The DOI matches its Crossref record; 155 of the 155 references it cites were found in a registry or an index.
TBK1, a central kinase in innate immune sensing of nucleic acids and beyond
Open accessAbstract
Sensing of intracellular and extracellular environments is one of the fundamental processes of cell. Surveillance of aberrant nucleic acids, derived either from invading pathogens or damaged organelle, is conducted by pattern recognition receptors (PRRs) including RIG-I-like receptors, cyclic GMP-AMP synthase, absent in melanoma 2, and a few members of toll-like receptors. TANK-binding kinase 1 (TBK1), along with its close analogue I-kappa-B kinase epsilon, is a central kinase in innate adaptor complexes linking activation of PRRs to mobilization of transcriptional factors that transcribe proinflammatory cytokines, type I interferon (IFN-α/β), and myriads interferon stimulated genes. However, it still remains elusive for the precise mechanisms of activation and execution of TBK1 in signaling platforms formed by innate adaptors mitochondrial antiviral signaling protein (MAVS), stimulator of interferon genes protein (STING), and TIR-domain-containing adapter-inducing interferon-β (TRIF), as well as its complex regulations. An atlas of TBK1 substrates is in constant expanding, setting TBK1 as a key node of signaling network and a dominant player in contexts of cell biology, animal models, and human diseases. Here, we review recent advancements of activation, regulations, and functions of TBK1 under these physiological and pathological contexts.
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 plays a central role in coordinating the innate immune response in response to cytosolic nucleic acids (e.g. cGAS-STING-TBK1-IRF3-IFN type I pathway) 3 , and enhanced sensitivity to TNF α has been shown to drive cGAS-STING-dependent interferon response and impact cell viability 42 .”
From Targeting TBK1 to overcome resistance to cancer immunotherapy (2023) · cites this paper as [3]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“TBK1 integrates upstream signals from pattern recognition receptors and cytosolic nucleic acid sensors to regulate the activation of interferon regulatory factor 3 (IRF3) and consequent induction of type I interferons (IFNα / β ) and interferon-stimulated genes (ISGs) critical to the host immune response 3 .”
From Targeting TBK1 to overcome resistance to cancer immunotherapy (2023) · cites this paper as [3]
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
Pattern Recognition Receptors and Inflammation
Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895
Cyclic GMP-AMP Synthase Is a Cytosolic DNA Sensor That Activates the Type I Interferon Pathway
Sun, L., Wu, J., Du, F., Chen, X., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1232458 · Cited by 4,996
Systematic RNA interference reveals that oncogenic KRAS-driven cancers require TBK1
Barbie, D. A., Tamayo, P., Boehm, J. S., Kim, S. Y., Moody, S. E., Dunn, I. F., Schinzel, A. C., Sandy, P., Meylan, E., Scholl, C., et al. (2009) · Nature · doi:10.1038/nature08460 · Cited by 3,922
STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
Ishikawa, H., & Barber, G. N. (2008) · Nature · doi:10.1038/nature07317 · Cited by 3,576
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
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
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
Cyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA
Wu, J., Sun, L., Chen, X., Du, F., Shi, H., Chen, C., & Chen, Z. J. (2012) · Science · doi:10.1126/science.1229963 · Cited by 2,628
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
Regulation 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
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
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
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
cGAS surveillance of micronuclei links genome instability to innate immunity
Mackenzie, K. J., Carroll, P., Martin, C.-A., Murina, O., Fluteau, A., Simpson, D. J., Olova, N., Sutcliffe, H., Rainger, J. K., Leitch, A., et al. (2017) · Nature · doi:10.1038/nature23449 · Cited by 1,752
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
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
Chromosomal instability drives metastasis through a cytosolic DNA response
Bakhoum, S. F., Ngo, B., Laughney, A. M., Cavallo, J.-A., Murphy, C. J., Ly, P., Shah, P., Sriram, R. K., Watkins, T. B. K., Taunk, N. K., et al. (2018) · Nature · doi:10.1038/nature25432 · Cited by 1,593
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
The Adaptor Protein MITA Links Virus-Sensing Receptors to IRF3 Transcription Factor Activation
Zhong, B., Yang, Y., Li, S., Wang, Y., Li, Y., Diao, F., Lei, C., He, X., Zhang, L., Tien, P., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.09.003 · Cited by 1,514
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
STING 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
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
Hou, F., Sun, L., Zheng, H., Skaug, B. A., Jiang, Q., & Chen, Z. J. (2011) · Cell · doi:10.1016/j.cell.2011.06.041 · Cited by 1,306
Phosphorylation of the Autophagy Receptor Optineurin Restricts Salmonella Growth
Wild, P., Farhan, H., McEwan, D. G., Wagner, S., Rogov, V. V., Brady, N. R., Richter, B., Korac, J., Waidmann, O., Choudhary, C., et al. (2011) · Science · doi:10.1126/science.1205405 · Cited by 1,298
Autophagy 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 immune sensing of cytosolic chromatin fragments through cGAS promotes senescence
Glück, S., Guey, B., Gulen, M. F., Wolter, K., Kang, T.-W., Schmacke, N. A., Bridgeman, A., Rehwinkel, J., Zender, L., & Ablasser, A. (2017) · Nature Cell Biology · doi:10.1038/ncb3586 · Cited by 1,196
Quigley, H. A. (2011) · The Lancet · doi:10.1016/s0140-6736(10)61423-7 · Cited by 1,130
Zhang, X., Shi, H., Wu, J., Zhang, X., Sun, L., Chen, C., & Chen, Z. J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.022 · Cited by 1,118
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
Everts, B., Amiel, E., Huang, S. C.-C., Smith, A. M., Chang, C.-H., Lam, W. Y., Redmann, V., Freitas, T. C., Blagih, J., van der Windt, G. J. W., et al. (2014) · Nature Immunology · doi:10.1038/ni.2833 · Cited by 1,064
cGAS is essential for cellular senescence
Yang, H., Wang, H., Ren, J., Chen, Q., & Chen, Z. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705499114 · Cited by 1,009
Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways
Cirulli, E. T., Lasseigne, B. N., Petrovski, S., Sapp, P. C., Dion, P. A., Leblond, C. S., Couthouis, J., Lu, Y.-F., Wang, Q., Krueger, B. J., et al. (2015) · Science · doi:10.1126/science.aaa3650 · Cited by 966
Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906
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
Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response
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
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia
Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Müller, K., Marroquin, N., Nordin, F., Hübers, A., Weydt, P., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4000 · Cited by 786
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
STING agonist formulated cancer vaccines can cure established tumors resistant to PD-1 blockade
Fu, J., Kanne, D. B., Leong, M., Glickman, L. H., McWhirter, S. M., Lemmens, E., Mechette, K., Leong, J. J., Lauer, P., Liu, W., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa4306 · Cited by 720
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
Dobbs, N., Burnaevskiy, N., Chen, D., Gonugunta, V. K., Alto, N. M., & Yan, N. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.07.001 · Cited by 656
TBK-1 Promotes Autophagy-Mediated Antimicrobial Defense by Controlling Autophagosome Maturation
Pilli, M., Arko-Mensah, J., Ponpuak, M., Roberts, E., Master, S., Mandell, M. A., Dupont, N., Ornatowski, W., Jiang, S., Bradfute, S. B., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.04.015 · Cited by 655
Post-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
NF‐κB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK‐related kinase
Pomerantz, J. L., & Baltimore, D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.23.6694 · Cited by 599
STING activation of tumor endothelial cells initiates spontaneous and therapeutic antitumor immunity
Demaria, O., Gassart, A. D., Coso, S., Gestermann, N., Domizio, J. D., Flatz, L., Gaide, O., Michielin, O. A., Hwu, P., Petrova, T. V., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512832112 · Cited by 585
McWhirter, S. M., Fitzgerald, K. A., Rosains, J., Rowe, D. C., Golenbock, D. T., & Maniatis, T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2237236100 · Cited by 542
Recognition of Endogenous Nucleic Acids by the Innate Immune System
Roers, A., Hiller, B., & Hornung, V. (2016) · Immunity · doi:10.1016/j.immuni.2016.04.002 · Cited by 541
TBK1 Suppresses RIPK1-Driven Apoptosis and Inflammation during Development and in Aging
Xu, D., Jin, T., Zhu, H., Chen, H., Ofengeim, D., Zou, C., Mifflin, L., Pan, L., Amin, P., Li, W., et al. (2018) · Cell · doi:10.1016/j.cell.2018.07.041 · Cited by 461
Petrasek, J., Iracheta‐Vellve, A., Csák, T., Satishchandran, A., Kodys, K., Kurt‐Jones, E. A., Fitzgerald, K. A., & Szabó, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308331110 · Cited by 449
A conserved PLPLRT/SD motif of STING mediates the recruitment and activation of TBK1
Zhao, B., Du, F., Xu, P., Shu, C., Sankaran, B., Bell, S. L., Liu, M., Lei, Y., Gao, X., Fu, X., et al. (2019) · Nature · doi:10.1038/s41586-019-1228-x · Cited by 447
Self-citationReilly, S. M., Chiang, S.-H., Decker, S. J., Chang, L. C., Uhm, M., Larsen, M. J., Rubin, J. R., Mowers, J. C., White, N. M. A., Hochberg, I., et al. (2013) · Nature Medicine · doi:10.1038/nm.3082 · Cited by 442
Clark, K., Plater, L., Peggie, M. W., & Cohen, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000414 · Cited by 389
Activation of STAT6 by STING Is Critical for Antiviral Innate Immunity
Chen, H., Sun, H., You, F., Sun, W., Zhou, X., Chen, L., Yang, J., Wang, Y., Tang, H., Guan, Y., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.022 · Cited by 383
Bonnard, M., Mirtsos, C., Suzuki, S., Graham, K., Huang, J., Ng, M., Itié, A., Wakeham, A., Shahinian, A., Henzel, W. J., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.18.4976 · Cited by 381
Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKε‐mediated IRF activation
Schröder, M., Baran, M., & Bowie, A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.143 · Cited by 374
Chien, Y., Kim, S., Bumeister, R., Loo, Y., Kwon, S. W., Johnson, C., Balakireva, M. G., Roméo, Y., Kopelovich, L., Gale, M., et al. (2006) · Cell · doi:10.1016/j.cell.2006.08.034 · Cited by 367
Moore, A. S., & Holzbaur, E. L. F. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523810113 · Cited by 362
Moretti, J., Roy, S., Bozec, D., Martinez, J., Chapman, J. R., Ueberheide, B. M., Lamming, D. W., Chen, Z. J., Horng, T., Yeretssian, G., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.034 · Cited by 341
The tumour suppressor CYLD is a negative regulator of RIG‐I‐mediated antiviral response
Friedman, C. S., O’Donnell, M. A., Legarda, D., Ng, A., Cardenas, W. B., Yount, J. S., Moran, T. M., Basler, C. F., Komuro, A., Horvath, C. M., et al. (2008) · EMBO Reports · doi:10.1038/embor.2008.136 · Cited by 334
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
Novel cross-talk within the IKK family controls innate immunity
Clark, K., Peggie, M., Plater, L., Sorcek, R. J., Young, E. R. R., Madwed, J. B., Hough, J., McIver, E. G., & Cohen, P. (2011) · Biochemical Journal · doi:10.1042/bj20101701 · Cited by 326
Agonist-Mediated Activation of STING Induces Apoptosis in Malignant B Cells
Tang, C.-H. A., Zundell, J. A., Ranatunga, S., Lin, C., Nefedova, Y., Valle, J. R. D., & Hu, C. A. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-1885 · Cited by 322
The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon
Wang, C., Chen, T., Zhang, J., Yang, M., Li, N., Xu, X., & Cao, X. (2009) · Nature Immunology · doi:10.1038/ni.1742 · Cited by 317
Pottier, C., Bieniek, K. F., Finch, N., van de Vorst, M., Baker, M., Perkersen, R., Brown, P., Ravenscroft, T., van Blitterswijk, M., Nicholson, A. M., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1436-x · Cited by 312
Molecular and cellular pathways of neurodegeneration in motor neurone disease
Shaw, P. J. (2005) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2004.048652 · Cited by 311
Immune-mediated Mechanisms in the Pathoprogression of Amyotrophic Lateral Sclerosis
Zhao, W., Beers, D. R., & Appel, S. H. (2013) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-013-9489-x · Cited by 309
Intrinsic antiproliferative activity of the innate sensor STING in T lymphocytes
Cerboni, S., Jeremiah, N., Gentili, M., Gehrmann, U., Conrad, C., Stolzenberg, M., Pïcard, C., Neven, B., Fischer, A., Amigorena, S., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20161674 · Cited by 303
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
Casadio, M., Ciancanelli, M. J., Ou, Y.-H., Lorenzo, L., Klaudel‐Dreszler, M., Pauwels, E., Sancho‐Shimizu, V., de Diego, R. P., Abhyankar, A., Israelsson, E., et al. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20111316 · Cited by 292
Onorati, M., Li, Z., Liu, F., Sousa, A. M. M., Nakagawa, N., Li, M., Dell’Anno, M. T., Gulden, F. O., Pochareddy, S., Tebbenkamp, A. T. N., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.038 · Cited by 292
Wu, S., Zhang, Q., Zhang, F., Meng, F., Liu, S., Zhou, R., Wu, Q., Li, X., Shen, L., Huang, J., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0352-z · Cited by 278
Self-citationSiu, K., Kok, K., Ng, M.-H. J., Poon, V. K., Yuen, K., Zheng, B.-J., & Jin, D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.008227 · Cited by 276
Jimenez-Dalmaroni, M. J., Gerswhin, M. E., & Adamopoulos, I. E. (2015) · Autoimmunity Reviews · doi:10.1016/j.autrev.2015.08.009 · Cited by 271
Crystal Structure and Mechanism of Activation of TANK-Binding Kinase 1
Larabi, A., Devos, J. M., Ng, S., Nanao, M., Round, A. R., Maniatis, T., & Panne, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.034 · Cited by 253
TBK1 at the Crossroads of Inflammation and Energy Homeostasis in Adipose Tissue
Zhao, P., Wong, K. I., Sun, X., Reilly, S. M., Uhm, M., Liao, Z., Skorobogatko, Y., & Saltiel, A. R. (2018) · Cell · doi:10.1016/j.cell.2018.01.007 · Cited by 250
Luo, W., Li, S., Li, C., Lian, H., Yang, Q., Zhong, B., & Shu, H. (2016) · Nature Immunology · doi:10.1038/ni.3510 · Cited by 249
Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation
Ma, X., Helgason, E., Phung, Q. T., Quan, C. L., Iyer, R. S., Lee, M. W., Bowman, K. K., Starovasnik, M. A., & Dueber, E. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121552109 · Cited by 246
An, H., Zhao, W., Hou, J., Zhang, Y., Xie, Y., Zheng, Y., Xu, H., Qian, C., Zhou, J., Yu, Y., et al. (2006) · Immunity · doi:10.1016/j.immuni.2006.10.014 · Cited by 244
Copy number variations on chromosome 12q14 in patients with normal tension glaucoma
Fingert, J. H., Robin, A. L., Stone, J. L., Roos, B. R., Davis, L. K., Scheetz, T. E., Bennett, S. R., Wassink, T. H., Kwon, Y. H., Alward, W. L. M., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr123 · Cited by 228
Dalrymple, N. A., Cimica, V., & Mackow, E. R. (2015) · mBio · doi:10.1128/mbio.00553-15 · Cited by 228
IκB kinase ε and TANK-binding kinase 1 activate AKT by direct phosphorylation
Xie, X., Zhang, D., Zhao, B., Lu, M.-K., You, M., Condorelli, G., Wang, C.-Y., & Guan, K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016132108 · Cited by 226
TBK1 Directly Engages Akt/PKB Survival Signaling to Support Oncogenic Transformation
Ou, Y.-H., Torres, M. J., Ram, R. R., Formstecher, É., Roland, C. L., Cheng, T., Brekken, R. A., Wurz, R. P., Tasker, A. S., Polverino, T., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.019 · Cited by 224
Structure and Ubiquitination-Dependent Activation of TANK-Binding Kinase 1
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
ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response
Li, Y., Li, C., Xue, P., Zhong, B., Mao, A., Ran, Y., Chen, H., Wang, Y., Yang, F., & Shu, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900818106 · Cited by 221
TRIM23 mediates virus-induced autophagy via activation of TBK1
Sparrer, K. M. J., Gableske, S., Zurenski, M. A., Parker, Z. M., Full, F., Baumgart, G. J., Kato, J., Pacheco–Rodriguez, G., Liang, C., Pornillos, O., et al. (2017) · Nature Microbiology · doi:10.1038/s41564-017-0017-2 · Cited by 221
cGAS–STING and Cancer: Dichotomous Roles in Tumor Immunity and Development
Ng, K. W., Marshall, E. A., Bell, J. C., & Lam, W. L. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.07.013 · Cited by 219
Human TBK1: A Gatekeeper of Neuroinflammation
Ahmad, L., Zhang, S.-Y., Casanova, J.-L., & Sancho-Shimizu, V. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.04.006 · Cited by 208
Melki, I., Rose, Y., Uggenti, C., Eyck, L. V., Frémond, M., Kitabayashi, N., Rice, G., Jenkinson, E. M., Boulai, A., Jeremiah, N., et al. (2017) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.10.031 · Cited by 208
Dynamic control of type I IFN signalling by an integrated network of negative regulators
Porritt, R. A., & Hertzog, P. J. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.02.002 · Cited by 206
Yu, S., Chen, J., Wu, M., Chen, H., Kato, N., & Yuan, Z. (2010) · Journal of General Virology · doi:10.1099/vir.0.020552-0 · Cited by 206
Hippo signalling governs cytosolic nucleic acid sensing through YAP/TAZ-mediated TBK1 blockade
Zhang, Q., Meng, F., Chen, S., Plouffe, S. W., Wu, S., Liu, S., Li, X., Zhou, R., Wang, J., Zhao, B., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3496 · Cited by 206
Self-citationSong, 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
Ryzhakov, G., & Randow, F. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601743 · Cited by 196
RIG-I-like receptor regulation in virus infection and immunity
Chan, Y., & Gack, M. U. (2015) · Current Opinion in Virology · doi:10.1016/j.coviro.2015.01.004 · Cited by 196
Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in Innate Immunity
Cadena, C., Ahmad, S., Xavier, A., Willemsen, J., Park, S., Park, J. W., Oh, S.-W., Fujita, T., Hou, F., Binder, M., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.017 · Cited by 192
Wang, 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
Self-citationHepatitis C virus NS4B blocks the interaction of STING and TBK1 to evade host innate immunity
Ding, Q., Cao, X., Lu, J. L., Huang, B. S., Liu, Y.-J., Kato, N., Shu, H., & Zhong, J. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.03.019 · Cited by 187
Zheng, Q., Hou, J., Zhou, Y., Yang, Y., Xie, B., & Cao, X. (2015) · Cell Research · doi:10.1038/cr.2015.108 · Cited by 187
Control of TANK-binding Kinase 1-mediated Signaling by the γ134.5 Protein of Herpes Simplex Virus 1
Verpooten, D., Ma, Y., Hou, S., Yan, Z., & He, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805905200 · Cited by 186
Becker, A. M., Dao, K. H., Han, B. K., Kornu, R., Lakhanpal, S., Mobley, A. B., Li, Q., Lian, Y., Wu, T., Reimold, A. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067003 · Cited by 184
tenOever, B. R., Sharma, S., Zou, W., Sun, Q., Grandvaux, N., Julkunen, I., Hemmi, H., Yamamoto, M., Akira, S., Yeh, W., et al. (2004) · Journal of Virology · doi:10.1128/jvi.78.19.10636-10649.2004 · Cited by 181
Lei, C., Zhong, B., Zhang, Y., Zhang, J., Wang, S., & Shu, H. (2010) · Immunity · doi:10.1016/j.immuni.2010.11.021 · Cited by 180
Morton, S., Hesson, L. B., Peggie, M. W., & Cohen, P. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.047 · Cited by 180
Structural basis for the prion-like MAVS filaments in antiviral innate immunity
Xu, H., He, X., Zheng, H., Huang, L. J.-S., Hou, F., Yu, Z., de la Cruz, M. J., Borkowski, B., Zhang, X., Chen, Z. J., et al. (2014) · eLife · doi:10.7554/elife.01489 · Cited by 179
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
IFN-Induced TPR Protein IFIT3 Potentiates Antiviral Signaling by Bridging MAVS and TBK1
Liu, X.-Y., Chen, W., Wei, B., Shan, Y., & Wang, C. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100963 · Cited by 167
Inhibition of IKKɛ and TBK1 Improves Glucose Control in a Subset of Patients with Type 2 Diabetes
Oral, E. A., Reilly, S. M., Gomez, A. V., Meral, R., Butz, L., Ajluni, N., Chenevert, T. L., Korytnaya, E., Neidert, A., HENCH, R. P., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.06.006 · Cited by 165
SIKE is an IKKε/TBK1‐associated suppressor of TLR3‐ and virus‐triggered IRF‐3 activation pathways
Huang, J., Liu, T., Xu, L., Chen, D., Zhai, Z., & Shu, H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600863 · Cited by 155
Mowers, J. C., Uhm, M., Reilly, S. M., Simon, J., Leto, D. E., Chiang, S.-H., Chang, L. C., & Saltiel, A. R. (2013) · eLife · doi:10.7554/elife.01119 · Cited by 152
Targeting an IKBKE cytokine network impairs triple-negative breast cancer growth
Barbie, T. U., Alexe, G., Aref, A. R., Li, S., Zhu, Z., Zhang, X., Imamura, Y., Thai, T. C., Huang, Y., Bowden, M., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci75661 · 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
USP38 Inhibits Type I Interferon Signaling by Editing TBK1 Ubiquitination through NLRP4 Signalosome
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
Minegishi, Y., Iejima, D., Kobayashi, H., Chi, Z.-L., Kawase, K., Yamamoto, T., Seki, T., Yuasa, S., Fukuda, K., & Iwata, T. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt210 · Cited by 138
The kinase TBK1 controls IgA class switching by negatively regulating noncanonical NF-κB signaling
Jin, J., Xiao, Y., Chang, J.-H., Yu, J., Hu, H., Starr, R., Brittain, G. C., Chang, M., Cheng, X., & Sun, S.-C. (2012) · Nature Immunology · doi:10.1038/ni.2423 · Cited by 136
Zheng, D., Chen, G., Guo, B., Cheng, G., & Tang, H. (2008) · Cell Research · doi:10.1038/cr.2008.294 · Cited by 134
Li, Z., Liu, G., Sun, L., Teng, Y., Guo, X., Jia, J., Sha, J., Yang, X. Y., Chen, D., & Sun, Q. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004783 · Cited by 133
Involvement of the ubiquitin‐like domain of TBK1/IKK‐i kinases in regulation of IFN‐inducible genes
Ikeda, F., Hecker, C., Rozenknop, A., Nordmeier, R. D., Rogov, V. V., Hofmann, K., Akira, S., Dötsch, V., & Đikić, I. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601773 · Cited by 127
MDA5 and LGP2: Accomplices and Antagonists of Antiviral Signal Transduction
Rodriguez, K. R., Bruns, A. M., & Horvath, C. M. (2014) · Journal of Virology · doi:10.1128/jvi.00640-14 · Cited by 121
Regulation of T-cell activation and migration by the kinase TBK1 during neuroinflammation
Yu, J., Zhou, X., Chang, M., Nakaya, M., Chang, J.-H., Xiao, Y., William Lindsey, J., Dorta-Estremera, S., Cao, W., Zal, A., et al. (2015) · Nature Communications · doi:10.1038/ncomms7074 · Cited by 118
Unterstab, G., Ludwig, S., Anton, A., Planz, O., Dauber, B., Krappmann, D., Heins, G., Ehrhardt, C., & Wolff, T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502883102 · Cited by 114
TBK1 Is a Synthetic Lethal Target in Cancer with VHL Loss
Hu, L., Xie, H., Liu, X., Potjewyd, F., James, L. I., Wilkerson, E., Herring, L. E., Xie, L., Chen, X., Cabrera, J. C., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0837 · Cited by 110
Self-citationTBKBP1 and TBK1 form a growth factor signalling axis mediating immunosuppression and tumourigenesis
Zhu, L., Li, Y., Xie, X., Zhou, X., Gu, M., Jie, Z., Ko, C.-J., Gao, T., Hernandez, B. E., Cheng, X., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0429-8 · Cited by 109
Alff, P. J., Sen, N., Gorbunova, E. E., Gavrilovskaya, I. N., & Mackow, E. R. (2008) · Journal of Virology · doi:10.1128/jvi.00290-08 · Cited by 104
Hasan, M., Gonugunta, V. K., Dobbs, N., Ali, A., Palchik, G. A., Calvaruso, M. A., DeBerardinis, R. J., & Yan, N. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611113114 · Cited by 102
Korherr, C., Gille, H., Schäfer, R., Koenig‐Hoffmann, K., Dixelius, J., Egland, K. A., Pastan, I. H., & Brinkmann, U. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511319103 · Cited by 99
Mørk, N., Kofod‐Olsen, E., Sørensen, K. B., Bach, E., Orntoft, T. F., Østergaard, L. J., Paludan, S. R., Christiansen, M., & Mogensen, T. H. (2015) · Genes and Immunity · doi:10.1038/gene.2015.46 · Cited by 98
Lu, L. L., Puri, M., Horvath, C. M., & Sen, G. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710089200 · Cited by 96
Long term neurological outcome of herpes encephalitis
Lahat, E., Barr, J., Barkai, G., Paret, G., Brand, N., & Barzilai, A. (1999) · Archives of Disease in Childhood · doi:10.1136/adc.80.1.69 · Cited by 92
Qu, F., Gao, H., Zhu, S., Shi, P., Zhang, Y., Liu, Y., Jallal, B., Yao, Y., Shi, Y., & Qian, Y. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00268-12 · Cited by 90
Kachaner, D., Filipe, J. C.-R., Laplantine, E., Bauch, A., Bennett, K. L., Superti‐Furga, G., Israël, A., & Weil, R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.030 · Cited by 89
Optineurin Insufficiency Impairs IRF3 but Not NF-κB Activation in Immune Cells
Munitić, I., Torchia, M. L. G., Meena, N. P., Zhu, G., Li, C. C., & Ashwell, J. D. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301696 · Cited by 87
Gatot, J., Gioia, R., Chau, T., Patrascu, F., Warnier, M., Close, P., Chapelle, J.-P., Muraille, É., Brown, K., Siebenlist, U. K., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701690200 · Cited by 84
The Golgi apparatus acts as a platform for TBK1 activation after viral RNA sensing
Pourcelot, M., Zemirli, N., da Costa, L. S., Loyant, R., Garcin, D., Vitour, D., Munitić, I., Vázquez, A., & Arnoult, D. (2016) · BMC Biology · doi:10.1186/s12915-016-0292-z · Cited by 79
Cutting Edge: Inhibiting TBK1 by Compound II Ameliorates Autoimmune Disease in Mice
Hasan, M., Dobbs, N., Khan, S., White, M. A., Wakeland, E. K., Li, Q., & Yan, N. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500162 · Cited by 76
Xiang, W., Zhang, Q., Lin, X., Wu, S., Zhou, Y., Meng, F., Fan, Y., Shen, T., Xiao, M., Xia, Z., et al. (2016) · Science Advances · doi:10.1126/sciadv.1501889 · Cited by 75
Self-citationConfirmation of TBK1 duplication in normal tension glaucoma
Kawase, K., Allingham, R. R., Meguro, A., Mizuki, N., Roos, B. R., Solivan-Timpe, F., Robin, A. L., Ritch, R. H., & Fingert, J. H. (2012) · Experimental Eye Research · doi:10.1016/j.exer.2011.12.021 · Cited by 74
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
The role of TBK1 and IKKϵ in the expression and activation of Pellino 1
Smith, H., Liu, X., Dai, L. X., Goh, E. T. H., Chan, A. T., Xi, J., Seh, C. C., Qureshi, I. A., Lescar, J., Ruedl, C., et al. (2011) · Biochemical Journal · doi:10.1042/bj20101421 · Cited by 63
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
Zhang, L., Zhao, X., Zhang, M., Zhao, W., & Gao, C. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302634 · Cited by 62
Ritter, J., Zhu, Z., Thai, T. C., Mahadevan, N. R., Mertins, P., Knelson, E. H., Piel, B. P., Han, S., Jaffe, J. D., Carr, S. A., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1310 · Cited by 60
Elevated expression of TANK-binding kinase 1 enhances tamoxifen resistance in breast cancer
Wei, C., Cao, Y., Yang, X., Zheng, Z., Guan, K., Wang, Q., Tai, Y., Zhang, Y., Ma, S., Cao, Y., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316255111 · Cited by 58
Hammaker, D. R., Boyle, D. L., & Firestein, G. S. (2011) · Lara D. Veeken · doi:10.1093/rheumatology/ker154 · Cited by 54
Muñoz, M. C., Giani, J. F., Mayer, M. A., Toblli, J. E., Turyn, D., & Dominici, F. P. (2009) · Journal of Endocrinology · doi:10.1677/joe-08-0276 · Cited by 52
E3 ubiquitin ligases, the powerful modulator of innate antiviral immunity
Zheng, Y., & Gao, C. (2019) · Cellular Immunology · doi:10.1016/j.cellimm.2019.04.003 · Cited by 50
Discovery of azabenzimidazole derivatives as potent, selective inhibitors of TBK1/IKKε kinases
Wang, T., Block, M. A., Cowen, S. D., Davies, A. M., Devereaux, E., Gingipalli, L., Johannes, J. W., Larsen, N., Su, Q., Tucker, J. A., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.01.018 · Cited by 45
Liu, S., Chen, S., Li, X., Wu, S., Zhang, Q., Jin, Q., Hu, L. T., Zhou, R., Yu, Z., Meng, F., et al. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.05.010 · Cited by 45
Self-citationMIP-T3 Is a Negative Regulator of Innate Type I IFN Response
Ng, M.-H. J., Ho, T., Kok, K., Siu, K., Li, J., & Jin, D. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100719 · Cited by 44
Selective TBK1/IKKi dual inhibitors with anticancer potency
Li, J., Huang, J., Jeong, J.-H., Park, S.-J., Wei, R., Peng, J., Luo, Z., Chen, Y., Feng, Y., & Luo, J. (2013) · International Journal of Cancer · doi:10.1002/ijc.28507 · Cited by 42
Loss of Tbk1 kinase activity protects mice from diet-induced metabolic dysfunction
Cruz, V. H., Arner, E. N., Wynne, K. W., Scherer, P. E., & Brekken, R. A. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.06.007 · Cited by 40
Saul, V. V., Niedenthal, R. K., Pich, A., Weber, F., & Schmitz, M. L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.10.008 · Cited by 39
Nakhaei, P., Sun, Q., Solis, M., Mésplède, T., Bonneil, É., Paz, S., Lin, R., & Hiscott, J. B. (2011) · Journal of Virology · doi:10.1128/jvi.05989-11 · Cited by 32
Spontaneous activation of RNA-sensing pathways in autoimmune disease
Crampton, S. P., & Bolland, S. M. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.09.011 · Cited by 24
Li, S., Wang, L., Berman, M. A., Kong, Y., & Dorf, M. E. (2011) · Immunity · doi:10.1016/j.immuni.2011.10.002 · Cited by 12
Cellular and In Vivo Properties of MPI‐0485520, a Novel and Potent Small Molecule Inhibitor of IKKe
Richards, B. T., Cronin, M., Seager, N., Niederjohn, J., Baichwal, V. R., Chan, A., Robinson, R., Hess, M. W., Davis, T., Papac, D. I., et al. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.753.6 · Cited by 6
Cited by
Sorted by citations
Pattern recognition receptors in health and diseases
Li, D., & Wu, M. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00687-0 · Cited by 1,961
Toll-like receptor 3 (TLR3) regulation mechanisms and roles in antiviral innate immune responses
Chen, Y., Lin, J., Zhao, Y., Ma, X., & Yi, H. (2021) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2000808 · Cited by 260
SARS-CoV-2 Infects Human Engineered Heart Tissues and Models COVID-19 Myocarditis
Bailey, A. L., Dmytrenko, O., Greenberg, L., Bredemeyer, A. L., Ma, P., Liu, J., Penna, V., Winkler, E. S., Sviben, S., Brooks, E., et al. (2021) · JACC: Basic to Translational Science · doi:10.1016/j.jacbts.2021.01.002 · Cited by 193
Targeting TBK1 to overcome resistance to cancer immunotherapy
Sun, Y., Revach, O.-Y., Anderson, S., Kessler, E. A., Wolfe, C. H., Jenney, A., Mills, C. E., Robitschek, E. J., Davis, T. G. R., Kim, S., et al. (2023) · Nature · doi:10.1038/s41586-023-05704-6 · Cited by 174
Meng, F., Yu, Z., Zhang, D., Chen, S., Guan, H., Zhou, R., Wu, Q., Zhang, Q. Y., Liu, S., Ramani, M. K. V., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.040 · Cited by 130
Self-citation
Metadata
- Authors
- Zhou, R., Zhang, Q., & Xu, P.
- Affiliations
- Zhejiang University (CN)
- First Affiliated Hospital Zhejiang University (CN)
- Venue
- Acta Biochimica et Biophysica Sinica
- Published
- 2020-05-01
- Volume
- 52
- Issue
- 7
- Pages
- 757-767
- ISSN
- 1672-9145 (ISSN-L)
- OpenAlex
- W3032346199
- Cited by
- 104
- References
- 155
- Citations by year
- 2026: 21 · 2025: 9 · 2024: 28 · 2023: 18 · 2022: 11 · 2021: 15 · 2020: 2
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
- Locations
- Acta Biochimica et Biophysica Sinica (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Initiative Postdocs Supporting Program
- National Natural Science Foundation of China (81902915, 31830052)
- National Natural Science Foundation of China Distinguished Young Scholars Program (31725017)
- 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
- TBK1, innate immunity, nucleic acid sensing, pattern recognition receptors, RIG-I-like receptors, STING, MAVS, TRIF, type I interferon, inflammatory cytokines, interferon-stimulated genes, kinase activation, kinase substrates, antiviral signaling
- MeSH terms
- Animals, Humans, Nucleic Acids, Transcription, Genetic, Signal Transduction, Interferon-alpha, Interferon-beta, Protein Serine-Threonine Kinases, Receptors, Pattern Recognition
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