The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
The E3 Ubiquitin Ligase Ro52 Negatively Regulates IFN-β Production Post-Pathogen Recognition by Polyubiquitin-Mediated Degradation of IRF3
Open accessAbstract
Induction of type I IFNs is a fundamental cellular response to both viral and bacterial infection. The role of the transcription factor IRF3 is well established in driving this process. However, equally as important are cellular mechanisms for turning off type I IFN production to limit this response. In this respect, IRF3 has previously been shown to be targeted for ubiquitin-mediated degradation postviral detection to turn off the IFN-β response. In this study, we provide evidence that the E3 ligase Ro52 (TRIM21) targets IRF3 for degradation post-pathogen recognition receptor activation. We demonstrate that Ro52 interacts with IRF3 via its C-terminal SPRY domain, resulting in the polyubiquitination and proteasomal degradation of the transcription factor. Ro52-mediated IRF3 degradation significantly inhibits IFN-β promoter activity, an effect that is reversed in the presence of the proteasomal inhibitor MG132. Specific targeting of Ro52 using short hairpin RNA rescues IRF3 degradation following polyI:C-stimulation of HEK293T cells, with a subsequent increase in IFN-β production. Additionally, shRNA targeting of murine Ro52 enhances the production of the IRF3-dependent chemokine RANTES following Sendai virus infection of murine fibroblasts. Collectively, this demonstrates a novel role for Ro52 in turning off and thus limiting IRF3-dependent type I IFN production by targeting the transcription factor for polyubiquitination and subsequent proteasomal degradation.
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
“Several TRIM proteins regulate production and action of IFN-β during innate immune response.”
From TRIM33 switches off Ifnb1 gene transcription during the late phase of macrophage activation (2015) · cites this paper as [36]
Experimental — accuracy not yet measured
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
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
IKKε and TBK1 are essential components of the IRF3 signaling pathway
Fitzgerald, K. A., McWhirter, S. M., Faia, K. L., Rowe, D. C., Latz, E., Golenbock, D. T., Coyle, A. J., Liao, S.-M., & Maniatis, T. (2003) · Nature Immunology · doi:10.1038/ni921 · Cited by 2,680
Self-citationInnate immune recognition of viral infection
Kawai, T., & Akira, S. (2006) · Nature Immunology · doi:10.1038/ni1303 · Cited by 1,899
Triggering the Interferon Antiviral Response Through an IKK-Related Pathway
Sharma, S., tenOever, B. R., Grandvaux, N., Zhou, G., Lin, R., & Hiscott, J. B. (2003) · Science · doi:10.1126/science.1081315 · Cited by 1,685
TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
Gack, M. U., Shin, Y. C., Joo, C.-H., Urano, T., Liang, C., Sun, L., Takeuchi, O., Akira, S., Chen, Z. J., Inoue, S., et al. (2007) · Nature · doi:10.1038/nature05732 · Cited by 1,683
Sato, M., Suemori, H., Hata, N., Asagiri, M., Ogasawara, K., Nakao, K., Nakaya, T., Katsuki, M., Noguchi, S., Tanaka, N., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)00053-4 · Cited by 1,342
The International Consortium for Systemic Lupus Erythematosus Genetics (SLEGEN), Harley, J. B., Alarcón-Riquelme, M. E., Criswell, L. A., Jacob, C. O., Kimberly, R. P., Moser, K. L., Tsao, B. P., Vyse, T. J., & Langefeld, C. D. (2008) · Nature Genetics · doi:10.1038/ng.81 · Cited by 1,309
Kawai, T., Takeuchi, O., Fujita, T., Inoue, J., Mühlradt, P. F., Sato, S., Hoshino, K., & Akira, S. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.10.5887 · Cited by 1,115
Kawai, T., Sato, S., Ishii, K. J., Coban, C., Hemmi, H., Yamamoto, M., Terai, K., Matsuda, M., Inoue, J., Uematsu, S., et al. (2004) · Nature Immunology · doi:10.1038/ni1118 · Cited by 1,058
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 310
Lin, Y.-S., Chang, Y., Pu, T.-Y., Chuang, T., & Hsu, L.-C. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01151-9 · Cited by 19
Lin, L., Yu, H., Li, L., Yang, W., Chen, X., Gong, Y., Lei, Q., Li, Z., Zhou, Z., Dai, L., et al. (2023) · Science Signaling · doi:10.1126/scisignal.abn5410 · Cited by 16
Cancer-associated mutation abolishes the impact of TRIM21 on the invasion of breast cancer cells
Jin, Y., Zhao, X., Zhang, Q., Zhang, Y., Fu, X., Hu, X., & Wan, Y. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.10.019 · Cited by 16
Martin‐Vicente, M., Resino, S., & Martínez, I. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-022-00793-3 · Cited by 18
Emerging roles of the Th17/IL-17-axis in glomerulonephritis
Ramani, K., & Biswas, P. S. (2015) · Cytokine · doi:10.1016/j.cyto.2015.07.029 · Cited by 17
Fonseca, D., Pisanelli, G., Seoane, R., Miorin, L., & García‐Sastre, A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114960 · Cited by 16
NBR1 mediates autophagic degradation of IRF3 to negatively regulate type I interferon production
Cai, Y., Zhu, Y., Zheng, J., Zhang, Y., & Chen, W. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.07.043 · Cited by 15
Ro52/SSA sensitizes cells to death receptor‐induced apoptosis by down‐regulating c‐FLIP(L)
Zhang, J., Fang, L., Zhu, X., Qiao, Y., Yu, M., Wang, L., Chen, Y., Yin, W., & Hua, Z. (2012) · Cell Biology International · doi:10.1042/cbi20110322 · Cited by 15
Depletion of the 26 S Proteasome Adaptor Ecm29 Increases Toll-Like Receptor 3 Signaling
Gorbea, C. M., Rechsteiner, M., Vallejo, J. G., & Bowles, N. E. (2013) · Science Signaling · doi:10.1126/scisignal.2004301 · Cited by 15
Wallenhammar, A., Anandapadamanaban, M., Lemak, A. S., Mirabello, C., Lundström, P., Wallner, B., & Sunnerhagen, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0181551 · Cited by 15
Anti-Viral Tetris: Modulation of the Innate Anti-Viral Immune Response by A20
Arguello, M., Paz, S., Ferran, C. J., Moll, H. P., & Hiscott, J. B. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-0398-6_4 · Cited by 15
Zhang, W., & Zou, X. (2013) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2013.31 · Cited by 13
A Conserved Host and Pathogen Recognition Site on Immunoglobulins: Structural and Functional Aspects
Wines, B. D., Trist, H. M., Farrugia, W., Ngo, C., Trowsdale, J., Areschoug, T., Lindahl, G., Fraser, J. D., & Ramsland, P. A. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0106-3_6 · Cited by 14
Velayutham, T. S., Kumar, S., Zhang, X., Kose, N., Walker, D. H., Winslow, G. M., Crowe, J. E., & McBride, J. W. (2019) · Infection and Immunity · doi:10.1128/iai.00383-19 · Cited by 14
HSV-2 Cellular Programming Enables Productive HIV Infection in Dendritic Cells
Crisci, E., Svanberg, C., Ellegård, R., Khalid, M., Hellblom, J., Okuyama, K., Bhattacharya, P., Nyström, S. N., Shankar, E. M., Eriksson, K., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02889 · Cited by 14
A Interacting Model: How TRIM21 Orchestrates with Proteins in Intracellular Immunity
Huang, Y., Gao, X., He, Q., & Liu, W.-T. (2023) · Small Methods · doi:10.1002/smtd.202301142 · Cited by 13
Roles of TRIM21/Ro52 in connective tissue disease-associated interstitial lung diseases
Gong, X., He, S., & Cai, P. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1435525 · Cited by 13
Huang, S., Huang, J., Cui, M., Wu, X., Wang, M., Zhu, D., Chen, S., Liu, M., Zhao, X., Wu, Y., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00930-22 · Cited by 13
Kunishita, Y., Yoshimi, R., Kamiyama, R., Kishimoto, D., Komiya, T., Sakurai, N., Sugiyama, Y., Takase‐Minegishi, K., Kirino, Y., Nagaoka, S., et al. (2021) · Lupus · doi:10.1177/09612033211042293 · Cited by 12
Regulation of Tripartite Motif-Containing Proteins on Immune Response and Viral Evasion
Zhang, X., Li, F., & Wang, X. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.794882 · Cited by 13
Trim21: a novel negative regulator in DNA sensor signaling
Yang, B., Wang, J., & Sun, B. (2013) · Cellular and Molecular Immunology · doi:10.1038/cmi.2013.12 · Cited by 12
Liu, X., Cui, L., Tao, Y., Xia, S., Hou, J., Cao, X., & Xu, S. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114608 · Cited by 11
Zhang, Z., Li, Z., Peng, Y., Li, Z., Xv, N., Jin, L., Cao, Y., Jiang, C., & Chen, Z. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114916 · Cited by 11
Meridor, K., Sagy, I., & Molad, Y. (2021) · Modern Rheumatology · doi:10.1093/mr/roab118 · Cited by 11
Yang, L., Liu, X., Zhang, L., Li, X., Zhang, X., Niu, G., Ji, W., Chen, S. E., Ouyang, H., & Ren, L. (2022) · Viruses · doi:10.3390/v14010156 · Cited by 11
Kim, D. S., Park, Y., Tsokos, G. C., Cho, M., & Kwok, S. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01490-5 · Cited by 10
Copy number variation and population-specific immune genes in the model vertebrate zebrafish
Schäfer, Y., Palitzsch, K., Leptin, M., Whiteley, A. R., Wiehe, T., & Suurväli, J. (2024) · eLife · doi:10.7554/elife.98058 · Cited by 9
Luo, Y.-S., Li, W., Cai, Y., Zhang, J., Gui, H., Zhang, K., & Cheng, Z. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.1014191 · Cited by 9
Zhang, B., Cai, T., He, H., Huang, X., Luo, Y., Huang, S., Luo, J., & Guo, X. (2023) · Genes · doi:10.3390/genes14081555 · Cited by 9
TRIMming down Flavivirus Infections
Cannac, M., & Nisole, S. (2024) · Viruses · doi:10.3390/v16081262 · Cited by 9
Tumurkhuu, G., Perri, G., Moore, R., Huo, L., Kumar, A. N., Ainsworth, R. I., OLIVER, T. R., Santos, G. D. L., Gibb, D. R., Carrière, J., et al. (2025) · Arthritis & Rheumatology · doi:10.1002/art.43273 · Cited by 10
Self-citationFan, C., Su, H., Liao, Z., Su, J., Yang, C., Zhang, Y., & Su, J. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2000555 · Cited by 9
Duck TRIM29 negatively regulates type I IFN production by targeting MAVS
Li, W., Song, Y., Du, Y., Huang, Z., Zhang, M., Chen, Z., He, Z., Ding, Y., Zhang, J., Zhao, L., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1016214 · Cited by 9
Extractable Nuclear Antigens and SLE: Specificity and Role in Disease Pathogenesis
Keogan, M. T., Kearns, G. M., & Jefferies, C. A. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-374994-9.10015-4 · Cited by 9
Self-citationSroka, M., Bagavant, H., Biswas, I., Ballard, A., & Deshmukh, U. S. (2018) · PubMed · Cited by 9
Current progress on innate immune evasion mediated by Npro protein of pestiviruses
Wen, S., Li, X., Lv, X., Liu, K., Ren, J., Zhai, J., & Song, Y. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1136051 · Cited by 8
RNF149 modulates the type I IFN innate antiviral immune responses through degrading IRF3
Wu, M., Cai, J., Qiao, G., Li, X., Zhou, J. Y., Xu, F., Ye, Y., Wang, Y., Xu, X., Li, J., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013051 · Cited by 9
Regulation of innate antiviral immunity by protein ubiquitination
Cai, B., Liu, B. L., & Gao, C. (2018) · Scientia Sinica Vitae · doi:10.1360/n052018-00161 · Cited by 8
Unusual Paraneoplastic Presentation of Cholangiocarcinoma
Opneja, A., Mahajan, S., Kapoor, S., Marur, S., Yang, S. H., & Manno, R. (2015) · Case Reports in Medicine · doi:10.1155/2015/806835 · Cited by 8
Zhou, Z., Wei, K., & Zhang, J. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.12.009 · Cited by 8
Presence and possible impact of Fcγ receptors on resident kidney cells in health and disease
Typiak, M. J., Audzeyenka, I., & Dubaniewicz, A. (2022) · Immunology and Cell Biology · doi:10.1111/imcb.12570 · Cited by 8
Rhesus monkey TRIM5α protein SPRY domain contributes to AP-1 activation
Na, L., Tang, Y.-D., Wang, C., Liu, C., & Wang, X. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000127 · Cited by 8
Huang, W., Yf, W., Ji, N., Xiao, H., Chen, K., Guo, J., Feng, J., Mustafa, N., Wang, J., Feng, H., et al. (2025) · The Journal of Immunology · doi:10.1093/jimmun/vkaf064 · Cited by 7
Berube, A. N., Gmyrek, G. B., Royer, D. J., & Carr, D. J. J. (2022) · Viruses · doi:10.3390/v14030589 · Cited by 7
Is there a link between the human TRIM21 and Trypanosoma cruzi Clone 36 genes in Chagas’ disease?
Winkler, M. A., & Pan, A. A. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.07.013 · Cited by 7
Safonova, T. N., Zaitseva, G. V., Loginov, V. I., Burdenniy, A. M., & Сергеевна, Л. С. (2019) · Russian Annals of Ophthalmology · doi:10.17116/oftalma2019135052192 · Cited by 7
Wang, S., Chu, F., Xia, R., Guan, J., Zhou, L., Fang, X., Dai, T., Xie, F., Zhang, L., & Zhou, F. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111661 · Cited by 6
Interferon and autoantigens: intersection in autoimmunity
Antiochos, B., & Casciola-Rosen, L. A. (2023) · Frontiers in Medicine · doi:10.3389/fmed.2023.1165225 · Cited by 6
Zhao, Y., Li, W., Li, Q., He, S., He, Q., Long, L., Liu, N., & Ma, J. (2021) · Oral Oncology · doi:10.1016/j.oraloncology.2021.105576 · Cited by 6
Regulation of virus-triggered type I interferon signaling by cellular and viral proteins
Zhong, B., Wang, Y., & Shu, H. (2010) · Frontiers in Biology · doi:10.1007/s11515-010-0013-x · Cited by 6
TRIM21 regulation of IRF-mediated type I interferon signaling in systemic autoimmune diseases
Panlu, K., Wang, Y., Zhu, X., Lin, Z., Fang, T., Yao, X., Xie, Z., & Wang, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1695818 · Cited by 6
Nikolic, R. P. A., Ben‐Chetrit, E., Fritzler, M. J., Buhler, K. A., Shokravi, A., Barreth, N., Chan, E. K. L., Andrade, L. E. C., Lin, M., Grewal, J., et al. (2026) · Annals of the Rheumatic Diseases · doi:10.1016/j.ard.2026.04.007 · Cited by 5
Positive Selection and Duplication of Bat TRIM Family Proteins
Xie, J., Tan, B., & Zhang, Y. (2023) · Viruses · doi:10.3390/v15040875 · Cited by 5
Liu, Y., He, Y., Cao, J., Lu, H., Zou, R., Zuo, Z., Li, R., Zhang, Y., & Sun, J. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127138 · Cited by 5
Wu, S., Chen, Z., Zhang, Z., Xu, J., Li, H., Lin, M.-X., Xie, W., Chen, Y., Lin, X., & Lin, X. (2025) · Journal of Virology · doi:10.1128/jvi.02309-24 · Cited by 5
Amezcua-Guerra, L. M., Pérez-García, L. F., Jiménez-Rojas, V., Márquez-Velasco, R., & Silveira, L. H. (2023) · Gaceta Médica de México · doi:10.24875/gmm.m22000739 · Cited by 5
Wang, M., Liu, C., Wang, W., Dong, M., Zhang, P., Liu, Y., Wang, L., & Song, L. (2019) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2019.01.013 · Cited by 5
Bilirubin metabolism in the liver orchestrates antiviral innate immunity in the body
Du, Q., He, W., Chen, X., Liu, J., Guan, M., Chen, Y., Chen, M., Yuan, Y., Zuo, Y., Miao, Y., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115481 · Cited by 4
Black carp RNF115 restricts IRF3/7-mediated antiviral signaling in innate immunity
He, Y., Wang, Q., Xiao, L., Wu, H., Xiao, J., Zou, J., & Feng, H. (2024) · Water Biology and Security · doi:10.1016/j.watbs.2024.100310 · Cited by 4
Autoantigens and Autoantibodies in the Pathogenesis of Sjögren’s Syndrome
Tinazzi, E., Patuzzo, G., & Lunardi, C. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803604-4.00009-5 · Cited by 4
E3 ligase RAD18 targets phosphorylated IRF3 to terminate IFNB1 transcription
Cai, Y., Zheng, J., Zhao, L., Wang, X., Zhang, P., Wang, J., Zhang, Y., Shi, R., Han, J., Han, W., et al. (2025) · Nature Immunology · doi:10.1038/s41590-025-02256-x · Cited by 3
Fu, Y., Gao, J., Li, Y., Yang, X., & Zhang, Y. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108414 · Cited by 3
RetractedSathyan, K. R., Premraj, A., & Puthiyedathu, S. T. (2023) · Journal of Aquatic Animal Health · doi:10.1002/aah.10187 · Cited by 3
TRIM dsDNA sensor to restrict innate immune response
Cai, Z., & Wang, J. (2013) · Cellular and Molecular Immunology · doi:10.1038/cmi.2013.6 · Cited by 3
Zhu, J.-W., Mu, D., Liu, F., Luo, M., Luo, R., & Zheng, Y. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.08.001 · Cited by 3
Jawed, B., Kanwal, R., Zakir, S. K., Gaudio, F., Esposito, J. E., Ishaqui, A. A., Martinotti, S., Botteghi, M., & Toniato, E. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1764253 · Cited by 2
Amezcua-Guerra, L. M., Pérez-García, L. F., Jiménez-Rojas, V., Márquez-Velasco, R., & Silveira, L. H. (2023) · Gaceta Médica de México · doi:10.24875/gmm.22000299 · Cited by 2
Yoshida, A., Nagata, S., Okazaki, Y., Hanaoka, H., Gono, T., & Kuwana, M. (2023) · Diagnostics · doi:10.3390/diagnostics13243621 · Cited by 2
Friend or foe of tripartite motif-containing protein 21 in cardiovascular disease: A review
Gong, X., Xu, L., & Cai, P. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142682 · Cited by 2
Teimoori, A., Mirshahabi, H., Khansarinejad, B., Soleimanjahi, H., Karimi, H., Rasti, M., & Malekshahi, S. S. (2022) · Journal of Immunoassay and Immunochemistry · doi:10.1080/15321819.2022.2118061 · Cited by 1
Cutaneous lupus erythematosus: insights from molecular pathogenesis to targeted therapies
Alduraibi, F. K., Goldsmith, J., & Chien, P. (2025) · Exploration of Immunology · doi:10.37349/ei.2025.1003222 · Cited by 1
Li, B., & Liu, Y. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112610 · Cited by 1
TRIM21 facilitates inflammasome assembly and contributes to autoinflammatory disease
Carrière, J., Yun, C., Khare, S., Ismaeel, S., Jäger, E., Martins, V. D., Sims, K. A., Chu, L. H., Nguyen, H., de Almeida, L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-73350-3 · Cited by 1
Autoantibodies in Sjögren’s Syndrome and Laboratory Markers
Kapsogeorgou, E. K., & Tzioufas, A. G. (2016) · Rare diseases of the immune system · doi:10.1007/978-3-319-24535-5_21 · Cited by 1
Role of M3 Muscarinic Acethylcholine Receptor Antibodies as a New Marker in Primary Sjögren Syndrome
Reina, S., Pisoni, C. N., Arana, R. M., Ganzinelli, S., & Borda, E. (2017) · Pharmacology & Pharmacy · doi:10.4236/pp.2017.87017 · Cited by 1
Eames, H. L., & Udalova, I. A. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1311-4_22 · Cited by 1
Winkler, M. A., & Pan, A. A. (2024) · Parasitology Research · doi:10.1007/s00436-024-08329-4 · Cited by 1
Ozato, K., Zhu, F., Tang, Q., Chang, T.-H., Peng, H., Deng, H., Li, X., & Wu, X. (2011) · Cited by 1
Pathogenesis of Autoimmune-Associated Long QT Syndrome
Boutjdir, M., Lazzerini, P. E., Capecchi, P. L., Pasini, F. L., & El‐Sherif, N. (2019) · Springer eBooks · doi:10.1007/978-3-030-22672-5_12 · Cited by 1
Interferon Type I Driven Immune Activation in Generalized Autoimmune Diseases
Brkić, Z. (2010) · RePub (Erasmus University Rotterdam) · Cited by 1
Ubiquitin Dependent Regulation of Innate Antiviral Signaling
Parvatiyar, M. S. (2010)
Green, J. B. A., Kim, N. H., & Kirsner, R. S. (2009) · Journal of Investigative Dermatology · doi:10.1038/jid.2009.191
Si, M., Yin, H. Y., Yang, Z., Li, X., Yang, Q., Yan, J., & Li, J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.10.052
Dendritic cells in Sjögren's syndrome-functional analyses
Lier, G. S. (2009) · NORA - Norwegian Open Research Archives
The Negative Regulation of the Antiviral Signaling Pathway
Charoenthongtrakul, S. (2013)
Negative regulation of host innate antiviral signaling
Zhou, Q. (2015)
Asano, Y. (2016) · Springer eBooks · doi:10.1007/978-4-431-55855-2_31
RO52/ TRIM21 IN B CELL PATHOLOGY
Brauner, S. (2013)
Mosaddeghi, P., Nezafat, N., Negahdaripour, M., Eslami, M., & Ghasemi, Y. (2018) · Current Signal Transduction Therapy · doi:10.2174/1574362413666180517093038
The Molecular Mechanism of Host Responses to Viral Infection
Schock, S. (2014) · eScholarship (California Digital Library)
Winkler, M. A., & Pan, A. A. (2021) · Research Square · doi:10.21203/rs.3.rs-553828/v1
Winkler, M. A., & Pan, A. A. (2021) · Research Square · doi:10.21203/rs.3.rs-553828/v2
Wang, S. L., Wu, Y., Konaté, M. M., Lu, J., Antony, S., Meitzler, J. L., Jiang, G., Dahan, I. M., Juhasz, A. N., Diebold, B. A., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.14.491678
Winkler, M. A., & Pan, A. A. (2023) · Research Square · doi:10.21203/rs.3.rs-3002014/v1
THE POSSIBLE RELATIONSHIPS BETWEEN SOME GENE POLYMORPHISMS AND SJOGREN’S SYNDROME
Terzi, U., & Ateş, İ. (2023) · Ankara Universitesi Eczacilik Fakultesi Dergisi · doi:10.33483/jfpau.1328811
Pan, A. A., & Winkler, M. A. (2024) · Research Square · doi:10.21203/rs.3.rs-3002014/v2
DUBs: a potential therapeutic target for SLE
MingJiu, Z. H. A. O., Gu, M., WenJun, L. U. O., ZHANG, M., Huang, J., & Bin, Z. (2024) · Scientia Sinica Vitae · doi:10.1360/ssv-2024-0146
Lee, C.-C., Chiu, L., Lee, S.-C., & Chan, T. (2026) · Clinical Immunology · doi:10.1016/j.clim.2026.110663
Asmi, F. E. (2013) · theses.fr (ABES) · doi:10.70675/df019c80z38c5z4420zb1cez6ffa93288b56
Metadata
- Authors
- Higgs, R., Gabhann, J. N., Larbi, N. B., Breen, E. P., Fitzgerald, K. A., & Jefferies, C. A.
- Affiliations
- Royal College of Surgeons in Ireland (IE)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Higgs, Rowan
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-08-01
- Volume
- 181
- Issue
- 3
- Pages
- 1780-1786
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- PMC
- PMC2824853
- OpenAlex
- W2129691636
- Cited by
- 310
- References
- 47
- Citations by year
- 2026: 14 · 2025: 13 · 2024: 10 · 2023: 21 · 2022: 17 · 2021: 25 · 2020: 14 · 2019: 17 · 2018: 20 · 2017: 14 · 2016: 13 · 2015: 17 · 2014: 18 · 2013: 24 · 2012: 19
- FWCI
- 7.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- Health Research Board
- Science Foundation Ireland
- National Institutes of Health (AI067497, AI067497 to K.A.F)
- National Institute of Allergy and Infectious Diseases (R01AI067497, R37AI067497, AI-067497, R56AI067497)
- 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 › Cancer Research › NF-κB Signaling Pathways
- Keywords
- Ro52, TRIM21, IRF3, type I interferon, interferon-beta, E3 ubiquitin ligase, polyubiquitination, proteasomal degradation, SPRY domain, interferon regulation, RANTES, Sendai virus, viral infection, chemokine production
- MeSH terms
- DEAD Box Protein 58, SS-A Antigen, Cell Line, Humans, Promoter Regions, Genetic, Protein Binding, Receptors, Immunologic, Ribonucleoproteins, Signal Transduction, Interferon-beta, Polyubiquitin, Ubiquitin-Protein Ligases, Interferon Regulatory Factor-3, Toll-Like Receptor 3, Toll-Like Receptor 4, DEAD-box RNA Helicases
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