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STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
Open accessAbstract
The cellular innate immune system is essential for recognizing pathogen infection and for establishing effective host defence. But critical molecular determinants responsible for facilitating an appropriate immune response-following infection with DNA and RNA viruses, for example-remain to be identified. Here we report the identification, following expression cloning, of a molecule (STING; stimulator of interferon genes) that appears essential for effective innate immune signalling processes. It comprises five putative transmembrane regions, predominantly resides in the endoplasmic reticulum and is able to activate both NF-kappaB and IRF3 transcription pathways to induce expression of type I interferon (IFN-alpha and IFN-beta ) and exert a potent anti-viral state following expression. In contrast, loss of STING rendered murine embryonic fibroblasts extremely susceptible to negative-stranded virus infection, including vesicular stomatitis virus. Further, STING ablation abrogated the ability of intracellular B-form DNA, as well as members of the herpesvirus family, to induce IFN-beta, but did not significantly affect the Toll-like receptor (TLR) pathway. Yeast two-hybrid and co-immunoprecipitation studies indicated that STING interacts with RIG-I and with SSR2 (also known as TRAPbeta), which is a member of the translocon-associated protein (TRAP) complex required for protein translocation across the endoplasmic reticulum membrane following translation. Ablation by RNA interference of both TRAPbeta and translocon adaptor SEC61beta was subsequently found to inhibit STING's ability to stimulate expression of IFN-beta. Thus, as well as identifying a regulator of innate immune signalling, our results imply a potential role for the translocon in innate signalling pathways activated by select viruses as well as intracellular DNA.
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“TBK1 also activates NF‐κB to induce expression of IFN and inflammatory cytokines.65, 66, 67”
From Cellular senescence and senescence-associated secretory phenotype via the cGAS-STING signaling pathway in cancer (2020) · cites this paper as [65]
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“cGAMP produced by cGAS activation binds to STING which is located on the membrane of endoplasmic reticulum (ER)391 and leads to the translocation of STING from ER to the Golgi where it is further modified.392”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [391]
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“the stimulator of interferon genes (STING) has been shown to be a major pathway for the detection of immunogenic tumors and initiation of a spontaneous T cell response18–21.”
From Epigenetic state determines the in vivo efficacy of STING agonist therapy (2023) · cites this paper as [20]
Experimental — accuracy not yet measuredIn the citing paper
“TBK1 associated with STING also facilitates dsDNA-mediated activation of NF-κB to promote proinflammatory gene transcription (Abe and Barber, 2014; Ishikawa and Barber, 2008).”
From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as Ishikawa and Barber, 2008
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Cites
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 4,022
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
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
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
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
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
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
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
Distinct RIG-I and MDA5 Signaling by RNA Viruses in Innate Immunity
Loo, Y.-M., Fornek, J., Crochet, N., Bajwa, G., Perwitasari, O., Martinez-Sobrido, L., Akira, S., Gill, M. A., García-Sastre, A., Katze, M. G., et al. (2008) · Journal of Virology · doi:10.1128/jvi.01080-07 · Cited by 1,071
Recognition of Cytosolic DNA Activates an IRF3-Dependent Innate Immune Response
Stetson, D. B., & Medzhitov, R. M. (2006) · Immunity · doi:10.1016/j.immuni.2005.12.003 · Cited by 1,003
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Guo (2020) · doi:10.1186/s40779-020-00240-0 · Cited by 4,735
Pathogen Recognition and Inflammatory Signaling in Innate Immune Defenses
Mogensen, T. H. (2009) · Clinical Microbiology Reviews · doi:10.1128/cmr.00046-08 · Cited by 3,296
Interferon-stimulated genes: A complex web of host defenses
Schneider, W. M., Chevillotte, M. D., & Rice, C. M. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120231 · Cited by 3,067
STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
Ishikawa, H., Ma, Z., & Barber, G. N. (2009) · Nature · doi:10.1038/nature08476 · Cited by 2,759
Self-citationRegulation and function of the cGAS–STING pathway of cytosolic DNA sensing
Chen, Q., Sun, L., & Chen, Z. J. (2016) · Nature Immunology · doi:10.1038/ni.3558 · Cited by 2,333
The cGAS–STING pathway as a therapeutic target in inflammatory diseases
Decout, A., Katz, J. D., Venkatraman, S., & Ablasser, A. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00524-z · Cited by 2,309
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 2,368
Deng, L., Liang, H., Xu, M., Yang, X., Burnette, B., Arina, A., Li, X.-D., Mauceri, H., Beckett, M., Darga, T., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.10.019 · Cited by 2,182
Molecular mechanisms and cellular functions of cGAS–STING signalling
Hopfner, K.-P., & Hornung, V. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0244-x · Cited by 2,052
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
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
Immune Signaling by RIG-I-like Receptors
Loo, Y.-M., & Gale, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.05.003 · Cited by 1,875
Macrophages as tools and targets in cancer therapy
Mantovani, A., Allavena, P., Marchesi, F., & Garlanda, C. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00520-5 · Cited by 1,807
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
Role of neuroinflammation in neurodegeneration development
Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668
The roles of TLRs, RLRs and NLRs in pathogen recognition
Kawai, T., & Akira, S. (2009) · International Immunology · doi:10.1093/intimm/dxp017 · Cited by 1,725
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Unterholzner, L., Keating, S. E., Baran, M., Horan, K. A., Jensen, S. B., Sharma, S., Sirois, C. M., Jin, T., Latz, E., Xiao, T. S., et al. (2010) · Nature Immunology · doi:10.1038/ni.1932 · Cited by 1,643
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Burdette, D. L., Monroe, K. M., Sotelo-Troha, K., Iwig, J. S., Eckert, B., Hyodo, M., Hayakawa, Y., & Vance, R. E. (2011) · Nature · doi:10.1038/nature10429 · Cited by 1,570
Corrales, L., Glickman, L. H., McWhirter, S. M., Kanne, D. B., Sivick, K. E., Katibah, G. E., Woo, S.-R., Lemmens, E., Banda, T., Leong, J. J., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.031 · Cited by 1,560
Signaling in innate immunity and inflammation
Newton, K., & Dixit, V. M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006049 · Cited by 1,513
Innate Immune Pattern Recognition: A Cell Biological Perspective
Brubaker, S. W., Bonham, K. S., Zanoni, I., & Kagan, J. C. (2015) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112240 · Cited by 1,475
DNA sensing by the cGAS–STING pathway in health and disease
Motwani, M., Pesiridis, S., & Fitzgerald, K. A. (2019) · Nature Reviews Genetics · doi:10.1038/s41576-019-0151-1 · Cited by 1,467
Spranger, S., Dai, D., Horton, B., & Gajewski, T. F. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.04.003 · Cited by 1,441
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
Cytoplasmic chromatin triggers inflammation in senescence and cancer
Dou, Z., Ghosh, K., Vizioli, M. G., Zhu, J., Sen, P., Wangensteen, K. J., Simithy, J., Lan, Y., Lin, Y., Zhou, Z., et al. (2017) · Nature · doi:10.1038/nature24050 · Cited by 1,335
Self-citationSTING 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 1,357
STING: infection, inflammation and cancer.
Barber, G. N. (2015) · Nature Reviews Immunology · doi:10.1038/nri3921 · Cited by 1,313
Self-citationThe cGAS–cGAMP–STING pathway connects DNA damage to inflammation, senescence, and cancer
Li, T., & Chen, Z. J. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20180139 · Cited by 1,293
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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
RetractedAutophagy induction via STING trafficking is a primordial function of the cGAS pathway
Gui, X., Yang, H., Li, T., Tan, X., Shi, P., Li, M., Du, F., & Chen, Z. J. (2019) · Nature · doi:10.1038/s41586-019-1006-9 · Cited by 1,269
Innate immunity to virus infection
Takeuchi, O., & Akira, S. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00737.x · Cited by 1,269
New insights into the immunopathogenesis of systemic lupus erythematosus
Tsokos, G. C., Lo, M. S., Costa‐Reis, P., & Sullivan, K. E. (2016) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2016.186 · Cited by 1,251
Innate Immune Sensing and Signaling of Cytosolic Nucleic Acids
Wu, J., & Chen, Z. J. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120156 · Cited by 1,212
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
Structural basis of STING binding with and phosphorylation by TBK1
Zhang, C., Shang, G., Gui, X., Zhang, X., Bai, X.-C., & Chen, Z. J. (2019) · Nature · doi:10.1038/s41586-019-1000-2 · Cited by 1,095
cGAS in action: Expanding roles in immunity and inflammation
Ablasser, A., & Chen, Z. J. (2019) · Science · doi:10.1126/science.aat8657 · Cited by 1,077
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Towards personalized, tumour-specific, therapeutic vaccines for cancer
Hu, Z., Ott, P. A., & Wu, C. J. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2017.131 · Cited by 1,067
van der Poll, T., Shankar‐Hari, M., & Wiersinga, W. J. (2021) · Immunity · doi:10.1016/j.immuni.2021.10.012 · Cited by 1,094
The cGAS-cGAMP-STING Pathway of Cytosolic DNA Sensing and Signaling
Cai, X., Chiu, Y., & Chen, Z. J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.040 · Cited by 1,017
Mitochondria in the Regulation of Innate and Adaptive Immunity
Weinberg, S. E., Sena, L. A., & Chandel, N. S. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.002 · Cited by 960
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Demaria, O., Cornen, S., Daëron, M., Morel, Y., Medzhitov, R., & Vivier, E. (2019) · Nature · doi:10.1038/s41586-019-1593-5 · Cited by 957
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Gotwals, P. J., Cameron, S. B., Cipolletta, D., Cremasco, V., Crystal, A., Hewes, B., Mueller, B., Quaratino, S., Sabatos-Peyton, C. A., Petruzzelli, L., et al. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.17 · Cited by 968
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Xu, X., Pang, Y., & Fan, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02253-4 · Cited by 1,016
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Ramanjulu, J. M., Pesiridis, G. S., Yang, J., Concha, N., Singhaus, R., Zhang, S.-Y., Tran, J.-L., Moore, P., Lehmann, S., Eberl, H. C., et al. (2018) · Nature · doi:10.1038/s41586-018-0705-y · Cited by 912
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McLaughlin, M., Patin, E. C., Pedersen, M., Wilkins, A. C., Dillon, M. T., Melcher, A. A., & Harrington, K. J. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-0246-1 · Cited by 921
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Çivril, F., Deimling, T., Mann, C. C. D. O., Ablasser, A., Moldt, M., Witte, G., Hornung, V., & Hopfner, K. (2013) · Nature · doi:10.1038/nature12305 · Cited by 916
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Zhang, Z., Yuan, B., Bao, M., Lu, N., Kim, T., & Liu, Y. (2011) · Nature Immunology · doi:10.1038/ni.2091 · Cited by 874
Wang, C., Guan, Y., Lv, M., Zhang, R., Guo, Z., Wei, X., Du, X., Yang, J., Li, T., Wan, Y., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.03.017 · Cited by 869
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
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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
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Zhang, X., Bai, X., & Chen, Z. J. (2020) · Immunity · doi:10.1016/j.immuni.2020.05.013 · Cited by 859
Goubau, D., Deddouche, S., & Sousa, C. R. E. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.007 · Cited by 875
Pernas, L. F., & Scorrano, L. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 845
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Shang, G., Zhang, C., Chen, Z. J., Bai, X., & Zhang, X. (2019) · Nature · doi:10.1038/s41586-019-0998-5 · Cited by 797
CD47 blockade triggers T cell–mediated destruction of immunogenic tumors
Liu, X., Pu, Y., Cron, K. R., Deng, L., Kline, J. P., Frazier, W. A., Xu, H., Peng, H., Fu, Y., & Xu, M. M. (2015) · Nature Medicine · doi:10.1038/nm.3931 · Cited by 770
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
Abe, T., & Barber, G. N. (2014) · Journal of Virology · doi:10.1128/jvi.00037-14 · Cited by 767
Self-citationPaludan, S. R., & Bowie, A. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.004 · Cited by 795
Viral evasion and subversion of pattern-recognition receptor signalling
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Activation of STING requires palmitoylation at the Golgi
Mukai, K., Konno, H., Akiba, T., Uemura, T., Waguri, S., Kobayashi, T., Barber, G. N., Arai, H., & Taguchi, T. (2016) · Nature Communications · doi:10.1038/ncomms11932 · Cited by 752
Self-citationMitochondria: master regulators of danger signalling
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Härtlova, A., Erttmann, S. F., Raffi, F. A., Schmalz, A. M., Resch, U., Anugula, S., Lienenklaus, S., Nilsson, L. M., Kröger, A., Nilsson, J. A., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.01.012 · Cited by 716
Activation of cyclic GMP-AMP synthase by self-DNA causes autoimmune diseases
Gao, D., Li, T., Li, X.-D., Chen, X., Li, Q., Wight‐Carter, M., & Chen, Z. J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516465112 · Cited by 685
Konno, H., Konno, K., & Barber, G. N. (2013) · Cell · doi:10.1016/j.cell.2013.09.049 · Cited by 687
Self-citationCyclic GMP-AMP Synthase Is Activated by Double-Stranded DNA-Induced Oligomerization
Li, X., Shu, C., Yi, G., Chaton, C. T., Shelton, C. L., Diao, J., Zuo, X., Kao, C. C., Herr, A. B., & Li, P. (2013) · Immunity · doi:10.1016/j.immuni.2013.10.019 · Cited by 681
Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP
Ablasser, A., Schmid-Burgk, J. L., Hemmerling, I., Horvath, G. L., Schmidt, T., Latz, E., & Hornung, V. (2013) · Nature · doi:10.1038/nature12640 · Cited by 682
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Jiang, M., Chen, P., Wang, L., Li, W., Chen, B., Liu, Y., Wang, H., Zhao, S., Ye, L., He, Y., et al. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00916-z · Cited by 647
Gaidt, M. M., Ebert, T. S., Chauhan, D., Ramshorn, K., Pinci, F., Zuber, S., O’Duill, F., Schmid-Burgk, J. L., Hoss, F., Buhmann, R., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.039 · Cited by 638
Jensen, S., & Thomsen, A. R. (2012) · Journal of Virology · doi:10.1128/jvi.05738-11 · Cited by 604
RNA recognition and signal transduction by RIG‐I‐like receptors
Yoneyama, M., & Fujita, T. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00727.x · Cited by 595
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 612
Li, N., Zhou, H., Wu, H., Wu, Q., Duan, M., Deng, W., & Tang, Q. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101215 · Cited by 595
IRF7: activation, regulation, modification and function
Ning, S., Pagano, J. S., & Barber, G. N. (2011) · Genes and Immunity · doi:10.1038/gene.2011.21 · Cited by 611
Self-citationXia, T., Konno, H., Ahn, J., & Barber, G. N. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.029 · Cited by 589
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Kumar, H., Kawai, T., & Akira, S. (2009) · Biochemical Journal · doi:10.1042/bj20090272 · Cited by 609
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Yum, S., Li, M., Fang, Y., & Chen, Z. J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100225118 · Cited by 610
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“Upon recognition of pathogenic or self-DNA, the cytosolic DNA sensor cyclic GMP-AMP (cGAMP) synthetase (cGAS) produces the second messenger cGAMP, which in turn activates stimulator of interferon genes (STING) signaling and subsequent production of type I interferons (IFNs) and pro-inflammatory cytokines (Ishikawa and…”
BackgroundcGAS is essential for the antitumor effect of immune checkpoint blockade
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Jeremiah, N., Neven, B., Gentili, M., Callebaut, I., Maschalidi, S., Stolzenberg, M.-C., Goudin, N., Frémond, M.-L., Nitschke, P., Molina, T. J., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci79100 · Cited by 562
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Li, C., Lee, A., Grigoryan, L., Arunachalam, P. S., Scott, M. K. D., Trisal, M., Wimmers, F., Sanyal, M., Weidenbacher, P. A., Feng, Y., et al. (2022) · Nature Immunology · doi:10.1038/s41590-022-01163-9 · Cited by 505
Zhang, X., Wu, J., Du, F., Xu, H., Sun, L., Chen, Z., Brautigam, C. A., Zhang, X., & Chen, Z. J. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.003 · Cited by 505
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Metadata
- Authors
- Ishikawa, H., & Barber, G. N.
- Affiliations
- University of Miami (US)
- Corresponding author
- Barber, Glen N.
- Venue
- Nature
- Published
- 2008-08-24
- Volume
- 455
- Issue
- 7213
- Pages
- 674-678
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2804933
- OpenAlex
- W2060004514
- Semantic Scholar
- cd831bfb6fd9847baedbe5161ddd21d405728bee
- Cited by
- 3,576
- References
- 29
- Citations by year
- 2026: 310 · 2025: 394 · 2024: 359 · 2023: 332 · 2022: 322 · 2021: 315 · 2020: 270 · 2019: 195 · 2018: 163 · 2017: 161 · 2016: 115 · 2015: 118 · 2014: 112 · 2013: 123 · 2012: 83
- FWCI
- 28.23
- Type
- journal article
- Language
- en
- Update notices
- erratum (2008-11-13)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI079336)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Keywords
- STING, endoplasmic reticulum, innate immunity, interferon-beta, IRF3, NF-κB, RIG-I, Sec61β, translocon, TRAP complex, vesicular stomatitis virus, herpesvirus, negative-strand RNA viruses, viral DNA sensing, antiviral defense, protein translocation, pattern recognition receptors
- MeSH terms
- STING Protein, Animals, Cell Line, Endoplasmic Reticulum, Fibroblasts, Humans, Immunity, Innate, Interferons, Membrane Proteins, Mice, Inbred C57BL, Signal Transduction, Mice, Knockout, Mice
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