Cited by 4,766NF-κB Signaling PathwaysImmune Response and InflammationSignaling Pathways in Disease

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Phosphorylation Meets Ubiquitination: The Control of NF-κB Activity

Karin, Michael, Ben-Neriah, Yinon·2000·Annual Review of Immunology

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Abstract

NF-kappaB (nuclear factor-kappaB) is a collective name for inducible dimeric transcription factors composed of members of the Rel family of DNA-binding proteins that recognize a common sequence motif. NF-kappaB is found in essentially all cell types and is involved in activation of an exceptionally large number of genes in response to infections, inflammation, and other stressful situations requiring rapid reprogramming of gene expression. NF-kappaB is normally sequestered in the cytoplasm of nonstimulated cells and consequently must be translocated into the nucleus to function. The subcellular location of NF-kappaB is controlled by a family of inhibitory proteins, IkappaBs, which bind NF-kappaB and mask its nuclear localization signal, thereby preventing nuclear uptake. Exposure of cells to a variety of extracellular stimuli leads to the rapid phosphorylation, ubiquitination, and ultimately proteolytic degradation of IkappaB, which frees NF-kappaB to translocate to the nucleus where it regulates gene transcription. NF-kappaB activation represents a paradigm for controlling the function of a regulatory protein via ubiquitination-dependent proteolysis, as an integral part of a phosphorylationbased signaling cascade. Recently, considerable progress has been made in understanding the details of the signaling pathways that regulate NF-kappaB activity, particularly those responding to the proinflammatory cytokines tumor necrosis factor-alpha and interleukin-1. The multisubunit Ika…

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“…with LPS, the activations of STATs, AKT, and MAPKs mediate signaling cascades leading to the activations of NF-κB and AP-1 in activated macrophages (Guha and Mackman, 2001; Kaminska, 2005), which also coordinate the inductions of a variety of inflammatory proteins (Karin and Ben-Neriah, 2000).”
Background
Circadian clock component PERIOD2 regulates diurnal expression of Na+/H+ exchanger regulatory factor-1 and its scaffolding function
Tsurudome, Y., Koyanagi, S., Kanemitsu, T., Katamune, C., Oda, M., Kanado, Y., Kato, M. S., Morita, A., Tahara, Y., Matsunaga, N., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-27280-w · Cited by 11
Calpain Inhibition Decreases Inflammatory Protein Expression In Vessel Walls In A Model Of Chronic Myocardial Ischemia
Potz, B. A., Sabe, A. A., Elmadhun, N. Y., Sabe, S. A., Braun, B., Clements, R., Usheva, A., & Sellke, F. (2016) · Surgery · doi:10.1016/j.surg.2016.11.009 · Cited by 10
Doxorubicin-induced nephrotoxicity: the protective role of a standardized ethanolic extract of Andrographis paniculata leaves
Arozal, W., Eziefule, O. M., Wanandi, S. I., Louisa, M., Dewi, S., Nafrialdi, Siregar, N. C., & Makambwa, E. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1585965 · Cited by 9
“These interactions likely stabilize NF-κ B in its active conformation, promoting transcription of pro-in ﬂ ammatory genes (Karin and Ben-Neriah, 2000).”
BSRF1 modulates IFN-β-mediated antiviral responses by inhibiting NF-κB activity via an IKK-dependent mechanism in Epstein-Barr virus infection
Chen, S., Deng, Y., Huang, C., Xie, X., Long, Z., Lao, S., Gao, X., Wang, K., Wang, S., Li, X., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141600 · Cited by 9
SQLE-mediated squalene metabolism promotes tumor immune evasion in pancreatic cancer
Pan, J., Liang, H.-X., Zhou, L., Lu, W., Huo, B.-T., Liu, R., & Huang, P. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1512981 · Cited by 9
Syringin from Tinospora crispa downregulates pro-inflammatory mediator production through MyD88-dependent pathways in lipopolysaccharide (LPS)-induced U937 macrophages
Arshad, L., Haque, M., Harikrishnan, H., Ibrahim, S., & Jantan, I. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09722-z · Cited by 9
Cellular and epigenetic perspective of protein stability and its implications in the biological system
Manav, N., Jit, B. P., Kataria, B., & Sharma, A. K. (2024) · Epigenomics · doi:10.1080/17501911.2024.2351788 · Cited by 9
RETRACTED ARTICLE: Tumour microenvironment programming by an RNA–RNA-binding protein complex creates a druggable vulnerability in IDH-wild-type glioblastoma
Wu, L.-L., Zhao, Z., Shin, Y., Yin, Y.-Y., Raju, A., Vaiyapuri, T., Idzham, K., Son, M., Lee, Y., Sa, J., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01428-5 · Cited by 9
Retracted
RSK3 switches cell fate: from stress-induced senescence to malignant progression
Huna, A., Flaman, J., Lodillinsky, C., Zhu, K., Makulyte, G., Pakulska, V., Couté, Y., Ruisseaux, C., Saintigny, P., Hernández‐Vargas, H., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02909-5 · Cited by 8
“A critical step in the activation of the NF-κB pathway is the degradation of IκBα [45].”
Background
Multilevel Regulation of NF‐κB Signaling by NSD2 Suppresses Kras‐Driven Pancreatic Tumorigenesis
Feng, W.-X., Niu, N.-N., Lu, P., Chen, Z., Rao, H.-Y., Zhang, W., Ma, C., Liu, C., Xu, Y., Gao, W.-Q., et al. (2023) · bioRxiv · doi:10.1002/advs.202309387 · Cited by 9
Tmem178 negatively regulates IL-1β production through inhibition of the NLRP3 inflammasome
Khanna, K., Yan, H., Mehra, M., Rohatgi, N., Mbalaviele, G., Mellins, E., & Faccio, R. (2023) · Arthritis & Rheumatology · doi:10.1002/art.42666 · Cited by 9
“Similar to osteoclasts, 15 we did not detect differences in the phosphorylation and degradation of I κ B-α , a readout for NF-κ B activation, 20 between WT and Tmem178 − / − bone marrow – derived macrophages (BMDMs) stimulated with LPS (Supplementary Figure 1A –”
Background
Transcriptomic profiling of lipopolysaccharide-challenged bovine mammary epithelial cells treated with forsythoside A
Gao, Y., Liu, J., Zhang, H., Zhang, X., Gui, R., Zhang, K.-F., Li, Y., Zhou, M., Tong, C., Huang, S.-C., et al. (2023) · Animal Biotechnology · doi:10.1080/10495398.2023.2165936 · Cited by 9
Molecular cloning and functional characterization of HMGB1 and HMGB2 in large yellow croaker Larimichthys crocea.
Luo, Z., Li, Y., Wang, Y.-L., Zhang, Z.-P., & Zou, P.-F. (2022) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2022.07.018 · Cited by 9
A Newly Synthesized Flavone from Luteolin Escapes from COMT-Catalyzed Methylation and Inhibits Lipopolysaccharide-Induced Inflammation in RAW264.7 Macrophages via JNK, p38 and NF-κB Signaling Pathways
Ye, L., Yang, X., Wu, Z., Sun, H., Huang, D., & Sun, Z.-Q. (2021) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2104.04027 · Cited by 11
“The presence of several stimuli, including LPS, leads to the phosphorylation and degradation of IκBα, followed by p65 phosphorylation and translocation of NF-κB into the nucleus, where NF-κB subsequently binds to corresponding sites and activates the transcription of many pro-inflammatory genes ultimately [72-75].”
Background
Macrophage Migration Inhibitory Factor Alters Functional Properties of CA1 Hippocampal Neurons in Mouse Brain Slices
Bancroft, E. A., Srinivasan, R., & Shapiro, L. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010276 · Cited by 9
Malarial Inflammation-Driven Pathophysiology and Its Attenuation by Triterpene Phytotherapeutics
Mavondo, G. A., Mkhwanazi, B. N., Mzingwane, M. L., Dangarembizi, R., Zambuko, B., Moyo, O., Musiwaro, P., Chikuse, F. F., Rakabopa, C., Mpofu, T., et al. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.88731 · Cited by 10
Exogenous Pancreatic Kallikrein Improves Diabetic Cardiomyopathy in Streptozotocin-Induced Diabetes
Wu, M., Yang, Y.-P., Wang, M., Zeng, F., Li, Q., Liu, W., Guo, S.-Z., He, M., Wang, Y., Huang, J., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00855 · Cited by 9
“The mRNA expression of (B) CD68, (C) MCP-1, (D) TNF-α, and (E) IL-6.”
Influential
IKK s and tumor cell plasticity
Göktuna, S. İ., Diamanti, M. A., & Chau, T. L. (2018) · FEBS Journal · doi:10.1111/febs.14444 · Cited by 12
Regulatory effects and molecular mechanism of Trigonostemon reidioides on lipopolysaccharide-induced inflammatory responses in RAW264.7 cells
Shin, J.-Y., Kang, J.-S., Byun, H.-W., & Ahn, E.-K. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7297 · Cited by 9
“NF-κ B is normally present in the cytoplasm of non-stimulated cells, and nuclear translocation of NF-κ B is required for it to initiate transcription of inflammation-associated target genes (18).”
Enterotoxigenic Escherichia coli Flagellin Inhibits TNF-Induced NF-κB Activation in Intestinal Epithelial Cells
Wang, G., Geisbrecht, B., Rueter, C., & Hardwidge, P. (2017) · Pathogens · doi:10.3390/pathogens6020018 · Cited by 9
“Upon TNF stimulation or microbial infection, the IκB kinase (IKK) complex is activated and phosphorylates IκBα which is then polyubiquitinated and degraded, resulting in nuclear translocation of NF-κB subunits [11].”
Background
In vitro and in vivo inhibitory effects of 6-hydroxyrubiadin on lipopolysaccharide-induced inflammation
Wu, Y.-T., Jin, F., Wang, Y.-L., Li, F., Ren, Z., & Wang, Y.-F. (2017) · Immunopharmacology and immunotoxicology · doi:10.1080/08923973.2017.1295053 · Cited by 9
Proteomics in biomarker discovery: uncovering disease-specific interactome and post-translational modification networks
Palabıyık, A. A., & Palabıyık, E. (2025) · Journal of Proteins and Proteomics · doi:10.1007/s42485-025-00190-y · Cited by 15
The miR‐29‐3p family suppresses inflammatory osteolysis
Shin, B., Hrdlicka, H. C., Karki, S., Fraser, B., Lee, S., & Delany, A. M. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.31299 · Cited by 8
B(a)P induces ovarian granulosa cell apoptosis via TRAF2-NFκB-Caspase1 axis during early pregnancy.
Xu, H., Chen, F.-Y., Liu, Z., Gao, R.-F., He, J.-L., Li, F.-F., Li, N., Mu, X.-Y., Liu, T.-H., Wang, Y.-X., et al. (2024) · Environmental Research · doi:10.1016/j.envres.2024.118865 · Cited by 8
Flavonoid Diversity and Roles in the Lipopolysaccharide-Mediated Inflammatory Response of Monocytes and Macrophages
Rullah, K., Shamsudin, N. F., Koeberle, A., Tham, C. L., Aluwi, M. F. F. M., Leong, S. W., Jantan, I., & Lam, K. W. (2024) · Future Medicinal Chemistry · doi:10.4155/fmc-2023-0174 · Cited by 10
6-Pentyl-α-Pyrone from Trichoderma gamsii Exert Antioxidant and Anti-Inflammatory Properties in Lipopolysaccharide-Stimulated Mouse Macrophages
Lim, J. S., Hong, J.-H., Lee, D. Y., Li, X., Lee, D. E., Choi, J. U., Lee, K. Y., Kim, K. H., & Cho, Y.-C. (2023) · Antioxidants · doi:10.3390/antiox12122028 · Cited by 11
An antibody that targets cell-surface Glucose-regulated Protein-78 inhibits expression of inflammatory cytokines and plasminogen activator inhibitors by macrophages
Gunner, C. B., Azmoon, P., Mantuano, E., Das, L., Zampieri, C., Pizzo, S., & Gonias, S. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30401 · Cited by 8
“IκBα phosphorylation and the accompanying decrease in total IκBα abundance report NFκB activation.(28) To examine IκBα phosphorylation, BMDMs were transferred to SFM for 30min and then treated with TLR agonists in the presence and absence of N88 (1 μg/mL) for 1 h.”
BackgroundMethodInfluential
Mechanism of Jiawei Zhengqi Powder in the Treatment of Ulcerative Colitis Based on Network Pharmacology and Molecular Docking
Zhao, C., Zhi, C., & Zhou, J.-H. (2023) · BioMed Research International · doi:10.1155/2023/8397111 · Cited by 8
EV-Mediated Chemoresistance in the Tumor Microenvironment: Is NF-κB a Player?
Nolfi, M. D. V., Vecchiotti, D., Flati, I., Verzella, D., Padova, M. D., Alesse, E., Capece, D., & Zazzeroni, F. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.933922 · Cited by 7
Cordycepin from Medicinal Fungi Cordyceps militaris Mitigates Inflammaging-Associated Testicular Damage via Regulating NF-κB/MAPKs Signaling in Naturally Aged Rats
Kopalli, S., Cha, K.-M., Cho, J., Kim, S.-K., & Koppula, S. (2022) · Mycobiology · doi:10.1080/12298093.2022.2035515 · Cited by 8
“Phosphorylated IjBa is subsequently ubiquitinated and degraded, leading to release and activation of NF-jB complex [55].”
Background
Identification of Key eRNAs for Spinal Cord Injury by Integrated Multinomial Bioinformatics Analysis
Huang, R., Wang, S., Zhu, R., Xian, S.-Y., Huang, Z., Cheng, L.-M., & Zhang, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.728242 · Cited by 8
MicroRNA‑124‑5p delays the progression of cerebral aneurysm by regulating FoxO1
Wang, R.-K., Sun, Y., Li, G.-Y., Yang, H.-T., Liu, X., Li, K., Zhu, X. C., & Yu, G.-Y. (2021) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2021.10606 · Cited by 10
“NF‐κB is one of the key components to regulate the expression of proinflammatory genes and it induces the expression of proinflammatory cytokines, chemokines and adhesion molecules (35).”
Influence of Liver Cirrhosis on Blood Glucose, Insulin Sensitivity and Islet Function in Mice.
Bai, X.-P., Fan, Y., Zhang, L., Yang, G.-H., & Li, X. (2021) · American Journal of the Medical Sciences · doi:10.1016/j.amjms.2021.07.005 · Cited by 8
Galectin-3 Modulates Microglia Inflammation in vitro but Not Neonatal Brain Injury in vivo under Inflammatory Conditions
Sävman, K., Wang, W., Rafati, A., Svedin, P., Nair, S., Golubinskaya, V., Ardalan, M., Brown, K. L., Karlsson-Bengtsson, A., & Mallard, C. (2021) · Developmental Neuroscience · doi:10.1159/000517687 · Cited by 8
Novel therapeutic approaches for cutaneous T cell lymphomas
Pavlidis, A., Piperi, C., & Papadavid, E. (2021) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2021.1919085 · Cited by 10
Astilbe Chinensis ethanol extract suppresses inflammation in macrophages via NF-κB pathway
Gil, T.-Y., Jin, B.-R., Hong, C.-H., Park, J. H., & An, H.-J. (2020) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-020-03073-5 · Cited by 8
The Epstein-Barr virus-encoded G protein-coupled receptor BILF1 upregulates ICAM-1 through a mechanism involving the NF-қB pathway
Guo, Q.-W., Gao, J., Cheng, L., Yang, X., Li, F., & Jiang, G. (2020) · Bioscience, biotechnology and biochemistry · doi:10.1080/09168451.2020.1777525 · Cited by 8
Cardioprotective molecular mechanism of syringic acid against isoproterenol induced post- myocardial toxicity in male albino wistar rats
Sammeturi, M., Shaik, A. H., Maruthi Prasad, E., Mohammad, A., & Kodidhela, L. D. (2020) · doi:10.1016/j.jksus.2019.11.030 · Cited by 8
Geniposide reduces Staphylococcus aureus internalization into bovine mammary epithelial cells by inhibiting NF-κB activation.
Wei, Z.-K., Su, K., Jiang, P., Shi, M., Wang, J.-J., & Xie, G. (2018) · Microbial Pathogenesis · doi:10.1016/j.micpath.2018.10.002 · Cited by 8
Klotho Protein Protects Human Keratinocytes from UVB-Induced Damage Possibly by Reducing Expression and Nuclear Translocation of NF-κB
Zhang, B.-B., Xu, J., Quan, Z., Qian, M., Liu, W., Zheng, W.-F., Yin, F., Du, J.-R., Zhi, Y., & Song, N.-J. (2018) · Medical Science Monitor · doi:10.12659/msm.910687 · Cited by 8
“Considerable progress has been made in understanding the details of the signaling pathways that regulate NF-kB activity, particularly those responding to the proinflammatory cytokines tumor necrosis factor-a (TNF-a) and interleukin-1 (IL-1) [12].”
BackgroundInfluential
The Viral Tegument Protein pp65 Impairs Transcriptional Upregulation of IL-1β by Human Cytomegalovirus through Inhibition of NF-kB Activity
Biolatti, M., Dell’Oste, V., Scutera, S., Gugliesi, F., Griffante, G., Andrea, M. D., Musso, T., & Landolfo, S. (2018) · Viruses · doi:10.3390/v10100567 · Cited by 8
“Under normal physiological conditions, NF-κB is sequestered in the cytosol by a family of IκB inhibitors in an inactive state [9,23,27].”
Background
Anti-inflammation effect of rebaudioside A by inhibition of the MAPK and NF-κB signal pathway in RAW264.7 macrophage
Choi, D.-H., Cho, U., & Hwang, H. (2018) · Journal of Applied Biological Chemistry · doi:10.3839/jabc.2018.030 · Cited by 8
“Rebaudioside A는 천연 항염증 소 재 연구와 유사하게 LPS 자극에 의해 증가된 NF-κB의 transcriptional regulation 뿐 아니라 NF-κB translational 단계에 모두 관여 하였다[21,22].”
Influential
Expression of FK506‐binding protein 51 (FKBP51) in Mycosis fungoides
Mascolo, M., Romano, M., Ilardi, G., Romano, S., Baldo, A., Scalvenzi, M., Argenziano, G., Merolla, F., Russo, D., Varricchio, S., et al. (2018) · Journal of the European Academy of Dermatology and Venereology · doi:10.1111/jdv.14614 · Cited by 8
Prognostic significance of preoperative IKBKE expression in esophageal squamous cell carcinoma
Yang, W., Qu, Y., Tan, B., Jia, Y.-B., Wang, N.-N., Hu, P., & Wang, J.-B. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s156818 · Cited by 8
The protective effects of PCPA against monocrotaline-induced pulmonary arterial hypertension are mediated through the downregulation of NFAT-1 and NF-κB
Bai, Y., Li, Z.-X., Wang, H.-L., Lian, G.-C., & Wang, Y. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3001 · Cited by 8
“Upon activation, I κ B is phosphorylated by IKK, and thus I κ B α is degraded and NF-κ B is released and then translocates to the nucleus (27,28).”
The NF ‐ κB Signalling Pathway: Mechanisms, Consequences and Therapeutic Targets
Pourdad, B., & Pourdad, A. (2026) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.71229 · Cited by 8
“Upon stimulus-dependent phosphorylation, IKKβ catalyses the specific phosphorylation of classical IκBs, dictating their rapid proteasomal clearance and unleashing NF-κB dimers to govern diverse cellular programs [45, 46, 51–53].”
Celebrating the 40-Year Milestone: NF-ĸB in Oncoimmunity
Alipourgivi, F., & Lu, T. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.218087 · Cited by 7
A review on ribosomal protein S3 (RPS3): Roles in cancer and its resistance to drugs.
Kim, T.-S., Yi, Y., Kim, D. J., & Seong, Y.-S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144955 · Cited by 7
Synergistic pathways in Parkinson's disease: The promise of FGF21 and ACE2
Liu, T., Li, J., Yang, Z., & Wei, J. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102804 · Cited by 8
Impact of Thermal Manipulation of Broiler Eggs on Growth Performance, Splenic Inflammatory Cytokine Levels, and Heat Shock Protein Responses to Post-Hatch Lipopolysaccharide (LPS) Challenge
Al‐Zghoul, M. B., Hundam, S., Mayyas, M., Gerrard, D. E., & Dalloul, R. A. (2025) · Animals · doi:10.3390/ani15121736 · Cited by 6
SO2 derivatives impair ovarian function by inhibiting Serpine1/NF-κB pathway-mediated ovarian granulosa cell survival.
Wu, S., Zhang, X.-D., Lu, Y., Ma, Y.-J., Qi, X., Wang, X., & Tan, J.-C. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.137116 · Cited by 7
AKR1C3 mediates gastric cancer cell invasion and metastasis via the AKT and JNK/p-NF-κB signaling pathways
Lin, L., Xiao, X., Guo, X., Zhong, C., Zhuang, M., Xu, J., Wang, Y., & Chen, F. (2024) · Scientific Reports · doi:10.1038/s41598-024-82039-w · Cited by 8
The Influence of Removable Complete Denture on Pro‐Oxidant Antioxidant Balance and Redox‐Sensitive Inflammation Biomarker NF‐ĸB in the Oral Cavity: An Interventional Follow‐Up Study
Bošković, M., Sokolović, D., Stanković, S., Ristic, I. S., Popović, J., & Kocić, G. (2024) · Clinical and Experimental Dental Research · doi:10.1002/cre2.70007 · Cited by 7
Dragon’s blood attenuates LPS-induced intestinal epithelial barrier dysfunction via upregulation of FAK-DOCK180-Rac1-WAVE2-Arp3 and downregulation of TLR4/NF-κB signaling pathways
Liu, H., Yan, R., Li, Y.-Z., Wang, J.-P., Deng, Y., & Li, Y.-J. (2024) · Journal of Natural Medicines · doi:10.1007/s11418-024-01824-z · Cited by 7
Mechanisms of food-derived bioactive compounds inhibiting TLR4 activation and regulating TLR4-mediated inflammation: A comprehensive review and future directions
Xiao, S., Li, W., Zhang, P., Zhang, G., Lin, H., & Hu, X. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.104587 · Cited by 7
Xanthoangelol alleviates Ischemic Stroke Injury by Inhibiting the Inflammatory Activation of Microglia
Wang, W.-Q., Ma, B.-Y., Li, Z., Zhong, C., Liu, L.-Y., Zhou, Y., Yang, B., Zheng, Y., & Wang, Y.-Q. (2024) · Clinical Traditional Medicine and Pharmacology · doi:10.1016/j.ctmp.2024.200151 · Cited by 7
Exploring the association between rosacea and acne by integrated bioinformatics analysis
Liang, J., Chen, Y., Wang, Z.-H., Wang, Y., Mu, S., Zhang, D., Wang, Z., & Zeng, W.-H. (2024) · Scientific Reports · doi:10.1038/s41598-024-53453-x · Cited by 7
Glutamine Supplementation: A Possible Strategy to Help Mitigate Health Risks of Heat‐Related Illness
Zuhl, M., Specht, J. W., Beatty, S., & Mermier, C. M. (2024) · Journal of Nutrition and Metabolism · doi:10.1155/jnme/1638244 · Cited by 7
The Yin and Yang of IκB Kinases in Cancer
Abdrabou, A. M. (2023) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases2010002 · Cited by 7
“Somatic mutations affecting lysine 171 within the IKBKB gene, responsible for encoding the critical activating kinase (IKK β ) in the canonical NF κ B signaling pathway, were observed in splenic marginal zone lymphomas and multiple myeloma.”
Background
Protective effects of α-terpineol and Bacillus coagulans on intestinal function in weaned piglets infected with a recombinant Escherichia coli expressing heat-stable enterotoxin STa
Wu, T., Zhang, Q., Xu, H., Li, P., Zhao, D., Wang, L., Yi, D., & Hou, Y. (2023) · Frontiers in Veterinary Science · doi:10.3389/fvets.2023.1118957 · Cited by 7
Exploring new pathways in endocrine-resistant breast cancer
de Pinho, I. S., Abreu, C., Gomes, I., Casimiro, S., Pacheco, T. R., Sousa, R., & Costa, L. (2022) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2022.00086 · Cited by 8
“The canonical pathway is activated following stimulation by inflammatory cytokines [interleukin-1 (IL-1), lipopolysaccharide (LPS), TNFα, T- and B-cell mitogens], growth factors, viral proteins, and extracellular physical and chemical stress [146, 147].”
Background
12-Deoxyphorbol-13-Hexadecanoate Abrogates OVX-Induced Bone Loss in Mice and Osteoclastogenesis via Inhibiting ROS Level and Regulating RANKL-Mediated NFATc1 Activation
He, Q., Yang, J., Chen, D., Li, Y., Gong, D., Ge, H., Wang, Z., Wang, H., & Chen, P. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.899776 · Cited by 6
“Mounting evidence suggested that the activity of the NF-κB transcription factor was inhibited by IκBα (Karin and Ben-Neriah, 2000).”
Background
A randomized double blinded placebo controlled clinical trial for the evaluation of green coffee extract on immune health in healthy adults
Narayanaperumal, J., D'souza, A., Miriyala, A., Sharma, B., & Gopal, G. (2022) · Journal of Traditional and Complementary Medicine · doi:10.1016/j.jtcme.2022.01.007 · Cited by 9
Microsatellite Status and IκBα Expression Levels Predict Sensitivity to Pharmaceutical Curcumin in Colorectal Cancer Cells
Lu, L.-L., Przybylla, R., Shang, Y.-R., Dai, M., Krohn, M., Krämer, O., Mullins, C., & Linnebacher, M. (2022) · Cancers · doi:10.3390/cancers14041032 · Cited by 7
Maternal High-Fat Diet Alters the Characteristics of Astrocytes and Worsens the Outcome of Stroke in Rat Offspring, Which Improves After FGF21 Administration
Li, Y., Lin, M., Lin, P., Xia, N., Li, X., Lin, L., & Yang, Y. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.731698 · Cited by 7
“In the inflammatory response, NF-κB is considered as a typical proinflammatory signaling pathway, mainly based on the activation of nuclear factor kappa-B (NF-κB) by pro-inflammatory cytokines such as interleukin-1 (IL-1) and tumor necrosis factor-alpha (TNF-α) (Barnes, 1997; Karin and Ben-Neriah, 2000; Karin et al.,…”
Background
Proteome-wide profiling of transcriptional machinery on accessible chromatin with biotinylated transposons
Zhang, H., Qin, Z., Yue, X., Liu, Y., Sun, X., Feng, J., Xu, Z. Z., Zhao, J., Li, K., Qiu, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abh1022 · Cited by 7
SUMOylation of Dorsal attenuates Toll/NF-κB signaling
Hegde, S., Sreejan, A., Gadgil, C. J., & Ratnaparkhi, G. (2021) · bioRxiv · doi:10.1093/genetics/iyac081 · Cited by 7
Response to abatacept is associated with the inhibition of proteasome β1i expression in T cells of patients with rheumatoid arthritis
Ghannam, K., Gamboa, L. M., Kedor, C., Spengler, L., Kuckelkorn, U., Häupl, T., Burmester, G., & Feist, E. (2020) · RMD Open · doi:10.1136/rmdopen-2020-001248 · Cited by 7
Mathematical modeling of canonical and non-canonical NF-κB pathways in TNF stimulation
Ji, B., Zhang, Y., Zhen, C., Fagan, M. J., & Yang, Q. Z. (2020) · Computer Methods and Programs in Biomedicine · doi:10.1016/j.cmpb.2020.105677 · Cited by 7
Niclosamide and its derivative DK‐520 inhibit RANKL‐induced osteoclastogenesis
Jiao, Y., Chen, C., Hu, X.-J., Feng, X., Shi, Z.-Q., Cao, J., Li, Q., & Zhu, Y. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.12921 · Cited by 7
Phospholipase C-related catalytically inactive protein regulates lipopolysaccharide-induced hypothalamic inflammation-mediated anorexia in mice.
Yamawaki, Y., Shirawachi, S., Mizokami, A., Nozaki, K., Ito, H., Asano, S., Oue, K., Aizawa, H., Yamawaki, S., Hirata, M., et al. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.104563 · Cited by 7
“IκB is phosphorylated by IKK, which induces the subsequent ubiquitination and degradation of IκB, followed by promotion of NF-κB activation (Karin and Ben-Neriah, 2000).”
Background
Retraction: A005, a novel inhibitor of phosphatidylinositol 3-kinase/mammalian target of rapamycin, prevents osteosarcoma-induced osteolysis
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BackgroundInfluential

Authors: Karin, M., & Ben-Neriah, Y.
Affiliations: Hebrew University of Jerusalem (IL)
Department of Pharmacology, Laboratory of Gene Regulation and Signal Transduction University of California, San Diego, La Jolla, California, 92093-0636;
ORCID: Karin, Michael
Venue: Annual Review of Immunology
Publisher: Annual Reviews
Published: 2000-04
Volume: 18
Issue: 1
Pages: 621-663
ISSN: 0732-0582 (ISSN-L)
1545-3278
DOI: 10.1146/annurev.immunol.18.1.621
OpenAlex: W2147921405
Cited by: 4,766
References: 243
Citations by year: 2026: 78 · 2025: 109 · 2024: 86 · 2023: 101 · 2022: 114 · 2021: 112 · 2020: 129 · 2019: 114 · 2018: 129 · 2017: 153 · 2016: 156 · 2015: 135 · 2014: 186 · 2013: 201 · 2012: 194
FWCI: 22.12
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (R01 CA76188, R01CA076188)
National Institute of Allergy and Infectious Diseases (R01AI043477, R01 AI43477)
National Institute of Environmental Health Sciences (R37ES004151, R37 ES04151)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: NF-κB, IκB phosphorylation, ubiquitination, IκB kinase, IKKα, IKKβ, E3 ubiquitin ligase, proteolysis, NF-κB nuclear translocation, TNF signaling, IL-1 signaling, Rel family transcription factors, inflammation, transcriptional regulation
MeSH terms: NF-KappaB Inhibitor alpha, Amino Acid Sequence, Animals, DNA-Binding Proteins, Humans, Molecular Sequence Data, Phosphorylation, Transcription Factors, Ubiquitins, Signal Transduction, Down-Regulation, NF-kappa B, Protein Serine-Threonine Kinases, I-kappa B Proteins, I-kappa B Kinase, NF-kappa B p50 Subunit

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Phosphorylation Meets Ubiquitination: The Control of NF-κB Activity

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