The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon

Toll-like receptor signalling

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

The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses

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

De-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

Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain

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

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

PLA1A Participates in the Antiviral Innate Immune Response by Facilitating the Recruitment of TANK-Binding Kinase 1 to Mitochondria

Gao, X., Chen, D., Hu, X., Zhou, Y., Wang, Y., Wu, C., Chen, J., Wang, Y., Pei, R., & Chen, X. (2018) · Journal of Innate Immunity · doi:10.1159/000489832 · Cited by 19

Therapeutic targeting of TANK-binding kinase signaling towards anticancer drug development: Challenges and opportunities

Alam, M., Ansari, M. M., Noor, S., Mohammad, T., Hasan, G. M., Kazim, S. N., & Hassan, M. I. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.03.157 · Cited by 21

Oligomerization of the Nrdp1 E3 Ubiquitin Ligase Is Necessary for Efficient Autoubiquitination but Not ErbB3 Ubiquitination

Printsev, I., Yen, L., Sweeney, C. A., & Carraway, K. L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.527036 · Cited by 19

LSM14A inhibits porcine reproductive and respiratory syndrome virus (PRRSV) replication by activating IFN-β signaling pathway in Marc-145

Li, Z., Chen, R., Zhao, J., Qi, Z., Ji, L., Zhen, Y., & Liu, B. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2251-8 · Cited by 19

Posttranslational Modification Control of Inflammatory Signaling

Si, Y., Zhang, Y., Chen, Z., Zhou, R., Zhang, Y., Hao, D., & Yan, D. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-5987-2_2 · Cited by 18

Inherent Beta Cell Dysfunction Contributes to Autoimmune Susceptibility

Kim, Y. K., Sussel, L., & Davidson, H. W. (2021) · Biomolecules · doi:10.3390/biom11040512 · Cited by 18

Viruses utilize ubiquitination systems to escape TLR/RLR-mediated innate immunity

Huang, S., Cheng, A., Wang, M., Yin, Z., Huang, J., & Jia, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1065211 · Cited by 20

The coronavirus nsp15 endoribonuclease: A puzzling protein and pertinent antiviral drug target

Loy, B. V., Stevaert, A., & Naesens, L. M. J. (2024) · Antiviral Research · doi:10.1016/j.antiviral.2024.105921 · Cited by 18

The ER structural protein Rtn4A stabilizes and enhances signaling through the receptor tyrosine kinase ErbB3

Hatakeyama, J., Wald, J. H., Rafidi, H., Cuevas-Navarro, A., Sweeney, C. A., & Carraway, K. L. (2016) · Science Signaling · doi:10.1126/scisignal.aaf1604 · Cited by 18

Negative Regulation of the Innate Immune Response through Proteasomal Degradation and Deubiquitination

Budroni, V., & Versteeg, G. A. (2021) · Viruses · doi:10.3390/v13040584 · Cited by 21

Regulation of cellular innate antiviral signaling by ubiquitin modification

Lin, D., & Zhong, B. (2015) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmu133 · Cited by 18

Highlights of the advances in basic immunology in 2011

Liu, J., Liu, S., & Cao, X. (2012) · Cellular and Molecular Immunology · doi:10.1038/cmi.2012.12 · Cited by 18

Protein Tyrosine Phosphatase with Proline-Glutamine-Serine-Threonine–Rich Motifs Negatively Regulates TLR-Triggered Innate Responses by Selectively Inhibiting IκB Kinase β/NF-κB Activation

Zhang, P., Liu, X., Li, Y., Zhu, X., Zhan, Z., Meng, J., Li, N., & Cao, X. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202384 · Cited by 17

The Us2 Gene Product of Herpes Simplex Virus 2 modulates NF-κB activation by targeting TAK1

Lu, X., Huang, C., Zhang, Y., Lin, Y., Wang, X., Li, Q., Liu, S., Tang, J., & Zhou, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-08856-4 · Cited by 17

Nrdp1 Increases Ischemia Induced Primary Rat Cerebral Cortical Neurons and Pheochromocytoma Cells Apoptosis Via Downregulation of HIF-1α Protein

Zhang, Y., Yang, K., Wang, T., Li, W., Jin, X., & Liu, W. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00293 · Cited by 17

MiR-146a Promotes Tolerogenic Properties of Dendritic Cells and through Targeting Notch1 Signaling

Tang, H., Lai, Y., Zheng, J., Chen, K., Jiang, H., & Xu, G. (2020) · Immunological Investigations · doi:10.1080/08820139.2019.1708385 · Cited by 17

Major yolk protein and HSC70 are essential for the activation of the TLR pathway via interacting with MyD88 in Apostichopus japonicus

Lv, Z., Li, C., Guo, M. Z., Shao, Y., Zhang, W., & Zhao, X. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.02.019 · Cited by 17

Toll-Like Receptors, Associated Biochemical Signaling Networks, and S100 Ligands

Gupta, S., Tsoporis, J. N., Jia, S., dos Santos, C. C., Parker, T. G., & Marshall, J. C. (2020) · Shock · doi:10.1097/shk.0000000000001704 · Cited by 16

Zebrafish MARCH7 negatively regulates IFN antiviral response by degrading TBK1

Xiong, S.-T., Ying, Y.-R., Long, Z., Li, J., Zhang, Y.-B., Xiao, T., & Zhao, X. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.124384 · Cited by 16

Lumpy skin disease virus ORF127 protein suppresses type I interferon responses by inhibiting K63‐linked ubiquitination of tank binding kinase 1

Liang, Z., Wang, S., Yao, K., Ren, S., Cheng, P., Qu, M., Ma, X., Gao, X., Yin, X., Wang, X., et al. (2024) · The FASEB Journal · doi:10.1096/fj.202301987rr · Cited by 15

OTUD5 promotes the inflammatory immune response by enhancing MyD88 oligomerization and Myddosome formation

Liu, Y., Yuan, J., Zhang, Y., Qin, F., Bai, X., Sun, W., Chen, T., Liu, F., Zheng, Y., Qi, X., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01293-7 · Cited by 17

Toll-Like Receptor-2 Ligand Peptidoglycan Upregulates Expression and Ubiquitin Ligase Activity of CHIP through JNK Pathway

Meng, Y., Chen, C., Wang, L., Wang, X., Tian, C., Du, J., & Li, H. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000354509 · Cited by 16

Early innate immune response triggered by the human respiratory syncytial virus and its regulation by ubiquitination/deubiquitination processes

Martin‐Vicente, M., Resino, S., & Martínez, I. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-022-00793-3 · Cited by 18

Molecular characterization, expression patterns, and functional analysis of toll-interacting protein (Tollip) in Japanese eel Anguilla japonica

Feng, J., Lin, P., Wang, Y., & Zhang, Z. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.04.053 · Cited by 16

USP7 Promotes deubiquitination and stabilization of MyD88 to enhance immune responses

Zhang, N., Wang, F., Zhang, G., Zhang, Q., Liu, Y., Wang, Q., Elsharkawy, M. S., Zheng, M., Wen, J., Zhao, G., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.900243 · Cited by 15

TLR4 agonist activity of Alcaligenes lipid a utilizes MyD88 and TRIF signaling pathways for efficient antigen presentation and T cell differentiation by dendritic cells

Sun, X., Hosomi, K., Shimoyama, A., Yoshii, K., Lan, H., Wang, Y., Yamaura, H., Nagatake, T., Ishii, K. J., Akira, S., et al. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.109852 · Cited by 15

THO Complex Subunit 7 Homolog Negatively Regulates Cellular Antiviral Response against RNA Viruses by Targeting TBK1

He, T., Xie, T., Li, J., Yang, Y., Li, C., Wang, W., Cao, L., Rao, H., Ju, C., & Xu, L. (2019) · Viruses · doi:10.3390/v11020158 · Cited by 15

TRIM28 facilitates type I interferon activation by targeting TBK1

Hua, F., Nass, T., & Parvatiyar, K. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1279920 · Cited by 16

Molecular mechanisms involved in pathogenicity of SARS-CoV-2: Immune evasion and implications for therapeutic strategies

Latifi-Pupovci, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113368 · Cited by 16

Bcl6 Sets a Threshold for Antiviral Signaling by Restraining IRF7 Transcriptional Program

Xu, F., Kang, Y., Zhuang, N., Lü, Z., Zhang, H., Xu, D., Ding, Y., Yin, H., & Shi, L. (2016) · Scientific Reports · doi:10.1038/srep18778 · Cited by 14

miR-29b directly targets activation-induced cytidine deaminase in human B cells and can limit its inappropriate expression in naïve B cells

Recaldin, T., Hobson, P. S., Mann, E. H., Ramadani, F., Cousins, D. J., Lavender, P., & Fear, D. J. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.07.028 · Cited by 14

Non-coding RNAs and Exosomal Non-coding RNAs in Traumatic Brain Injury: the Small Player with Big Actions

Mohamadzadeh, O., Hajinouri, M., Moammer, F., Zadeh, S. S. T., Shafiei, G. O., Jafari, A., Ostadian, A., Talaei, S. A., Hamblin, M. R., Yazdi, A. J., et al. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03321-y · Cited by 12

Lower expression of N rdp1 in human glioma contributes tumor progression by reducing apoptosis

Shi, H., Du, J. T., Wang, L., Zheng, B., Gong, H., Wu, Y., Tang, Y., Gao, Y., & Yu, R. (2014) · IUBMB Life · doi:10.1002/iub.1320 · Cited by 12

VEGF-induced Nrdp1 deficiency in vascular endothelial cells promotes cancer metastasis by degrading vascular basement membrane

Li, Q.-Q., Guo, M., He, G.-H., Xi, K.-H., Zhou, M., Shi, R., & Chen, G. (2024) · Oncogene · doi:10.1038/s41388-024-03038-9 · Cited by 12

Proteomic Survey of Ubiquitin-Linked Nuclear Proteins in Interferon-Stimulated Macrophages

Kim, J. Y., Anderson, D. E., Huynh, W., Dey, A., & Ozato, K. (2011) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2011.0006 · Cited by 12

High-Confidence Interactome for RNF41 Built on Multiple Orthogonal Assays

Masschaele, D., Wauman, J., Vandemoortele, G., Sutter, D. D., Ceuninck, L. D., Eyckerman, S., & Tavernier, J. H. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00704 · Cited by 11

Ctenopharyngodon idella Tollip regulates MyD88-induced NF-κB activation

Wu, C., Deng, H., Li, D., Fan, L., Dong, Y., Zhi, X., Mao, H., & Hu, C. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104162 · Cited by 11

The role of mesenchymal stem cells in attenuating inflammatory bowel disease through ubiquitination

Liao, H. X., Mao, X., Wang, L., Wang, N., Ocansey, D. K. W., Wang, B., & Mao, F. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1423069 · Cited by 10

TRAF6 integrates innate immune signals to regulate glucose homeostasis via Parkin-dependent and Parkin-independent mitophagy

Levi-D’Ancona, E., Walker, E. M., Zhu, J., Deng, Y., Sidarala, V., Stendahl, A. M., Reck, E. C., Henry-Kanarek, B. A., Lietzke, A. C., Chai, B., et al. (2025) · Science Advances · doi:10.1126/sciadv.adw4153 · Cited by 10

Gene Expression Dysregulation in Whole Blood of Patients with Clostridioides difficile Infection

Tsakiroglou, M., Evans, A., Carracedo, A. D., Little, M., Hornby, R., Roberts, P., Zhang, E., Miyajima, F., & Pirmohamed, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312653 · Cited by 9

Dynamic regulation of TBK1 lactylation shapes antiviral immune responses

Xie, Y., Zhang, Y., Peng, W., Zhang, L., Hu, Z., Jiang, H., Zeng, K. W., Lu, J., Tan, S., Han, Z., et al. (2026) · Cellular and Molecular Immunology · doi:10.1038/s41423-025-01385-5 · Cited by 9

Zebrafish CERKL Enhances Host TBK1 Stability and Simultaneously Degrades Viral Protein via Ubiquitination Modulation

Chen, D., Lu, L.-F., Xiong, F., Wang, X., Jiang, J., Zhang, C., Li, Z.-C., Han, K.-J., & Li, S. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2101007 · Cited by 9

High doses of recombinant mannan‐binding lectin inhibit the binding of influenza A(H1N1)pdm09 virus with cells expressing DC‐SIGN

Yu, L., Shang, S., Tao, R., Wang, C., Zhang, L., Peng, H., & Chen, Y. (2017) · Apmis · doi:10.1111/apm.12695 · Cited by 9

IRG1 catalyzed energy metabolite itaconic acid restrains type I interferon-dependent immune responses by alkylation of TBK1

Chai, L., Li, C., Wang, X., Qin, Y., Sun, H., Du, J., Liu, Y., Hu, D., Xiong, J., Zhao, Z., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116336 · 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

RNF19a inhibits antiviral immune response to RNA viruses through degradation of TBK1

Yang, Y., Cao, X., Huang, L., & Yang, A. (2022) · Molecular Immunology · doi:10.1016/j.molimm.2021.12.021 · Cited by 8

Nrdp1 governs differentiation of the melanocyte lineage via Erbb3b signaling in the zebrafish embryogenesis

Maddirevula, S., Anuppalle, M., Huh, T., Kim, S. H., & Rhee, M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.05.025 · Cited by 8

Ubiquitin Ligase Nrdp1 Controls Autophagy-Associated Acrosome Biogenesis and Mitochondrial Arrangement during Spermiogenesis

Luo, Z.-Y., Jiang, T.-X., Zhang, T., Xu, P., & Qiu, X. (2023) · Cells · doi:10.3390/cells12182211 · Cited by 7

MARCH1 negatively regulates TBK1-mTOR signaling pathway by ubiquitinating TBK1

Li, X., Cheng, K., Shang, M.-D., Yang, Y., Hu, B., Wang, X., Wei, X.-D., Han, Y., Zhang, X., Dong, M.-H., et al. (2024) · BMC Cancer · doi:10.1186/s12885-024-12667-y · Cited by 7

Reduced expression of Nrdp1 predicts a poor prognosis in human hepatocellular carcinoma

Shao, X., Lu, Q., Wang, G., Huang, W., Yang, L., & Chen, Z. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s160638 · Cited by 7

miRNAs in SARS-CoV-2 Infection: An Update

Azhar, A., Khan, W. H., Alhosaini, K. A., & Kamal, M. A. (2022) · Current Drug Metabolism · doi:10.2174/1389200223666220321102824 · Cited by 7

Ubiquitin‑specific protease 8 ameliorates lipopolysaccharide‑induced spleen injury via suppression of NF‑κB and MAPK signaling pathways

Bi, W., Zhang, J., Zeng, Z., Zhou, R., Zhao, J., Yan, W., Wang, L., Li, X., & Zhu, L. (2022) · Molecular Medicine Reports · doi:10.3892/mmr.2022.12887 · Cited by 7

Reduced RING finger protein 10 expression in macrophages is associated with aging‐related inflammation

Cao, X., Liu, L., Zhang, Y., & Yang, Y. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.13049 · Cited by 6

The Ca 2+ -dependent phosphatase calcineurin dephosphorylates TBK1 to suppress antiviral innate immunity

Qu, Y., Wang, S., Jiang, H., Wang, Q., Liao, Y., Qiu, X., Tan, L., Song, C., Ding, C., Sun, Y., et al. (2024) · Journal of Virology · doi:10.1128/jvi.00016-24 · Cited by 6

A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C stability promotes prostate cancer metastasis by inducing actin remodeling

Xu, S., Xiong, S., Li, Z., Li, Z., Song, Y., Dong, Q., Yang, L., Xiong, Y., Zhan, X., Yang, H., et al. (2024) · Oncogene · doi:10.1038/s41388-024-03120-2 · Cited by 7

Decreased RNF41 expression leads to insulin resistance in skeletal muscle of obese women

Breuker, C., Amouzou, C., Fabre, O., Lambert, K., Seyer, P., Bourret, A., Salehzada, T., Mercier, J. G., Sultan, A., & Bisbal, C. (2018) · Metabolism · doi:10.1016/j.metabol.2018.01.014 · 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

Mind Bomb Proteins in the Antiviral Arsenal

Kumagai, Y., & Akira, S. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.003 · Cited by 5

Inducible downregulation of miR-93 feedback promotes innate responses against RNA virus by amplifying interferon signaling.

Zhao, Y., Liu, F., Dong, J., Fu, H. Y., Luo, J., Ji, J., Gao, X., & Guo, W. (2022) · PubMed · Cited by 5

Cyclin-dependent kinase 5 negatively regulates antiviral immune response by disrupting myeloid differentiation primary response protein 88 self-association

Ren, J.-P., Cong, H., Gao, L., Jiang, D., Li, X.-T., Wang, Y., Wang, J., & Tang, T.-S. (2023) · Virulence · doi:10.1080/21505594.2023.2223394 · Cited by 5

Role of RP105 and A20 in negative regulation of toll-like receptor activity in fibrosis: potential targets for therapeutic intervention

Bale, S., Varga, J., & Bhattacharyya, S. (2021) · AIMS Allergy and Immunology · doi:10.3934/allergy.2021009 · Cited by 5

Structural modeling of protein ensembles between E3 RING ligases and SARS-CoV-2: The role of zinc binding domains

Chasapis, C. T., Perlepes, S. P., Bjørklund, G., & Peana, M. (2022) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2022.127089 · Cited by 5

Overexpression of Nrdp1/FLRF sensitizes cells to oxidative stress

Zhou, A., Pan, D., Yang, X., & Zhou, J. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.06.052 · Cited by 5

Human DUBs’ gene expression and regulation in antiviral signaling in response to poly (I:C) treatment

Liu, K., Qiu, D., Liang, X., Huang, Y., Zhao, J., Qiu, X., Zhang, Q., Xiao, Z., & Qin, Y. (2020) · Molecular Immunology · doi:10.1016/j.molimm.2020.11.006 · Cited by 4

Association between RNF41 gene c.-206 T > A genetic polymorphism and risk of congenital heart diseases in the Chinese Mongolian population

Zhang, Y., Jin, S. Q., Li, W. X., Gao, G. Q., Zhang, K., & Huang, J. (2016) · Genetics and Molecular Research · doi:10.4238/gmr.15028089 · Cited by 4

Deficiency of a novel lncRNA-HRAT protects against myocardial ischemia reperfusion injury by targeting miR-370-3p/RNF41 pathway

Zheng, X., Zhong, T., Fan, Y., Duan, J., Tang, Y., Liu, Y., Li, M., Sun, D., & Yin, D. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.951463 · Cited by 4

Somatic USP8 alteration affects the immune landscape of corticotroph pituitary adenomas– a pilot study

Greidinger, D., Halperin, R., Zemet, R., Maixner, N., & Tirosh, A. (2024) · HORMONES · doi:10.1007/s42000-024-00569-4 · Cited by 4

Loss of RNF41 promotes bladder cancer metastasis through increasing NUDC stability to enhance tubulin polymerization

Zheng, F., Li, S., Xiong, S., Li, Z., Yuan, R., Wang, Z., Wan, H., Liu, J., Dong, Q., Liu, X., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07758-y · Cited by 3

The Roles of E3 Ubiquitin Ligases in Cerebral Ischemia–Reperfusion Injury

Li, M., Yu, X., Liu, Q., Fang, Z. H., & Wang, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146723 · Cited by 3

Association of SPOP Expression with the Immune Response to Salmonella Infection in Chickens

Wang, F., Li, Q., Wang, Q., Zheng, M., Wen, J., & Zhao, G. (2020) · Animals · doi:10.3390/ani10020307 · Cited by 3

USP46 promotes the interferon antiviral signaling in black carp by deubiquitinating TBK1

Shu, J., Yang, C., Miao, Y., Li, J., Zheng, T., Xiao, J., Kong, W., Xu, Z. C., & Feng, H. (2024) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2024.105170 · Cited by 3

Nrdp1-mediated degradation of BRUCE decreases cell viability and induces apoptosis in human 786-O renal cell carcinoma cells

Shao-jun, C., Jian-hai, L., Yao, X., Peng, B., Xu, Y., Liu, M., & Zheng, J. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3356 · Cited by 3

Transcriptional Effects of E3 Ligase Nrdp1 on Hypertrophy in Neonatal Rat Cardiomyocytes by Microarray and Integrated Gene Network Analysis

Zhang, Y., Su, L., & Zhang, K. (2016) · Cardiology · doi:10.1159/000447235 · Cited by 3

CgNrdp1, a conserved negative regulating factor of MyD88-dependent Toll like receptor signaling in oyster Crassostrea gigas

Sun, R., Qiu, L., Yi, Q., Wang, M., Yue, F., Wang, L., & Song, L. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.12.057 · Cited by 3

Ubiquitination: A Double‐Edged Mechanism in Coronavirus Infections

Liu, S., Shao, C., Ding, Y., Wang, Y., Jin, L., Tan, D., Li, S., Deng, X., Zhou, Y., & Xia, Z. (2025) · Journal of Medical Virology · doi:10.1002/jmv.70589 · Cited by 2

RSK1 reprograms the ubiquitin pathway to promote immune suppression

Peng, Q., Chen, Y., Zhao, J., Zhu, J., Zhuo, H., Zheng, Y., Weng, L., He, R., Tian, E., Zhang, Y., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116323 · Cited by 2

LSM14A inhibits porcine reproductive and respiratory syndrome virus (PRRSV) replication by activating IFN-b signaling pathway in Marc-145

LiRui, Z., & Liu, Z. (2015) · Cited by 2

Prediction of Ubiquitin Ligase Nrdp1-Associated Proteins in Glioma Database

Liu, Y. U., Jin, M., Gao, Y., Wang, Y., Xue, S., Wang, L., & Xuan, C. (2020) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-020-00926-1 · Cited by 2

TANK-Binding Kinase 1 (TBK1): Structure, Function, and Regulation

Marion, J. D. (2018) · Springer eBooks · doi:10.1007/978-1-4614-1531-2_374 · Cited by 1

Mild Hypothermia Protects Brain Injury After Intracerebral Hemorrhage in Mice Via Enhancing the Nrdp1/MyD88 Signaling Pathway

Zhou, C., Wang, J., Shao, G., Xia, X., Wu, L., Yu, A., & Yang, Z. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00576-6 · Cited by 1

Hypermethylation of Ring finger protein 41 promoter is associated with early hepatitis B virus-related cirrhosis

Zhu, H., Zhang, F., Tian, Z., Xu, M., Fan, Y., Gao, S., & Wang, K. (2025) · Frontiers in Medicine · doi:10.3389/fmed.2025.1631990 · Cited by 1

Fish CDK2 recruits Dtx4 to degrade TBK1 through ubiquitination in the antiviral response

Lu, L.-F., Zhang, C., Li, Z.-C., Cui, B.-J., Wang, Y.-Y., Han, K.-J., Xu, X., Zhou, C.-J., Zhou, X.-Y., Wu, Y., et al. (2026) · eLife · doi:10.7554/elife.98357.4 · Cited by 1

TANK-Binding Kinase 1 (TBK1): Structure, Function, and Regulation

Marion, J. D. (2014) · Springer eBooks · doi:10.1007/978-1-4614-6436-5_374-1 · Cited by 1

[Research progress on the role of TANK-binding kinase 1 in anti-virus innate immune response].

Wang, X., Zhang, Y., & Chen, W. (2016) · PubMed Central · doi:10.3785/j.issn.1008-9292.2016.09.16 · Cited by 1

Characterization of Anti-Fungal Inflammasome Responses and the Role of Caspase-8 in Innate Immune Signaling: A Dissertation

Ganesan, S. (2014) · eScholarship@UMassChan · doi:10.13028/m28c8f · Cited by 1

Fish CDK2 recruits Dtx4 to degrade TBK1 through ubiquitination in the antiviral responsePreprint

Lu, L.-F., Zhang, C., Li, Z.-C., Cui, B.-J., Wang, Y., Han, K.-J., Xu, X., Zhou, C.-J., Zhou, X.-Y., Wu, Y., et al. (2024) · eLife · doi:10.7554/elife.98357 · Cited by 1

Exploring the molecular basis to the regulatory effects of Cannabinoids on toll-like receptor signalling

Clifford, E. (2010) · Maynooth University ePrints and eTheses Archive (Maynooth University)

Interactions between Neuronal Innate Immune Pattern Recognition Receptor Pathways and Neurotropic Arboviruses: Host Measures, Viral Countermeasures, and Potential Therapeutics.

Peltier, D. (2010) · Deep Blue (University of Michigan)

Ubiquitin Dependent Regulation of Innate Antiviral Signaling

Parvatiyar, M. S. (2010)

The Negative Regulation of the Antiviral Signaling Pathway

Charoenthongtrakul, S. (2013)

A hiperglicemia altera o perfil inflamatório e imunometabólico de macrófagos derivados de medula óssea de camundongos

Ayala, T. S. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.9.2019.tde-07052019-143006 · Cited by 1

Regulation of intracellular traffic by TBK1 and its relevance to ALS

Villarroel‐Campos, D. (2020) · UCL Discovery (University College London)

microRNA在固有免疫受体调控中的作用及相关研究进展

李, 盈., & 张, 悦. (2012) · Scientia Sinica Vitae · doi:10.1360/zc2012-42-12-967

Signaling pathways implicated in SARS-CoV-2 infection

Bhattacharyya, S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-95578-2.00007-8

Epoxyeicosatrienoic acids and sEH inhibition prevent cardiac dysfunction in CVB3-induced myocarditis by positively regulating type I interferon signalingPreprint

Zhou, Z., Zhang, M., Zhao, C., Gao, X., Zheng, W., Wu, J., Chen, C., Hu, J., Fleming, I., & Wang, D. W. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.03.527086

Regulation of Phagocytosis in Macrophages

Poloamina, V. I. (2023) · Physiology · doi:10.5772/intechopen.109847

Role of Neuronal Nrdp1-USP8-Hypoxia Inducible Factor-1 Alpha Signal Axis in Hypoxic Injury after Cerebral Ischemia

Yang, L., Ren, B., & Han, Y. (2024) · Indian Journal of Pharmaceutical Sciences · doi:10.36468/pharmaceutical-sciences.1327

Fish CDK2 recruits Dtx4 to degrade TBK1 through ubiquitination in the antiviral responsePreprint

Lu, L.-F., Zhang, C., Li, Z.-C., Cui, B.-J., Wang, Y., Han, K.-J., Xu, X., Zhou, C.-J., Zhou, X.-Y., Wu, Y., et al. (2024) · eLife · doi:10.7554/elife.98357.1

Reviewer #1 (Public Review): Fish CDK2 recruits Dtx4 to degrade TBK1 through ubiquitination in the antiviral response

(2024) · eLife · doi:10.7554/elife.98357.1.sa1

eLife Assessment: Fish CDK2 recruits Dtx4 to degrade TBK1 through ubiquitination in the antiviral response

Cunha, L. D. (2024) · eLife · doi:10.7554/elife.98357.1.sa2

E3泛素连接酶Nrdpl“优先”促进TLR介导的I型干扰素的产生

曹雪涛 (2010) · 科学中国人

The role of novel E3 ubiquitin ligase in the regulation of TLR3 signaling pathway

Lin, Y.-S., Chang, Y., Lai, T., Lee, C., Chuang, T., & Hsu, L.-C. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.204.supp.226.26

Transforming Growth Factor-β Differentially Inhibits MyD88-dependent, but Not TRAM- and TRIF-dependent, Lipopolysaccharide-induced TLR4 Signaling

Naiki, Y., Michelsen, K. S., Zhang, W., Chen, S., Doherty, T. M., & Arditi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400503200 · Cited by 183

N4BP1 coordinates ubiquitin-dependent crosstalk within the IκB kinase family to limit Toll-like receptor signaling and inflammation

Gitlin, A. D., Maltzman, A., Kanno, Y., Heger, K., Reja, R., Schubert, A. F., Wierciszewski, L. J., Pantua, H., Kapadia, S. B., Harris, S. F., et al. (2024) · Immunity · doi:10.1016/j.immuni.2024.04.004 · Cited by 28

Phosphatase PTP1B negatively regulates MyD88- and TRIF-dependent proinflammatory cytokine and type I interferon production in TLR-triggered macrophages

Xu, H., An, H., Hou, J., Han, C., Wang, P., Yu, Y., & Cao, X. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.05.006 · Cited by 100