Mitochondria in innate immune signaling

Pattern Recognition Receptors and Inflammation

Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895 · see citing works

Innate immune recognition

Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394 · see citing works

Neutrophil Emigration in the Skin, Lungs, and Peritoneum: Different Requirements for CD11/CD18 Revealed by CD18-deficient Mice

Mizgerd, J. P., Kubo, H., Kutkoski, G. J., Bhagwan, S. D., Scharffetter-Kochanek, K., Beaudet, A. L., & Doerschuk, C. M. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.8.1357 · Cited by 7,332 · see citing works

Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death

Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., & Shao, F. (2015) · Nature · doi:10.1038/nature15514 · Cited by 6,659 · see citing works

A role for mitochondria in nlrp3 inflammasome activation

Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602 · see citing works

Cyclic GMP-AMP Synthase Is a Cytosolic DNA Sensor That Activates the Type I Interferon Pathway

Sun, L., Wu, J., Du, F., Chen, X., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1232458 · Cited by 4,996 · see citing works

Succinate is an inflammatory signal that induces IL-1β through HIF-1α

Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176 · see citing works

The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses

Yoneyama, M., Kikuchi, M., Natsukawa, T., Shinobu, N., Imaizumi, T., Miyagishi, M., Taira, K., Akira, S., & Fujita, T. (2004) · Nature Immunology · doi:10.1038/ni1087 · Cited by 3,935 · see citing works

Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses

Kato, H., Takeuchi, O., Sato, S., Yoneyama, M., Yamamoto, M., Matsui, K., Uematsu, S., Jung, A., Kawai, T., Ishii, K. J., et al. (2006) · Nature · doi:10.1038/nature04734 · Cited by 3,888 · see citing works

Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF‐kappa B transcription factor and HIV‐1.

Schreck, R., RIEBER, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,816 · see citing works

Circulating mitochondrial DAMPs cause inflammatory responses to injury

Zhang, Q., Raoof, M., Chen, Y., Sumi, Y., Sursal, T., Junger, W., Brohi, K., Itagaki, K., & Hauser, C. J. (2010) · Nature · doi:10.1038/nature08780 · Cited by 3,812 · see citing works

Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling

Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686 · see citing works

Mitochondrial Fission, Fusion, and Stress

Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works

STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling

Ishikawa, H., & Barber, G. N. (2008) · Nature · doi:10.1038/nature07317 · Cited by 3,576 · see citing works

Identification and Characterization of MAVS, a Mitochondrial Antiviral Signaling Protein that Activates NF-κB and IRF3

Seth, R. B., Sun, L., Ea, C.-K., & Chen, Z. J. (2005) · Cell · doi:10.1016/j.cell.2005.08.012 · Cited by 3,329 · see citing works

A guide to immunometabolism for immunologists

O'Neill, L. A. J., Kishton, R. J., & Rathmell, J. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.70 · Cited by 3,315 · see citing works

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219 · see citing works

NOX enzymes and the biology of reactive oxygen

Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · see citing works

Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome

Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049 · see citing works

Cutting Edge: NF-κB Activating Pattern Recognition and Cytokine Receptors License NLRP3 Inflammasome Activation by Regulating NLRP3 Expression

Bauernfeind, F. G., Horvath, G. L., Stutz, A., Alnemri, E. S., MacDonald, K. L., Speert, D. P., Fernandes‐Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901363 · Cited by 3,006 · see citing works

Cyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA

Wu, J., Sun, L., Chen, X., Du, F., Shi, H., Chen, C., & Chen, Z. J. (2012) · Science · doi:10.1126/science.1229963 · Cited by 2,574 · see citing works

IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction

Kawai, T., Takahashi, K., Sato, S., Coban, C., Kumar, H., Kato, H., Ishii, K. J., Takeuchi, O., & Akira, S. (2005) · Nature Immunology · doi:10.1038/ni1243 · Cited by 2,562 · see citing works

5'-Triphosphate RNA Is the Ligand for RIG-I

Hornung, V., Ellegast, J., Kim, S., Brzózka, K., Jung, A., Kato, H., Poeck, H., Akira, S., Conzelmann, K.-K., Schlee, M., et al. (2006) · Science · doi:10.1126/science.1132505 · Cited by 2,474 · see citing works

Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus

Meylan, E., Curran, J., Hofmann, K., Moradpour, D., Binder, M., Bartenschlager, R., & Tschopp, J. (2005) · Nature · doi:10.1038/nature04193 · Cited by 2,401 · see citing works

Succinate Dehydrogenase Supports Metabolic Repurposing of Mitochondria to Drive Inflammatory Macrophages

Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291 · see citing works

Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis

Shimada, K., Crother, T. R., Karlin, J., Dagvadorj, J., Chiba, N., Chen, S., Ramanujan, V. K., Wolf, A. J., Vergnes, L., Ojcius, D. M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.009 · Cited by 2,282 · see citing works

Pathogen Recognition by the Innate Immune System

Kumar, H., Kawai, T., & Akira, S. (2011) · International Reviews of Immunology · doi:10.3109/08830185.2010.529976 · Cited by 2,264 · see citing works

RIG-I-mediated antiviral responses to single-stranded RNA bearing 5’-phosphates

Pichlmair, A., Schulz, O., Tan, C. P., Näslund, T. I., Liljeström, P., Weber, F., & Reis e Sousa, C. (2006) · Science · doi:10.1126/science.1132998 · Cited by 2,210 · see citing works

Control of adaptive immunity by the innate immune system

Iwasaki, A., & Medzhitov, R. (2015) · Nature Immunology · doi:10.1038/ni.3123 · Cited by 2,160 · see citing works

Regulation of Adaptive Immunity by the Innate Immune System

Iwasaki, A., & Medzhitov, R. M. (2010) · Science · doi:10.1126/science.1183021 · Cited by 2,139 · see citing works

Network Integration of Parallel Metabolic and Transcriptional Data Reveals Metabolic Modules that Regulate Macrophage Polarization

Jha, A. K., Huang, S. C.-C., Sergushichev, A., Lampropoulou, V., Ivanova, Y., Loginicheva, E., Chmielewski, K., Stewart, K. M., Ashall, J., Everts, B., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.005 · Cited by 2,066 · see citing works

Mitochondrial DNA stress primes the antiviral innate immune response

West, A. P., Khoury-Hanold, W., Staron, M., Tal, M. C., Pineda, C. M., Lang, S. M., Bestwick, M., Duguay, B. A., Raimundo, N., MacDuff, D. A., et al. (2015) · Nature · doi:10.1038/nature14156 · Cited by 1,975 · see citing works

Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation

Liu, S., Cai, X., Wu, J., Cong, Q., Chen, X., Li, T., Du, F., Ren, J., Wu, Y.-T., Grishin, N. V., et al. (2015) · Science · doi:10.1126/science.aaa2630 · Cited by 1,927 · see citing works

VISA Is an Adapter Protein Required for Virus-Triggered IFN-β Signaling

Xu, L., Wang, Y., Han, K.-J., Li, L., Zhai, Z., & Shu, H. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.014 · Cited by 1,849 · see citing works

CGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING.

Ablasser, A., Goldeck, M., Cavlar, T., Deimling, T., Witte, G., Röhl, I., Hopfner, K.-P., Ludwig, J., & Hornung, V. (2013) · Nature · doi:10.1038/nature12306 · Cited by 1,695 · see citing works

Shared and Unique Functions of the DExD/H-Box Helicases RIG-I, MDA5, and LGP2 in Antiviral Innate Immunity

Yoneyama, M., Kikuchi, M., Matsumoto, K., Imaizumi, T., Miyagishi, M., Taira, K., Foy, E. M., Loo, Y., Gale, M., Akira, S., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2851 · Cited by 1,691 · see citing works

TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity

Gack, M. U., Shin, Y. C., Joo, C.-H., Urano, T., Liang, C., Sun, L., Takeuchi, O., Akira, S., Chen, Z. J., Inoue, S., et al. (2007) · Nature · doi:10.1038/nature05732 · Cited by 1,683 · see citing works

Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle–Wells syndrome

Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A., & Kolodner, R. D. (2001) · Nature Genetics · doi:10.1038/ng756 · Cited by 1,679 · see citing works

Tlr signalling augments macrophage bactericidal activity through mitochondrial ros

West, A. P., Brodsky, I. E., Rahner, C., Woo, D. K., Erdjument-Bromage, H., Tempst, P., Walsh, M. C., Choi, Y., Shadel, G. S., & Ghosh, S. (2011) · Nature · doi:10.1038/nature09973 · Cited by 1,659 · see citing works

Nucleotides released by apoptotic cells act as a find-me signal to promote phagocytic clearance

Elliott, M. R., Chekeni, F. B., Trampont, P. C., Lazarowski, E. R., Kadl, A., Walk, S. F., Park, D., Woodson, R. I., Ostankovich, M., Sharma, P., et al. (2009) · Nature · doi:10.1038/nature08296 · Cited by 1,654 · see citing works

Itaconate Links Inhibition of Succinate Dehydrogenase with Macrophage Metabolic Remodeling and Regulation of Inflammation

Lampropoulou, V., Sergushichev, A., Bambousková, M., Nair, S., Vincent, E. E., Loginicheva, E., Cervantes‐Barragán, L., Ma, X., Huang, S. C., Griss, T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.004 · Cited by 1,547 · see citing works

Mitochondria in innate immune responses

West, A. P., Shadel, G. S., & Ghosh, S. (2011) · Nature Reviews Immunology · doi:10.1038/nri2975 · Cited by 1,376 · see citing works

Oxidative metabolism and PGC-1β attenuate macrophage-mediated inflammation

Vats, D., Mukundan, L., Odegaard, J. I., Zhang, L., Smith, K. L., Morel, C. R., Greaves, D. R., Murray, P. J., & Chawla, A. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.011 · Cited by 1,369 · see citing works

Cell Type-Specific Involvement of RIG-I in Antiviral Response

Kato, H., Sato, S., Yoneyama, M., Yamamoto, M., Uematsu, S., Matsui, K., Tsujimura, T., Takeda, K., Fujita, T., Takeuchi, O., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.04.010 · Cited by 1,368 · see citing works

STING Specifies IRF3 Phosphorylation by TBK1 in the Cytosolic DNA Signaling Pathway

Tanaka, Y., & Chen, Z. J. (2012) · Science Signaling · doi:10.1126/scisignal.2002521 · Cited by 1,314 · see citing works

MAVS Forms Functional Prion-like Aggregates to Activate and Propagate Antiviral Innate Immune Response

Hou, F., Sun, L., Zheng, H., Skaug, B. A., Jiang, Q., & Chen, Z. J. (2011) · Cell · doi:10.1016/j.cell.2011.06.041 · Cited by 1,274 · see citing works

Intravascular Danger Signals Guide Neutrophils to Sites of Sterile Inflammation

McDonald, B., Pittman, K., Menezes, G. B., Hirota, S. A., Slaba, I., Waterhouse, C. C. M., Beck, P. L., Muruve, D. A., & Kubes, P. (2010) · Science · doi:10.1126/science.1195491 · Cited by 1,210 · see citing works

Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production

Michelucci, A., Cordes, T., Ghelfi, J., Pailot, A., Reiling, N., Goldmann, O., Binz, T., Wegner, A., Tallam, A., Rausell, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218599110 · Cited by 1,191 · see citing works

Mitochondrial DNA in innate immune responses and inflammatory pathology

West, A. P., & Shadel, G. S. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2017.21 · Cited by 1,115 · see citing works

Cyclic [G(2′,5′)pA(3′,5′)p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase.

Gao, P., Ascano, M., Wu, Y., Barchet, W., Gaffney, B. L., Zillinger, T., Serganov, A. A., Liu, Y., Jones, R. A., Hartmann, G., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.046 · Cited by 1,101 · see citing works

Cyclic GMP-AMP Containing Mixed Phosphodiester Linkages Is An Endogenous High-Affinity Ligand for STING

Zhang, X., Shi, H., Wu, J., Zhang, X., Sun, L., Chen, C., & Chen, Z. J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.022 · Cited by 1,086 · see citing works

Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells

Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2837 · Cited by 1,083 · see citing works

BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis

McArthur, K., Whitehead, L. W., Heddleston, J. M., Li, L., Padman, B. S., Oorschot, V., Geoghegan, N. D., Chappaz, S., Davidson, S., San Chin, H., et al. (2018) · Science · doi:10.1126/science.aao6047 · Cited by 1,072 · see citing works

Substrate Fate in Activated Macrophages: A Comparison between Innate, Classic, and Alternative Activation

Rodríguez-Prados, J.-C., Través, P. G., Cuenca, J., Rico, D., Aragonés, J., Martín-Sanz, P., Cascante, M., & Boscá, L. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901698 · Cited by 1,022 · see citing works

Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production

White, M. J., McArthur, K., Metcalf, D., Lane, R. M., Cambier, J. C., Herold, M. J., van Delft, M. F., Bedoui, S., Lessene, G., Ritchie, M. E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.036 · Cited by 983 · see citing works

Mitochondrial Cardiolipin Is Required for Nlrp3 Inflammasome Activation

Iyer, S. S., He, Q., Janczy, J. R., Elliott, E. I., Zhong, Z., Olivier, A. K., Sadler, J. J., Knepper-Adrian, V., Han, R., Qiao, L., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.001 · Cited by 939 · see citing works

Critical role for calcium mobilization in activation of the NLRP3 inflammasome

Murakami, T., Öckinger, J., Yu, J., Byles, V., McColl, A., Hofer, A. M., & Horng, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117765109 · Cited by 926 · see citing works

N-formylmethionyl peptides as chemoattractants for leucocytes.

Schiffmann, E., Corcoran, B. A., & Wahl, S. M. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.3.1059 · Cited by 889 · see citing works

Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome

Misawa, T., Takahama, M., Kozaki, T., Lee, H., Zou, J., Saitoh, T., & Akira, S. (2013) · Nature Immunology · doi:10.1038/ni.2550 · Cited by 863 · see citing works

ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization

Sun, W., Li, Y., Chen, L., Chen, H., You, F., Zhou, X., Zhou, Y., Zhai, Z., Chen, D., & Jiang, Z. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900850106 · Cited by 862 · see citing works

Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response

Saitoh, T., Fujita, N., Hayashi, T., Takahara, K., Satoh, T., Lee, H., Matsunaga, K., Kageyama, S., Omori, H., Noda, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911267106 · Cited by 854 · see citing works

Peroxisomes are signaling platforms for antiviral innate immunity

Dixit, E., Boulant, S., Zhang, Y.-J., Lee, A. S., Odendall, C., Shum, B. O. V., Hacohen, N., Chen, Z.-J. J., Whelan, S. P. J., Fransen, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.04.018 · Cited by 848 · see citing works

Apoptotic Caspases Prevent the Induction of Type I Interferons by Mitochondrial DNA

Rongvaux, A., Jackson, R., Harman, C. C. D., Li, T., West, A. P., de Zoete, M. R., Wu, Y., Yordy, B., Lakhani, S. A., Kuan, C.-Y., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.037 · Cited by 847 · see citing works

Initiation and perpetuation of <scp>NLRP</scp> 3 inflammasome activation and assembly

Elliott, E. I., & Sutterwala, F. S. (2015) · Immunological Reviews · doi:10.1111/imr.12286 · Cited by 821 · see citing works

Non-transcriptional Priming and Deubiquitination Regulate NLRP3 Inflammasome Activation

Juliana, C. A., Fernandes‐Alnemri, T., Kang, S., Farias, A., Qin, F., & Alnemri, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407130 · Cited by 771 · see citing works

International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the Formyl Peptide Receptor (FPR) Family

Ye, R. D., Boulay, F., Wang, J. M., Dahlgren, C., Gerard, C. J., Parmentier, M., Serhan, C. N., & Murphy, P. M. (2009) · Pharmacological Reviews · doi:10.1124/pr.109.001578 · Cited by 767 · see citing works

The innate immune DNA Sensor cGAS produces a noncanonical cyclic dinucleotide that activates human STING.

Diner, E. J., Burdette, D. L., Wilson, S. C., Monroe, K. M., Kellenberger, C. A., Hyodo, M., Hayakawa, Y., Hammond, M. C., & Vance, R. E. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.05.009 · Cited by 767 · see citing works

Oxygen sensing requires mitochondrial ROS but not oxidative phosphorylation

Brunelle, J. K., Bell, E. L., Quesada, N. M., Vercauteren, K., Tiranti, V., Zeviani, M., Scarpulla, R. C., & Chandel, N. S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.002 · Cited by 763 · see citing works

Mitochondrial disorders as windows into an ancient organelle

Vafai, S. B., & Mootha, V. K. (2012) · Nature · doi:10.1038/nature11707 · Cited by 733 · see citing works

Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity

Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 718 · see citing works

De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal‐onset multisystem inflammatory disease (NOMID): A new member of the expanding family of pyrin‐associated autoinflammatory diseases

Aksentijevich, I. A., Nowak, M., Mallah, M., Chae, J. J., Watford, W. T., Hofmann, S. R., Stein, L. D., Russo, R. A. G., Goldsmith, D. P., Dent, P. B., et al. (2002) · Arthritis & Rheumatism · doi:10.1002/art.10688 · Cited by 707 · see citing works

LGP2 is a positive regulator of RIG-I– and MDA5-mediated antiviral responses

Satoh, T., Kato, H., Kumagai, Y., Yoneyama, M., Sato, S., Matsushita, K., Tsujimura, T., Fujita, T., Akira, S., & Takeuchi, O. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912986107 · Cited by 697 · see citing works

Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome

Iyer, S. S., Pulskens, W. P., Sadler, J. J., Butter, L. M., Teske, G. J., Ulland, T. K., Eisenbarth, S. C., Florquin, S., Flavell, R. A., Leemans, J. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908698106 · Cited by 691 · see citing works

The Adaptor MAVS Promotes NLRP3 Mitochondrial Localization and Inflammasome Activation

Subramanian, N., Natarajan, K., Clatworthy, M. R., Wang, Z., & Germain, R. N. (2013) · Cell · doi:10.1016/j.cell.2013.02.054 · Cited by 675 · see citing works

MOMP, cell suicide as a BCL-2 family business

Kalkavan, H., & Green, D. R. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.179 · Cited by 667 · see citing works

ROS-dependent activation of the TRAF6-ASK1-p38 pathway is selectively required for TLR4-mediated innate immunity

Matsuzawa, A., Saegusa, K., Noguchi, T., Sadamitsu, C., Nishitoh, H., Nagai, S., Koyasu, S., Matsumoto, K., Takeda, K., & Ichijo, H. (2005) · Nature Immunology · doi:10.1038/ni1200 · Cited by 667 · see citing works

Endosymbiosis and Eukaryotic Cell Evolution

Archibald, J. M. (2015) · Current Biology · doi:10.1016/j.cub.2015.07.055 · Cited by 654 · cited 5× · see citing works

The RNA Helicase Lgp2 Inhibits TLR-Independent Sensing of Viral Replication by Retinoic Acid-Inducible Gene-I

Rothenfußer, S., Goutagny, N., DiPerna, G., Gong, M., Monks, B. G., Schoenemeyer, A., Yamamoto, M., Akira, S., & Fitzgerald, K. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.8.5260 · Cited by 645 · see citing works

Reconstitution of the RIG-I Pathway Reveals a Signaling Role of Unanchored Polyubiquitin Chains in Innate Immunity

Zeng, W., Sun, L., Jiang, X., Chen, X., Hou, F., Adhikari, A., Xu, M., & Chen, Z. J. (2010) · Cell · doi:10.1016/j.cell.2010.03.029 · Cited by 613 · see citing works

The Vaccine Adjuvant Chitosan Promotes Cellular Immunity via DNA Sensor cGAS-STING-Dependent Induction of Type I Interferons

Carroll, E. C., Jin, L., Mori, A., Muñoz‐Wolf, N., Oleszycka, E., Moran, H. B. T., Mansouri, S., McEntee, C. P., Lambe, E. M., Agger, E. M., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.004 · Cited by 599 · see citing works

Structure-Function Analysis of STING Activation by c[G(2′,5′)pA(3′,5′)p] and Targeting by Antiviral DMXAA

Gao, P., Ascano, M., Zillinger, T., Wang, W., Dai, P., Serganov, A. A., Gaffney, B. L., Shuman, S., Jones, R. A., Deng, L., et al. (2013) · Cell · doi:10.1016/j.cell.2013.07.023 · Cited by 595 · see citing works

NLRX1 is a regulator of mitochondrial antiviral immunity

Moore, C. B., Bergstralh, D. T., Duncan, J. A., Lei, Y. L., Morrison, T. E., Zimmermann, A. G., Accavitti-Loper, M. A., Madden, V. J., Sun, L., Ye, Z., et al. (2008) · Nature · doi:10.1038/nature06501 · Cited by 586 · see citing works

Endosymbiotic theories for eukaryote origin

Martin, W. F., Garg, S., & Zimorski, V. (2015) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2014.0330 · Cited by 583 · see citing works

Mitochondrial-nuclear communications

Ryan, M. T., & Hoogenraad, N. J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052305.091720 · Cited by 575 · see citing works

Cutting Edge: TNF-α Mediates Sensitization to ATP and Silica via the NLRP3 Inflammasome in the Absence of Microbial Stimulation

Franchi, L., Eigenbrod, T., & Núñez, G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900173 · Cited by 574 · see citing works

Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling

Tal, M. C., Sasai, M., Lee, H. K., Yordy, B., Shadel, G. S., & Iwasaki, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807694106 · Cited by 573 · see citing works

Role of Oxidants in NF-κB Activation and TNF-α Gene Transcription Induced by Hypoxia and Endotoxin

Chandel, N. S., Trzyna, W., McClintock, D. S., & Schumacker, P. T. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.2.1013 · Cited by 536 · see citing works

Memory TH2 cells induce alternatively activated macrophages to mediate protection against nematode parasites

Anthony, R. M., Urban, J. F., Alem, F., Hamed, H. A., Rozo, C. T., Boucher, J.-L., Van Rooijen, N., & Gause, W. C. (2006) · Nature Medicine · doi:10.1038/nm1451 · Cited by 522 · see citing works

Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA.

Nunnari, J. M., Marshall, W. F., Straight, A. F., Murray, A., Sedat, J. W., & Walter, P. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.7.1233 · Cited by 514 · see citing works

Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2

Guo, R., Zong, S., Wu, M., Gu, J., & Yang, M. (2017) · Cell · doi:10.1016/j.cell.2017.07.050 · Cited by 510 · see citing works

Endogenously oxidized mitochondrial DNA induces in vivo and in vitro inflammatory responses

Collins, L. V., Hajizadeh, S., Holme, E., Jonsson, I., & Tarkowski, A. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0703328 · Cited by 504 · see citing works

NLRP3 Phosphorylation Is an Essential Priming Event for Inflammasome Activation

Song, N., Liu, Z.-S., Xue, W., Bai, Z., Wang, Q., Dai, J., Liu, X., Huang, Y.-J., Cai, H., Zhan, X., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.017 · Cited by 494 · see citing works

The Maintenance of Mitochondrial DNA Integrity--Critical Analysis and UpdatePreprint

ALEXEYEV, M. F., Shokolenko, I. N., Wilson, G. L., & LeDoux, S. P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012641 · Cited by 461 · see citing works

Mitochondrial transcription factor A (TFAM): Roles in maintenance of mtDNA and cellular functions

Kang, D., Kim, S. H., & Hamasaki, N. (2006) · Mitochondrion · doi:10.1016/j.mito.2006.11.017 · Cited by 450 · see citing works

Role of Cardiolipin in Mitochondrial Signaling Pathways

Dudek, J. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00090 · Cited by 433 · see citing works

Type I interferon–mediated monogenic autoinflammation: The type I interferonopathies, a conceptual overview

Rodero, M. P., & Crow, Y. J. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20161596 · Cited by 433 · see citing works

UCP2 transports C4 metabolites out of mitochondria, regulating glucose and glutamine oxidation

Vozza, A., Parisi, G., De Leonardis, F., Lasorsa, F. M., Castegna, A., Amorese, D., Marmo, R., Calcagnile, V. M., Palmieri, L., Ricquier, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317400111 · Cited by 407 · see citing works

Mitochondrial control of immunity: beyond ATP

Mehta, M., Weinberg, S. E., & Chandel, N. S. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.66 · Cited by 398 · see citing works

The monogenic autoinflammatory diseases define new pathways in human innate immunity and inflammation

Manthiram, K., Zhou, Q., Aksentijevich, I. A., & Kastner, D. L. (2017) · Nature Immunology · doi:10.1038/ni.3777 · Cited by 397 · see citing works

Itaconic acid is a mammalian metabolite induced during macrophage activation

Strelko, C. L., Lu, W., Dufort, F. J., Seyfried, T. N., Chiles, T. C., Rabinowitz, J. D., & Roberts, M. F. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2070889 · Cited by 391 · see citing works

Cyclic GMP-AMP Synthase Is an Innate Immune DNA Sensor for Mycobacterium tuberculosis

Collins, A. C., Cai, H., Li, T., Franco, L. H., Li, X.-D., Nair, V. R., Scharn, C. R., Stamm, C. E., Levine, B., Chen, Z. J., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.05.005 · Cited by 384 · see citing works

Receptor interacting protein kinase 2–mediated mitophagy regulates inflammasome activation during virus infection

Lupfer, C., Thomas, P. G., Anand, P. K., Vogel, P., Milasta, S., Martinez, J., Huang, G., Green, M., Kundu, M., Chi, H., et al. (2013) · Nature Immunology · doi:10.1038/ni.2563 · Cited by 384 · see citing works

Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity

Hara, H., Tsuchiya, K., Kawamura, I., Fang, R., Hernández-Cuellar, E., Shen, Y., Mizuguchi, J., Schweighoffer, E., Tybulewicz, V. L. J., & Mitsuyama, M. (2013) · Nature Immunology · doi:10.1038/ni.2749 · Cited by 382 · see citing works

Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain

Letts, J. A., & Sazanov, L. A. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3460 · Cited by 376 · see citing works

Diverse intracellular pathogens activate type III interferon expression from peroxisomes

Odendall, C., Dixit, E., Stavru, F., Bierne, H., Franz, K. M., Durbin, A. F., Boulant, S., Gehrke, L., Cossart, P., & Kagan, J. C. (2014) · Nature Immunology · doi:10.1038/ni.2915 · Cited by 375 · see citing works

Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis

Aganna, E., Martinon, F., Hawkins, P. N., Ross, J. B., Swan, D., Booth, D. R., Lachmann, H. J., Gaudet, R., Woo, P. M., Feighery, C., et al. (2002) · Arthritis & Rheumatism · doi:10.1002/art.10509 · Cited by 367 · see citing works

The Roles of Mitochondrial Damage-Associated Molecular Patterns in Diseases

Nakahira, K., Hisata, S., & Choi, A. M. K. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6407 · Cited by 363 · see citing works

MITOCHONDRIAL DNA IS RELEASED BY SHOCK AND ACTIVATES NEUTROPHILS VIA P38 MAP KINASE

Zhang, Q., Itagaki, K., & Hauser, C. J. (2010) · Shock · doi:10.1097/shk.0b013e3181cd8c08 · Cited by 354 · see citing works

Differential Expression of NLRP3 among Hematopoietic Cells

Guarda, G., Zenger, M., Yazdi, A. S., Schroder, K., Ferrero, I., Menu, P., Tardivel, A., Mattmann, C., & Tschopp, J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002720 · Cited by 350 · see citing works

The Enigma of the Respiratory Chain Supercomplex

Milenkovic, D., Blaza, J. N., Larsson, N., & Hirst, J. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.009 · Cited by 344 · see citing works

Initiation and Beyond: Multiple Functions of the Human Mitochondrial Transcription Machinery

Bonawitz, N. D., Clayton, D. A., & Shadel, G. S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.024 · Cited by 337 · see citing works

The mitochondrial permeability transition pore: a mystery solved?

Bernardi, P. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00095 · Cited by 335 · see citing works

Chemokines and mitochondrial products activate neutrophils to amplify organ injury during mouse acute liver failure

Marques, P. E., Amaral, S. S., Pires, D. A., Nogueira, L. L., Soriani, F. M., Lima, B. H. F., Lopes, G. A. O., Russo, R. C., Ávila, T. V., Melgaço, J. G., et al. (2012) · Hepatology · doi:10.1002/hep.25801 · Cited by 332 · see citing works

Type 1 Interferons Induce Changes in Core Metabolism that Are Critical for Immune Function

Wu, D., Sanin, D. E., Everts, B., Chen, Q., Qiu, J., Buck, M. D., Patterson, A. E., Smith, A. M., Chang, C., Liu, Z., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.06.006 · Cited by 331 · see citing works

Behavior of Mitochondria in the Living Cell

Bereiter‐Hahn, J. (1990) · International review of cytology · doi:10.1016/s0074-7696(08)61205-x · Cited by 329 · see citing works

NLRX1 is a mitochondrial NOD‐like receptor that amplifies NF‐κB and JNK pathways by inducing reactive oxygen species production

Tattoli, I., Carneiro, L. A. M., Jéhanno, M., Magalhaes, J. G., Shu, Y., Philpott, D. J., Arnoult, D., & Girardin, S. E. (2008) · EMBO Reports · doi:10.1038/sj.embor.7401161 · Cited by 321 · see citing works

IL-1β/IL-6/CRP and IL-18/ferritin: Distinct Inflammatory Programs in Infections

Slaats, J., ten Oever, J., van de Veerdonk, F. L., & Netea, M. G. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005973 · Cited by 320 · see citing works

Mitochondrial N-formylmethionyl proteins as chemoattractants for neutrophils.

Carp, H. (1982) · The Journal of Experimental Medicine · doi:10.1084/jem.155.1.264 · Cited by 319 · see citing works

NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain

Stutz, A., Kolbe, C., Stahl, R., Horvath, G. L., Franklin, B. S., van Ray, O., Brinkschulte, R., Geyer, M., Meissner, F., & Latz, E. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20160933 · Cited by 317 · see citing works

Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway

Castanier, C., Garcin, D., Vazquez, A., & Arnoult, D. (2010) · The EMBO Reports · doi:10.1038/embor.2009.258 · Cited by 316 · see citing works

Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I

Peisley, A., Wu, B., Xu, H., Chen, Z. J., & Hur, S. (2014) · Nature · doi:10.1038/nature13140 · Cited by 315 · see citing works

Metabolism and function of mitochondrial cardiolipin

Ren, M., Phoon, C. K. L., & Schlame, M. (2014) · Progress in Lipid Research · doi:10.1016/j.plipres.2014.04.001 · Cited by 313 · see citing works

Mitochondrial respiratory-chain adaptations in macrophages contribute to antibacterial host defense

Garaude, J., Acín-Pérez, R., Martínez-Cano, S., Enamorado, M., Ugolini, M., Nistal-Villán, E., Hervás-Stubbs, S., Pelegrín, P., Sander, L. E., Enríquez, J. A., et al. (2016) · Nature Immunology · doi:10.1038/ni.3509 · Cited by 313 · see citing works

Microbial stimulation of different Toll-like receptor signalling pathways induces diverse metabolic programmes in human monocytes

Lachmandas, E., Boutens, L., Ratter, J. M., Hijmans, A., Hooiveld, G. J. E. J., Joosten, L. A. B., Rodenburg, R. J., Fransen, J. A. M., Houtkooper, R. H., van Crevel, R., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.246 · Cited by 310 · see citing works

Dephosphorylation of the RNA Sensors RIG-I and MDA5 by the Phosphatase PP1 Is Essential for Innate Immune Signaling

Wies, E., Wang, M. K., Maharaj, N. P., Chen, K., Zhou, S., Finberg, R. W., & Gack, M. U. (2013) · Immunity · doi:10.1016/j.immuni.2012.11.018 · Cited by 306 · see citing works

The Mitochondrial Proteins NLRX1 and TUFM Form a Complex that Regulates Type I Interferon and Autophagy

Lei, Y. L., Wen, H., Yu, Y., Taxman, D. J., Zhang, L., Widman, D. G., Swanson, K. V., Wen, K. W., Damania, B., Moore, C., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.03.025 · Cited by 297 · see citing works

Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection

Ichinohe, T., Yamazaki, T., Koshiba, T., & Yanagi, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312571110 · Cited by 284 · see citing works

INACTIVATION OF OXIDATIVE AND PHOSPHORYLATIVE SYSTEMS IN MITOCHONDRIA BY PREINCUBATION WITH PHOSPHATE AND OTHER IONS

Hunter, F. E., & Ford, L. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52312-2 · Cited by 279 · see citing works

NLRX1 Negatively Regulates TLR-Induced NF-κB Signaling by Targeting TRAF6 and IKK

Xia, X., Cui, J., Wang, H. Y., Zhu, L., Matsueda, S., Wang, Q., Yang, X., Hong, J. K., Songyang, Z., Chen, Z. J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.022 · Cited by 276 · see citing works

The Mitochondrial Antiviral Protein MAVS Associates with NLRP3 and Regulates Its Inflammasome Activity

Park, S., Juliana, C. A., Hong, S., Datta, P., Hwang, I., Fernandes‐Alnemri, T., Yu, J., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301170 · Cited by 266 · see citing works

IFNs Modify the Proteome of Legionella-Containing Vacuoles and Restrict Infection Via IRG1-Derived Itaconic Acid

Naujoks, J., Tabeling, C., Dill, B. D., Hoffmann, C., Brown, A. S., Kunze, M., Kempa, S., Peter, A., Mollenkopf, H.-J., Dorhoi, A., et al. (2016) · PLOS Pathogens · doi:10.1371/journal.ppat.1005408 · Cited by 261 · see citing works

Mitochondrial Membrane Potential Is Required for MAVS-Mediated Antiviral Signaling

Koshiba, T., Yasukawa, K., Yanagi, Y., & Kawabata, S.-I. (2011) · Science Signaling · doi:10.1126/scisignal.2001147 · Cited by 257 · see citing works

Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA

Boulay, F., Tardif, M., Brouchon, L., & Vignais, P. V. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91143-g · Cited by 256 · see citing works

Mitofusin 2 Inhibits Mitochondrial Antiviral Signaling

Yasukawa, K., Oshiumi, H., Takeda, M., Ishihara, N., Yanagi, Y., Seya, T., Kawabata, S.-I., & Koshiba, T. (2009) · Science Signaling · doi:10.1126/scisignal.2000287 · Cited by 255 · see citing works

The role of cardiolipin in the structural organization of mitochondrial membranes

Schlame, M., & Ren, M. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.04.019 · Cited by 248 · see citing works

The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation

Rodgers, M. A., Bowman, J. W., Fujita, H., Orazio, N., Shi, M., Liang, Q., Amatya, R., Kelly, T. J., Iwai, K., Ting, J., et al. (2014) · Journal of Experimental Medicine · doi:10.1084/jem.20132486 · Cited by 247 · see citing works

Molecular Mechanisms of the Crosstalk Between Mitochondria and NADPH Oxidase Through Reactive Oxygen Species—Studies in White Blood Cells and in Animal Models

Kröller‐Schön, S., Steven, S., Kossmann, S., Scholz, A., Daub, S., Oelze, M. W., Xia, N., Hausding, M., Mikhed, Y., Zinßius, E., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4953 · Cited by 246 · see citing works

Mitochondrial Cardiolipin Involved in Outer-Membrane Protein Biogenesis: Implications for Barth Syndrome

Gebert, N., Joshi, A., Kutik, S., Becker, T., McKenzie, M., Guan, X. L., Mooga, V. P., Stroud, D. A., Kulkarni, G., Wenk, M. R., et al. (2009) · Current Biology · doi:10.1016/j.cub.2009.10.074 · Cited by 239 · see citing works

A broken Krebs cycle in macrophages

O’Neill, L. A. J. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.017 · Cited by 232 · see citing works

Biosynthesis, remodeling and turnover of mitochondrial cardiolipin

Schlame, M., & Greenberg, M. L. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.010 · Cited by 230 · see citing works

Mitochondrial Permeability Transition: New Findings and Persisting Uncertainties

Izzo, V., Bravo-San Pedro, J. M., Sica, V., Kroemer, G., & Galluzzi, L. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.04.006 · Cited by 205 · see citing works

Resistance to Caspase-Independent Cell Death Requires Persistence of Intact Mitochondria

Tait, S. W. G., Parsons, M. J., Llambi, F., Bouchier‐Hayes, L., Connell, S., Muñoz‐Pinedo, C., & Green, D. R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.014 · Cited by 204 · see citing works

An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix

Arnoult, D., Soares, F., Tattoli, I., Castanier, C., Philpott, D. J., & Girardin, S. E. (2009) · Journal of Cell Science · doi:10.1242/jcs.051193 · Cited by 203 · see citing works

Cutting Edge: Mitochondrial Assembly of the NLRP3 Inflammasome Complex Is Initiated at Priming

Elliott, E. I., Miller, A. N., Banoth, B., Iyer, S. S., Stotland, A. B., Weiss, J. P., Gottlieb, R. A., Sutterwala, F. S., & Cassel, S. L. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1701723 · Cited by 198 · see citing works

Pleiotropic roles of formyl peptide receptors

Le, Y., Oppenheim, J. J., & Wang, J. (2001) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(01)00003-x · Cited by 191 · see citing works

It's time to redefine inflammation

Antonelli, M. J., & Kushner, I. (2017) · The FASEB Journal · doi:10.1096/fj.201601326r · Cited by 188 · see citing works

cGAS and Ifi204 Cooperate To Produce Type I IFNs in Response to Francisella Infection

Storek, K. M., Talmor, N., Ohlson, M. B., & Monack, D. M. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402764 · Cited by 184 · see citing works

Acute lipopolysaccharide priming boosts inflammasome activation independently of inflammasome sensor induction

Schroder, K., Sagulenko, V., Zamoshnikova, A., Richards, A. A., Cridland, J. A., Irvine, K. M., Stacey, K. J., & Sweet, M. J. (2012) · Immunobiology · doi:10.1016/j.imbio.2012.07.020 · Cited by 182 · see citing works

Virus-Infection or 5′ppp-RNA Activates Antiviral Signal through Redistribution of IPS-1 Mediated by MFN1

Onoguchi, K., Onomoto, K., Takamatsu, S., Jogi, M., Takemura, A., Morimoto, S., Julkunen, I., Namiki, H., Yoneyama, M., & Fujita, T. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001012 · Cited by 180 · see citing works

The E3 Ubiquitin Ligase RNF5 Targets Virus-Induced Signaling Adaptor for Ubiquitination and Degradation

Zhong, B., Zhang, Y., Tan, B., Liu, T., Wang, Y., & Shu, H. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903748 · Cited by 177 · see citing works

Use the Protonmotive Force: Mitochondrial Uncoupling and Reactive Oxygen Species

Berry, B. J., Trewin, A. J., Amitrano, A. M., Kim, M., & Wojtovich, A. P. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.025 · Cited by 175 · see citing works

Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to chromosome 19

Lu, B., Gerard, N. P., Eddy, R. L., Shows, T. B., & Gerard, C. J. (1992) · Genomics · doi:10.1016/0888-7543(92)90265-t · Cited by 173 · see citing works

Import, Maturation, and Function of SOD1 and Its Copper Chaperone CCS in the Mitochondrial Intermembrane Space

Kawamata, H., & Manfredi, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3212 · Cited by 171 · see citing works

Deubiquitinases Regulate the Activity of Caspase-1 and Interleukin-1β Secretion via Assembly of the Inflammasome

López‐Castejón, G., Luheshi, N., Compan, V., High, S., Whitehead, R. C., Flitsch, S. L., Kirov, A., Prudovsky, I. A., Swanton, E., & Brough, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422238 · Cited by 166 · see citing works

The N-formyl peptide receptors and the anaphylatoxin C5a receptors: An overview

Rabiet, M., HUET, E., & Boulay, F. (2007) · Biochimie · doi:10.1016/j.biochi.2007.02.015 · Cited by 166 · see citing works

Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria

Xu, L., Xiao, N., Liu, F., Ren, H., & Gu, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811029106 · Cited by 159 · see citing works

NLRX1 Sequesters STING to Negatively Regulate the Interferon Response, Thereby Facilitating the Replication of HIV-1 and DNA Viruses

Guo, H., König, R., Deng, M., Rieß, M., Mo, J., Zhang, L., Petrucelli, A., Yoh, S. M., Barefoot, B. E., Samo, M., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.03.001 · Cited by 153 · see citing works

Enhancement of Reactive Oxygen Species Production and Chlamydial Infection by the Mitochondrial Nod-like Family Member NLRX1

Sater, A. A. A., Sadier, N. S., Lam, V. W., Singh, B., Pettengill, M. A., Soares, F., Tattoli, I., Lipinski, S., Girardin, S. E., Rosenstiel, P. C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.137885 · Cited by 151 · see citing works

Requirement of NOX2 and Reactive Oxygen Species for Efficient RIG-I-Mediated Antiviral Response through Regulation of MAVS Expression

Soucy-Faulkner, A., Mukawera, E., Fink, K., Martel, A., Jouan, L., Nzengue, Y., Lamarre, D., Velde, C. V., & Grandvaux, N. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000930 · Cited by 142 · see citing works

Intramitochondrial phospholipid trafficking

Tatsuta, T., & Langer, T. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.006 · Cited by 129 · see citing works

The Emerging Roles of STING in Bacterial Infections

Marinho, F. V., Benmerzoug, S., Oliveira, S. C., Ryffel, B., & Quesniaux, V. F. J. (2017) · Trends in Microbiology · doi:10.1016/j.tim.2017.05.008 · Cited by 124 · see citing works

Identification of an LGP2-associated MDA5 agonist in picornavirus-infected cells

Deddouche, S., Goubau, D., Rehwinkel, J., Chakravarty, P., Begum, S., Maillard, P. V., Borg, A., Matthews, N., Feng, Q., van Kuppeveld, F. J. M., et al. (2014) · eLife · doi:10.7554/elife.01535 · Cited by 118 · see citing works

NLRX1 dampens oxidative stress and apoptosis in tissue injury via control of mitochondrial activity

Stokman, G., Kors, L., Bakker, P. J., Rampanelli, E., Claessen, N., Teske, G. J. D., Butter, L. M., van Andel, H., Weerman, M. A. V. D. B., Larsen, P. W. B., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20161031 · Cited by 112 · see citing works

Monocyte activation by necrotic cells is promoted by mitochondrial proteins and formyl peptide receptors

Crouser, E. D., Shao, G., JULIAN, M. W., Macre, J. E., Shadel, G. S., Tridandapani, S., Huang, Q., & Wewers, M. D. (2009) · Critical Care Medicine · doi:10.1097/ccm.0b013e3181a001ae · Cited by 108 · see citing works

Mitochondrial Damage Associated Molecular Patterns From Femoral Reamings Activate Neutrophils Through Formyl Peptide Receptors and P44/42 MAP Kinase

Hauser, C. J., Sursal, T., Rodriguez, E. K., Appleton, P. T., Zhang, Q., & Itagaki, K. (2010) · Journal of Orthopaedic Trauma · doi:10.1097/bot.0b013e3181ec4991 · Cited by 107 · see citing works

Polo-like Kinase 1 (PLK1) Regulates Interferon (IFN) Induction by MAVS

Vitour, D., Dabo, S., Pour, M. A., Vilasco, M., Vidalain, P., Jacob, Y., Mesel‐Lemoine, M., Paz, S., Arguello, M., Lin, R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.018275 · Cited by 101 · see citing works

Structure and Function of Leukocyte Chemoattractant Receptors

Ye, R. D., & Boulay, F. (1997) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60073-3 · Cited by 99 · see citing works

The Role of Cardiolipin in Cardiovascular Health

Shen, Z., Ye, C., McCain, K., & Greenberg, M. L. (2015) · BioMed Research International · doi:10.1155/2015/891707 · Cited by 97 · see citing works

LGP2 Plays a Critical Role in Sensitizing mda-5 to Activation by Double-Stranded RNA

Childs, K., Randall, R. E., & Goodbourn, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064202 · Cited by 96 · see citing works

TAK1-ECSIT-TRAF6 Complex Plays a Key Role in the TLR4 Signal to Activate NF-κB

Wi, S. M., Moon, G., Kim, J., Kim, S., Shim, J., Chun, E., & Lee, K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.597187 · Cited by 95 · see citing works

Co-regulation of nuclear respiratory factor-1 by NFκB and CREB links LPS-induced inflammation to mitochondrial biogenesis

Suliman, H. B., Sweeney, T. E., Withers, C. M., & Piantadosi, C. A. (2010) · Journal of Cell Science · doi:10.1242/jcs.064089 · Cited by 93 · see citing works

NLRX1 promotes immediate IRF1-directed antiviral responses by limiting dsRNA-activated translational inhibition mediated by PKR

Feng, H., Lenarcic, E. M., Yamane, D., Wauthier, E., Mo, J., Guo, H., McGivern, D. R., González‐López, O., Misumi, I., Reid, L. M., et al. (2017) · Nature Immunology · doi:10.1038/ni.3853 · Cited by 93 · see citing works

Toll‐like receptor 4 mediates mitochondrial DNA damage and biogenic responses after heat‐inactivated E. coli

Suliman, H. B., Welty‐Wolf, K. E., Carraway, M. S., Schwartz, D. A., Hollingsworth, J. W., & Piantadosi, C. A. (2005) · The FASEB Journal · doi:10.1096/fj.04-3500fje · Cited by 92 · see citing works

Mammalian SOD2 is exclusively located in mitochondria and not present in peroxisomes

Karnati, S., Lüers, G. H., Pfreimer, S., & Baumgart‐Vogt, E. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1099-4 · Cited by 91 · see citing works

An Essential Role for ECSIT in Mitochondrial Complex I Assembly and Mitophagy in Macrophages

Carneiro, F. R. G., Lepelley, A., Seeley, J. J., Hayden, M. S., & Ghosh, S. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.051 · Cited by 90 · see citing works

The E3 Ubiquitin Ligase Tripartite Motif 33 Is Essential for Cytosolic RNA–Induced NLRP3 Inflammasome Activation

Weng, L., Mitoma, H., Tricot, C., Bao, M., Liu, Y., Zhang, Z., & Liu, Y.-J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401448 · Cited by 90 · see citing works

Novel role for endogenous mitochondrial formylated peptide-driven formyl peptide receptor 1 signalling in acute respiratory distress syndrome

Dorward, D., Lucas, C. D., Doherty, M., Chapman, G. B., Scholefield, E., Morris, A. C., Felton, J., Kipari, T., Humphries, D. C., Robb, C., et al. (2017) · Thorax · doi:10.1136/thoraxjnl-2017-210030 · Cited by 89 · see citing works

Repair of 8-oxoG is slower in endogenous nuclear genes than in mitochondrial DNA and is without strand bias

Thorslund, T., Sunesen, M., Bohr, V. A., & Stevnsner, T. (2002) · DNA repair · doi:10.1016/s1568-7864(02)00003-4 · Cited by 88 · see citing works

NLRX1 does not inhibit MAVS-dependent antiviral signalling

Soares, F., Tattoli, I., Wortzman, M. E., Arnoult, D., Philpott, D. J., & Girardin, S. E. (2012) · Innate Immunity · doi:10.1177/1753425912467383 · Cited by 88 · see citing works

Cellular redox dysfunction in the development of cardiovascular diseases

Kanaan, G. N., & Harper, M. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.07.027 · Cited by 87 · see citing works

Mitochondrial Transcription Factor A, an Endogenous Danger Signal, Promotes TNFα Release via RAGE- and TLR9-Responsive Plasmacytoid Dendritic Cells

Julian, M. W., Shao, G., VanGundy, Z. C., Papenfuss, T. L., & Crouser, E. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072354 · Cited by 85 · see citing works

Dichotomous roles for externalized cardiolipin in extracellular signaling: Promotion of phagocytosis and attenuation of innate immunity

Balasubramanian, K., Maeda, A., Lee, J. S., Mohammadyani, D., Dar, H. H., Jiang, J. F., Croix, C. M. S., Watkins, S. C., Tyurin, V. A., Tyurina, Y. Y., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aaa6179 · Cited by 83 · see citing works

Leukocyte Chemoattractant Receptors in Human Disease Pathogenesis

Zabel, B. A., Rott, A., & Butcher, E. C. (2014) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104640 · Cited by 76 · see citing works

Nod-Like Receptor X-1 Is Required for Rhinovirus-Induced Barrier Dysfunction in Airway Epithelial Cells

Unger, B. L., Ganesan, S., Comstock, A. T., Faris, A. N., Hershenson, M. B., & Sajjan, U. S. (2014) · Journal of Virology · doi:10.1128/jvi.03039-13 · Cited by 74 · see citing works

NLRX1/NOD5 deficiency does not affect MAVS signalling

Rebsamen, M., Vázquez, J., Tardivel, A., Guarda, G., Curran, J. A., & Tschopp, J. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.64 · Cited by 74 · see citing works

Mitochondrial transcription factor A is a proinflammatory mediator in hemorrhagic shock

Wang, P. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.959 · Cited by 73 · see citing works

Participation of c-FLIP in NLRP3 and AIM2 inflammasome activation

Wu, Y., Kuo, W.-C., Wu, Y.-J., Yang, K.-T., Chen, S.-T., Jiang, S.-T., Gordy, C. L., He, Y., & Lai, M.-Z. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.165 · Cited by 73 · see citing works

Ubiquitin-mediated modulation of the cytoplasmic viral RNA sensor RIG-I

Oshiumi, H., Matsumoto, M., & Seya, T. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr111 · Cited by 72 · see citing works

Innate immunity: quo vadis?

Medzhitov, R. M. (2010) · Nature Immunology · doi:10.1038/ni0710-551 · Cited by 71 · see citing works

Cardiolipin-protein complexes and initiation of complement activation after coronary artery occlusion.

Rossen, R. D., Michael, L. H., Hawkins, H. K., Youker, K. A., Dreyer, W. J., BAUGHN, R. E., & Entman, M. L. (1994) · Circulation Research · doi:10.1161/01.res.75.3.546 · Cited by 71 · see citing works

Mitochondrial Ubiquitin Ligase MARCH5 Promotes TLR7 Signaling by Attenuating TANK Action

Shi, H.-X., Liu, X., Wang, Q., Tang, P.-P., Liu, X.-Y., Shan, Y.-F., & Wang, C. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002057 · Cited by 67 · see citing works

Structural Determinants for the Interaction of Formyl Peptide Receptor 2 with Peptide Ligands

He, H.-Q., Troksa, E. L., Caltabiano, G., Pardo, L., & Ye, R. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.509216 · Cited by 64 · see citing works

Interaction of mitochondrial initiation factor 2 with mitochondrial fMet-tRNA

Spencer, A. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh886 · Cited by 61 · see citing works

Mitochondrial-derived N-formyl peptides: Novel links between trauma, vascular collapse and sepsis

Wenceslau, C. F., McCarthy, C. G., Goulopoulou, S., Szasz, T., NeSmith, E. G., & Webb, R. C. (2013) · Medical Hypotheses · doi:10.1016/j.mehy.2013.06.026 · Cited by 56 · see citing works

Differential Regulation of the PGC Family of Genes in a Mouse Model of Staphylococcus aureus Sepsis

Sweeney, T. E., Suliman, H. B., Hollingsworth, J. W., & Piantadosi, C. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011606 · Cited by 54 · see citing works

Translocation of protein kinase C in human polymorphonuclear neutrophils. Regulation by cytosolic Ca2(+)-independent and Ca2(+)-dependent mechanisms.

O’Flaherty, J. T., Jacobson, D. P., Redman, J. F., & Rossi, A. G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38823-4 · Cited by 51 · see citing works

The Synthetic Peptide Trp-Lys-Tyr-Met-Val-D-Met Inhibits Human Monocyte-Derived Dendritic Cell Maturation via Formyl Peptide Receptor and Formyl Peptide Receptor-Like 2

Kang, H. K., Lee, H., Kim, M.-K., Park, K. S., Park, Y. M., Kwak, J., & Bae, Y. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.2.685 · Cited by 48 · see citing works

Cardiolipin-protein complexes and initiation of complement activation after coronary artery occlusion.

DRossen, R., HMichael, L., KHawkins, H., KYouker, JDreyer, W., EBaughn, R., & LEntman, M. (1994) · Circulation Research · Cited by 48 · see citing works

Potent NLRP3 Inflammasome Activation by the HIV Reverse Transcriptase Inhibitor Abacavir

Toksoy, A., Sennefelder, H., Adam, C., Hofmann, S., Trautmann, A., Goebeler, M., & Schmidt, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.749473 · Cited by 46 · see citing works

Structural changes of the ligand and of the receptor alters the receptor preference for neutrophil activating peptides starting with a formylmethionyl group

Forsman, H. F., Winther, M., Gabl, M., Skovbakke, S. L., Boulay, F., Rabiet, M., & Dahlgren, C. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.10.021 · Cited by 39 · see citing works

Pattern recognition receptors in health and diseases

Li, D., & Wu, M. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00687-0 · Cited by 1,830 · see citing works

Mitochondria in oxidative stress, inflammation and aging: from mechanisms to therapeutic advances

Xu, X., Pang, Y., & Fan, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02253-4 · Cited by 939 · see citing works

Mitochondria in health, disease, and aging

Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 622 · see citing works

Comprehensive Multi-omics Analysis Reveals Mitochondrial Stress as a Central Biological Hub for Spaceflight Impact

da Silveira, W. A., Fazelinia, H., Rosenthal, S. B., Laiakis, E. C., Kim, M. S., Meydan, C., Kidane, Y., Rathi, K. S., Smith, S. M., Stear, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.11.002 · Cited by 402 · see citing works

Mitochondria, Oxidative Stress and Innate Immunity

Chen, Y., Zhou, Z., & Min, W. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01487 · Cited by 315 · see citing works

Mitochondria Are a Subset of Extracellular Vesicles Released by Activated Monocytes and Induce Type I IFN and TNF Responses in Endothelial Cells

Puhm, F., Afonyushkin, T., Resch, U., Obermayer, G., Rohde, M., Penz, T., Schuster, M., Wagner, G., Rendeiro, A. F., Melki, I., et al. (2019) · Circulation Research · doi:10.1161/circresaha.118.314601 · Cited by 306 · see citing works

Chronic Inflammation in Chronic Kidney Disease Progression: Role of Nrf2

Stenvinkel, P., Chertow, G. M., Devarajan, P., Levin, A., Andreoli, S. P., Bangalore, S., & Warady, B. A. (2021) · Kidney International Reports · doi:10.1016/j.ekir.2021.04.023 · Cited by 301 · see citing works

Neutrophil diversity and function in health and disease

Zhang, F., Xia, Y., Su, J., Quan, F., Zhou, H., Li, Q., Feng, Q., Lin, C., Wang, D., & Jiang, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02049-y · Cited by 283 · see citing works

Role of Mitochondria in Radiation Responses: Epigenetic, Metabolic, and Signaling Impacts

Averbeck, D., & Rodriguez‐Lafrasse, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011047 · Cited by 242 · see citing works

Role of metabolic reprogramming in pro-inflammatory cytokine secretion from LPS or silica-activated macrophages

Marrocco, A., & Ortiz, L. A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.936167 · Cited by 166 · see citing works

Metabolic reprogramming consequences of sepsis: adaptations and contradictions

Liu, J., Zhou, G., Wang, X., & Liu, D. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04490-0 · Cited by 159 · see citing works

Mitochondria-derived cell-to-cell communication

Dache, Z. A. A., & Thierry, A. R. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112728 · Cited by 155 · see citing works

Elucidating Role of Reactive Oxygen Species (ROS) in Cisplatin Chemotherapy: A Focus on Molecular Pathways and Possible Therapeutic Strategies

Mirzaei, S., Hushmandi, K., Zabolian, A., Saleki, H., Torabi, S. M., Ranjbar, A., SeyedSaleh, S., Sharifzadeh, S. O., Khan, H. Z., Ashrafizadeh, M., et al. (2021) · Molecules · doi:10.3390/molecules26082382 · Cited by 150 · see citing works

Mitochondria as a target for neuroprotection: role of methylene blue and photobiomodulation

Yang, L., Youngblood, H. A., Wu, C., & Zhang, Q. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00197-z · Cited by 143 · see citing works

Role of Mitochondria in Physiology of Chondrocytes and Diseases of Osteoarthritis and Rheumatoid Arthritis

Kan, S., Duan, M., Liu, Y., Wang, C., & Xie, J. (2021) · Cartilage · doi:10.1177/19476035211063858 · Cited by 143 · see citing works

The role of inflammation in hypertension: novel concepts

Patrick, D. M., Beusecum, J. P. V., & Kirabo, A. (2020) · Current Opinion in Physiology · doi:10.1016/j.cophys.2020.09.016 · Cited by 136 · see citing works

The cGAS‐STING pathway: The role of self‐DNA sensing in inflammatory lung disease

Ma, R., Serrano, T. P. O., Davis, J., Prigge, A. D., & Ridge, K. M. (2020) · The FASEB Journal · doi:10.1096/fj.202001607r · Cited by 133 · see citing works

Mitochondria: at the crossroads of regulating lung epithelial cell function in chronic obstructive pulmonary disease

Aghapour, M., Remels, A. H. V., Pouwels, S. D., Bruder, D., Hiemstra, P. S., Cloonan, S. M., & Heijink, I. H. (2019) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00329.2019 · Cited by 122 · see citing works

Biomarkers of mitochondrial dysfunction in autism spectrum disorder: A systematic review and meta-analysis

Frye, R. E., Rincon, N., McCarty, P. J., Brister, D., Scheck, A. C., & Rossignol, D. A. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106520 · Cited by 127 · see citing works

Role of Mitochondria in Viral Infections

Elesela, S., & Lukacs, N. W. (2021) · Life · doi:10.3390/life11030232 · Cited by 113 · see citing works

Mitochondria: In the Cross Fire of SARS-CoV-2 and Immunity

Burtscher, J., Cappellano, G., Omori, A., Koshiba, T., & Millet, G. P. (2020) · iScience · doi:10.1016/j.isci.2020.101631 · Cited by 107 · see citing works

DNA damage-triggered activation of cGAS-STING pathway induces apoptosis in human keratinocyte HaCaT cells

Li, C., Liu, W., Wang, F., Hayashi, T., Mizuno, K., Hattori, S., Fujisaki, H., & Ikejima, T. (2021) · Molecular Immunology · doi:10.1016/j.molimm.2020.12.037 · Cited by 104 · see citing works

Reactive Oxygen Species: A Crosslink between Plant and Human Eukaryotic Cell Systems

Guo, W., Xing, Y., Luo, X., Li, F., Ren, M., & Liang, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713052 · Cited by 107 · see citing works

Mitochondrial Dysfunction: A Key Player in Brain Aging and Diseases

Bartman, S., Coppotelli, G., & Ross, J. M. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46030130 · Cited by 101 · see citing works

Nanotherapies for sepsis by regulating inflammatory signals and reactive oxygen and nitrogen species: New insight for treating COVID-19

Chen, L., Huang, Q., Zhao, T., Sui, L., Wang, S., Xiao, Z., Nan, Y., & Ai, K. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102046 · Cited by 98 · see citing works

Mechanistic Studies of Idiosyncratic DILI: Clinical Implications

Uetrecht, J. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00837 · Cited by 91 · see citing works

CircPVT1 promotes ER‐positive breast tumorigenesis and drug resistance by targeting ESR1 and MAVS

Jia, Y., Wang, L., Hu, G.-S., Zhang, Y., Du, J., Ding, J., Ji, X., Shen, H., Huang, H., Ye, F., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112408 · Cited by 87 · see citing works

Mitochondrial Oxidative Stress in Brain Microvascular Endothelial Cells: Triggering Blood-Brain Barrier Disruption.

Wang, Y., Wu, J., Wang, J.-X., He, L.-X., Lai, H., Zhang, T., Wang, X., & Li, W. (2023) · Mitochondrion (Amsterdam. Print) · doi:10.1016/j.mito.2023.01.007 · Cited by 80 · see citing works

Role of released mitochondrial DNA in acute lung injury

Long, G., Gong, R., Wang, Q., Zhang, D., & Huang, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.973089 · Cited by 83 · see citing works

From Mitochondria to Atherosclerosis: The Inflammation Path

Suarez-Rivero, J. M., Pastor‐Maldonado, C. J., Povea-Cabello, S., Álvarez-Córdoba, M., Villalón-García, I., Talaverón-Rey, M., Suárez-Carrillo, A., Munuera-Cabeza, M., & Sánchez-Alcázar, J. A. (2021) · Biomedicines · doi:10.3390/biomedicines9030258 · Cited by 77 · see citing works

FUNDC2 promotes liver tumorigenesis by inhibiting MFN1-mediated mitochondrial fusion

Li, S., Han, S., Zhang, Q., Zhu, Y., Zhang, H., Wang, J., Zhao, Y., Zhao, J., Su, L., Li, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31187-6 · Cited by 77 · see citing works

Mitochondrial control of innate immune responses

Chen, S., Liao, Z., & Xu, P. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1166214 · Cited by 77 · see citing works

Role of mitochondria in physiological activities, diseases, and therapy

Wang, L., Zhou, X., & Lu, T. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00284-5 · Cited by 79 · see citing works

Mitochondria and Viral Infection: Advances and Emerging Battlefronts

Sorouri, M., Chang, T., & Hancks, D. C. (2022) · mBio · doi:10.1128/mbio.02096-21 · Cited by 69 · see citing works

4-octyl itaconate ameliorates alveolar macrophage pyroptosis against ARDS via rescuing mitochondrial dysfunction and suppressing the cGAS/STING pathway

Wu, Y., Xu, W., Li, Z., Wang, S., Wei, J., Liu, M., Zhou, H., Li, Q., Shi, X., & Lv, X. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110104 · Cited by 72 · see citing works

Amyloid β-dependent mitochondrial toxicity in mouse microglia requires P2X7 receptor expression and is prevented by nimodipine

Chiozzi, P., Sarti, A. C., Sanz, J. M., Giuliani, A. L., Adinolfi, E., Vultaggio-Poma, V., Falzoni, S., & Virgilio, F. D. (2019) · Scientific Reports · doi:10.1038/s41598-019-42931-2 · Cited by 71 · see citing works

Mitochondrial Dysfunction in Rheumatoid Arthritis

Ma, C., Wang, J., Hong, F., & Yang, S. (2022) · Biomolecules · doi:10.3390/biom12091216 · Cited by 71 · see citing works

The role of mitochondrial dysfunction in periodontitis: From mechanisms to therapeutic strategy

Jiang, W., Wang, Y., Cao, Z., Chen, Y., Si, C., Sun, X., & Huang, S. (2023) · Journal of Periodontal Research · doi:10.1111/jre.13152 · Cited by 70 · see citing works

Mitochondrial Dysfunction and Coenzyme Q10 Supplementation in Post-Viral Fatigue Syndrome: An Overview

Mantle, D., Hargreaves, I. P., Domingo, J. C., & Castro‐Marrero, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25010574 · Cited by 70 · see citing works

Micronuclei, inflammation and auto-immune disease

Kirsch‐Volders, M., Bolognesi, C., Ceppi, M., Bruzzone, M., & Fenech, M. F. (2020) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2020.108335 · Cited by 70 · see citing works

Clinical Manifestations and Pathogenesis of Acute Necrotizing Encephalopathy: The Interface Between Systemic Infection and Neurologic Injury

Shukla, P., Mandalla, A., Elrick, M. J., & Venkatesan, A. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2021.628811 · Cited by 69 · see citing works

SARS-CoV-2: A Master of Immune Evasion

Rubio‐Casillas, A., Redwan, E. M. M. M., & Uversky, V. N. (2022) · Biomedicines · doi:10.3390/biomedicines10061339 · Cited by 70 · see citing works

TAT‐dextran–mediated mitochondrial transfer enhances recovery from models of reperfusion injury in cultured cardiomyocytes

Maeda, H., Kami, D., Maeda, R., Murata, Y., Jo, J., Kitani, T., Tabata, Y., Matoba, S., & Gojo, S. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15120 · Cited by 69 · see citing works

Altitude and COVID‐19: Friend or foe? A narrative review

Millet, G. P., Debevec, T., Brocherie, F., Burtscher, M., & Burtscher, J. (2020) · Physiological Reports · doi:10.14814/phy2.14615 · Cited by 63 · see citing works

Emerging perspectives on mitochondrial dysfunction and inflammation in Alzheimer’s disease

Yoo, S., Park, J., Kim, S., & Jung, Y. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.1.274 · Cited by 65 · see citing works

A novel mechanism for the protection against acute lung injury by melatonin: mitochondrial quality control of lung epithelial cells is preserved through SIRT3-dependent deacetylation of SOD2

Li, N., Xiong, R., Li, G., Fu, T., Li, D., Xu, C., Wu, X., & Geng, Q. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04628-0 · Cited by 64 · see citing works

The central role of mitochondrial fitness on antiviral defenses: An advocacy for physical activity during the COVID-19 pandemic

Burtscher, J., Burtscher, M., & Millet, G. P. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101976 · Cited by 65 · see citing works

Circulating Mitochondrial DNA Stimulates Innate Immune Signaling Pathways to Mediate Acute Kidney Injury

Liu, J., Jia, Z., & Gong, W. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.680648 · Cited by 63 · see citing works

STING mediates neuroinflammatory response by activating NLRP3 ‐related pyroptosis in severe traumatic brain injury

Zhang, L., Xin, Y., Wu, Z., Song, R., Miao, H., Zheng, W., Li, Y., Zhang, D., & Zhao, X. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15678 · Cited by 65 · see citing works

Simultaneous Activation of Immunogenic Cell Death and cGAS-STING Pathway by Liver- and Mitochondria-Targeted Gold(I) Complexes for Chemoimmunotherapy of Hepatocellular Carcinoma

Li, F., Wen, Z., Wu, C., Yang, Z., Wang, Z., Diao, W., Chen, D., Xu, Z., Lu, Y., & Liu, W. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01785 · Cited by 63 · see citing works

Bioenergetics and translational metabolism: implications for genetics, physiology and precision medicine

Hill, B. G., Shiva, S., Ballinger, S. W., Zhang, J., & Darley-Usmar, V. M. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0268 · Cited by 65 · see citing works

Insights from Animal Models on the Pathophysiology of Hyperphenylalaninemia: Role of Mitochondrial Dysfunction, Oxidative Stress and Inflammation

Wyse, Â. T. D. S., dos Santos, T. M., Seminotti, B., & Leipnitz, G. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02304-1 · Cited by 63 · see citing works

Mitochondrial hyperfusion: a friend or a foe

Das, R., & Chakrabarti, O. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190987 · Cited by 58 · see citing works

Mitochondrion: a sensitive target for Pb exposure

Han, Q., Zhang, W. K., Guo, J., Zhu, Q., Chen, H., Xia, Y., & Zhu, G. (2021) · The Journal of Toxicological Sciences · doi:10.2131/jts.46.345 · Cited by 61 · see citing works

A novel protein CYTB-187AA encoded by the mitochondrial gene CYTB modulates mammalian early development

Hu, Z., Yang, L., Zhang, M., Tang, H., Huang, Y., Su, Y., Ding, Y., Li, C. V., Wang, M., Zhou, Y., et al. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.04.012 · Cited by 62 · see citing works

Targeting Host Defense System and Rescuing Compromised Mitochondria to Increase Tolerance against Pathogens by Melatonin May Impact Outcome of Deadly Virus Infection Pertinent to COVID-19

Tan, D. X., & Hardeland, R. (2020) · Molecules · doi:10.3390/molecules25194410 · Cited by 60 · see citing works

SARS-CoV-2 and mitochondrial health: implications of lifestyle and ageing

Nunn, A. V. W., Guy, G. W., Brysch, W., Botchway, S. W., Frasch, W. D., Calabrese, E. J., & Bell, J. D. (2020) · Immunity & Ageing · doi:10.1186/s12979-020-00204-x · Cited by 59 · see citing works

Modulated Ultrasmall γ‐Fe2O3 Nanocrystal Assemblies for Switchable Magnetic Resonance Imaging and Photothermal‐Ferroptotic‐Chemical Synergistic Cancer Therapy

Yang, B.-C., Zhang, Y., Sun, L.-X., Wang, J., Zhao, Z., Huang, Z., Mao, W., Xue, R., Chen, R.-S., Luo, J.-J., et al. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202211251 · Cited by 53 · see citing works

Astragaloside IV, as a potential anticancer agent

Xia, D., Li, W., Tang, C., & Jiang, J. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1065505 · Cited by 55 · see citing works

FABP4 deactivates NF‐κB‐IL1α pathway by ubiquitinating ATPB in tumor‐associated macrophages and promotes neuroblastoma progression

Miao, L., Zhuo, Z., Tang, J., Huang, X., Liu, J., Wang, H., Xia, H., & He, J. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.395 · Cited by 55 · see citing works

IFNγ causes mitochondrial dysfunction and oxidative stress in myositis

Abad, C., Pinal‐Fernandez, I., Guillou, C., Bourdenet, G., Drouot, L., Cosette, P., Giannini, M., Debrut, L., Jean, L., Bernard, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49460-1 · Cited by 54 · see citing works

Inflammation and oxidative stress in salt sensitive hypertension; The role of the NLRP3 inflammasome

Ertuğlu, L. A., Mutchler, A. P., Yu, J. D., & Kirabo, A. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1096296 · Cited by 53 · see citing works

ISG15, a Small Molecule with Huge Implications: Regulation of Mitochondrial Homeostasis

Albert, M., Bécares, M., Falqui, M., Fernandez-Lozano, C., & Guerra, S. (2018) · Viruses · doi:10.3390/v10110629 · Cited by 50 · see citing works

Signaling pathway network alterations in human ovarian cancers identified with quantitative mitochondrial proteomics

Li, N., & Zhan, X. (2019) · The EPMA Journal · doi:10.1007/s13167-019-00170-5 · Cited by 52 · see citing works

Rheumatoid arthritis and mitochondrial homeostasis: The crossroads of metabolism and immunity

Liu, C., Jing, W., Su, C.-H., Liu, L., Xinghua, Z., Yuan, B., Xiaozheng, D., & Wang, H. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.1017650 · Cited by 54 · see citing works

Role of oxidative stress in mitochondrial dysfunction and their implications in intervertebral disc degeneration: Mechanisms and therapeutic strategies

Zhou, H., Wu, C., Jin, Y., Wu, O., Chen, L., Guo, Z., Xinzhou, W., Chen, Q., Kwan, K. Y.-H., Li, Y. M., et al. (2024) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2024.08.016 · Cited by 52 · see citing works

Mitochondria as the Essence of Yang Qi in the Human Body

Luo, J., Shiwei, S., Xia, J., Wang, J., & Gu, Z. (2022) · Phenomics · doi:10.1007/s43657-022-00060-3 · Cited by 50 · see citing works

Novel Coronavirus Disease 2019 (COVID-19) and Cytokine Storms for More Effective Treatments from an Inflammatory Pathophysiology

Yokota, S., Miyamae, T., Kuroiwa, Y., & Nishioka, K. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10040801 · Cited by 49 · see citing works

m6A methylation-induced NR1D1 ablation disrupts the HSC circadian clock and promotes hepatic fibrosis

Chen, L., Xia, S., Wang, F., Zhou, Y., Wang, S., Yang, T., Yang, L., Xu, M., Zhou, Y., Kong, D., et al. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106704 · Cited by 49 · see citing works

Systemic inflammatory response syndrome is triggered by mitochondrial damage (Review)

Kong, C., Song, W., & Fu, T. (2022) · Molecular Medicine Reports · doi:10.3892/mmr.2022.12663 · Cited by 48 · see citing works

Enhancing anti-tumour innate immunity by targeting the DNA damage response and pattern recognition receptors in combination with radiotherapy

Hak, C. C. W., Rullan, A., Patin, E. C., Pedersen, M., Melcher, A. A., & Harrington, K. J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.971959 · Cited by 48 · see citing works

Moderate exercise induces trained immunity in macrophages

Murugathasan, M., Jafari, A., Amandeep, A., Hassan, S. A., Chihata, M., & Sater, A. A. A. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00130.2023 · Cited by 49 · see citing works

Mitochondrial unfolded protein response: A novel pathway in metabolism and immunity

Zhu, L., Luo, X., Fu, N., & Chen, L. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105603 · Cited by 47 · see citing works

From mitochondrial dysfunction to neuroinflammation in Parkinson’s disease: Pathogenesis and mitochondrial therapeutic approaches

Ebadpour, N., Mahmoudi, M., Kheder, R. K., Abavisani, M., Baridjavadi, Z., Abdollahi, N., & Esmaeili, S. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113015 · Cited by 48 · see citing works

Neuroinflammation and Mitochondrial Dysfunction Link Social Stress to Depression

Hollis, F., Pope, B. S., Gorman‐Sandler, E., & Wood, S. K. (2022) · Current topics in behavioral neurosciences · doi:10.1007/7854_2021_300 · Cited by 47 · see citing works

Quercetin Reprograms Immunometabolism of Macrophages via the SIRT1/PGC-1α Signaling Pathway to Ameliorate Lipopolysaccharide-Induced Oxidative Damage

Peng, J., Yang, Z., Li, H., Hao, B., Cui, D., Shang, R., Lv, Y., Liu, Y., Pu, W., Zhang, H., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065542 · Cited by 48 · see citing works

The mitochondrial antioxidant SS-31 attenuated lipopolysaccharide-induced apoptosis and pyroptosis of nucleus pulposus cells via scavenging mitochondrial ROS and maintaining the stability of mitochondrial dynamics

Peng, X., Wang, K., Zhang, C., Bao, J.-P., Cabral, V. L. F., Gao, J.-W., Zhou, Z.-M., & Wu, X. (2021) · Free Radical Research · doi:10.1080/10715762.2021.2018426 · Cited by 44 · see citing works

Low-Dose Non-Targeted Effects and Mitochondrial Control

Averbeck, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411460 · Cited by 47 · see citing works

MARCH5‐dependent NLRP3 ubiquitination is required for mitochondrial NLRP3‐NEK7 complex formation and NLRP3 inflammasome activation

Park, Y., Dodantenna, N., Kim, Y., Kim, T., Lee, H., Yoo, Y., Heo, J., Lee, J. H., Kwon, M., Kang, H. C., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2023113481 · Cited by 44 · see citing works

Mitochondrial transplantation: A promising therapy for mitochondrial disorders

Jiao, Q., Li, X., & Chen, Y. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.124194 · Cited by 45 · see citing works

Elevated expression of Piezo1 activates the cGAS-STING pathway in chondrocytes by releasing mitochondrial DNA.

Sun, L., Wang, Y., Kan, T., Wang, H., Cui, J.-Q., Wang, L., Liu, C.-L., Li, H.-J., Yu, Z.-F., & Yan, M.-N. (2025) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2025.02.778 · Cited by 40 · see citing works

A Novel Benzofuran Derivative Moracin N Induces Autophagy and Apoptosis Through ROS Generation in Lung Cancer

Gao, C., Sun, X., Wu, Z., Yuan, H., Han, H., Huang, H., Shu, Y., Xu, M., Gao, R.-L., Li, S., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00391 · Cited by 44 · see citing works

Salt-Sensitivity of Blood Pressure and Insulin Resistance

Ertuğlu, L. A., Elijovich, F., Laffer, C. L., & Kirabo, A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.793924 · Cited by 44 · see citing works

The role of mitochondria in aging, cell death, and tumor immunity

Wang, Q., Yuan, Y., Liu, J., Li, C., & Jiang, X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1520072 · Cited by 43 · see citing works

E3 Ubiquitin Ligase RNF114 Inhibits Innate Immune Response to Red-Spotted Grouper Nervous Necrosis Virus Infection in Sea Perch by Targeting MAVS and TRAF3 to Mediate Their Degradation

Xiang, Y., Zhang, W., Jia, P., Lu, X., Liu, W., Yi, M., & Jia, K. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000083 · Cited by 42 · see citing works

Immunoregulatory Effects of Mitochondria Transferred by Extracellular Vesicles

She, Z., Xie, M., Hun, M., Abdirahman, A. S., Li, C., Wu, F., Luo, S., Wan, W., Wen, C., & Tian, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.628576 · Cited by 42 · see citing works

Propacin, a coumarinolignoid isolated from durian, inhibits the lipopolysaccharide-induced inflammatory response in macrophages through the MAPK and NF-κB pathways

Huang, Y., Wang, Y., Xu, J., Feng, J., & He, X. (2019) · Food & Function · doi:10.1039/c9fo02202c · Cited by 41 · see citing works

Salt Sensitivity of Blood Pressure in Blacks and Women: A Role of Inflammation, Oxidative Stress, and Epithelial Na + Channel

Sahinoz, M., Elijovich, F., Ertuğlu, L. A., Ishimwe, J., Pitzer, A. L., Saleem, M., Mwesigwa, N., Kleyman, T. R., Laffer, C. L., & Kirabo, A. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0212 · Cited by 40 · see citing works

Why choose cyclosporin A as first-line therapy in COVID-19 pneumonia

Sánchez‐Pernaute, O., Romero-Bueno, F., & Selva-O’Callaghan, A. (2020) · Reumatología Clínica · doi:10.1016/j.reuma.2020.03.001 · Cited by 40 · see citing works

Cell type-specific mechanistic target of rapamycin-dependent distortion of autophagy pathways in lupus nephritis

Caza, T. N., Wijewardena, C., Al-Rabadi, L. F., & Perl, A. (2022) · Translational research · doi:10.1016/j.trsl.2022.03.004 · Cited by 40 · see citing works

Latest Advances in Chondrocyte-Based Cartilage Repair

Li, Y., Lim, R., & Owens, B. D. (2024) · Biomedicines · doi:10.3390/biomedicines12061367 · Cited by 39 · see citing works

Selected Functions and Disorders of Mitochondrial Metabolism under Lead Exposure

Chlubek, M., & Baranowska‐Bosiacka, I. (2024) · Cells · doi:10.3390/cells13141182 · Cited by 39 · see citing works

Impact of ageing and disuse on neuromuscular junction and mitochondrial function and morphology: Current evidence and controversies

Motanova, E. S., Pirazzini, M., Negro, S., Rossetto, O., & Narici, M. V. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102586 · Cited by 40 · see citing works

Mitochondrial biology in airway pathogenesis and the role of NRF2

Cho, H., & Kleeberger, S. R. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01182-5 · Cited by 38 · see citing works

Mitochondria May Mediate Prenatal Environmental Influences in Autism Spectrum Disorder

Frye, R. E., Cakir, J., Rose, S., Palmer, R. F., Austin, C. E., Curtin, P. C. P., & Arora, M. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11030218 · Cited by 38 · see citing works

Calycosin Alleviates Sepsis-Induced Acute Lung Injury via the Inhibition of Mitochondrial ROS-Mediated Inflammasome Activation

Xia, Y., Cao, Y., Sun, Y., Hong, X., Tang, Y., Yu, J., Hu, H., Ma, W., Qin, K., & Bao, R. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.690549 · Cited by 38 · see citing works

Novel insights into NOD-like receptors in renal diseases

Jin, J., Zhou, T.-J., Ren, G., Cai, L., & Meng, X. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00886-7 · Cited by 37 · see citing works

CMPK2 is a host restriction factor that inhibits infection of multiple coronaviruses in a cell-intrinsic manner

Zhu, M., Lv, J., Wang, W., Guo, R., Zhong, C., Antia, A., Zeng, Q., Li, J., Liu, Q., Zhou, J., et al. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002039 · Cited by 37 · see citing works

MDM2 contributes to oxidized low-density lipoprotein-induced inflammation through modulation of mitochondrial damage in endothelial cells

Zeng, Y., Xu, J., Hua, Y. Q., Peng, Y., & Xu, X. L. (2020) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2020.05.020 · Cited by 37 · see citing works

Mitochondria: Powering the Innate Immune Response to Mycobacterium tuberculosis Infection

Patrick, K. L., & Watson, R. O. (2021) · Infection and Immunity · doi:10.1128/iai.00687-20 · Cited by 36 · see citing works

Mitochondria: Metabolic regulators of innate immune responses to pathogens and cell stress

Lartigue, L., & Faustin, B. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.014 · Cited by 50 · see citing works

Mitochondria as Molecular Platforms Integrating Multiple Innate Immune Signalings

Monlun, M., Hyernard, C., Blanco, P., Lartigue, L., & Faustin, B. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.10.028 · Cited by 85 · see citing works

Mitochondrial control of innate immune responses

Chen, S., Liao, Z., & Xu, P. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1166214 · Cited by 77 · see citing works

Reprogramming of mitochondrial metabolism by innate immunity

Garaude, J. (2019) · Current Opinion in Immunology · doi:10.1016/j.coi.2018.09.010 · Cited by 33 · see citing works

Mitochondrial Damage-Associated Molecular Patterns and Metabolism in the Regulation of Innate Immunity

Lyu, Y., Wang, T., Huang, S., & Zhang, Z. (2023) · Journal of Innate Immunity · doi:10.1159/000533602 · Cited by 74 · see citing works