The DOI matches its Crossref record; 102 of the 103 references it cites were found in a registry or an index.
Mitochondria in innate immune responses
Open accessAbstract
The innate immune system has a key role in the mammalian immune response. Recent research has demonstrated that mitochondria participate in a broad range of innate immune pathways, functioning as signalling platforms and contributing to effector responses. In addition to regulating antiviral signalling, mounting evidence suggests that mitochondria facilitate antibacterial immunity by generating reactive oxygen species and contribute to innate immune activation following cellular damage and stress. Therefore, in addition to their well-appreciated roles in cellular metabolism and programmed cell death, mitochondria appear to function as centrally positioned hubs in the innate immune system. Here, we review the emerging knowledge about the roles of mitochondria in innate immunity.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Cardiolipin, N-formylated peptides, mtDNA, ATP and reactive oxygen species are known mitochondrial damage-associated molecular patterns (9, 28–30).”
From Autoantibodies in Systemic Lupus Erythematosus Target Mitochondrial RNA (2019) · cites this paper as [29]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Mitochondria and their components (e.g. N-formylated peptides and mtDNA) are recognized as damage-associated molecular patterns (DAMPs), which activate the innate immune system and elicit an inflammatory response6,21–23.”
From Anti-mitochondrial autoantibodies in systemic lupus erythematosus and their association with disease manifestations (2019) · cites this paper as [22]
In the citing paper
“The enzyme family of NADPH oxidases (Nox) [13,83] and the respiratory electron transport chain (ETC) of mitochondria [84,85,86] are the two major sources of ROS in many eukaryotic cells.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [84]
In the citing paper
“Complex I produces O2●− into the mitochondrial matrix where it is dismutated by SOD2 to H2O2 [67,84,85,86].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [84]
In the citing paper
“Mitochondria-derived ROS (mtROS) are mainly produced by complexes I and III as O2●−.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [84]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
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
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
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
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
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
Sterile inflammation: sensing and reacting to damage
Chen, G. Y., & Nuñez, G. (2010) · Nature Reviews Immunology · doi:10.1038/nri2873 · Cited by 3,051
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
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
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Flagged first, then by citations
1 of the 103 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 601–700 of 1,000
Lei, X., Li, S., Luo, C., Wang, Y., Liu, Y., Xu, Z., Huang, Q., Zou, F., Chen, Y., Peng, F., et al. (2020) · Mediators of Inflammation · doi:10.1155/2020/3934769 · Cited by 29
Park, G., Moon, B. C., Ryu, S. M., Kim, W. J., & Lim, H.-S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8878153 · Cited by 29
Photodynamic Therapy-Mediated Immune Responses in Three-Dimensional Tumor Models
Nkune, N. W., Simelane, N. W. N., Montaseri, H., & Abrahamse, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312618 · Cited by 29
Navasa, N., Martín, I., Iglesias‐Pedraz, J. M., Beraza, N., Atondo, E., Izadi, H., Ayaz, F., Fernández-Álvarez, S., Hatle, K. M., Som, A., et al. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu389 · Cited by 29
Mitochondria-mediated defense mechanisms against pathogens in Caenorhabditis elegans
Kwon, S., Kim, E. J. E., & Lee, S. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.6.111 · Cited by 30
Öğülür, İ., Pat, Y., Yazıcı, D., Ardıçlı, S., Ardıçlı, Ö., Mitamura, Y., Akdiş, M., & Akdiş, C. A. (2024) · Current Opinion in Immunology · doi:10.1016/j.coi.2024.102493 · Cited by 31
Pan, X., Zhao, Y. Q., Wang, J., Feng, S., Yu, X., & Wu, M. (2024) · Journal of Materials Chemistry B · doi:10.1039/d4tb01785d · Cited by 28
Zhou, Q., Luo, J., Chai, X., Yang, J., Zhong, S., Zhang, Z., Chang, X., & Wang, H. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114679 · Cited by 31
Pulmonary innate inflammatory responses to agricultural occupational contaminants
Sethi, R. S., Schneberger, D., Charavaryamath, C., & Singh, B. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2573-4 · Cited by 29
COVID-19: The Emerging Immunopathological Determinants for Recovery or Death
Ahmad, T., Chaudhuri, R., Joshi, M. C., Almatroudi, A., Rahmani, A. H., & Ali, S. M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.588409 · Cited by 30
Perspectives on formaldehyde dysregulation: Mitochondrial DNA damage and repair in mammalian cells
Nadalutti, C. A., Prasad, R., & Wilson, S. H. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103134 · Cited by 28
Liu, K., Zhao, X., Guo, M., Zhu, J., Li, D., Ding, J., Han, X., & Wu, J. (2022) · Toxicology Letters · doi:10.1016/j.toxlet.2022.01.003 · Cited by 28
Gao, X., Zeng, R., Qi, J., Ho, C., Li, B., Chen, Z., Chen, S., Xiao, C., Hu, H., Cai, M., et al. (2022) · Food Chemistry X · doi:10.1016/j.fochx.2022.100321 · Cited by 28
Hu, B., Zhong, G., Ding, S., Xu, K., Peng, X., Dong, W.-R., & Zhou, J. (2023) · Virulence · doi:10.1080/21505594.2023.2232707 · Cited by 29
Martins, A. C., Virgolini, M. B., Ávila, D. S., Scharf, P. R. D. S., Li, J., Tinkov, A. A., Skalny, A. V., Bowman, A. B., da Rocha, J. B. T., & Aschner, M. (2023) · Cells · doi:10.3390/cells12172124 · Cited by 29
Li, D., Tan, X., Zheng, L., Tang, H., Hu, S., Zhai, Q., Jing, X., Liang, P., Zhang, Y., He, Q., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202301733 · Cited by 28
Unchwaniwala, N., Sherer, N. M., & Loeb, D. D. (2016) · Journal of Virology · doi:10.1128/jvi.01229-16 · Cited by 28
Going against the Tide: Selective Cellular Protein Synthesis during Virally Induced Host Shutoff
Cao, S., Dhungel, P., & Yang, Z. (2017) · Journal of Virology · doi:10.1128/jvi.00071-17 · Cited by 28
NLRX1 Regulation Following Acute Mitochondrial Injury
Chu, X., Wu, S., & Raju, R. P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02431 · Cited by 29
Sharma, A., Sanjay, S., Jaiswal, V., Park, M., & Lee, H. (2023) · Biomaterials Advances · doi:10.1016/j.bioadv.2023.213363 · Cited by 28
Kumar, M., Sharma, S., Kumar, J., Barik, S., & Mazumder, S. (2024) · Current Research in Immunology · doi:10.1016/j.crimmu.2024.100077 · Cited by 28
Shadab, A., Abbasi‐Kolli, M., Saharkhiz, M., Ahadi, S. H., Shokouhi, B., & Nahand, J. S. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116673 · Cited by 27
Evolutionary perspective on sex differences in the expression of neurological diseases
Geary, D. C. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.06.001 · Cited by 27
Guardians of the Cell: Effector-Triggered Immunity Steers Mammalian Immune Defense
Kufer, T. A., Creagh, E. M., & Bryant, C. E. (2019) · Trends in Immunology · doi:10.1016/j.it.2019.08.001 · Cited by 29
Induction of foxo3a protects turtle neurons against oxidative stress
Reiterer, M., & Milton, S. (2020) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2020.110671 · Cited by 27
Dai, Z., Li, D., Du, X., Ge, Y., Hursh, D. A., & Bi, X. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009140 · Cited by 27
Mitochondrial RNA , a new trigger of the innate immune system
Grochowska, J., Czerwińska, J., Borowski, L. S., & Szczęsny, R. J. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1690 · Cited by 30
Dimogkioka, A. R., Lees, J., Lacko, E., & Tokatlidis, K. (2021) · RSC Advances · doi:10.1039/d1ra04497d · Cited by 27
Meng, J., Lv, Z., Wang, Y., & Chen, C. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.11.018 · Cited by 29
Host–pathogen interactions in malaria: cross-kingdom signaling and mitochondrial regulation
Luckhart, S., Pakpour, N., & Giulivi, C. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.07.002 · Cited by 27
Muramyl peptides activate innate immunity conjointly via YB1 and NOD2
Ламан, А. Г., Lathe, R., Shepelyakovskaya, A. O., Gartseva, A., Brovko, F. A., Guryanova, S. V., Alekseeva, L. G., Meshcheryakova, E. A., & Ivanov, V. T. (2016) · Innate Immunity · doi:10.1177/1753425916668982 · Cited by 27
Yu, S., Go, G., & Kim, W. (2019) · Foods · doi:10.3390/foods8110553 · Cited by 27
Weatherly, L. M., Shane, H. L., Friend, S. A., Lukomska, E., Baur, R., & Anderson, S. E. (2020) · Toxicological Sciences · doi:10.1093/toxsci/kfaa056 · Cited by 27
Faro, V. L., Nolte, I. M., ten Brink, J. B., Snieder, H., Jansonius, N. M., Bergen, A. A. B., & Study, L. C. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.781189 · Cited by 27
Roles of mitochondrial genetics in cancer metastasis
Welch, D. R., Foster, C., & Rigoutsos, I. (2022) · Trends in cancer · doi:10.1016/j.trecan.2022.07.004 · Cited by 26
Fu, X., Jiang, X., Chen, X., Zhu, L., & Zhang, G. (2019) · Mediators of Inflammation · doi:10.1155/2019/7072917 · Cited by 26
Mitophagy in Antiviral Immunity
Wang, H., Zheng, Y., Huang, J., & Li, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.723108 · Cited by 26
A Bibliometric Analysis of the Innate Immune DNA Sensing cGAS-STING Pathway from 2013 to 2021
Shi, X., Wang, S., Wu, Y., Li, Q., Zhang, T., Min, K., Feng, D., Liu, M., Wei, J., Zhu, L., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.916383 · Cited by 26
TARBP2 negatively regulates IFN-β production and innate antiviral response by targeting MAVS
Ling, T., Li, S.-N., Weng, G.-X., Wang, W., Li, C., Cao, L., Rao, H., Shu, H., & Xu, L. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.10.017 · Cited by 26
Luciferase-Based Biosensors in the Era of the COVID-19 Pandemic
Azad, T., van Rensburg, H. J. J., Morgan, J., Rezaei, R., Crupi, M. J. F., Chen, R., Ghahremani, M., Jamalkhah, M., Forbes, N. E., Ilkow, C. S., et al. (2021) · ACS Nanoscience Au · doi:10.1021/acsnanoscienceau.1c00009 · Cited by 28
Romaschenko, V. P., Zinovkin, R. A., Galkin, I. I., Zakharova, V., Panteleeva, A. A., Tokarchuk, A. V., Lyamzaev, K. G., Pletjushkina, O. Y., Chernyak, B. V., & Popova, E. N. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915050144 · Cited by 26
Engineered mitochondria exert potent antitumor immunity as a cancer vaccine platform
Luo, J., Mo, F., Zhang, Z., Hong, W., Lan, T., Cheng, Y., Fang, C., Bi, Z., Qin, F., Yang, H. J., et al. (2024) · Cellular and Molecular Immunology · doi:10.1038/s41423-024-01203-4 · Cited by 25
Koch, R. E., & Hill, G. E. (2018) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12400 · Cited by 25
Han, W., Fessel, J. P., Sherrill, T. P., Kocurek, E. G., Yull, F. E., & Blackwell, T. S. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1900820 · Cited by 25
Jiang, J., Xiao, J., Zhao, Z., Yuan, M., & Wang, J. (2021) · Materials Chemistry Frontiers · doi:10.1039/d1qm00589h · Cited by 25
Dorighello, G. G., Assis, L. H. P., Rentz, T., Morari, J., Santana, M. D. F. M., Passarelli, M., Ridgway, N. D., Vercesi, A. E., & Oliveira, H. C. F. (2022) · Antioxidants · doi:10.3390/antiox11091734 · Cited by 25
Oxidant Trade-Offs in Immunity: An Experimental Test in a Lizard
Tobler, M., Ballen, C. J., Healey, M., Wilson, M. R., & Olsson, M. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126155 · Cited by 25
Molecular characterization and functional analysis of duck TRAF6
Zhai, Y., Luo, F., Chen, Y., Zhou, S., Li, Z., Liu, M., Bi, D., & Jin, H. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.11.006 · Cited by 25
Importance of Toll-like Receptor 2 in Mitochondrial Dysfunction during Polymicrobial Sepsis
Gong, Y., Zou, L., Feng, Y., Li, D., Cai, J., Chen, D., & Chao, W. (2014) · Anesthesiology · doi:10.1097/aln.0000000000000470 · Cited by 26
Wang, M., Wang, L., Yi, Q., Gai, Y., & Song, L. (2015) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.09.035 · Cited by 25
Detection of hydrogen peroxide production in the isolated rat lung using Amplex red
Audi, S. H., Friedly, N., Dash, R. K., Beyer, A., Clough, A. V., & Jacobs, E. R. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1511051 · Cited by 25
Roles of Mitochondrial Respiratory Complexes during Infection
Escoll, P., Platon, L., & Buchrieser, C. (2019) · Immunometabolism · doi:10.20900/immunometab20190011 · Cited by 25
Methionine sulfoxide reductase (Msr) dysfunction in human brain disease
Reiterer, M., Schmidt‐Kastner, R., & Milton, S. (2019) · Free Radical Research · doi:10.1080/10715762.2019.1662899 · Cited by 26
Lin, C., Luo, L., Xun, Z., Zhu, C., Huang, Y., Ye, Y., Zhang, J., Chen, T., Wu, S., Zhan, F., et al. (2023) · Gut · doi:10.1136/gutjnl-2023-330389 · Cited by 25
Recent advances in FRET probes for mitochondrial imaging and sensing
Peng, F., Ai, X., Sun, J., Yang, L., & Gao, B. (2024) · Chemical Communications · doi:10.1039/d4cc00018h · Cited by 24
Emamnejad, R., Pagnin, M., & Petratos, S. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105788 · Cited by 25
López‐Ayllón, B. D., Marín, S., Fernández, M. F., García‐García, T., Fernández‐Rodríguez, R., de Lucas‐Rius, A., Redondo, N., Mendoza‐García, L., Foguet, C., Grigas, J., et al. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29752 · Cited by 24
Macrophage pyroptosis and its crucial role in ALI/ARDS
Cai, Y., Shang, L., Zhou, F., Zhang, M., Li, J., Wang, S., Lin, Q., Huang, J., & Yang, S. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1530849 · Cited by 24
Liu, Y., Zhang, M., Wang, T., & Zhang, J. (2025) · Journal of Asthma and Allergy · doi:10.2147/jaa.s529371 · Cited by 24
Carmichael, J. C., & Wills, J. W. (2019) · Journal of Virology · doi:10.1128/jvi.00494-19 · Cited by 24
Nitroreductase Increases Menadione-Mediated Oxidative Stress inAspergillus nidulans
Zhou, Y., Lv, H., Li, H., Li, J., Yan, Y., Liu, F., Hao, W., Zhou, Z., Wang, P., & Zhou, S. (2021) · Applied and Environmental Microbiology · doi:10.1128/aem.01758-21 · Cited by 24
Liu, K., Zhou, X., Fang, L., Dong, J., Cui, L., Li, J., Meng, X., Zhu, G., Li, J., & Wang, H. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109200 · Cited by 24
Mitochondrial proteomic analysis of human host cells infected with H3N2 swine influenza virus
Wu, X., Wang, H., Bai, L., Yu, Y., Sun, Z., Yan, Y., & Zhou, J. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.06.037 · Cited by 24
Hu, H., Doll, D. N., Sun, J., Lewis, S. E., Wimsatt, J., Kessler, M. J., Simpkins, J. W., & Ren, X. S. (2016) · Aging and Disease · doi:10.14336/ad.2015.0906 · Cited by 24
Cardoso, T. C., Rosa, A. C. G., Ferreira, H. L., Okamura, L. H., de Oliveira, B. R. S. M., Vieira, F. V., Silva-Frade, C., Gameiro, R., & Flores, E. F. (2016) · Journal of NeuroVirology · doi:10.1007/s13365-016-0444-5 · Cited by 24
Targeting mitochondria: how intravacuolar bacterial pathogens manipulate mitochondria
Fielden, L. F., Kang, Y., Newton, H. J., & Stojanovski, D. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2475-x · Cited by 25
SVCV impairs mitochondria complex Ⅲ resulting in accumulation of hydrogen peroxide
Zhao, L., Qi, L., Li, C., Li, L., Jin, L., & Yuan, J. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.01.053 · Cited by 24
Kim, Y. H., & Lee, S. (2018) · Redox Biology · doi:10.1016/j.redox.2018.06.011 · Cited by 24
TMEM173 Alternative Spliced Isoforms Modulate Viral Replication through the STING Pathway
Rodríguez‐García, E., Olagüe, C., Rius‐Rocabert, S., Ferrero, R., Lloréns, C., Larrea, E., Fortes, P., Prìeto, J., González‐Aseguinolaza, G., & Nistal‐Villán, E. (2018) · ImmunoHorizons · doi:10.4049/immunohorizons.1800068 · Cited by 26
Im, H., Samanta, P., Na, J., & Jung, J. (2019) · Bulletin of Environmental Contamination and Toxicology · doi:10.1007/s00128-019-02613-1 · Cited by 24
Kumar, P., Saini, K., Saini, V., & Mitchell, T. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.694865 · Cited by 24
Li, Q., Wang, S., Guo, P., Feng, Y., Yu, W., Zhang, H., Guo, J., Li, Y., Hu, L., Pan, J., et al. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.167315 · Cited by 23
Metabolic Modulation of Macrophage Function Post Myocardial Infarction
Zhao, M., Wang, D. D.-H., Liu, X., & Tian, R. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00674 · Cited by 23
From Cell Entry to Engraftment of Exogenous Mitochondria
Kami, D., & Gojo, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144995 · Cited by 24
Tzeng, H., & Chyuan, I. (2021) · Journal of the Formosan Medical Association · doi:10.1016/j.jfma.2021.03.019 · Cited by 23
Batool, M., Kim, M. S., & Choi, S. (2021) · Medicinal Research Reviews · doi:10.1002/med.21845 · Cited by 23
What to do with low O2: Redox adaptations in vertebrates native to hypoxic environments
Eaton, L., & Pamenter, M. E. (2022) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2022.111259 · Cited by 23
Bayne, A. N., Dong, J., Amiri, S., Farhan, S. M. K., & Trempe, J. (2023) · PLoS ONE · doi:10.1371/journal.pone.0284541 · Cited by 25
Chronic heat stress induces renal fibrosis and mitochondrial dysfunction in laying hens
Nanto-Hara, F., Yamazaki, M., Murakami, H., & Ohtsu, H. (2023) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-023-00878-5 · Cited by 23
Liao, R. J., Wu, Y., Qin, L., Jiang, Z., Gou, S., Zhou, L., Hong, Q., Li, Y., Shi, J., Yao, Y., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2023113448 · Cited by 25
Targeting mitochondria in the infection strategy of the hepatitis C virus
Quarato, G., Scrima, R., Agriesti, F., Moradpour, D., Capitanio, N., & Piccoli, C. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.06.008 · Cited by 26
Qian, J., Liu, L., Chen, L., Lu, X., & Zhu, C. (2014) · Human & Experimental Toxicology · doi:10.1177/0960327114542963 · Cited by 24
Liu, D., Shaukat, Z., Saint, R. B., & Gregory, S. L. (2015) · Oncotarget · doi:10.18632/oncotarget.6035 · Cited by 23
MAVS induces a host cell defense to inhibit CSFV infection
Wang, D., Lv, H., Li, C., Liu, Y., Wang, C., Lin, J., Wang, Y., Qian, G., Guo, K., & Zhang, Y. (2018) · Archives of Virology · doi:10.1007/s00705-018-3804-z · Cited by 23
Luo, Y., Zhang, Y.-N., Zhang, H., Lv, H., Zhang, M., Chen, L., & Du, Z. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.09.062 · Cited by 23
Josephson, H., Ntzouni, M. P., Skoglund, C., Linder, S., Turkina, M. V., & Vikström, E. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01069 · Cited by 23
Glon, D., Vilmen, G., Perdiz, D., Hernández, E., Beauclair, G., Quignon, F., Berlioz‐Torrent, C., Maréchal, V., Poüs, C., Lussignol, M., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010371 · Cited by 25
Aspects of innate immunity and Parkinson's disease
Huang, Y., & Halliday, G. M. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00033 · Cited by 22
Mitochondria and Chloroplasts Shared in Animal and Plant Tissues: Significance of Communication
Stefano, G. B. (2015) · Medical Science Monitor · doi:10.12659/msm.894481 · Cited by 22
Rhee, S.-M., Chae, H., & Kim, S. (2015) · Methods · doi:10.1016/j.ymeth.2015.04.003 · Cited by 22
Pathogenic Effects of IFIT2 and Interferon-β during Fatal Systemic Candida albicans Infection
Stawowczyk, M., Naseem, S., Montoya, V., Baker, D. P., Konopka, J. B., & Reich, N. C. (2018) · mBio · doi:10.1128/mbio.00365-18 · Cited by 24
Chen, J., Xia, L., Wang, W., Wang, Z., Hou, S., Xie, C., Cai, J. X., & Lu, Y. (2019) · Journal of Fish Diseases · doi:10.1111/jfd.13062 · Cited by 22
Im, H., Na, J., & Jung, J. (2020) · Aquatic Ecology · doi:10.1007/s10452-020-09804-7 · Cited by 22
Rivers, E., Rai, R., Lötscher, J., Hollinshead, M. S., Markelj, G., Thaventhiran, J. E. D., Worth, A. J. J., Cavazza, A., Hess, C., Bajaj‐Elliott, M., et al. (2020) · eLife · doi:10.7554/elife.55547 · Cited by 25
Clauzure, M., Valdivieso, Á. G., Dugour, A. V., Mori, C., Massip-Copiz, M. M., Aguilar, M. Á., Sotomayor, V., Asensio, C. J. A., Figueroa, J. M., & Santa-Coloma, T. A. (2021) · Immunology · doi:10.1111/imm.13336 · Cited by 22
Nakamya, M. F., Sil, S., Buch, S. J., & Hakami, R. M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.840364 · Cited by 22
Rhee, S. G., & Kil, I. S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.07.029 · Cited by 22
Ge, W., Wang, H., Wu, X., Dong, B., Zhang, R., & Tian, M. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c03024 · Cited by 22
Qi, S., Barnig, C., Charles, A., Poirot, A., Meyer, A., Clère-Jehl, R., Frederic de, B. L. A. Y., & Gény, B. (2017) · Annals of Allergy Asthma & Immunology · doi:10.1016/j.anai.2016.11.026 · Cited by 22
Antirotaviral Activity of Bovine and Ovine Dairy Byproducts
Parrón, J. A., Ripollés, D., Pérez, M. D., Calvo, M., Rasmussen, J. T., & Sánchez, L. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b01059 · Cited by 22
Metadata
- Authors
- West, A. P., Shadel, G. S., & Ghosh, S.
- Affiliations
- Yale University (US)
- Columbia University (US)
- Corresponding author
- Ghosh, Sankar
- Venue
- Nature Reviews Immunology
- Published
- 2011-05-20
- Volume
- 11
- Issue
- 6
- Pages
- 389-402
- ISSN
- 1474-1733 (ISSN-L)
- 1474-1741
- PMC
- PMC4281487
- OpenAlex
- W2033448006
- Cited by
- 1,376
- References
- 103
- Citations by year
- 2026: 119 · 2025: 78 · 2024: 103 · 2023: 97 · 2022: 102 · 2021: 129 · 2020: 101 · 2019: 83 · 2018: 85 · 2017: 109 · 2016: 95 · 2015: 97 · 2014: 75 · 2013: 46 · 2012: 44
- FWCI
- 5.04
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Immunology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R37 AI33443, R37AI033443)
- National Institute of Environmental Health Sciences (ES‑011)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- mitochondria, innate immunity, antiviral signaling, reactive oxygen species, antibacterial immunity, sterile inflammation, programmed cell death, cellular metabolism
- MeSH terms
- Animals, Bacterial Infections, Humans, Immunity, Innate, Mitochondria, Virus Diseases, Signal Transduction, Reactive Oxygen Species, Models, Immunological, Mitochondrial Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review