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The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon
Abstract
E3 ubiquitin ligases are important in both innate and adaptive immunity. Here we report that Nrdp1, an E3 ubiquitin ligase, inhibited the production of proinflammatory cytokines but increased interferon-beta production in Toll-like receptor-triggered macrophages by suppressing adaptor MyD88-dependent activation of transcription factors NF-kappaB and AP-1 while promoting activation of the kinase TBK1 and transcription factor IRF3. Nrdp1 directly bound and polyubiquitinated MyD88 and TBK1, which led to degradation of MyD88 and activation of TBK1. Knockdown of Nrdp1 inhibited the degradation of MyD88 and the activation of TBK1 and IRF3. Nrdp1-transgenic mice showed resistance to lipopolysaccharide-induced endotoxin shock and to infection with vesicular stomatitis virus. Our data suggest that Nrdp1 functions as both an adaptor protein and an E3 unbiquitin ligase to regulate TLR responses in different ways.
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“Importantly, parkin-deficient mice and mice expressing a dominant negative form of Nrdp1 are not reported to have significant neurodegenerative disease171819.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [19]
In the citing paper
“The lack of reported neurodegeneration in parkin-deficient and Nrdp1 mutant mice171819 makes it unlikely that this interaction explains our finding of neurodegeneration in Clec16a mutant mice.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [19]
Citations
Cites
Akira, S., & Takeda, K. (2004) · Nature reviews. Immunology · doi:10.1038/nri1391 · Cited by 8,312
Toll-like receptor control of the adaptive immune responses
Iwasaki, A., & Medzhitov, R. M. (2004) · Nature Immunology · doi:10.1038/ni1112 · Cited by 4,166
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
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
Unresponsiveness of MyD88-deficient mice to endotoxin.
Kawai, T., Adachi, O., Ogawa, T., Takeda, K., & Akira, S. (1999) · Immunity · doi:10.1016/s1074-7613(00)80086-2 · Cited by 2,367
Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function.
Adachi, O., Kawai, T., Takeda, K., Matsumoto, M., Tsutsui, H., Sakagami, M., Nakanishi, K., & Akira, S. (1998) · Immunity · doi:10.1016/s1074-7613(00)80596-8 · Cited by 2,358
TAK1 is a ubiquitin-dependent kinase of MKK and IKK
Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125
Self-citationDe-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,889
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
Self-citationVISA 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
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Kawai, T., & Akira, S. (2010) · Nature Immunology · doi:10.1038/ni.1863 · Cited by 9,304
Toll-Like Receptor Signaling Pathways
Kawasaki, T., & Kawai, T. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00461 · Cited by 3,245
Toll-Like Receptor Signaling and Its Role in Cell-Mediated Immunity
Duan, T., Du, Y., Xing, C., Wang, H. Y., & Wang, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.812774 · Cited by 1,080
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
Hou, J., Lin, L., Zhou, W., Wang, Z., Ding, G., Dong, Q., Qin, L., Wu, X., Zheng, Y., Yang, Y. S., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.001 · Cited by 695
Self-citationCao, X. (2015) · Nature reviews. Immunology · doi:10.1038/nri.2015.8 · Cited by 671
Self-citationMa, F., Xu, S., Liu, X., Zhang, Q., Xu, X., Liu, M., Hua, M.-M., Li, N., Yao, H., & Cao, X. (2011) · Nature Immunology · doi:10.1038/ni.2073 · Cited by 659
Self-citationPost-Translational Modification Control of Innate Immunity
Liu, J., Qian, C., & Cao, X. (2016) · Immunity · doi:10.1016/j.immuni.2016.06.020 · Cited by 641
Self-citationUbiquitin signaling in immune responses
Hu, H., & Sun, S. (2016) · Cell Research · doi:10.1038/cr.2016.40 · Cited by 492
Han, C., Jin, J., Xu, S., Liu, H., Li, N., & Cao, X. (2010) · Nature Immunology · doi:10.1038/ni.1908 · Cited by 465
Self-citationCOVID-19: Drug Targets and Potential Treatments
Gil, C., Ginex, T., Maestro, I., Nozal, V., Barrado-Gil, L., Cuesta-Geijo, M. Á., Urquiza, J., Ramírez, D., Alonso, C., Campillo, N. E., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00606 · Cited by 456
Wang, P., Hou, J., Lin, L., Wang, C., Liu, X., Li, D., Ma, F., Wang, Z., & Cao, X. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000491 · Cited by 431
Self-citationGordon, D. E., Jang, G. Μ., Bouhaddou, M., Xu, J., Obernier, K., O’Meara, M. J., Guo, J. Z., Swaney, D. L., Tummino, T. A., Hüttenhain, R., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.22.002386 · Cited by 419
Wicherska‐Pawłowska, K., Wróbel, T., & Rybka, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413397 · Cited by 451
Yang, P., An, H., Liu, X., Wen, M., Zheng, Y., Rui, Y., & Cao, X. (2010) · Nature Immunology · doi:10.1038/ni.1876 · Cited by 409
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Pandey, S., Kawai, T., & Akira, S. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016246 · Cited by 387
Li, S., Wang, L., Berman, M. A., Kong, Y., & Dorf, M. E. (2011) · Immunity · doi:10.1016/j.immuni.2011.06.014 · Cited by 334
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Mukherjee, A., Morosky, S. A., Delorme‐Axford, E., Dybdahl-Sissoko, N., Oberste, M. S., Wang, T., & Coyne, C. B. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001311 · Cited by 316
Cui, J., Li, Y., Zhu, L., Liu, D., Songyang, Z., Wang, H. Y., & Wang, R. (2012) · Nature Immunology · doi:10.1038/ni.2239 · Cited by 301
Recognition of viral nucleic acids in innate immunity
Yoneyama, M., & Fujita, T. (2009) · Reviews in Medical Virology · doi:10.1002/rmv.633 · Cited by 313
Chen, W., Han, C., Xie, B., Hu, X., Yu, Q., Shi, L., Wang, Q., Li, D., Wang, J., Zheng, P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.011 · Cited by 276
Self-citationLiu, X.-G., Zhan, Z.-Z., Xu, L., Ma, F., Li, D., Guo, Z.-H., Li, N., & Cao, X.-T. (2010) · Journal of Immunology · doi:10.4049/jimmunol.1001573 · Cited by 286
Self-citationLiu, X., Zhan, Z., Li, D., Xu, L., Ma, F., Zhang, P., Yao, H., & Cao, X. (2011) · Nature Immunology · doi:10.1038/ni.2015 · Cited by 261
Self-citationSun, Y., Li, Q., Gui, H., Xu, D.-P., Yang, Y.-L., Su, D.-F., & Liu, X. (2013) · Cell Research · doi:10.1038/cr.2013.116 · Cited by 230
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Tu, D., Zhu, Z., Zhou, A. Y., Yun, C., Lee, K., Toms, A. V., Li, Y., Dunn, G. P., Chan, E. M., Thai, T. C., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.033 · Cited by 222
Ubiquitin in the activation and attenuation of innate antiviral immunity
Heaton, S. M., Borg, N. A., & Dixit, V. M. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20151531 · Cited by 208
Song, G., Liu, B., Li, Z., Wu, H. M., Wang, P., Zhao, K., Jiang, G., Zhang, L., & Gao, C. (2016) · Nature Immunology · doi:10.1038/ni.3588 · Cited by 201
Li, X., Zhang, Q., Ding, Y., Liu, Y., Zhao, D., Zhao, K., Shen, Q., Liu, X., Zhu, X., Li, N., et al. (2016) · Nature Immunology · doi:10.1038/ni.3464 · Cited by 206
Self-citationThe RING finger protein family in health and disease
Cai, C., Tang, Y., Zhai, J., & Zheng, C. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01152-2 · Cited by 204
Ubiquitination in the antiviral immune response
Davis-Gardner, M. E., & Gack, M. U. (2015) · Virology · doi:10.1016/j.virol.2015.02.033 · Cited by 197
Inflammatory response of macrophages in infection
Zhang, L., & Wang, C.-C. (2014) · Hepatobiliary & pancreatic diseases international · doi:10.1016/s1499-3872(14)60024-2 · Cited by 194
Self-citationWang, D., Fang, L., Li, P., Sun, L., Fan, J., Zhang, Q., Luo, R., Liu, X., Li, K., Chen, H., et al. (2011) · Journal of Virology · doi:10.1128/jvi.02589-10 · Cited by 188
Zheng, Q., Hou, J., Zhou, Y., Yang, Y., Xie, B., & Cao, X. (2015) · Cell Research · doi:10.1038/cr.2015.108 · Cited by 187
Self-citationSensing and Signaling in Antiviral Innate Immunity
O'Neill, L. A. J., & Bowie, A. (2010) · Current Biology · doi:10.1016/j.cub.2010.01.044 · Cited by 183
Helgason, E., Phung, Q. T., & Dueber, E. C. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.059 · Cited by 184
Li, S., Zheng, H., Mao, A., Zhong, B., Li, Y., Liu, Y., Gao, Y., Ran, Y., Tien, P., & Shu, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.074971 · Cited by 179
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Bao, M., & Liu, Y.-J. (2012) · Protein & Cell · doi:10.1007/s13238-012-2104-8 · Cited by 189
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Parvatiyar, K., Barber, G. N., & Harhaj, E. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.109819 · Cited by 169
Rajsbaum, R., Versteeg, G. A., Schmid, S., Maestre, A. M., Belicha-Villanueva, A., Martínez-Romero, C., Patel, J. R., Morrison, J., Pisanelli, G., Miorin, L., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.04.018 · Cited by 168
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Qian, C., & Cao, X. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06786.x · Cited by 167
Self-citationDeciphering the complexity of Toll-like receptor signaling
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Chen, L., Zheng, L., Chen, P., & Liang, G. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00884 · Cited by 158
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
Self-citationNegative regulation of TBK1‐mediated antiviral immunity
Zhao, W. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.052 · Cited by 151
Zhang, M., Wang, L., Zhao, X., Zhao, K., Hong, M., Zhao, W., & Gao, C. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20120024 · Cited by 146
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Lin, M., Zhao, Z., Yang, Z., Meng, Q., Tan, P., Xie, W., Qin, Y., Wang, R., & Cui, J. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.029 · Cited by 145
Wang, S., Wang, K., Li, J., & Zheng, C. (2013) · Journal of Virology · doi:10.1128/jvi.01211-13 · Cited by 141
Post‐translational regulation of antiviral innate signaling
Zhou, Y., He, C., Wang, L., & Ge, B.-X. (2017) · European Journal of Immunology · doi:10.1002/eji.201746959 · Cited by 139
Mao, A., Li, S., Zhong, B., Li, Y., Yan, J., Li, Q., Teng, C., & Shu, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071043 · Cited by 134
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Pereira, M. C. A., & Gazzinelli, R. T. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1133354 · Cited by 134
Liuyu, T., Yu, K., Ye, L., Zhang, Z., Zhang, M., Ren, Y., Cai, Z., Zhu, Q., Lin, D., & Zhong, B. (2018) · Cell Research · doi:10.1038/s41422-018-0107-6 · Cited by 127
Zhao, W., Wang, L., Zhang, M., Yuan, C., & Gao, C. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103255 · Cited by 127
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Li, Y., & Shi, X. (2012) · Cellular and Molecular Immunology · doi:10.1038/cmi.2012.55 · Cited by 127
Fang, H., Wu, Y., Huang, X., Wang, W., Ang, B., Cao, X., & Wan, T. Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.266528 · Cited by 122
Self-citationAutophagy in regulation of Toll-like receptor signaling
Into, T., Inomata, M., Takayama, E., & Takigawa, T. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.020 · Cited by 121
Wang, W., Jiang, M., Liu, S., Zhang, S., Liu, W., Ma, Y., Zhang, L., Zhang, J., & Cao, X. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604277113 · Cited by 120
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Mujoo, K., Choi, B.-K., Huang, Z., Zhang, N., & An, Z. (2014) · Oncotarget · doi:10.18632/oncotarget.2655 · Cited by 107
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Janova, H., Böttcher, C., Holtman, I. R., Regen, T., van Rossum, D., Götz, A., Ernst, A., Fritsche, C., Gertig, U., Saiepour, N., et al. (2016) · Glia · doi:10.1002/glia.22955 · Cited by 105
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Zhou, R., Zhang, Q., & Xu, P. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa051 · Cited by 104
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Kesar, V., & Odin, J. A. (2013) · Liver International · doi:10.1111/liv.12315 · Cited by 105
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Qingjun, L., Zhou, H., Langdon, W. Y., & Zhang, J. (2014) · Cell Cycle · doi:10.4161/cc.29213 · Cited by 101
Self-citationMechanism of inhibiting type I interferon induction by hepatitis B virus X protein
Jiang, J., & Tang, H. (2010) · Protein & Cell · doi:10.1007/s13238-010-0141-8 · Cited by 106
K33-linked polyubiquitination of Zap70 by Nrdp1 controls CD8+ T cell activation
Yang, M., Chen, T., Li, X., Zhou, Y., Tang, S., Wang, C., Gu, Y. H., Liu, Y., Xu, S., Li, W., et al. (2015) · Nature Immunology · doi:10.1038/ni.3258 · Cited by 97
Self-citationMechanisms of Antiviral Immune Evasion of SARS-CoV-2
Beyer, D. K., & Forero, A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167265 · Cited by 96
Sui, C., Xiao, T., Zhang, S., Zeng, H., Zheng, Y., Liu, B., Xu, G., Gao, C., & Zhang, Z. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2100684 · Cited by 93
Yang, M., Wang, C., Zhu, X., Tang, S., Shi, L., Cao, X., & Chen, T. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20102667 · Cited by 93
Self-citationQin, Y., Liu, Q., Tian, S., Xie, W., Cui, J., & Wang, R. (2016) · Cell Research · doi:10.1038/cr.2016.27 · Cited by 94
ABIN1 Protein Cooperates with TAX1BP1 and A20 Proteins to Inhibit Antiviral Signaling
Gao, L., Coope, H. J., Grant, S. M., Ma, A. I., Ley, S. C., & Harhaj, E. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.283762 · Cited by 88
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Borrow, P., Martínez‐Sobrido, L., & de la Torre, J. C. (2010) · Viruses · doi:10.3390/v2112443 · Cited by 89
Into, T., Inomata, M., Niida, S., Murakami, Y., & Shibata, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126904 · Cited by 92
A Structural View of Negative Regulation of the Toll-like Receptor-Mediated Inflammatory Pathway
Guven‐Maiorov, E., Keskin, Ö., Gürsoy, A., & Nussinov, R. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.06.048 · Cited by 87
Zhang, Z.-D., Xiong, T.-C., Yao, S., Wei, M., Chen, M., Lin, D., & Zhong, B. (2020) · Nature Communications · doi:10.1038/s41467-020-19318-3 · Cited by 87
Kumar, R., Verma, H., Singhvi, N., Sood, U., Gupta, V., Singh, M., KUMARI, R. R., Hira, P., Nagar, S., Talwar, C., et al. (2020) · mSystems · doi:10.1128/msystems.00505-20 · Cited by 81
The VP3 structural protein of foot‐and‐mouth disease virus inhibits the IFN‐β signaling pathway
Li, D., Yang, W., Yang, F., Liu, H., Zhu, Z., Lian, K., Lei, C., Li, S., Liu, X., Zheng, H., et al. (2016) · The FASEB Journal · doi:10.1096/fj.15-281410 · Cited by 80
Wang, P., Du, H., Zhou, C., Song, J., Liu, X., Cao, X., Mehta, J. L., Shi, Y., Su, D., & Miao, C. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu220 · Cited by 76
Self-citationZhao, Q., Liang, D., Sun, R., Jia, B., Xia, T., Xiao, H. Q., & Lan, K. (2014) · Journal of Virology · doi:10.1128/jvi.02591-14 · Cited by 74
The methyltransferase PRMT6 attenuates antiviral innate immunity by blocking TBK1–IRF3 signaling
Zhang, H., Han, C., Li, T., Li, N., & Cao, X. (2018) · Cellular and Molecular Immunology · doi:10.1038/s41423-018-0057-4 · Cited by 71
Self-citationWang, G., Chen, G., Zheng, D., Cheng, G., & Tang, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017192 · Cited by 70
Dynamic regulation of innate immunity by ubiquitin and ubiquitin-like proteins
Liu, X., Wang, Q., Chen, W., & Wang, C. (2013) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2013.07.002 · Cited by 70
Self-citationMitochondrial Ubiquitin Ligase MARCH5 Promotes TLR7 Signaling by Attenuating TANK Action
Shi, H.-X., Liu, X., Wang, Q., Tang, P.-P., Liu, X.-Y., Shan, Y.-F., & Wang, C. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002057 · Cited by 67
Self-citationZhou, Y., Chen, T., Li, X., Yang, M., Tang, S., Zhu, X., Gu, Y. H., Su, X., Meng, X., Li, W., et al. (2016) · eLife · doi:10.7554/elife.14087 · Cited by 71
Self-citationGuo, F., Zhang, C., Wang, F., Zhang, W. J., Shi, X., Zhu, Y., Fang, Z., Yang, B., & Sun, Y. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0473-8 · Cited by 66
Tai, A., Li, S., Pan, W. D., Tien, P., Zhong, B., Shu, H., & Wu, S. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005179 · Cited by 64
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Wauman, J., Ceuninck, L. D., Vanderroost, N., Lievens, S., & Tavernier, J. H. (2011) · Journal of Cell Science · doi:10.1242/jcs.078055 · Cited by 67
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Li, D., Lei, C., Xu, Z.-S., Yang, F., Liu, H., Zhu, Z., Li, S., Liu, X., Shu, H., & Zheng, H. (2016) · Scientific Reports · doi:10.1038/srep21888 · Cited by 65
Zhang, L., Zhao, X., Zhang, M., Zhao, W., & Gao, C. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302634 · Cited by 62
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Li, F., Li, Y., Liang, H., Xu, T., Kong, Y., Huang, M., Xiao, J., Chen, X., Xia, H., Wu, Y., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120406 · Cited by 64
Deng, M., Tam, J. W., Wang, L., Liang, K., Li, S., Zhang, L., Guo, H., Luo, X., Zhang, Y., Petrucelli, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16014-0 · Cited by 61
Alexander, S. P. H., Armstrong, J. F., Davenport, A. P., Davies, J. A., Faccenda, E., Harding, S. D., Levi‐Schaffer, F., Maguire, J. J., Pawson, A. J., Southan, C., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15094 · Cited by 61
Li, X., Yang, M., Zhou, Y., Tang, S., Wang, L., Cao, X., & Chen, T. (2017) · Science Signaling · doi:10.1126/scisignal.aae0435 · Cited by 63
Self-citationZhang, Y., Li, L.-F., Munir, M., & Qiu, H.-J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01083 · Cited by 62
Tang, S., Chen, T., Zhou, Y., Zhu, X., Yang, M., Xie, B., Li, N., Cao, X., & Wang, J. (2014) · Nature Communications · doi:10.1038/ncomms5657 · Cited by 60
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Metadata
- Authors
- Wang, C., Chen, T., Zhang, J., Yang, M., Li, N., Xu, X., & Cao, X.
- Affiliations
- Second Military Medical University (CN)
- Corresponding author
- Cao, Xuetao
- Venue
- Nature Immunology
- Published
- 2009-05-31
- Volume
- 10
- Issue
- 7
- Pages
- 744-752
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W2077995361
- Cited by
- 317
- References
- 46
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 19 · 2023: 13 · 2022: 27 · 2021: 14 · 2020: 35 · 2019: 14 · 2018: 21 · 2017: 11 · 2016: 26 · 2015: 18 · 2014: 22 · 2013: 19 · 2012: 14
- FWCI
- 8.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- Nrdp1, E3 ubiquitin ligase, Toll-like receptor signaling, type I interferon, interferon-beta, IRF3, NF-κB, AP-1, macrophages, polyubiquitination, vesicular stomatitis virus, endotoxic shock, innate immunity
- MeSH terms
- Animals, Carrier Proteins, Cell Line, Cells, Cultured, Female, Humans, Interferon Type I, Lipopolysaccharides, Macrophages, Male, Mice, Inbred C57BL, Mice, Transgenic, Protein Binding, Immunoblotting, Protein Serine-Threonine Kinases, Macrophages, Peritoneal, Vesiculovirus, Rhabdoviridae Infections, Sepsis, Reverse Transcriptase Polymerase Chain Reaction, Ubiquitin-Protein Ligases, Toll-Like Receptors, Mice, Myeloid Differentiation Factor 88, Host-Pathogen Interactions
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