481-08 · Cited by 64
The cyclophilin inhibitor alisporivir prevents hepatitis C virus–mediated mitochondrial dysfunction
Quarato, G., D’Aprile, A., Gavillet, B., Vuagniaux, G., Moradpour, D., Capitanio, N., & Piccoli, C. (2011) · Hepatology · doi:10.1002/hep.25514 · Cited by 56
Insights into tuberculosis from the zebrafish model
Berg, R. D., & Ramakrishnan, L. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.10.002 · Cited by 56
Self-citationDifferential Regulation of Primitive Myelopoiesis in the Zebrafish by Spi-1/Pu.1 and C/ebp1
Su, F., Juarez, M. A., Cooke, C. L., LaPointe, L. D., Shavit, J. A., Yamaoka, J. S., & Lyons, S. E. (2007) · Zebrafish · doi:10.1089/zeb.2007.0505 · Cited by 48
Real-Time Measurement of Intracellular Reactive Oxygen Species Using Mito Tracker Orange (CMH2TMRos)
Kweon, S.-M., Kim, H., Lee, Z., Kim, S., Kim, S.-I., Paik, S., & Ha, K. (2001) · Bioscience Reports · doi:10.1023/a:1013290316939 · Cited by 36
Subbian, S., Mehta, P. K., Cirillo, S. L. G., & Cirillo, J. D. (2007) · BMC Microbiology · doi:10.1186/1471-2180-7-4 · Cited by 28
Soler, M., Camacho, M., Molins‐Pujol, A. M., & Vila, L. (2001) · The Journal of Infectious Diseases · doi:10.1086/317639 · Cited by 15
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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
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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