The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production
Open accessAbstract
Activated caspases are a hallmark of apoptosis induced by the intrinsic pathway, but they are dispensable for cell death and the apoptotic clearance of cells in vivo. This has led to the suggestion that caspases are activated not just to kill but to prevent dying cells from triggering a host immune response. Here, we show that the caspase cascade suppresses type I interferon (IFN) production by cells undergoing Bak/Bax-mediated apoptosis. Bak and Bax trigger the release of mitochondrial DNA. This is recognized by the cGAS/STING-dependent DNA sensing pathway, which initiates IFN production. Activated caspases attenuate this response. Pharmacological caspase inhibition or genetic deletion of caspase-9, Apaf-1, or caspase-3/7 causes dying cells to secrete IFN-β. In vivo, this precipitates an elevation in IFN-β levels and consequent hematopoietic stem cell dysfunction, which is corrected by loss of Bak and Bax. Thus, the apoptotic caspase cascade functions to render mitochondrial apoptosis immunologically silent.
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 cited source says what the claim attributes to it.
In the citing paper
“In the absence of active caspases, mtDNA released following mitochondrial outer membrane permeabilization triggers type I interferon responses in a cGAS–STING-dependent manner143,144”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [144]
Experimental — accuracy not yet measuredIn the citing paper
“These include: (1) the prominent ability of CASP8 to inhibit necroptosis (see above), which is generally associated with the establishment of robust inflammatory responses linked to NF-κB activation [496 925–928]; (2) the capacity of CASP3 to drive PS exposure (see above), which generally supports the phagocytic removal of dying and dead cells while delivering anti-inflammatory signals to”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [932]
In the citing paper
“MtDNA has been reported to activate immunity through two distinct pathways, namely Toll-like receptor 9 (TLR9; Zhang et al, 2010;Oka et al, 2012;Liu et al, 2015), and cGAS activation (White et al, 2014;West et al, 2015).”
From Mitochondrial DNA and TLR9 drive muscle inflammation upon Opa1 deficiency (2018) · cites this paper as White et al, 2014
In the citing paper
“Thus, cytosolic mtDNA activates the DNA sensor cGAS and promotes STING-IRF3-dependent signaling (Rongvaux et al, 2014;White et al, 2014;West et al, 2015).”
From Mitochondrial DNA and TLR9 drive muscle inflammation upon Opa1 deficiency (2018) · cites this paper as White et al, 2014
In the citing paper
“Interestingly, these events were attenuated by caloric restriction (White et al., 2014), an intervention which has been shown to extend lifespan in a plethora of organisms and decrease the burden of senescent cells (Fontana et al., 2018; Mercken et al., 2012).”
From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as White et al., 2014
In the citing paper
“Finally, ABT-737 (an experimental inhibitor of multiple BCL2 family members) is known for its ability to drive robust type I IFN secretion by cancer cells downstream of mtDNA-driven CGAS activation, especially in the context of caspases inhibition (Rongvaux et al., 2014; White et al., 2014).”
From Immunomodulation by targeted anticancer agents (2021) · cites this paper as White et al., 2014
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
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625
Smyth, G. K. (2004) · Statistical Applications in Genetics and Molecular Biology · doi:10.2202/1544-6115.1027 · Cited by 11,829
Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
limma: Linear Models for Microarray Data
Smyth, G. K. (2005) · Statistics for Biology and Health · doi:10.1007/0-387-29362-0_23 · Cited by 5,796
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 · cited 1×
“Recent evidence indicates that cGAS is activated via a direct interaction with cytosolic DNA (Civril et al., 2013; Sun et al., 2013).”
The BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,806 · cited 1×
“Apoptosis comprises two convergent pathways: the intrinsic and extrinsic (Youle and Strasser, 2008).”
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988 · cited 1×
“, they can survive and generate viable progeny) (Lindsten et al., 2000; Wei et al., 2001).”
Bioinformatics and Computational Biology Solutions Using R and Bioconductor
Gentleman, R. C., Carey, V. J., Huber, W. K., Irizarry, R. A., & Dudoit, S. (2005) · Statistics in the health sciences · doi:10.1007/0-387-29362-0 · Cited by 3,470
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407 · cited 1×
“To test this, we treated WT murine splenocytes with the proapoptotic BH3 mimetic drug ABT-737, which targets the prosurvival proteins Bcl-xL and Bcl-2 (Oltersdorf et al., 2005).”
A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., & Nagata, S. (1998) · Nature · doi:10.1038/34112 · Cited by 3,239 · cited 1×
“Unlike genomic damage, which is triggered by cleavage of iCAD, the inhibitor of caspase-activated DNase (CAD) (Enari et al., 1998), and PS exposure, which is facilitated by cleavage of Xkr8 (Suzuki et al.”
Flagged first, then by citations
Cited by
Sorted by citations
Items 901–982 of 982
Mitochondria in Cell Death Regulation
Inde, Z., Montero, J., & Sarosiek, K. A. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00189-9
Quantitative assessment of mitophagy in irradiated cancer cells
Guilbaud, E., Spada, S., Bloy, N., Galassi, C., Sato, A., Jiménez‐Cortegana, C., Aretz, A., Buqué, A., Yamazaki, T., Demaria, S., et al. (2022) · Methods in cell biology · doi:10.1016/bs.mcb.2022.09.002
Tong, J., Rufli, S., & Wong, W. W.-L. (2023) · doi:10.3791/64745-v
Wang, Y., Luo, M., Chen, Y., Wang, Y., Zhang, B., Ren, Z., Bao, L., Wang, Y., Wang, J. E., Fu, Y., et al. (2023) · doi:10.1158/0008-5472.c.6512614.v1
Moore, E. C., Clavijo, P. E., Davis, R., Cash, H. A., Waes, C. V., Kim, Y., & Allen, C. T. (2023) · doi:10.1158/2326-6066.c.6548710.v1
Messenger functions of cell death during development and homeostasis
Fort, L. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220925 · Cited by 2
Role of pyroptosis in COVID-19
Çelik, M., Ceylan, M. R., Karahan, M. A., Koyuncu, İ., Dinçer, N. G., & Alkan, S. (2023) · Journal of Clinical Medicine of Kazakhstan · doi:10.23950/jcmk/13142 · Cited by 2
Grothe, L. M. (2023) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9849
ARF1 prevents aberrant type I IFN induction by regulating STING activation and recyclingPreprint
Hirschenberger, M., Lepelley, A., Rupp, U., Klute, S., Hunszinger, V., Koepke, L., Merold, V., Didry‐Barca, B., Wondany, F., Bergner, T., et al. (2023) · medRxiv · doi:10.1101/2023.04.28.23289152
“For bacterial protein expression, soluble 1138 human ARF1 wild-type and mutants lacking its N-terminal 17 amino acids and human ARFGAP1 1139 domain (1-136) were cloned into modified pET16 vector with N-terminal His6-MBP-SUMO tag.”
MethodShi, L., Zha, H., Zhou, P., Xia, Y., Li, H., Huang, H., Yue, R., Song, Z., & Zhu, J. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4455346
Passarella, S., Brandes, K., Dankert, E., Cavalli, P., Kröger, A., Dieterich, D. C., & Landgraf, P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.25.559304
“assumption is consistent with previous reports showing that the activity of caspases prevents mtDNA-dependent IFN-I production (Rongvaux et al., 2014; White et al., 2014).”
ResultAli, A. M., Ali, A. A., & Ali, A. A. (2023) · International Journal of Science and Technology Research Archive · doi:10.53771/ijstra.2023.5.2.0294
Homologous recombination promotes mitotic death to suppress the innate immune responsePreprint
Szmyd, R., Casolin, S., French, L., Manjón, A. G., Dhawan, A., Nelson, C. B., Cavalli, L., Page, S. G., Hau, E. K. C., Pickett, H. A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.04.592546
Hwang, S., Baker, C. D., & Field, M. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.30.605854
“This suggests that the Shmt2 heterozygosity-induced mtDNA release into the cytosol does not activate cGAS/STING pathway in MEF cells; conversely, HAP1 cells lacking SHMT2 expression was associated with cGAS/STING activation.”
BackgroundPANoptosis as a Therapeutic Target for COVID-19
Si, Y., Zhu, X., Zhang, Y., Zhou, Z., Liu, Y., & Ma, H. (2026) · Current Microbiology · doi:10.1007/s00284-026-04950-x
Mitochondria-derived vesicles: from quality control to inflammation and extracellular vesicles
Todkar, K. J., Amari, L., & Germain, M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00007-7
Bioinformatics for the Identification of STING-Related Genes in Diabetic Retinopathy
Wang, Y., Liu, S., Zhou, Q., Feng, Y., Xu, Q., Luo, L., & Lv, H. (2024) · Current Eye Research · doi:10.1080/02713683.2024.2430223
AMPK- and cGAS-Mediated Dual Sensing of Glucose and dsDNA Synergizes to Enhance Antitumor ImmunityPreprint
Zhou, R., Pei, J., Chen, S., Shen, Q., Wu, Q., Liu, S., Chen, C., Feng, X., Zou, J., Liang, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.15.638470
Gradzka-Boberda, S., Parui, I., Chakraborty, P., Anthony, D. P., Puthussery, B. K., Weber, A., Brokatzky, D., Giansanti, P., Mergner, J., Öllinger, R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.25.640042
DFFB suppresses interferon to enable cancer persister cell regrowthPreprint
Williams, A. F., Gervasio, D. A. G., Turkal, C. E., Stuhlfire, A. E., Wang, M., Mauch, B. E., Plawat, R., Nguyen, A. H., Paw, M. H., Hairani, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.15.670603
The kinase CK1α coordinates the initiation and termination of the cGAS-STING pathway
Jardine, J., Tarrillon, M., André‐Grégoire, G., Trillet, K., Josso, V., Merlet, L., Moreau, R., Jaunasse, C., Antigny, L., Marionneau‐Lambot, S., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01844-0 · Cited by 1
Control of Cell Survival and Apoptosis
Gray, D. H. D., & Strasser, A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-128-24465-4.00506-8
Walker, D. W., Aparicio, R., Alessi, R., Solans, A., Mojdeh, M., Sharma, V., Oh, P., Zelich, M. J., Frank, T., & Hur, J. (2025) · Research Square · doi:10.21203/rs.3.rs-7634140/v1
Chen, Z., Ho, I.-L., Liu, J., Soeung, M., Yen, E.-Y., Sainani, S., Dyke, C. A., Shah, R., Kwon, H. J., Han, G., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-4211 · Cited by 1
“…also been shown to correlate with the increased production of proinflammatory cytokines and chemokines, thus perpetuating inflammatory responses (53). mtDNA is situated close to the ETC, the primary source of ROS, within the mitochondrial matrix and is thus susceptible to metabolic…”
Gong, Z., Jia, Q., Guo, J., Li, C., Xu, S., Jin, Z., Chu, H., Wan, Y. Y., Zhu, B., & Zhou, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26560856
Li, Y., Chen, H., Yang, Q., Wan, L., Zhao, J., Wu, Y., Wang, J., Yang, Y., Niu, M., Liu, H., et al. (2022) · Figshare · doi:10.6084/m9.figshare.19234345
Li, J., Tan, J., Wang, T., Yu, S., Guo, G., Li, K., Yang, L., Zeng, B., Mei, X., Gao, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739291
Mitochondria, apoptosis, and necrosis
Şenol, H. B., Yılmaz, E. A., & Özdemir, Ö. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-24836-8.00002-x
Shen, Q., Pan, X., Li, J., Li, Y., Lin, J., Liu, F., Jiang, X., Zhang, C., & Pang, B. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-025-07659-w
Zhang, H., Song, X., Zhao, L., Wang, C., Chen, S., Wang, Y., Zhang, L., Xu, F., Zhang, H., Wang, Q., et al. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04054-5
Efficacy and mechanism of action of sovleplenib for aplastic anemia
Sheng, T., Sun, W., Xin, S., Zhou, C., & Liu, H. (2026) · Hematology · doi:10.1080/16078454.2026.2618419
Li, P., Qin, Y., Liang, X., Mo, Y., & Chen, D. (2026) · Therapeutic Advances in Medical Oncology · doi:10.1177/17588359261421552
Gou, C., Mu, H., Wang, Y., Liu, Y., Peng, Z., Li, Y., Xing, M., & Qi, M. (2026) · Antioxidants · doi:10.3390/antiox15020271
“Its activation triggers a downstream cascade of caspase proteolytic cleavage events, ultimately culminating in programmed cell death [51].”
Pourcelot, M. (2016) · theses.fr (ABES) · doi:10.70675/fe9bf786z6d4ez45d5zb047z4cff0d131b1c
Gentili, M. (2017) · theses.fr (ABES) · doi:10.70675/93617cb4za4e9z4fdez831az0bf2b31aea90
Il-26 : une cytokine pro-inflammatoire stimulant les cellules immunitaires innées myéloïdes
Poli, C. (2017) · theses.fr (ABES) · doi:10.70675/154b0002zc293z47a9z8bfbz9909e15c15e6
APOBEC3A cytidine deaminase, a potent mutator enzyme leading to nuclear DNA damages
Li, X. (2018) · theses.fr (ABES) · doi:10.70675/c6c54ef9za374z4871zb0e0z9d11e8ea3d84
Role of mitochondrial respiration in Listeria monocytogenes infection
Spier, A. (2021) · theses.fr (ABES) · doi:10.70675/cd44057azc986z44a5zbfd6zc91fa993e0bf
Characterisation of SG33 Myxoma virus replication and oncolytic activity in pancreatic cancer models
Quillien, L. (2021) · theses.fr (ABES) · doi:10.70675/eadfa28azee41z4b56z88f3zc40b7ff9f900
Infections virales, stress mitochondrial, et cytidines désaminases APOBEC3
Khalfi, P. (2021) · theses.fr (ABES) · doi:10.70675/de3add71zf189z451cz9f97z14b635db330c
Étude de la fonction de la DNASE1L3 en contexte auto-immun et anti-tumoral
Santa, P. (2024) · theses.fr (ABES) · doi:10.70675/2af1f0cfz45caz418azb93ez88367c4a54c8
Liu, X., & Liu, R. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1768672
“…changes in mitochondrial outer membrane permeability (MOMP) can allow mtDNA to enter the cytoplasm and activate cGAS, but this process is inhibited by apoptotic caspases (De Gaetano et al., 2021; Jenner and Garcia-Saez, 2024; Rongvaux et al., 2014; West, 2015; White et al., 2014).”
Zhang, X., Jiang, F., Ling, C., Liu, F., Feng, Z., Wu, N., & Zhu, Y. (2026) · Neuropharmacology and Therapy · doi:10.15212/npt-2025-0022
Nanotherapy for Pancreatitis: From Single-Cell Targeting Toward Multicellular-Coordinated Regulation
Li, B., Li, X., Deng, Y., Deng, J., & Zhang, X. M. (2026) · International Journal of Nanomedicine · doi:10.2147/ijn.s601636
Huang, C., Wu, D., Hung, L., Wu, C., Luo, S.-F., Ka, S., Chen, A., Ho, L., & Lai, J. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02910-3
Mitochondrial translocation of immunostimulatory RNA RN7SL1 suppresses innate immune responses
Liang, Y., Wang, L., Qin, G., Liu, X., Yang, H., Zhang, Z., Yuan, J., Zhou, W., & Fang, X. (2026) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2026079
Luo, X., Dong, Y., Chen, Z., Jiang, Y., Chen, T., Liu, W., Xie, C., Dong, Q., Mu, X., Li, J., et al. (2026) · Frontiers in Neurology · doi:10.3389/fneur.2026.1806183
“Additionally, MOMP during regulated cell death triggers autophagy and caspase activation, further contributing to the inflammatory cascade (79, 80).”
Tanisha, M. H., Siddique, M. A., Ahmed, Z., Mustafa, N., & Tasneem, F. (2026) · Health Science Reports · doi:10.1002/hsr2.72501 · Cited by 1
“I interferons, known as DAMPs, fostering an immune response against cancer [37, 38].”
Yang, S., Wu, S., Chen, S., Li, X., Chelepis, I., Willcox, S., Barnett, K. C., Hu, X., Huang, G., Brickey, W. J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.22.726336
Bozhdansky, V., Bacharach, E., & Ehrlich, M. (2026) · Molecular Therapy Oncology · doi:10.1016/j.omton.2026.201211
PARP7 inhibitors enhance the immunogenic effects of radiation in pancreatic cancer cells
Bragato, N., Dias, A. B., Ohradanova‐Repic, A., Dupanovic, A., Horvat, F., Fischer, P., Appel, L.-M., Walch, L., Kleinwächter, A., Rohrer, A. M., et al. (2026) · Molecular Therapy Oncology · doi:10.1016/j.omton.2026.201258 · Cited by 1
Yu, X., Wu, H., Guo, K., Liu, Z., Zhou, L., Wu, H., Wang, S., Fu, J., Cui, X., Fu, Z., et al. (2026) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.70257
“Under pharmacological pressure, resistant clones can adapt to bypass mitochondrial vulnerability by activating compensatory pathways, including glutaminolysis, fatty acid β-oxidation and protective autophagy [35, 39].”
A peptide-based screen for cell death inhibitors identifies the cytoprotective compound CDL36Preprint
Inde, Z., Keppler, S., Gelles, J. D., Fraser, C., Presser, A., Mohammed, J. N., Jung, M., Garvey, D. S., Moldoveanu, T., Chipuk, J. E., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.09.737573
Neutrophil extracellular traps and acute kidney injury: a narrative review
Zhou, S., Lu, J., Zheng, J., Liao, Y., Chen, S., Wu, H. W., Xiong, J., Li, X., & Tang, Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1853708
Caspase-3 cleaves CYLD to restrict interferon signaling during mitochondrial apoptosis
Macé, Y., Douanne, T., Jardine, J., Trillet, K., Moreau, R., Re, J., Ellison, C. J., Laguette, N., Elliott, P. R., Gavard, J., et al. (2026) · EMBO Reports · doi:10.1038/s44319-026-00876-4
“In addition to cell death, MOMP triggers the release of mtDNA into the cytosol through BAX and BAK pores, activating IRF3 transcription factor and the subsequent production of type I IFN via the cGAS-STING pathway (Rongvaux et al, 2014; White et al, 2014; Riley et al, 2018) (Fig.”
InfluentialChen, H., Qu, H., Pan, Y., Cheng, W., Wu, J., Wang, N., Shen, J., Meng, W., Wang, Z., & Xue, X. (2026) · Advanced Materials · doi:10.1002/adma.74146
“…for enhanced specificity [9, 10]. mtDNA released upon mitochondrial membrane disruption can activate the STING pathway [11, 12], yet this response is often weak and transient, failing to sustain robust STING clustering and introducing greater variability compared to exogenous agonists [13, 14].”
Huang, Z. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1927695
“Mitochondrial DNA also links mitochondrial injury to cGAS–STING signaling and type I interferon responses (Rongvaux et al., 2014; West et al., 2015; White et al., 2014).”
CAFs shape the immunosuppressive microenvironment of pancreatic cancer through the Lin28b-STING Axis
Fan, M., Zhang, Z., Xu, W., Liu, Y., Wang, R., Hao, W., Huo, S., Guo, Y., Wang, L., Lv, A., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76495-3
“Aberrant HER2 signaling in tumor cells facilitates AKT1 translocation to the ER-resident STING complex, resulting in TBK1 phosphorylation that inhibits kinase activation and downstream IRF3 signaling 26 .”
InfluentialYang, L., Liu, J., Luo, S., Zeng, Q., Li, D., & Deng, Y. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06109-y
“Nuclear DNA, mitochondrial DNA (mtDNA), and oxidized mitochondrial DNA (ox-mtDNA) may also become aberrantly exposed or accumulate in the cytosol after ischemic injury, providing upstream stimuli for DNA-sensing pathways [4–7].”
Nazar, S. S., Ajaykumar, A. V., & Ayyappan, J. P. (2026) · Cell Biochemistry and Function · doi:10.1002/cbf.70280
Chen, L., Yan, Z., Fang, Z., Yu, Z., Jiang, M., & Zou, Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1900975
Wen, Y., Zhang, P., Liao, X., Liu, J., Zhang, Y., & Liu, X. (2026) · Antioxidants · doi:10.3390/antiox15091134
Zhang, X., Chang, A., Liu, Y., & Yu, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1935135
Chakraborty, A., Pal, A., Debnath, M., Sahu, J., Pal, A., Mukherjee, J., Samanta, R., & Chatterjee, P. N. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1918926
RNF213 M1-ubiquitinates damaged mitochondria to activate pro-inflammatory NF-κB signalingPreprint
Heilig, R., Glover, H., Mellor, C. E. L., Cloix, C., McIlwraith, M. J., Flanagan, L., Paul, N. R., Thomason, P., Prasad, B., Ahmed, A., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.21.752888
Self-citationLiu, D., Su, J., Chen, F., Liu, L., Qi, X., Wang, Q., Wu, G., 孙慧君, Zhu, Z., & Che, X. (2026) · Inflammation Research · doi:10.1007/s00011-026-02363-x
“Con - versely, BAX and Caspase 9, which are critical mediators of the mitochondrial intrinsic apoptotic pathway, were upregu - lated after MLN4924 treatment [32].”
Su, Y., Gong, Z., Mu, J., Huang, L., Yang, P., Zhang, C., Zhao, L., Yang, L., Deng, J., & Liao, X. (2026) · Advanced Science · doi:10.1002/advs.77713
The role of mitochondrial DNA and RNA in promoting liver disease pathogenesis
Raj, S., Warhade, A., Kumari, N., Pandey, S., & Babuta, M. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1855694
“Another study has shown that mt-dsRNA can also activate immune cells through TLR8 activation which induces MyD88-mediated NF-κ B activation leading to the release of TNF-α , IL-6 (Krüger et al., 2015).”
InfluentialAkhtar, M. S., Aslam, M., & Beg, M. M. A. (2026) · Biomolecules · doi:10.3390/biom16101427
“Apoptotic caspases normally suppress mitochondrial DNA-induced stimulator-of-interferon-genes signaling, but mitochondrial outer membrane permeabilization, oxidant injury, and defective quality control can increase mitochondrial DNA efflux [55–58].”
Wei, H., Wang, J., Jiang, J., & Dai, S. (2026) · Medicinal Research Reviews · doi:10.1002/med.70108
The Genetic and Epigenetic Mechanisms of mtDNA in Regulation of Inflammation and Metabolism
Zhang, Y., 郑言江, Duan, H., & Li, Y. (2026) · The FASEB Journal · doi:10.1096/fj.202600927r
Mitochondrial regulation of tumor-associated macrophage function
Xu, J., Liu, Y., Zhang, H., Yuan, Z., Sheng, Y., Wang, X., Liu, H., Zhong, F., Zhang, H., Xiong, H., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1971517
“Mitochondrial DNA stress can induce interferon responses (164), whereas apoptotic caspases can limit this signaling (165, 166).”
Yanbin, G., Wu, Y., Tan, Y., Xue, S., & Lu, M. (2026) · Experimental Cell Research · doi:10.1016/j.yexcr.2026.115191
After delivery: How recipient cells shape the fate and function of transplanted mitochondria
Zhang, Z., Qin, B., Qin, B., & Zhang, H. (2026) · Clinical and Translational Medicine · doi:10.1002/ctm2.70857
“23,67,68 Mitochondrial peptides and lipids provide additional danger-associated signals.”
Wang, M., Li, J., Wang, X., Chai, X., Luo, J., Zhang, Y., Chang, X., Sun, Y., & Wang, H. (2026) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2026.101537 · Cited by 2
A cell death ballet in two acts
Muñoz‐Pinedo, C., & Martin, S. J. (2026) · Science · doi:10.1126/science.aem1247
Wang, H., Wen, L., Wang, H., Liu, Y., & Mo, Z. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1976652
BindingDB Entry 50015584: STING, a promising target for small molecular immune modulator: A review.
BindingDB (2023) · UC San Diego · doi:10.7270/q2vd73ds
Liposome permeabilisation assays to monitor pore formation by cell death proteins
Davies, K. A., Wardak, A. Z., & Miller, M. S. (2026) · Methods in cell biology · doi:10.1016/bs.mcb.2026.10.002
Fang, Y., Zhang, J., Ma, Y., Xiang, L., Wang, Y., Li, S., Cheng, Y., Li, Y., Ma, L., Zhang, H., et al. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.115493
Metadata
- Authors
- 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., Huang, D. C. S., & Kile, B. T.
- Affiliations
- The University of Melbourne (AU)
- Walter and Eliza Hall Institute of Medical Research (AU)
- National Jewish Health (US)
- Corresponding author
- White, Michael J.
- Kile, Benjamin T.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 159
- Issue
- 7
- Pages
- 1549-1562
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4520319
- OpenAlex
- W2028107828
- Cited by
- 983
- References
- 68
- Citations by year
- 2026: 89 · 2025: 88 · 2024: 118 · 2023: 107 · 2022: 111 · 2021: 94 · 2020: 93 · 2019: 61 · 2018: 76 · 2017: 63 · 2016: 39 · 2015: 40
- FWCI
- 21.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R21AI099346)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- caspases, apoptosis, type I interferon, STING, cGAS, mitochondrial DNA, Bak, Bax, caspase-9, Apaf-1, caspase-3, caspase-7, interferon-beta, hematopoietic stem cells
- MeSH terms
- STING Protein, Animals, Crosses, Genetic, DNA, Mitochondrial, Female, Hematopoietic Stem Cells, Interferon Type I, Male, Membrane Proteins, Mice, Inbred C57BL, Signal Transduction, Apoptosis, Caspases, Caspase 9
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