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VDAC oligomers form mitochondrial pores to release mtDNA fragments and promote lupus-like disease
Open accessAbstract
VDACs are MOM's ruin: Mitochondrial DNA (mtDNA) is normally kept within the mitochondria. It can be released into the cytosol in response to stress and thus encounter cytosolic DNA sensors, triggering type I interferon responses. During apoptosis, mtDNA release is mediated by macropores in the mitochondrial outer membrane (MOM) created by oligomerization of the proteins BAX and BAK. Kim et al. found that during oxidative stress, mtDNA escapes instead through macropores formed by oligomerization of voltage-dependent anion channels (VDACs) (see the Perspective by Crow). In a mouse model of lupus, an inhibitor of VDAC oligomerization diminished mtDNA release and downstream signaling events. This treatment reduced lupus-like symptoms in the model, suggesting a potential therapeutic route for conditions mediated by mtDNA release. Science , this issue p. 1531 ; see also p. 1445
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“in peripheral blood mononuclear cells, the level of VDAC oligomers and cytosolic mtDNA is higher in patients with SLE than in healthy individuals”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [148]
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“Cytosolic release of mtDNA can occur in live cells (as opposed to apoptotic cells) via pores formed by VDAC oligomers independent of BAX–BAK macropores and can activate the cGAS–STING pathway, as shown in mouse embryo fibroblasts deficient in Endog (a nuclear DNA-encoded mitochondrial endonuclease)148”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [148]
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“splenocytes from lupus-prone mice have more VDAC pores and cytosolic mtDNA than splenocytes from wild-type mice”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [148]
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“treatment with VBIT-4, a VDAC oligomerization inhibitor, can abrogate the SLE-like symptoms of lupus-prone mice, which is paralleled by a concomitant decrease in cytosolic mtDNA”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [148]
In the citing paper
“Interestingly, a recent study has proposed a role for voltage-dependent anion channel (VDAC) oligomerization in mediating mtDNA release into the cytoplasm (Kim et al., 2019).”
From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as Kim et al., 2019
In the citing paper
“It was shown that mouse fibroblasts deficient in the mitochondrial endonuclease γ, which display increased oxidative stress, had higher levels of cytosolic mtDNA and this could be attenuated by knocking down VDAC 1 and 3 (Kim et al., 2019).”
From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as Kim et al., 2019
In the citing paper
“Moreover, cytoplasmic mtDNA that accumulates in response to mitochondrial endonuclease γ deficiency, has also been shown to induce expression of ISGs in mouse fibroblasts (Kim et al., 2019), suggesting that cytosolic mtDNA is a major trigger of inflammatory pathways.”
From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as Kim et al., 2019
In the citing paper
“Furthermore, inhibiting VDAC oligomerization by using the inhibitor VBIT-4 has been shown to decrease mtDNA release and IFN signaling in a mouse model of systemic lupus erythematosus and ameliorated the disease severity (Kim et al., 2019), suggesting that inhibition of VDAC oligomerization and perhaps mPTP might represent an effective therapeutic strategy to improve diseases involving cytosolic mt”
From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as Kim et al., 2019
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1 retracted
RETRACTED ARTICLE: Parkin and PINK1 mitigate STING-induced inflammation
Sliter, D. A., Martinez, J., Hao, L., Chen, X., Sun, N., Fischer, T. D., Burman, J. L., Li, Y., Zhang, Z., Narendra, D. P., et al. (2018) · Nature · doi:10.1038/s41586-018-0448-9 · Cited by 1,287
RetractedHochberg, M. C. (1997) · Arthritis & Rheumatism · doi:10.1002/art.1780400928 · Cited by 11,409
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
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
SYSTEMIC LUPUS ERYTHEMATOSUS DISEASE ACTIVITY INDEX
Gladman, D. D., Ibañez, D., & Urowitz, M. B. (2007) · Elsevier eBooks · doi:10.1016/b978-0-323-04434-9.50060-9 · Cited by 2,928
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
Lood, C., Blanco, L. P., Purmalek, M. M., Carmona-Rivera, C., De Ravin, S. S., Smith, C. K., Malech, H. L., Ledbetter, J. A., Elkon, K. B., & Kaplan, M. J. (2016) · Nature Medicine · doi:10.1038/nm.4027 · Cited by 1,570
Self-citationProtein-binding assays in biological liquids using microscale thermophoresis
Wienken, C. J., Baaske, P., Rothbauer, U., Braun, D., & Duhr, S. (2010) · Nature Communications · doi:10.1038/ncomms1093 · Cited by 1,145
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
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
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Yang, S., Kim, H., Liao, G., Ta, N., Tu, H.-C., Ramani, S., Chen, C.-Y., Li, Z.-Y., Tanno, N., Hsieh, J. J.-D., et al. (2026) · Science · doi:10.1126/science.aea2181 · Cited by 3
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Xu, R., Li, J., Zhu, J. F., Guo, F., Zhang, C., Chen, K., & Xu, J. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167674 · Cited by 2
Self-citationFerens, F. G., Summers, W. A. T., Bharaj, A., Stetefeld, J., & Court, D. A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.739001 · Cited by 2
Шемарова, И. В. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115682 · Cited by 2
An inflammation-associated lncRNA induces neuronal damage via mitochondrial dysfunction
Olazagoitia‐Garmendia, A., Márquez, H. R., Trobisch, T., Moreno‐Castro, C., Etxebarria, A. R., Mentxaka, J., Tripathi, A. K., Yang, B., Ruíz, I. M., Anguíta, J., et al. (2025) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2025.102533 · Cited by 2
Stettler, P., Aeschlimann, S., Schimanski, B., & Schneider, A. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013506 · Cited by 2
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Perl, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820583-9.00014-2 · Cited by 2
Rouya, C., Yambire, K. F., Derbyshire, M. L., Alwaseem, H., & Tavazoie, S. F. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.21.558912 · Cited by 2
Ma, W., Ma, J., Zhang, K., Zheng, X., Wang, P., Feng, L., Ming, S., Zhuang, X., Zhou, J., Gao, C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.29.656919 · Cited by 2
Song, X., Ling, X., Liu, H., Zhao, Q., Li, X., Lai, W., & Wang, H. (2024) · Chemical Research in Chinese Universities · doi:10.1007/s40242-024-4120-7 · Cited by 1
Zhou, L., Wu, Z., Yi, X., Xie, D., Wang, J., & Wu, W. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.119905 · Cited by 1
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Cai, D., Chen, C., Meekrathok, P., Zeng, W., Wang, Z., Peng, Z., Mo, Y., Xu, X., Wang, J., & Qiu, J. (2025) · EMBO Reports · doi:10.1038/s44319-025-00614-2 · Cited by 1
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Lei, J., Liu, M., Huang, X., Zhai, X., Ji, H., & Wen, Z. (2025) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-025-09111-9 · Cited by 1
Peng, X., Zhu, L., Wan, C., Dong, L., Yang, W., Zhu, Q., Xie, H., & Zhang, J. (2025) · Toxicology Letters · doi:10.1016/j.toxlet.2025.111807 · Cited by 1
Zhang, H., Chang, A., Xu, X., Peng, H., Zhang, K., Yang, J., Li, W., Wang, X., Wang, W., Yin, X., et al. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48020138 · Cited by 1
Self-citationAmer, T., Haimovici, A., Kirschnek, S., Vier, J., Moeed, A., Ukachukwu, U., Neugebauer, D., Neubert, P., Helmstädter, M., Kayser, S., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01667-z · Cited by 1
Lv, J., Zhang, H., Yu, W., Jiang, P., Yin, C., Xu, W., Cao, Y., & Gao, R. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116411 · Cited by 1
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Tupin, F., González-Chapa, J. A., Chung, J. H., Lood, C., & Boilard, É. (2026) · Circulation Research · doi:10.1161/circresaha.125.326987 · Cited by 1
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Chen, C., Liao, W.-T., Chao, T. H., Chen, Y., Weng, S., Shiao, S.-H., Kao, C.-Y., Li, Y.-J., Cheng, K.-A., & Chang, Z.-F. (2026) · Nature Communications · doi:10.1038/s41467-026-73487-1 · Cited by 1
Ge, Y., Yu, T., Yu, S., Sun, A., Zhang, S., Zhang, M., Wang, Q., Liu, J., Zhang, X., Zeng, L., et al. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08871-2 · Cited by 1
He, X., Lv, X., Zhang, Y., Huang, H., Cheng, J., Zou, S., Han, Y., Sun, L., Wang, S., Xiong, Y., et al. (2026) · Kidney International · doi:10.1016/j.kint.2026.04.017 · Cited by 1
Tian, X., Wen, Z., You, Z., Mao, Y., Huang, Q., Zeng, L., Hu, W., Wei, D., Qian, H., Zhang, M., et al. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.05.315 · Cited by 1
Wang, Y., Xu, J., Zhu, Z., Zhang, Y., Hu, H., Gao, Y., Tao, Y., Yao, F., Zhou, S., Zhong, W., et al. (2026) · Clinical and Translational Medicine · doi:10.1002/ctm2.70695 · Cited by 1
Self-citationGe, H., Liao, M., Shen, Y., Zhao, Y., Fan, B., Li, J., Sun, M., Yang, S., Mao, L., Geng, X., et al. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04618-5 · Cited by 2
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Ren, Y., Zhu, G., Yucai, Z., Yun, C., Jie, G., & Yiping, Z. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112642 · Cited by 1
Qiu, W., Chen, W., Yang, S., Xi, H., Liao, J., Su, R., & Tang, Z. (2026) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6c03617 · Cited by 1
Self-citationZhao, X., Huang, S., Li, Q., Yang, Y., & Zhang, C. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1866184 · Cited by 1
Zhang, X., Wang, Y., Huang, H., Guo, X., Ye, W., Cao, L., Wang, Z., Hou, Y., Wang, Y., Yang, J., et al. (2026) · Arthritis & Rheumatology · doi:10.1002/art.70261 · Cited by 1
Huang, F., Sun, K., Diao, L., Lu, K., Fan, Y., & Xie, G. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1928003 · Cited by 1
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
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Cai, D., Xu, X., Zeng, W., Wang, Z., Chen, C., Mo, Y., Meekrathok, P., Wang, D., Peng, P., Peng, Z., et al. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.08.027 · Cited by 1
Self-citationZhou, S., Li, B., Wu, D., Chen, Y., Zeng, W., Huang, J., Tan, L., Mao, G., & Liu, F. (2024) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlae114 · Cited by 1
Sun, X., Li, M.-L., Ma, Y., Chen, K. G., Jiang, S., Hayashi, T., Itoh, K., Mizuno, K., Hattori, S., Fujisaki, H., et al. (2025) · Molecular Immunology · doi:10.1016/j.molimm.2025.08.011 · Cited by 1
Maximov, V. N. M., Shebanov, N., Nikitchina, N., Rapoport, R., Maor, Y., Tarassov, I., Pines, O., & Entelis, N. (2026) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2026.102959 · Cited by 1
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Chen, Y., Liu, Y., Hu, H., & Li, S. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115853 · Cited by 1
Wu, Z., Jia, R., Zhang, Q., Huang, L.-Y., Yan, J.-T., Zhang, Y. H., & Fan, Y. (2026) · Biomarker Research · doi:10.1186/s40364-026-00906-2 · Cited by 2
Mitochondrial homeostasis: the central hub governing the progression of atherosclerosis
Liu, H., Zhao, S., Gao, H., Wang, Y., Gao, J., Guo, P., Yang, Y., Cui, W., Zhang, S. M., Shi, Y., et al. (2026) · Precision Clinical Medicine · doi:10.1093/pcmedi/pbag010 · Cited by 1
Møhlenberg, M., Jørgensen, S. E., van der Sluis, R. M., Zillinger, T., Hinke, D. M., Hollensen, A. K., Hansen, A. L., Effort, C. H. G., COVID-19 DNABR Group, French COVID Cohort Study Group, et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2522111123 · Cited by 1
Chu, Z., Yang, T., Zhang, Y., Zhu, Q., Wang, D., Tang, H., Zhang, G., Jiang, M., Zhou, L., Xu, L., et al. (2026) · Materials Today Bio · doi:10.1016/j.mtbio.2026.103078 · Cited by 1
Zang, J., Chu, J., Sun, W., Yang, C., Qu, Z., Bie, H., Wang, Y., Guo, J., & Xu, D. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04320-6 · Cited by 1
Wang, B., Hao, Y., Hong, W., Bai, Z., Qin, F., Ai, J., Liu, J., Alu, A., Gao, Z., Wu, Y., et al. (2026) · Nano Today · doi:10.1016/j.nantod.2026.103039 · Cited by 1
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Abuhassan, Q., Saeed, T. N., Al-Hussainy, A. F., Roopashree, R., Mishra, S., Nanda, A., Mukherjee, G., Rizaev, J., Taher, S. G., Alwan, M., et al. (2026) · Journal of Molecular Neuroscience · doi:10.1007/s12031-026-02532-x · Cited by 1
Wang, R., Fang, W., Qiao, Y., Zhang, X., Gao, Y., Gao, Z., Guo, Y., & Wei, L. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158268 · Cited by 1
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Bılır, A., Yıldırım, B., & Karalök, M. H. (2026) · Cells · doi:10.3390/cells15100890 · Cited by 1
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Yang, X., Cheng, K., Chen, C., Zhang, Y., & Wang, D. W. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27177734 · Cited by 1
Li, J., Zhao, X., Shen, Y., Huang, L., Guo, J., & Wang, J. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168388 · Cited by 1
Zhang, C., & Yang, Z. (2026) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2026.112118 · Cited by 1
Daniali, M., Channer, B., Curley, E. O., Amirfallah, A., Kist, T., Montilla, J., Kosashvili, S., Sheldon, L., Stauch, K. L., Jackson, J. G., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118118 · Cited by 1
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Kaplan, M. J. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2200173 · Cited by 1
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Arif, T., Mukherjee, K., Li, X., Catrow, J. L., Cox, J., & Bieker, J. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.11.693792 · Cited by 1
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Magaziner, S. J., Collins, J. C., Miller, B., Zheng, P., Wang, A. K., Hadjadj, J., Balandrán, J. C., Sirenko, M., English, M., Bertlin, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.26.727520 · Cited by 1
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Giaglis, S., Daoudlarian, D., Kyburz, D., Venhoff, N., & Walker, U. A. (2021) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2021-eular.1833
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Connelly, K., & Hoi, A. Y.-B. (2021) · Springer eBooks · doi:10.1007/978-3-030-85161-3_4
Hauck, F. H. (2021) · Trillium Immunologie · doi:10.47184/ti.2021.03.04
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Osiewacz, H. D. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737293312.793571684
Rojas, G. A. S., Gonzalez, M. A., Farfán-Cano, H. R., Farfán-Cano, G. G., & Rojas, K. J. S. (2021) · Revista Ecuatoriana de Ciencia Tecnología e Innovación en Salud Pública · doi:10.31790/inspilip.v5i1.45
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Ilzorkina, A. I., Belosludtseva, N. V., Semenova, A. A., Dubinin, M. V., & Belosludtsev, K. N. (2024) · Биофизика · doi:10.31857/s0006302924040068
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Blanco, L. P., Romo‐Tena, J., Wang, X., Lightfoot, Y. L., & Kaplan, M. J. (2024) · Research Square · doi:10.21203/rs.3.rs-5349113/v1
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Todkar, K. J., Amari, L., & Germain, M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00007-7
Xu, Q., Jiang, Z., Li, S., Pan, Y., Cao, Z., Hua, S., Yang, R., He, X., Wu, H., Wen, H., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.5029678
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Ilzorkina, A. I., Belosludtseva, N. V., Semenova, A. A., Dubinin, M. V., & Belosludtsev, K. N. (2024) · BIOPHYSICS · doi:10.1134/s0006350924700714
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
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Zeng, W., Peng, P., Chen, C., Wang, D., Cao, L., Wang, Z., Xia, Y., & Qiu, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.10.658522
Sjögren, M., Dunér, P., Marinis, Y. Z. D., Neumann, A., Leandersson, K., Rasmussen, M., Wollheim, C. B., & Salehi, A. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.07.663218
Radiation-dependent Nucleic Acid Sensing, and Its Possible Impact on Radiotherapy
Pickering, R. J., & Zierhut, C. (2025) · The Cancer Journal · doi:10.1097/ppo.0000000000000775
Guo, D., Xu, S., Feng, J., Peng, Y., Xu, F., Liu, Y., Liu, B., Yin, X., Wei, H., Tian, Q., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5384578
Pittalà, M. G. G., Cucina, A., Nibali, S. C., Cunsolo, V., Francesco, A. D., Battiato, G., Reina, S., Foti, S., Pinto, V. D., & Saletti, R. (2025) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-025-06074-w
Izumi, Y., O'Dell, K. M. C., Covey, D. F., Qian, M., Mennerick, S. J., & Zorumski, C. F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.24.684242
Zhang, W. Z., Hoffman, K. L., Schiffer, K. T., Oromendia, C., Rice, M. C., Barjaktarevic, I., Peters, S. P., Putcha, N., Bowler, R. P., Wells, J. M., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14490545
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
Chang, Y., Wang, C., Zhu, J., Zheng, S., Sun, S., Wu, Y., Jiang, X., Li, L., Ma, R., & Li, G. (2024) · Figshare · doi:10.6084/m9.figshare.26605984
Self-citationChang, Y., Wang, C., Zhu, J., Zheng, S., Sun, S., Wu, Y., Jiang, X., Li, L., Ma, R., & Li, G. (2024) · Figshare · doi:10.6084/m9.figshare.26605987
Self-citationSun, K., Lü, F., Hou, L., Zhang, X., Pan, C., Liu, H., Zheng, Z., Guo, Z., Ruan, Z., Hou, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26333322
Wang, K., Du, Y., Li, P., Guan, C., Zhou, M., Wu, L., Liu, Z., & Huang, Z. (2024) · Figshare · doi:10.6084/m9.figshare.25357851
Self-citationSun, K., Lü, F., Hou, L., Zhang, X., Pan, C., Liu, H., Zheng, Z., Guo, Z., Ruan, Z., Hou, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26333416
Srivastava, A., Srivastava, P., Mathur, S., Mishra, S., Abbas, S., Gupta, A., Mishra, P., Tiwari, M., & Sharma, L. K. (2022) · Figshare · doi:10.6084/m9.figshare.21582319
Assaf, S., Sarig, O., Ishtewy, R., Zoabi, Y., Feller, Y., Malovitski, K., Mohamad, J., Bergson, S., Bilu, C., Shoshan‐Barmatz, V., et al. (2025) · Skin Health and Disease · doi:10.1093/skinhd/vzaf107
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Liu, Y., Tan, Y., Huan, S., Wu, Z., & Lei, Z. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.150472
Neutrophils impair B cell differentiation via mitochondrial and lipid metabolism in lupusPreprint
Bradford, H. F., Montamat, G., Barrenechea, L. G., Spinazzola, A., Lowe, D. M., Salama, A. D., Mauri, C., & Antonelou, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.03.703615
The complex role of mitochondrial dysfunction in the development of obese asthma
Jiang, P., & Zhang, Z. (2026) · Journal of Asthma · doi:10.1080/02770903.2026.2633350
Host mitochondrial DNA in bacterial pathogenesis: Friend, Foe, or Both?
Ahmadian, M., Shoraka, S., Elahi, Y., Abdollahi, A. K., Karimi-Jashni, A., & Hassani, Z. (2026) · Archives of Microbiology · doi:10.1007/s00203-026-04784-y
Vasquez, A. J. (2026) · Research Square · doi:10.21203/rs.3.rs-8935902/v1
Metadata
- Authors
- Kim, J., Gupta, R., Blanco, L. P., Yang, S., Shteinfer-Kuzmine, A., Wang, K., Zhu, J., Yoon, H. E., Wang, X., Kerkhofs, M., Kang, H., Brown, A. L., Park, S.-J., Xu, X., Zandee van Rilland, E., Kim, M. K., Cohen, J. I., Kaplan, M. J., Shoshan-Barmatz, V., & Chung, J. H.
- Affiliations
- National Heart, Lung, and Blood Institute (US)
- Ben-Gurion University of the Negev (IL)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (US)
- Department of Life Sciences and National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
- National Institutes of Health (US)
- Mokobio Biotechnology R&D Center, Rockville, MD 20850, USA.
- Laboratory of Obesity and Aging Research, Cardiovascular Branch, National Heart Lung and Blood Institute, Bethesda, MD 20892, USA.
- Corresponding author
- Chung, Jay H.
- ORCID
- Venue
- Science
- Published
- 2019-12-20
- Volume
- 366
- Issue
- 6472
- Pages
- 1531-1536
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC8325171
- OpenAlex
- W2996537134
- Cited by
- 793
- References
- 37
- Citations by year
- 2026: 172 · 2025: 147 · 2024: 147 · 2023: 123 · 2022: 82 · 2021: 86 · 2020: 35 · 2019: 1
- FWCI
- 16.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Lirias (KU Leuven) (submittedVersion, other-oa)
- Funders
- National Institutes of Health
- Korea Health Industry Development Institute (HI14C1176)
- Korea Research Institute of Bioscience and Biotechnology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Rheumatology › Systemic Lupus Erythematosus Research
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- VDAC1, mitochondrial DNA release, mitochondrial outer membrane permeabilization, mitochondrial stress, type I interferon signaling, systemic lupus erythematosus, neutrophil extracellular traps, N-terminal domain
- MeSH terms
- Protein Domains, Animals, Disease Models, Animal, DNA, Mitochondrial, Endodeoxyribonucleases, Humans, Interferons, Lupus Erythematosus, Systemic, Oxidative Stress, Voltage-Dependent Anion Channels, Mitochondrial Membranes, Mice, Rats, Protein Multimerization
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