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Nonproteolytic Functions of Ubiquitin in Cell Signaling

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Ubiquitylation in innate and adaptive immunity

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The Role of Ubiquitin in NF-κB Regulatory Pathways

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A Ubiquitin Replacement Strategy in Human Cells Reveals Distinct Mechanisms of IKK Activation by TNFα and IL-1β

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Modulation of the Interferon Antiviral Response by the TBK1/IKKi Adaptor Protein TANK

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Parkin Mediates Neuroprotection through Activation of IκB Kinase/Nuclear Factor-κB Signaling

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Dimerization and Ubiquitin Mediated Recruitment of A20, a Complex Deubiquitinating Enzyme

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Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF- B signaling

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The ubiquitin-proteasome system in cardiac physiology and pathology

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IκB Kinase β Phosphorylates the K63 Deubiquitinase A20 To Cause Feedback Inhibition of the NF-κB Pathway

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Proteasome-mediated degradation of IκBα and processing of p105 in Crohn disease and ulcerative colitis

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Phosphorylation of NF‐κB p65 at Ser468 controls its COMMD1‐dependent ubiquitination and target gene‐specific proteasomal elimination

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Nuclear IKK activity leads to dysregulated Notch-dependent gene expression in colorectal cancer

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Hepatic activation of IKK/NFκB signaling induces liver fibrosis via macrophage-mediated chronic inflammation

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ChlaDub1 ofChlamydia trachomatissuppresses NF-κB activation and inhibits IκBα ubiquitination and degradation

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Ubiquitin Lysine 63 Chain–Forming Ligases Regulate Apical Dominance inArabidopsis

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Edible blue-green algae reduce the production of pro-inflammatory cytokines by inhibiting NF-κB pathway in macrophages and splenocytes

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Inactivation of the CYLD Deubiquitinase by HPV E6 Mediates Hypoxia-Induced NF-κB Activation

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The Drosophila Inhibitor of Apoptosis (IAP) DIAP2 Is Dispensable for Cell Survival, Required for the Innate Immune Response to Gram-negative Bacterial Infection, and Can Be Negatively Regulated by the Reaper/Hid/Grim Family of IAP-binding Apoptosis Inducers

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Potential Roles for Ubiquitin and the Proteasome during Ribosome Biogenesis

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An Atypical E3 Ligase Zinc Finger Protein 91 Stabilizes and Activates NF-κB-inducing Kinase via Lys63-linked Ubiquitination

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RUNX2-modifying enzymes: therapeutic targets for bone diseases

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NFκB/p53 crosstalk—a promising new therapeutic target

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Is the ubiquitin-proteasome system impaired in Huntington’s disease?

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Deubiquitylating enzymes and disease

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Enterovirus 71 2C Protein Inhibits TNF-α–Mediated Activation of NF-κB by Suppressing IκB Kinase β Phosphorylation

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The ubiquitin proteasome system and myocardial ischemia

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Effects of protein phosphorylation on ubiquitination and stability of the translational inhibitor protein 4E-BP1

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Zinc oxide particles induce inflammatory responses in vascular endothelial cells via NF-κB signaling

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Exposure to hydrogen peroxide diminishes NF-κB activation, IκB-α degradation, and proteasome activity in neutrophils

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Ubiquitin in NF-κB Signaling

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Temporal resolution of two-tracked NF-κB activation byLegionella pneumophila

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IκB Kinase ε Phosphorylates TRAF2 To Promote Mammary Epithelial Cell Transformation

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Molecular mechanisms of curcumins suppressing effects on tumorigenesis, angiogenesis and metastasis, focusing on NF-κB pathway

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The effect of proteasome inhibitor MG132 on experimental inflammatory bowel disease

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An RNAi screen identifies USP2 as a factor required for TNF‐α‐induced NF‐κB signaling

Metzig, M. O., Nickles, D., Falschlehner, C., Lehmann‐Koch, J., Straub, B. K., Roth, W., & Boutros, M. (2011) · International Journal of Cancer · doi:10.1002/ijc.26124 · Cited by 55

Unique aspects of transcriptional regulation in neurons - nuances in NFkappaB and Sp1-related factors

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Regulation of IκB Kinase (IKK) Complex by IKKγ-dependent Phosphorylation of the T-loop and C Terminus of IKKβ

Miller, B. S., Higashimoto, T., Lee, Y.-K., & Zandi, E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513793200 · Cited by 49

Combined Effect of Proteasome and Calpain Inhibition on Cisplatin-Resistant Human Melanoma Cells

Młynarczuk-Biały, I., Röckmann, H., Kuckelkorn, U., Schmidt, B., Umbreen, S., Gołąb, J., Ludwig, A., Montag, C., Wiebusch, L., Hagemeier, C., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2614 · Cited by 48

Constitutive Association of TGF-β–Activated Kinase 1 with the IκB Kinase Complex in the Nucleus and Cytoplasm of Human Neutrophils and Its Impact on Downstream Processes

Ear, T., Fortin, C. F., Simard, F. A., & McDonald, P. P. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902958 · Cited by 46

Post-translational control of NF-κB signaling by ubiquitination

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Aging and the ubiquitinome: Traditional and non-traditional functions of ubiquitin in aging cells and tissues

Grillari, J., Katinger, H. W. D., & Voglauer, R. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.07.003 · Cited by 40

Immunohistochemistry in diagnostic surgical pathology: contributions of protein life-cycle, use of evidence-based methods and data normalization on interpretation of immunohistochemical stains.

Idikio, H. (2009) · PubMed Central · Cited by 38

Substrate selection by the proteasome through initiation regions

Tomita, T., & Matouschek, A. T. (2019) · Protein Science · doi:10.1002/pro.3642 · Cited by 39

Post-Translational Modification of Cellular Proteins by Ubiquitin and Ubiquitin-Like Molecules: Role in Cellular Senescence and Aging

Grillari, J., Grillari‐Voglauer, R., & Jansen‐Dürr, P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_13 · Cited by 36

COVID-19 and Parkinson’s Disease: Shared Inflammatory Pathways Under Oxidative Stress

Chaudhry, Z. L., Klenja, D., Janjua, N. A., Cami‐Kobeci, G., & Ahmed, B. Y. (2020) · Brain Sciences · doi:10.3390/brainsci10110807 · Cited by 35

Crucial role of Toll-like receptors in the zinc/nickel-induced inflammatory response in vascular endothelial cells

Tsou, T., Liou, S.-H., Yeh, S., Tsai, F., & Chao, H. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.09.014 · Cited by 32

WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-κB activation pathway

Gao, D., Wang, R., Li, B., Yang, Y., Zhai, Z., & Chen, D. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0059-6 · Cited by 31

MG132 Alleviates Liver Injury Induced by Intestinal Ischemia/Reperfusion in Rats: Involvement of the AhR and NFκB Pathways

Jing, H., Shen, G., Wang, G., Zhang, F., Li, Y., Luo, F., Yao, J., & Tian, X. (2011) · Journal of Surgical Research · doi:10.1016/j.jss.2011.09.001 · Cited by 31

The Nuclear Factor-κB Pathway Regulates Cytochrome P450 3A4 Protein Stability

Zangar, R. C., Bollinger, N., Verma, S., Karin, N. J., & Lu, Y. W. (2008) · Molecular Pharmacology · doi:10.1124/mol.107.043976 · Cited by 30

SCFβTrCP1 Activates and Ubiquitylates TAp63γ

Gallegos, J. R., Litersky, J. M., Lee, H., Sun, Y., Nakayama, K., Nakayama, K., & Lu, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704686200 · Cited by 29

NF-κB: The Inducible Factors of HIV-1 Transcription and their Inhibitors

Yu, M., Xinyong, L., & Clercq, E. D. (2008) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955709787001677 · Cited by 31

The parkin protein as a therapeutic target in Parkinson's disease

Winklhofer, K. F. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.12.1543 · Cited by 28

Regulation of IκB Kinase Complex by Phosphorylation of γ-Binding Domain of IκB Kinase β by Polo-like Kinase 1

Higashimoto, T., Chan, N., Lee, Y.-K., & Zandi, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806258200 · Cited by 27

HSCARG Regulates NF-κB Activation by Promoting the Ubiquitination of RelA or COMMD1

Lian, M., & Zheng, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809752200 · Cited by 26

Alternative UPS drug targets upstream the 26S proteasome

Hjerpe, R., & Rodríguez, M. S. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.11.021 · Cited by 24

Aurora kinases are essential for PKC-induced invasion and matrix metalloproteinase-9 expression in MCF-7 breast cancer cells

Noh, E., Lee, Y., Hong, O., Jung, S. H., Youn, H. J., & Kim, J. (2015) · Oncology Reports · doi:10.3892/or.2015.4027 · Cited by 23

Zinc induces chemokine and inflammatory cytokine release from human promonocytes

Tsou, T., Chao, H., Yeh, S., Tsai, F., & Lin, H.-J. (2011) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2011.09.035 · Cited by 23

Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation

Han, Y., Li, R., Gao, J., Miao, S., & Wang, L. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.10.109 · Cited by 21

Dynamic Protein Complexes Regulate NF-κB Signaling

Wegener, E., & Krappmann, D. (2008) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-72843-6_10 · Cited by 21

Literature-related discovery: common factors for Parkinson’s Disease and Crohn’s Disease

Kostoff, R. N. (2014) · Scientometrics · doi:10.1007/s11192-014-1298-3 · Cited by 21

The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception

Bychkova, V. E., Dolgikh, D. A., Balobanov, V. A., & Finkelstein, A. V. (2022) · Molecules · doi:10.3390/molecules27144361 · Cited by 20

Overview of pyroptosis mechanism and in-depth analysis of cardiomyocyte pyroptosis mediated by NF-κB pathway in heart failure

Zhang, Z., Yang, Z., Wang, S., Wang, X., & Mao, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117367 · Cited by 22

Ubiquitin Ligases in Cancer: Ushers for Degradation

Newton, K., & Vucic, D. (2007) · Cancer Investigation · doi:10.1080/07357900701508041 · Cited by 20

Teuvincenone F Suppresses LPS-Induced Inflammation and NLRP3 Inflammasome Activation by Attenuating NEMO Ubiquitination

Zhao, X., Pu, D.-B., Zhao, Z., Zhu, H., Li, H., Shen, Y., Zhang, X., Zhang, R., Shen, J., Xiao, W., et al. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00565 · Cited by 18

Role of Monoubiquitylation on the Control of IκBα Degradation and NF-κB Activity

Silva-Ferrada, E. D., Torres-Ramos, M., Aillet, F., Campagna, M., Matute, C., Rivas, C., Rodríguez, M. S., & Lang, V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025397 · Cited by 20

Protein Kinase-Mediated Decision Between the Life and Death

Engin, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-49844-3_1 · Cited by 20

Innate link between NF-κB activity and ubiquitin-like modifiers

Lang, V., & Rodríguez, M. S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360853 · Cited by 17

FKBP51 protects 661w cell culture from staurosporine-induced apoptosis.

Daudt, D. R., & Yorio, T. (2011) · PubMed Central · Cited by 15

NF-κB and Therapeutic Approach

Lee, C., & Kim, S. (2009) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2009.17.3.219 · Cited by 14

The Cardiac 26S Proteasome

Powell, S. R. (2006) · Circulation Research · doi:10.1161/01.res.0000239412.40685.61 · Cited by 14

Role of Inflammation in the Development of COVID-19 to Parkinson’s Disease

Liu, T., Wu, H., Sun, L., & Wei, J. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s460161 · Cited by 12

Ubiquitination in host immune response to human papillomavirus infection

Zhou, Q., Zhu, K., & Cheng, H. (2011) · Archives of Dermatological Research · doi:10.1007/s00403-011-1141-0 · Cited by 12

Antitumor activity of CTFB, a novel anticancer agent, is associated with the down-regulation of nuclear factor-κB expression and proteasome activation in head and neck squamous carcinoma cell lines

Skvortsov, S., Skvortsova, I., Stasyk, T., Schiefermeier-Mach, N., Neher, A., Gunkel, A. R., Bonn, G. K., Huber, L. A., Lukas, P. H., Pleiman, C. M., et al. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0708 · Cited by 12

Study of Protein Phosphatase 2A (PP2A) Activity in LPS-Induced Tolerance Using Fluorescence-Based and Immunoprecipitation-Aided Methodology

Sun, L., Pappy, A. L., Pham, T., & Shanley, T. P. (2015) · Biomolecules · doi:10.3390/biom5031284 · Cited by 10

Helicobacter pylori regulates TIFA turnover in gastric epithelial cells.

Sokolova, O. V., Maubach, G., & Naumann, M. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151307 · Cited by 9

Proteasome inhibition in hypertrophied myocardium

Friehs, I. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00886.2008 · Cited by 9

Nematode serine protease inhibitor SPI-I8 negatively regulates host NF-κB signalling by hijacking MKRN1-mediated polyubiquitination of RACK1

Wu, F., Chen, Y., Chen, X., Tong, D., Zhou, J., Du, Z., Yao, C., Yang, Y., Du, A., & Ma, G. (2025) · Communications Biology · doi:10.1038/s42003-025-07803-8 · Cited by 6

Upregulation of proteasome activity rescues cardiomyocytes following pulse treatment with a proteasome inhibitor.

Wang, P., Calise, J., Powell, K., Divald, A., & Powell, S. R. (2014) · Europe PMC (PubMed Central) · Cited by 5

Delineating role of ubiquitination on nuclear factor-kappa B pathway by a computational modeling approach

Lee, J., Choi, K., & Choi, C. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.155 · Cited by 5

Smads keep TABs on inflammation

Seth, R. B., & Chen, Z. J. (2007) · Nature Immunology · doi:10.1038/ni0507-477 · Cited by 5

Effects of multi-walled carbon nanotubes on message and Micro-RNA in human lung BEAS-2B cells

Thai, S., Jones, C. P., Robinette, B. L., Nelson, G. B., Tennant, A. H., Ren, H., Vallanat, B., Fisher, A., Ross, J. A., & Kitchin, K. T. (2024) · Materials Express · doi:10.1166/mex.2024.2620 · Cited by 3

Ubiquitin‐Independent Mechanisms of Substrate Recognition and Degradation by the Proteasome

Hoyt, M. A., & Coffino, P. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch5c · Cited by 3

Ubiquitin Signaling and Cancer Pathogenesis

Haglund, K., & Đikić, I. (2007) · Wiley eBooks · doi:10.1002/9783527620234.ch1 · Cited by 2

Ubiquitin Conjugation and Deconjugation in NF-κB Signaling

Düwel, M., Hadian, K., & Krappmann, D. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4419-6676-6_7 · Cited by 11

Ubiquitin signalling in the NF-κB pathway

Chen, Z. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-758 · Cited by 1,184

Innate link between NF-κB activity and ubiquitin-like modifiers

Lang, V., & Rodríguez, M. S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360853 · Cited by 17

Ubiquitin, TAK1 and IKK: is there a connection?

Chen, Z. J., Bhoj, V, & Seth, R. B. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401869 · Cited by 115

Inhibition of NF‐κB cellular function via specific targeting of the IκB‐ubiquitin ligase

Yaron, A., Gonen, H., Alkalay, I., Hatzubai, A., Jung, S., Beyth, S., Mercurio, F., Manning, A. M., Ciechanover, A. J., & Ben‐Neriah, Y. (1997) · The EMBO Journal · doi:10.1093/emboj/16.21.6486 · Cited by 239