The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
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.
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
“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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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]
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“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
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
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
Cited by
Sorted by citations
Items 401–500 of 1,005
STING-dependent translation inhibition restricts RNA virus replication
Franz, K. M., Neidermyer, W. J., Tan, Y., Whelan, S. P. J., & Kagan, J. C. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716937115 · Cited by 183
KDM5 histone demethylases repress immune response via suppression of STING
Wu, L., Cao, J. P., Cai, W. L., Lang, S. M., Horton, J. R., Jansen, D. J., Liu, Z. Z., Chen, J. F.-Y., Zhang, M., Mott, B. T., et al. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2006134 · Cited by 182
Chemical Strategies to Boost Cancer Vaccines
Li, W., & Li, Y. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00833 · Cited by 175
Analysis of Drosophila STING Reveals an Evolutionarily Conserved Antimicrobial Function
Martin, M., Hiroyasu, A., Guzman, R. M., Roberts, S. A., & Goodman, A. G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.029 · Cited by 173
The Interferon System and Vaccinia Virus Evasion Mechanisms
Perdiguero, B., & Estéban, M. (2009) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2009.0073 · Cited by 178
STING signaling and host defense against microbial infection
Ahn, J., & Barber, G. N. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0333-0 · Cited by 180
Self-citationSuppression of systemic autoimmunity by the innate immune adaptor STING
Sharma, S., Campbell, A. M., Chan, J., Schattgen, S., Orlowski, G. M., Nayar, R., Huyler, A. H., Nündel, K., Mohan, C., Berg, L. J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420217112 · Cited by 172
Unterholzner, L., Sumner, R. P., Baran, M., Ren, H., Mansur, D. S., Bourke, N. M., Randow, F., Smith, G. L., & Bowie, A. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002247 · Cited by 176
Tom70 mediates activation of interferon regulatory factor 3 on mitochondria
Liu, X.-Y., Wei, B., Shi, H.-X., Shan, Y.-F., & Wang, C. (2010) · Cell Research · doi:10.1038/cr.2010.103 · Cited by 171
STING Pathway Activation Stimulates Potent Immunity against Acute Myeloid Leukemia
Curran, E. K., Chen, X., Corrales, L. P., Kline, D. E., Dubensky, T. W., Duttagupta, P. A., Kortylewski, M., & Kline, J. P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.023 · Cited by 171
Human DNA-PK activates a STING-independent DNA sensing pathway
Burleigh, K., Maltbaek, J. H., Cambier, S., Green, R. R., Gale, M., James, R. G., & Stetson, D. B. (2020) · Science Immunology · doi:10.1126/sciimmunol.aba4219 · Cited by 177
Crosstalk between cGAS–STING signaling and cell death
Murthy, A. M. V., Robinson, N., & Kumar, S. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00624-8 · Cited by 178
Dai, P., Wang, W., Cao, H., Avogadri, F., Dai, L., Drexler, I., Joyce, J. A., Li, X.-D., Chen, Z. J., Merghoub, T., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003989 · Cited by 175
Akira, S. (2011) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0106 · Cited by 177
Advances in the understanding of mitochondrial DNA as a pathogenic factor in inflammatory diseases
Boyapati, R. K., Tamborska, A., Dorward, D. A., & Ho, G. (2017) · F1000Research · doi:10.12688/f1000research.10397.1 · Cited by 170
The balance of STING signaling orchestrates immunity in cancer
Lanng, K. R. B., Lauridsen, E. L., & Jakobsen, M. R. (2024) · Nature Immunology · doi:10.1038/s41590-024-01872-3 · Cited by 179
Cell biology and immunology of Listeria monocytogenes infections: novel insights
Stavru, F., Archambaud, C., & Cossart, P. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00993.x · Cited by 172
TAX1BP1 and A20 Inhibit Antiviral Signaling by Targeting TBK1-IKKi Kinases
Parvatiyar, K., Barber, G. N., & Harhaj, E. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.109819 · Cited by 169
Self-citationThe E3 ubiquitin ligase RNF185 facilitates the cGAS-mediated innate immune response
Wang, Q., Huang, L., Hong, Z., Lv, Z., Mao, Z., Tang, Y., Kong, X., Li, S., Cui, Y., Liu, H., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006264 · Cited by 167
Exploring the links between cancer and placenta development
Costanzo, V., Bardelli, A., Siena, S., & Abrignani, S. (2018) · Open Biology · doi:10.1098/rsob.180081 · Cited by 174
Tursi, S. A., & Tükel, Ç. (2018) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00028-18 · Cited by 171
Fang, R., Jiang, Q., Guan, Y., Gao, P., Zhang, R., Zhao, Z., & Jiang, Z. (2021) · Immunity · doi:10.1016/j.immuni.2021.03.011 · Cited by 167
Genomic instability, inflammatory signaling and response to cancer immunotherapy
Chen, M., Linstra, R., & van Vugt, M. A. T. M. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188661 · Cited by 166
Xing, Y., Chen, J., Tu, J., Zhang, B., Chen, X., Shi, H., Baker, S. C., Feng, L., & Chen, Z. (2013) · Journal of General Virology · doi:10.1099/vir.0.051169-0 · Cited by 166
Type I interferon signaling, regulation and gene stimulation in chronic virus infection
Lukhele, S., Boukhaled, G. M., & Brooks, D. G. (2019) · Seminars in Immunology · doi:10.1016/j.smim.2019.05.001 · Cited by 173
STING is a cell-intrinsic metabolic checkpoint restricting aerobic glycolysis by targeting HK2
Zhang, L., Jiang, C., Zhong, Y., Sun, K., Jing, H., Song, J., Xie, J., Zhou, Y., Tian, M., Zhang, C., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01185-x · Cited by 174
Nuclear Membrane Rupture and Its Consequences
Maciejowski, J., & Hatch, E. M. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-020520-120627 · Cited by 170
Mechanism and therapeutic potential of targeting cGAS-STING signaling in neurological disorders
Huang, Y., Liu, B., Sinha, S. C., Amin, S., & Gan, L. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00672-x · Cited by 164
Intracellular Pathogen Detection by RIG-I-Like Receptors
Dixit, E., & Kagan, J. C. (2013) · Advances in immunology · doi:10.1016/b978-0-12-410524-9.00004-9 · Cited by 172
STING-Dependent Signaling Underlies IL-10 Controlled Inflammatory Colitis
Ahn, J., Son, S., Oliveira, S. C., & Barber, G. N. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.101 · Cited by 170
Self-citationThe Kinase IKKβ Regulates a STING- and NF-κB-Dependent Antiviral Response Pathway in Drosophila
Goto, A., Okado, K., Martins, N. E., Cai, H., Barbier, V., Lamiable, O., Troxler, L., Santiago, E., Kühn, L., Paik, D., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.07.013 · Cited by 169
USP18 recruits USP20 to promote innate antiviral response through deubiquitinating STING/MITA
Zhang, M., Zhang, M., Zhang, Q., Zhu, G.-F., Yuan, L., Zhang, D., Zhu, Q., Yao, J., Shu, H., & Zhong, B. (2016) · Cell Research · doi:10.1038/cr.2016.125 · Cited by 163
Clathrin-associated AP-1 controls termination of STING signalling
Liu, Y., Xu, P., Rivara, S., Liu, C., Ricci, J., Ren, X., Hurley, J. H., & Ablasser, A. (2022) · Nature · doi:10.1038/s41586-022-05354-0 · Cited by 166
Yuan, L., Mao, Y. J., Luo, W., Wu, W., Xu, H. Y., Wang, X. L., & Shen, Y. H. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.804005 · Cited by 163
The 6th R of Radiobiology: Reactivation of Anti-Tumor Immune Response
Boustani, J., Grapin, M., Laurent, P.-A., Apétoh, L., & Mirjolet, C. (2019) · Cancers · doi:10.3390/cancers11060860 · Cited by 178
Homeostatic regulation of STING by retrograde membrane traffic to the ER
Mukai, K., Ogawa, E., Uematsu, R., Kuchitsu, Y., Kiku, F., Uemura, T., Waguri, S., Suzuki, T., Dohmae, N., Arai, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20234-9 · Cited by 167
The cGAS-STING Pathway: A Promising Immunotherapy Target
Ou, L., Zhang, A., Cheng, Y., & Chen, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.795048 · Cited by 166
Jounai, N., Kobiyama, K., Takeshita, F., & Ishii, K. J. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00168 · Cited by 169
Ubiquitination of STING at lysine 224 controls IRF3 activation
Ni, G., Konno, H., & Barber, G. N. (2017) · Science Immunology · doi:10.1126/sciimmunol.aah7119 · Cited by 162
Self-citationMitochondrial DNA as an inflammatory mediator in cardiovascular diseases
Nakayama, H., & Otsu, K. (2018) · Biochemical Journal · doi:10.1042/bcj20170714 · Cited by 160
TRIM29 negatively controls antiviral immune response through targeting STING for degradation
Li, Q., Lin, L., Tong, Y., Liu, Y., Mou, J., Wang, X., Wang, X., Gong, Y., Zhao, Y., Liu, Y., et al. (2018) · Cell Discovery · doi:10.1038/s41421-018-0010-9 · Cited by 160
Lysosomes in senescence and aging
Tan, J. X., & Finkel, T. (2023) · EMBO Reports · doi:10.15252/embr.202357265 · Cited by 178
Wood, L. M., & Paterson, Y. Y. W. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00051 · Cited by 163
Agonists and inhibitors of the STING pathway: Potential agents for immunotherapy
Wu, J., Zhao, L., Hu, H., Li, W., & Li, Y. (2019) · Medicinal Research Reviews · doi:10.1002/med.21649 · Cited by 160
Similarities and interplay between senescent cells and macrophages
Behmoaras, J., & Gil, J. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202010162 · Cited by 158
Moore, E. C., Clavijo, P. E., Davis, R. J., Cash, H. A., Waes, C. V., Kim, Y., & Allen, C. T. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-16-0104 · Cited by 158
Extrachromosomal telomere repeat DNA is linked to ALT development via cGAS-STING DNA sensing pathway
Chen, Y., Shen, Y., Hsia, H.-Y., Tiang, Y. P., Sung, T.-L., & Chen, L. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3498 · Cited by 168
Liang, D., Huang, X., Guan-Jun, D., Hu, E., Sheng, C., Wang, T., Hu, Q., Ni, Y., & Ya-yi, H. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.011 · Cited by 156
Cyclic GMP-AMP synthase promotes the inflammatory and autophagy responses in Huntington disease
Sharma, M., Rajendrarao, S., Shahani, N., Ramírez-Jarquín, U. N., & Subramaniam, S. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002144117 · Cited by 155
New developments in the induction and antiviral effectors of type I interferon
Liu, S.-Y., Sanchez, D. J., & Cheng, G. (2010) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.11.003 · Cited by 159
Type I interferons: diversity of sources, production pathways and effects on immune responses
Swiecki, M. K., & Colonna, M. (2011) · Current Opinion in Virology · doi:10.1016/j.coviro.2011.10.026 · Cited by 162
Regulation of the innate immune response by threonine-phosphatase of Eyes absent
Okabe, Y., Sano, T., & Nagata, S. (2009) · Nature · doi:10.1038/nature08138 · Cited by 158
Zhu, Q., Man, S. M., Gurung, P., Liu, Z., Vogel, P., Lamkanfi, M., & Kanneganti, T. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1402051 · Cited by 157
Zhang, Y., Yeruva, L., Marinov, A. D., Prantner, D., Wyrick, P. B., Lupashin, V. V., & Nagarajan, U. M. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302718 · Cited by 157
African Swine Fever Virus MGF-505-7R Negatively Regulates cGAS–STING-Mediated Signaling Pathway
Li, D., Yang, W., Li, L., Li, P., Ma, Z., Zhang, J., Qi, X., Ren, J., Ru, Y., Niu, Q., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001110 · Cited by 153
100 years of Bacillus Calmette–Guérin immunotherapy: from cattle to COVID-19
Lobo, N., Brooks, N. A., Zlotta, A. R., Cirillo, J. D., Boorjian, S. A., Black, P. C., Meeks, J. J., Bivalacqua, T. J., Gontero, P., Steinberg, G. D., et al. (2021) · Nature Reviews Urology · doi:10.1038/s41585-021-00481-1 · Cited by 163
The role of TBK1 in cancer pathogenesis and anticancer immunity
Runde, A. P., Mack, R. M., Breslin, P., & Zhang, J. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02352-y · Cited by 159
Regulation of the cGAS-STING Pathway
Zhang, B., Xu, P., & Ablasser, A. (2025) · Annual Review of Immunology · doi:10.1146/annurev-immunol-101721-032910 · Cited by 164
Nitta, S., Sakamoto, N., Nakagawa, M., Kakinuma, S., Mishima, K., Kusano‐Kitazume, A., Kiyohashi, K., Murakawa, M., Nishimura‐Sakurai, Y., Azuma, S., et al. (2012) · Hepatology · doi:10.1002/hep.26017 · Cited by 152
Guo, H., König, R., Deng, M., Rieß, M., Mo, J., Zhang, L., Petrucelli, A., Yoh, S. M., Barefoot, B. E., Samo, M., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.03.001 · Cited by 160
Tan, Y. S., Sansanaphongpricha, K., Xie, Y., Donnelly, C. R., Luo, X., Heath, B. R., Zhao, X., Bellile, E. L., Hu, H., Chen, H., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-2807 · Cited by 155
Targeting Stimulator of Interferon Genes (STING): A Medicinal Chemistry Perspective
Zhang, H., You, Q., & Xu, X. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01039 · Cited by 153
The cGAS-STING Pathway in Bacterial Infection and Bacterial Immunity
Liu, N., Pang, X., Zhang, H., & Ji, P. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.814709 · Cited by 159
Antiviral immunity in drosophila
Kemp, C., & Imler, J. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.01.007 · Cited by 151
Guo, Y., Gu, R., Gan, D., Hu, F., Li, G., & Xu, G. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00637-3 · Cited by 155
Zhou, Q., Lin, H., Wang, S., Wang, S., Ran, Y., Liu, Y., Ye, W., Xiong, X., Zhong, B., Shu, H., et al. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.09.006 · Cited by 150
Antagonism of the STING Pathway via Activation of the AIM2 Inflammasome by Intracellular DNA
Corrales, L. P., Woo, S., Williams, J. B., McWhirter, S. M., Dubensky, T. W., & Gajewski, T. F. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1502538 · Cited by 155
DNA sensor cGAS-mediated immune recognition
Xia, P., Wang, S., Gao, P., Gao, G., & Fan, Z. (2016) · Protein & Cell · doi:10.1007/s13238-016-0320-3 · Cited by 154
cGAS and STING: At the intersection of DNA and RNA virus-sensing networks
Ni, G., Ma, Z., & Damania, B. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007148 · Cited by 152
Shmuel-Galia, L., Humphries, F., Lei, X., Ceglia, S., Wilson, R., Jiang, Z., Ketelut-Carneiro, N., Foley, S. E., Pechhold, S. B., Houghton, J., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.05.008 · Cited by 149
ESCRT-dependent STING degradation inhibits steady-state and cGAMP-induced signalling
Gentili, M., Liu, B., Papanastasiou, M., Dele-Oni, D. O., Schwartz, M. A., Carlson, R. J., Al’Khafaji, A. M., Krug, K., Brown, A., Doench, J. G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36132-9 · Cited by 151
Paz, S., Vilasco, M., Werden, S. J., Arguello, M., Joseph-Pillai, D., Zhao, T., Nguyên, T. L.-A., Sun, Q., MEURS, E. F., Lin, R., et al. (2011) · Cell Research · doi:10.1038/cr.2011.2 · Cited by 153
Kono, D. H., Haraldsson, M. K., Lawson, B. R., Pollard, K. M., Koh, Y. T., Du, X., Arnold, C. N., Baccalà, R., Silverman, G. J., Beutler, B., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905441106 · Cited by 148
A noncanonical function of cGAMP in inflammasome priming and activation
Swanson, K. V., Junkins, R. D., Kurkjian, C. J., Holley-Guthrie, E., Pendse, A. A., Morabiti, R. E., Petrucelli, A., Barber, G. N., Benedict, C. A., & Ting, J. P. ‐. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20171749 · Cited by 148
Self-citationKanduri, M., Cahill, N., Göransson, H., Enström, C., Ryan, F., Isaksson, A., & Rosenquist, R. (2009) · Blood · doi:10.1182/blood-2009-07-232868 · Cited by 148
Positive feedback regulation of type I interferon by the interferon‐stimulated gene STING
Ma, F., Li, B., Yu, Y., Iyer, S. S., Sun, M., & Cheng, G. (2015) · EMBO Reports · doi:10.15252/embr.201439366 · Cited by 155
Li, Y., Chen, R., Zhou, Q., Xu, Z.-S., Li, C., Wang, S., Mao, A., Zhang, X., He, W.-W., & Shu, H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203405109 · Cited by 150
Berg, R., Melchjorsen, J., Rintahaka, J., Diget, E. A., Søby, S., Horan, K., Gorelick, R. J., Matikainen, S., Larsen, C. S., Østergaard, L. J., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029291 · Cited by 145
Sensors of the innate immune system: their mode of action
Baccalà, R., González‐Quintial, R., Lawson, B. R., Stern, M. E., Kono, D. H., Beutler, B., & Theofilopoulos, A. N. (2009) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2009.136 · Cited by 145
Diner, B. A., Lum, K. K., Toettcher, J. E., & Cristea, I. M. (2016) · mBio · doi:10.1128/mbio.01553-16 · Cited by 148
Nanovaccines for cancer immunotherapy
Zhang, Y. X., Lin, S., Wang, X., & Zhu, G. (2019) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1559 · Cited by 146
Induction of type I interferons by bacteria
Monroe, K. M., McWhirter, S. M., & Vance, R. E. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01478.x · Cited by 149
Junkins, R. D., Gallovic, M. D., Johnson, B. M., Collier, M. A., Watkins-Schulz, R., Cheng, N., David, C. N., McGee, C. E., Sempowski, G. D., Shterev, I. D., et al. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.11.030 · Cited by 144
Mitochondrial DNA leakage induces odontoblast inflammation via the cGAS-STING pathway
Zhou, L., Zhang, Y.-F., Yang, F.-H., Mao, H., Chen, Z., & Zhang, L. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00738-7 · Cited by 145
Liu, Q., Wu, J., Zhang, X., Li, X., Wu, X., Zhao, Y., & Ren, J. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03961-9 · Cited by 143
Pattern recognition receptors: sentinels in innate immunity and targets of new vaccine adjuvants
Olive, C. (2012) · Expert Review of Vaccines · doi:10.1586/erv.11.189 · Cited by 152
McKee, A. S., Burchill, M. A., Munks, M. W., Jin, L., Kappler, J. W., Friedman, R. S., Jacobelli, J., & Marrack, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300392110 · Cited by 143
STING licensing of type I dendritic cells potentiates antitumor immunity
Wang, J., Li, S., Wang, M., Wang, X., Chen, S., Sun, Z., Ren, X., Huang, G., Sumer, B. D., Yan, N., et al. (2024) · Science Immunology · doi:10.1126/sciimmunol.adj3945 · Cited by 146
Nonstructural protein 3‐4A: the Swiss army knife of hepatitis C virus
Morikawa, K., Lange, C. M., Gouttenoire, J., Meylan, E., Brass, V., Pénin, F., & Moradpour, D. (2011) · Journal of Viral Hepatitis · doi:10.1111/j.1365-2893.2011.01451.x · Cited by 141
Induction of necroptotic cell death by viral activation of the RIG-I or STING pathway
Schock, S., Chandra, N. V., Sun, Y., Irie, T., Kitagawa, Y., Gotoh, B., Coscoy, L., & Winoto, A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2016.153 · Cited by 141
The cytosolic sensor STING is required for intestinal homeostasis and control of inflammation
Canesso, M. C. C., Lemos, L., Neves, T. C., Marim, F. M., Castro, T. B. R., Veloso, É., Queiroz, C. P., Ahn, J., Santiago, H. C., Martins, F. S., et al. (2017) · Mucosal Immunology · doi:10.1038/mi.2017.88 · Cited by 144
Self-citationDemystifying the cGAS-STING pathway: precision regulation in the tumor immune microenvironment
Wang, Q., Yu, Y., Zhuang, J., Liu, R., & Sun, C. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02380-0 · Cited by 152
Induction of type I interferon by RNA viruses: cellular receptors and their substrates
Baum, A., & García‐Sastre, A. (2009) · Amino Acids · doi:10.1007/s00726-009-0374-0 · Cited by 141
MAVS Self-Association Mediates Antiviral Innate Immune Signaling
Tang, E., & Wang, C. (2009) · Journal of Virology · doi:10.1128/jvi.02623-08 · Cited by 141
de Queiroz, N. M. G. P., Xia, T., Konno, H., & Barber, G. N. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-0504 · Cited by 144
Self-citationDiverse roles of STING-dependent signaling on the development of cancer
Ahn, J., Konno, H., & Barber, G. N. (2015) · Oncogene · doi:10.1038/onc.2014.457 · Cited by 140
Self-citationUbiquitin enzymes in the regulation of immune responses
Ebner, P., Versteeg, G. A., & Ikeda, F. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1325829 · Cited by 143
TMEM173 variants and potential importance to human biology and disease
Patel, S., & Jin, L. (2018) · Genes and Immunity · doi:10.1038/s41435-018-0029-9 · Cited by 146
Zou, M., Ke, Q., Nie, Q., Qi, R., Zhu, X., Liu, W., Hu, X., Sun, Q., Fu, J.-L., Tang, X., et al. (2022) · Cell Death & Differentiation · doi:10.1038/s41418-022-00967-4 · Cited by 138
Bacteriophages inhibit and evade cGAS-like immune function in bacteria
Huiting, E. D., Cao, X., Ren, J., Athukoralage, J. S., Luo, Z., Silas, S., An, N., Carion, H., Zhou, Y., Fraser, J. S., et al. (2023) · Cell · doi:10.1016/j.cell.2022.12.041 · Cited by 143
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
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