Cited by 263NF-κB Signaling PathwaysRedox biology and oxidative stressSignaling Pathways in Disease

The DOI matches its Crossref record; 65 of the 66 references it cites were found in a registry or an index.

Crucial Role of the Amino-Terminal Tyrosine Residue 42 and the Carboxyl-Terminal PEST Domain of IκBα in NF-κB Activation by an Oxidative Stress

Open access

Schoonbroodt, Sonia, Ferreira, Valérie, Best-Belpomme, Martin, Boelaert, Johan R, Legrand-Poels, Sylvie, Korner, Marie, Piette, Jacques·2000·The Journal of Immunology

DOI 10.4049/jimmunol.164.8.4292

Open this paper in CoChat — free account Open PDF

Abstract

Activation of transcription factor NF-κB involves the signal-dependent degradation of basally phosphorylated inhibitors such as IκBα. In response to proinflammatory cytokines or mitogens, the transduction machinery has recently been characterized, but the activation mechanism upon oxidative stress remains unknown. In the present work, we provide several lines of evidence that NF-κB activation in a T lymphocytic cell line (EL4) by hydrogen peroxide (H2O2) did not involve phosphorylation of the serine residues 32 and 36 in the amino-terminal part of IκBα. Indeed, mutation of Ser32 and Ser36 blocked IL-1β- or PMA-induced NF-κB activation, but had no effect on its activation by H2O2. Although IκBα was phosphorylated upon exposure to H2O2, tyrosine residue 42 and the C-terminal PEST (proline-glutamic acid-serine-threonine) domain played an important role. Indeed, mutation of tyrosine 42 or serine/threonine residues of the PEST domain abolished NF-κB activation by H2O2, while it had no effect on activation by IL-1β or PMA-ionomycin. This H2O2-inducible phosphorylation was not dependent on IκB kinase activation, but could involve casein kinase II, because an inhibitor of this enzyme (5,6-dichloro-1-β-d-ribofuranosyl-benzimidazole) blocks NF-κB activation. H2O2-induced IκBα phosphorylation was followed by its degradation by calpain proteases or through the proteasome. Taken together, our findings suggest that NF-κB activation by H2O2 involves a new mechanism that is totally distinct from those triggered by proinflammatory cytokines or mitogens.

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

Crossref · 10.4049/jimmunol.164.8.4292

Cites

65 of 65 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses
Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182
Function and Activation of NF-kappaB in the Immune System
Baeuerle, P. A., & Henkel, T. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.001041 · Cited by 4,745
Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF‐kappa B transcription factor and HIV‐1.
Schreck, R., RIEBER, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,793
NF-κB: Ten Years After
Baeuerle, P. A., & Baltimore, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81318-5 · Cited by 3,002
A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125
Structure, Regulation and Function of NF-kappaB
Siebenlist, U. K., Franzoso, G., & Brown, K. D. (1994) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.10.110194.002201 · Cited by 2,086
IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation
Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M. S., Mann, M., Manning, A. M., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,042
Identification and Characterization of an IκB Kinase
Régnier, C. H., Song, H. Y., Gao, X., Goeddel, D. V., Cao, Z., & Rothe, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80344-x · Cited by 1,176
REDOX REGULATION OF CELLULAR ACTIVATION
Nakamura, H., Nakamura, K., & Yodoi, J. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.351 · Cited by 1,106
The I kappa B proteins: multifunctional regulators of Rel/NF-kappa B transcription factors.Preprint
Beg, A. A., & Baldwin, A. S. (1993) · Genes & Development · doi:10.1101/gad.7.11.2064 · Cited by 803

Flagged first, then by citations

Show all 66 references

1 of the 66 references couldn’t be matched to a known paper.

Research works printed but not linked: 63

1997, Annu. Rev. Immunol., 351
1994, FASEB J., 1131
1994, Methods Enzymol., 135
1993, Blood, 1212
1999, J. Immunol., 351
1989, Biochem. J., 539
1997, J. Immunol., 5264
1986, Biochim. Biophys. Acta, 65
1991, Eur. J. Biochem., 523
1995, Mutat. Res., 103
1991, EMBO J., 2247
1994, Annu. Rev. Biol., 405
1994, Annu. Rev. Immunol., 141
1995, Adv. Cancer Res., 255
1993, Genes Dev., 2064
1991, Cell, 1281
1993, Genes Dev., 705
1997, Cell, 373
1997, Proc. Natl. Acad. Sci. USA, 9792
1997, Nature, 548
1997, Science, 860
1999, Mol. Cell. Biol., 4547
1999, J. Biol. Chem., 27339
1997, Biochem. J., 777
1995, Eur. J. Biochem., 447
1995, J. Biol. Chem., 6925
1995, Oncogene, 1835
1998, Br. J. Cancer, 1103
1997, J. Biol. Chem., 29419
1998, Mol. Cell. Biol., 19
1999, J. Biol. Chem., 787
1986, J. Pharmacobiodyn., 672
1996, Mol. Cell. Biol., 1401
1989, Biochem. J., 469
1996, Cell, 13
1998, Annu. Rev. Immunol., 225
1996, Cell, 787
1998, J. Biol. Chem., 3180
1997, EMBO J., 3133
1998, Proc. Natl. Acad. Sci. USA, 5718
1998, EMBO J., 5171
1998, Proc. Natl. Acad. Sci. USA, 13012
1996, Eur. J. Biochem., 544
1999, FASEB J., 1137
1995, Photochem. Photobiol., 463
1996, Mol. Cell. Biol., 899
1996, Mol. Cell. Biol., 1058
1996, J. Biol. Chem., 10690
1996, Mol. Cell. Biol., 3554
1996, Mol. Cell. Biol., 6037
1999, Eur. J. Biochem., 253
1997, Cell Growth Differ., 871
1997, Biochem. J., 621
1996, Biochem. Pharmacol., 1719
1997, Biochem. Biophys. Res. Commun., 157
1999, J. Biol. Chem., 30874
1997, Arch. Biochem. Biophys., 383
1998, Am. J. Physiol., L461
1998, Biochem. Biophys. Res. Commun., 193
1997, Basic Res. Cardiol., 155
1996, Curr. Opin. Cell Biol., 340
1998, Ophthalmic Res., 157
1996, Gastroenterology, 1897

Sorted by citations

Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Crosstalk of reactive oxygen species and NF-κB signaling
Morgan, M. J., & Liu, Z.-G. (2011) · Cell Research · doi:10.1038/cr.2010.178 · Cited by 3,505
Cellular response to oxidative stress: Signaling for suicide and survival*
Martindale, J. L., & Holbrook, N. J. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10119 · Cited by 2,314
Reactive Oxygen Species in Metabolic and Inflammatory Signaling
Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081
Ros and ros-mediated cellular signaling
Zhang, J., Wang, X., Vikash, V., Ye, Q., Wu, D., Liu, Y., & Dong, W. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4350965 · Cited by 1,980
NF-κB activation by reactive oxygen species: Fifteen years later
Gloire, G., Legrand-Poels, S., & Piette, J. G. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.04.011 · Cited by 1,561
Self-citation
Phosphorylation of NF-κB and IκB proteins: implications in cancer and inflammation
Viatour, P., Merville, M., Bours, V., & Chariot, A. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.11.009 · Cited by 1,516
ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease
Simpson, D. S. A., & Oliver, P. L. (2020) · Antioxidants · doi:10.3390/antiox9080743 · Cited by 1,044
“Multiple studies have shown that H2O2-mediated NFκB activation results from phosphorylation of IκB tyrosine residues [143,144].”
Background
A subset of neutrophils in human systemic inflammation inhibits T cell responses through Mac-1
Pillay, J., Kamp, V. M., van Hoffen, E., Visser, T., Tak, T., Lammers, J. J., Ulfman, L. H., Leenen, L. P. H., Pickkers, P., & Koenderman, L. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57990 · Cited by 829
The role of oxidative stress during inflammatory processes
Lugrin, J., Rosenblatt‐Velin, N., Parapanov, R., & Liaudet, L. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0241 · Cited by 766
NF-κB: pivotal mediator or innocent bystander in atherogenesis?
Collins, T., & Cybulsky, M. I. (2001) · Journal of Clinical Investigation · doi:10.1172/jci10373 · Cited by 727
Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway
Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674
Human hepatitis C virus NS5A protein alters intracellular calcium levels, induces oxidative stress, and activates STAT-3 and NF-κB
Gong, G., Waris, G., Tanveer, R., & Siddiqui, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171311298 · Cited by 580
Basic Principles and Emerging Concepts in the Redox Control of Transcription Factors
Brigelius‐Flohé, R., & Flohé, L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3534 · Cited by 590
Redox signaling in macrophages
Forman, H. J. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(01)00010-3 · Cited by 521
Hydrogen Peroxide Activates NF-κB through Tyrosine Phosphorylation of IκBα and Serine Phosphorylation of p65
Takada, Y., Mukhopadhyay, A., Kundu, G. C., Mahabeleshwar, G. H., Singh, S., & Aggarwal, B. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212389200 · Cited by 495
Good cop, bad cop: the different faces of NF-κB
Perkins, N. D., & Gilmore, T. D. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401838 · Cited by 489
NADPH Oxidase-Dependent Signaling in Endothelial Cells: Role in Physiology and Pathophysiology
Frey, R. S., Ushio‐Fukai, M., & Malik, A. B. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2220 · Cited by 432
Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance
Bubici, C., Papa, S., Dean, K., & Franzoso, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209936 · Cited by 399
Joining the cell survival squad: an emerging role for protein kinase CK2
Ahmed, K. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02279-1 · Cited by 385
Mitochondrially Associated Hepatitis B Virus X Protein Constitutively Activates Transcription Factors STAT-3 and NF-κB via Oxidative Stress
Waris, G., Huh, K.-W., & Siddiqui, A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.22.7721-7730.2001 · Cited by 323
Bidirectional regulation of NF-κB by reactive oxygen species: A role of unfolded protein response
Nakajima, S., & Kitamura, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.020 · Cited by 321
Redox-Sensitive Kinases of the Nuclear Factor-κB Signaling Pathway
Pantano, C., Reynaert, N. L., van der Vliet, A., & Janssen-Heininger, Y. M. W. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1791 · Cited by 306
Glutathione, Stress Responses, and Redox Signaling in Lung Inflammation
Rahman, I., Biswas, S. K., Jimenez, L. A., Torrès, M., & Forman, H. J. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.42 · Cited by 295
Curcumin (diferuloylmethane) down-regulates cigarette smoke-induced NF- B activation through inhibition of I B kinase in human lung epithelial cells: correlation with suppression of COX-2, MMP-9 and cyclin D1
Shishodia, S., Potdar, P. D., Gairola, C. G., & Aggarwal, B. B. (2003) · Carcinogenesis · doi:10.1093/carcin/bgg078 · Cited by 291
Macrophage Signaling and Respiratory Burst
Iles, K. E., & Forman, H. J. (2002) · Immunologic Research · doi:10.1385/ir:26:1-3:095 · Cited by 290
Role of Hydrogen Peroxide in NF-κB Activation: From Inducer to Modulator
Oliveira-Marques, V., Marinho, H. S., Cyrne, L., & Antunes, F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2601 · Cited by 308
Cigarette smoke condensate activates nuclear transcription factor-kappaB through phosphorylation and degradation of IkappaBalpha: correlation with induction of cyclooxygenase-2
Anto, R. J. (2002) · Carcinogenesis · doi:10.1093/carcin/23.9.1511 · Cited by 278
Oxidative stress, renal infiltration of immune cells, and salt-sensitive hypertension: all for one and one for all
Rodríguez‐Iturbe, B., Vaziri, N. D., Herrera-Acosta, J., & Johnson, R. J. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00269.2003 · Cited by 275
Oxidative stress in the pathogenesis of psoriasis
Zhou, Q., Mrowietz, U., & Rostami‐Yazdi, M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.033 · Cited by 282
The Cadherin Cytoplasmic Domain Is Unstructured in the Absence of β-Catenin
Huber, A. H., Stewart, D. B., Laurents, D. V., Nelson, W. J., & Weis, W. I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010377200 · Cited by 268
Her-2/neu overexpression induces NF-κB via a PI3-kinase/Akt pathway involving calpain-mediated degradation of IκB-α that can be inhibited by the tumor suppressor PTEN
Pianetti, S., Arsura, M., Romieu, R., Coffey, R. J., & Sonenshein, G. E. (2001) · Oncogene · doi:10.1038/sj.onc.1204257 · Cited by 265
Transcriptional responses to oxidative stress: Pathological and toxicological implications
Ma, Q. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.11.004 · Cited by 252
Oxidative stress interference with the nuclear factor- κB activation pathways
Schoonbroodt, S., & Piette, J. G. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00371-3 · Cited by 239
Self-citation
Synergistic Activation of HIV-1 Expression by Deacetylase Inhibitors and Prostratin: Implications for Treatment of Latent Infection
Reuse, S., Calao, M., Kabeya, K., Guiguen, A., Gatot, J., Quivy, V., Vanhulle, C., Lamine, A., Vaira, D., Demonté, D., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006093 · Cited by 242
Self-citation
Redox Regulation of Nuclear Post-Translational Modifications During NF-κB Activation
Gloire, G., & Piette, J. G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2463 · Cited by 224
Self-citation
Ca2+-dependent proteases in ischemic neuronal death
Yamashima, T. (2004) · Cell Calcium · doi:10.1016/j.ceca.2004.03.001 · Cited by 218
Cytokine-induced Activation of Nuclear Factor-κB Is Inhibited by Hydrogen Peroxide through Oxidative Inactivation of IκB Kinase
Korn, S. H., Wouters, E. F. �., Vos, N., & Janssen-Heininger, Y. M. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104321200 · Cited by 204
Regulation of gene expression by oxygen: NF-κB and HIF-1, two extremes
Michiels, C., Minet, E., Mottet, D., & Raes, M. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01045-6 · Cited by 202
Reactive oxygen species: Role in carcinogenesis, cancer cell signaling and tumor progression
Sarmiento-Salinas, F. L., Pérez-González, A., Acosta-Casique, A., Ix-Ballote, A., Díaz, A., Treviño, S., Rosas-Murrieta, N. H., Millán-Pérez-Peña, L., & Maycotte, P. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119942 · Cited by 211
The effect of reactive oxygen species on the synthesis of prostanoids from arachidonic acid.
Korbecki, J., Baranowska‐Bosiacka, I., Gutowska, I., & Chlubek, D. (2013) · PubMed · Cited by 195
Inflammatory cause of metabolic syndrome via brain stress and NF-κB
Cai, D., & Liu, T. (2012) · Aging · doi:10.18632/aging.100431 · Cited by 192
Regulating the regulator: NF-κB signaling in heart
Hall, G., Hasday, J. D., & Rogers, T. B. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.07.006 · Cited by 183
Hydrogen peroxide activates IκB kinases through phosphorylation of serine residues in the activation loops
Kamata, H., Manabe, T., Oka, S., Kamata, K., & Hirata, H. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02712-6 · Cited by 179
Pathogenic mechanisms and regulatory factors involved in alcoholic liver disease
Yan, C., Hu, W., Tu, J., Li, J., Liang, Q., & Han, S. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04166-8 · Cited by 195
Chronic Inflammatory Disorders and Their Redox Control: From Molecular Mechanisms to Therapeutic Opportunities
Chiurchiù, V., & Maccarrone, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3547 · Cited by 175
Ethyl pyruvate modulates inflammatory gene expression in mice subjected to hemorrhagic shock
Yang, R., Gallo, D. J., Baust, J., Uchiyama, T., Watkins, S. C., Delude, R. L., & Fink, M. P. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00022.2002 · Cited by 168
Roles of IKK kinases and protein kinase CK2 in activation of nuclear factor-kappaB in breast cancer.
Romieu, R., Landesman‐Bollag, E., Seldin, D. C., Traish, A. M., Mercurio, F., & Sonenshein, G. E. (2001) · PubMed · Cited by 160
Hydrogen peroxide in inflammation: Messenger, guide, and assassin
Wittmann, C., Chockley, P., Singh, S. K., Pase, L., Lieschke, G. J., & Grabher, C. (2012) · Advances in Hematology · doi:10.1155/2012/541471 · Cited by 143
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142
Reactive Oxygen Species as Intracellular Signaling Molecules in the Cardiovascular System
Krylatov, A. V., Маслов, Л. Н., Воронков, Н. С., Boshchenko, A. A., Popov, S. V., Gomez, L., Wang, H., Jaggi, A. S., & Downey, J. M. (2018) · Current Cardiology Reviews · doi:10.2174/1573403x14666180702152436 · Cited by 144
NF-κB activation by double-strand breaks
Habraken, Y., & Piette, J. G. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.07.015 · Cited by 144
Self-citation
Irisin alleviates LPS-induced liver injury and inflammation through inhibition of NLRP3 inflammasome and NF-κB signaling
Li, Q., Tan, Y., Chen, S., Xiao, X., Zhang, M., Wu, Q., & Dong, M. (2020) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2020.1808675 · Cited by 137
Specification of DNA Binding Activity of NF- B ProteinsPreprint
Wan, F., & Lenardo, M. J. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000067 · Cited by 138
A Quantitative Study of NF-κB Activation by H2O2: Relevance in Inflammation and Synergy with TNF-α
Oliveira-Marques, V., Cyrne, L., Marinho, H. S., & Antunes, F. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3893 · Cited by 133
Hepatitis C virus NS4B induces unfolded protein response and endoplasmic reticulum overload response-dependent NF-κB activation
Li, S., Ye, L., Yu, X., Xu, B., Li, K., Zhu, X., Liu, H., Wu, X., & Kong, L. (2009) · Virology · doi:10.1016/j.virol.2009.06.039 · Cited by 138
Berberine suppresses inflammatory agents-induced interleukin-1β and tumor necrosis factor-α productions via the inhibition of IκB degradation in human lung cells
Lee, C.-H., Chen, J., Hsiang, C., Wu, S., Wu, H.-C., & Ho, T. (2007) · Pharmacological Research · doi:10.1016/j.phrs.2007.06.003 · Cited by 129
Evidence That Glutathione Depletion Is a Mechanism Responsible for the Anti-Inflammatory Effects of Ethyl Pyruvate in Cultured Lipopolysaccharide-Stimulated RAW 264.7 Cells
Song, M., Kellum, J. A., Kaldas, H., & Fink, M. P. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.056622 · Cited by 128
Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-κB and STAT-3
Waris, G., Tardif, K. D., & Siddiqui, A. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01300-x · Cited by 127
Use of scopoletin to inhibit the production of inflammatory cytokines through inhibition of the IκB/NF-κB signal cascade in the human mast cell line HMC-1
Moon, P., Lee, B.-H., Jeong, H., An, H., Park, S., Kim, H., Ko, S., Um, J., Hong, S., & Kim, H. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.10.021 · Cited by 126
Reactive oxygen species as mediators of organ dysfunction caused by sepsis, acute respiratory distress syndrome, or hemorrhagic shock: potential benefits of resuscitation with Ringerʼs ethyl pyruvate solution
Fink, M. P. (2002) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200203000-00009 · Cited by 126
Detection of Oxidative Stress Induced by Nanomaterials in Cells—The Roles of Reactive Oxygen Species and Glutathione
Čapek, J., & Roušar, T. (2021) · Molecules · doi:10.3390/molecules26164710 · Cited by 128
Hepatitis C Virus NS5A and Subgenomic Replicon Activate NF-κB via Tyrosine Phosphorylation of IκBα and Its Degradation by Calpain Protease
Waris, G., Livolsi, A., Imbert, V., Peyron, J., & Siddiqui, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303248200 · Cited by 117
Retracted
Synergistic Activation of Human Immunodeficiency Virus Type 1 Promoter Activity by NF-κB and Inhibitors of Deacetylases: Potential Perspectives for the Development of Therapeutic Strategies
Quivy, V., Adam, E., Collette, Y., Demonté, D., Chariot, A., Vanhulle, C., Berkhout, B., Castellano, R., de Launoit, Y., Burny, A., et al. (2002) · Journal of Virology · doi:10.1128/jvi.76.21.11091-11103.2002 · Cited by 116
Self-citation
Role of reactive oxygen and nitrogen species in acute respiratory distress syndrome
Fink, M. P. (2002) · Current Opinion in Critical Care · doi:10.1097/00075198-200202000-00002 · Cited by 113
Nuclear Factor Kappa B Signaling Complexes in Acute Inflammation
Rius‐Pérez, S., Pérez, S., Martí‐Andrés, P., Monsalve, M., & Sastre, J. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7975 · Cited by 116
Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes
Singh, G. P., Ganapathi, M., Sandhu, K. S., & Dash, D. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20746 · Cited by 106
Ethyl Pyruvate Ameliorates Intestinal Epithelial Barrier Dysfunction in Endotoxemic Mice and Immunostimulated Caco-2 Enterocytic Monolayers
Sappington, P. L., Han, X., Yang, R., Delude, R. L., & Fink, M. P. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.043182 · Cited by 105
HDL counterbalance the proinflammatory effect of oxidized LDL by inhibiting intracellular reactive oxygen species rise, proteasome activation, and subsequent NF‐κB activation in smooth muscle cells
Robbesyn, F., Garcia, V., Augè, N., Vieira, O. V., Frisach, M., Salvayre, R., & Nègre‐Salvayre, A. (2003) · The FASEB Journal · doi:10.1096/fj.02-0240fje · Cited by 105
Phosphorylation by the Protein Kinase CK2 Promotes Calpain-Mediated Degradation of IκBα
Shen, J., Channavajhala, P. L., Seldin, D. C., & Sonenshein, G. E. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.9.4919 · Cited by 103
Role for casein kinase 2 in the regulation of HIF‐1 activity
Mottet, D., Ruys, S. P. D., Demazy, C., Raes, M. J., & Michiels, C. (2005) · International Journal of Cancer · doi:10.1002/ijc.21268 · Cited by 107
NF-κB as a target for cancer therapy
Melisi, D., & Chiao, P. J. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.2.133 · Cited by 99
Redox regulation of macrophages
Tran, N., & Mills, E. L. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103123 · Cited by 101
Ultraviolet A Radiation-Induced Immediate Iron Release Is a Key Modulator of the Activation of NF-κB in Human Skin Fibroblasts
Reelfs, O., Tyrrell, R. M., & Pourzand, C. (2004) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2004.22620.x · Cited by 91
Ethyl Pyruvate Ameliorates Liver Ischemia-Reperfusion Injury by Decreasing Hepatic Necrosis and Apoptosis
Tsung, A., Kaizu, T., Nakao, A., Shao, L., Bucher, B. T., Fink, M. P., Murase, N., & Geller, D. A. (2005) · Transplantation · doi:10.1097/01.tp.0000151681.07474.2e · Cited by 91
Potentiation of Tumor Necrosis Factor-Induced NF-κB Activation by Deacetylase Inhibitors Is Associated with a Delayed Cytoplasmic Reappearance of IκBα
Adam, E., Quivy, V., Bex, F., Chariot, A., Collette, Y., Vanhulle, C., Schoonbroodt, S., Goffin, V., Nguyên, T. L.-A., Gloire, G., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.17.6200-6209.2003 · Cited by 91
Self-citation
Hydrogen Peroxide Has Opposing Effects on IKK Activity and I κ B α Breakdown in Airway Epithelial Cells
Jaspers, I., Zhang, W., Fraser, A., Samet, J. M., & Reed, W. (2001) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.24.6.4344 · Cited by 91
The Effects of Calpain Inhibition on IkBα Degradation After Activation of PBMCs: Identification of the Calpain Cleavage Sites
Schaecher, K. E., Goust, J. M., & Banik, N. L. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000026410.56000.dd · Cited by 89
Regulatory mechanisms of viral hepatitis B and C
Waris, G., & Siddiqui, A. (2003) · Journal of Biosciences · doi:10.1007/bf02970150 · Cited by 85
Dehydroepiandrosterone Modulates Nuclear Factor-κB Activation in Hippocampus of Diabetic Rats
Aragno, M., Mastrocola, R., Brignardello, E., Catalano, M. G., Robino, G., Manti, R., Parola, M., Danni, O., & Boccuzzi, G. (2002) · Endocrinology · doi:10.1210/en.2002-220182 · Cited by 83
NF-κB activation by combinations of NEMO SUMOylation and ATM activation stresses in the absence of DNA damage
Wuerzberger‐Davis, S. M., Nakamura, Y., Seufzer, B. J., & Miyamoto, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209815 · Cited by 82
Degeneration of neuronal cells due to oxidative stress—microglial contribution
Koutsilieri, E., Scheller, C., Tribl, F., & Riederer, P. F. (2002) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(02)00021-4 · Cited by 81
Impact of Intravascular Hemolysis in Malaria on Liver Dysfunction
Dey, S., Bindu, S., Goyal, M., Pal, C., Alam, A., Iqbal, M. S., Kumar, R., Sarkar, S., & Bandyopadhyay, U. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.341255 · Cited by 82
Polydatin reducesStaphylococcus aureuslipoteichoic acid‐induced injury by attenuating reactive oxygen species generation and TLR 2‐ NF κB signalling
Zhao, G., Jiang, K., Wu, H., Qiu, C., Deng, G., & Peng, X. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13194 · Cited by 78
Perturbation of actin dynamics induces NF-κB activation in myelomonocytic cells through an NADPH oxidase-dependent pathway
Kustermans, G., Benna, J. E., Piette, J. G., & Legrand-Poels, S. (2005) · Biochemical Journal · doi:10.1042/bj20041318 · Cited by 80
Self-citation
Reactive Oxygen Species: A Double-Edged Sword in the Modulation of Cancer Signaling Pathway Dynamics
Nigam, M., Punia, B., Dimri, D. B., Mishra, A. P., Radu, A.-F., & Bungau, G. S. (2025) · Cells · doi:10.3390/cells14151207 · Cited by 83
Mitochondria as Oxidative Signaling Organelles in T-cell Activation: Physiological Role and Pathological Implications
Kamiński, M. M., Röth, D., Krammer, P. H., & Gülow, K. (2013) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-013-0235-0 · Cited by 73
Reactive Oxygen Species Across Death Pathways: Gatekeepers of Apoptosis, Ferroptosis, Pyroptosis, Paraptosis, and Beyond
Sendtner, N., Seitz, R., Brandl, N., Müller, M., & Gülow, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262010240 · Cited by 81
Neutrophils: The Role of Oxidative and Nitrosative Stress in Health and Disease
Manda‐Handzlik, A., & Demkow, U. A. (2015) · Advances in experimental medicine and biology · doi:10.1007/5584_2015_117 · Cited by 75
Antioxidant and Anti-Inflammatory Properties of Anthocyanins Extracted from Oryza sativa L. in Primary Dermal Fibroblasts
Palungwachira, P., Tancharoen, S., Phruksaniyom, C., Klungsaeng, S., Srichan, R., Kikuchi, K., & Nararatwanchai, T. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/2089817 · Cited by 80
Interplay between BMPs and Reactive Oxygen Species in Cell Signaling and Pathology
Sánchez‐de‐Diego, C., Valer, J. A., Pimenta-Lopes, C., Rosa, J. L., & Ventura, F. (2019) · Biomolecules · doi:10.3390/biom9100534 · Cited by 70
TPEN Induces Apoptosis Independently of Zinc Chelator Activity in a Model of Acute Lymphoblastic Leukemia and Ex Vivo Acute Leukemia Cells through Oxidative Stress and Mitochondria Caspase-3- and AIF-Dependent Pathways
Mendivil‐Perez, M., Velez‐Pardo, C., & Jiménez-Del-Río, M. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/313275 · Cited by 65
The p38 mitogen‐activated protein kinase regulates interleukin‐1β‐induced IL‐8 expression via an effect on the IL‐8 promoter in intestinal epithelial cells
Parhar, K. K. S., Ray, A., Steinbrecher, U. P., Nelson, C. C., & Salh, B. S. (2003) · Immunology · doi:10.1046/j.1365-2567.2003.01603.x · Cited by 69
Systems approaches to investigate the role of NF-κB signaling in aging
Haga, M., & Okada, M. (2022) · Biochemical Journal · doi:10.1042/bcj20210547 · Cited by 67
Large hepatitis delta antigen activates STAT‐3 and NF‐κB via oxidative stress
Williams, V., Brichler, S., Khan, E., Chami, M., Dény, P., Kremsdorf, D., & Gordien, E. (2012) · Journal of Viral Hepatitis · doi:10.1111/j.1365-2893.2012.01597.x · Cited by 72
Reactive Nitrogen Species and Cell Signaling: Implications for Death or Survival of Lung Epithelium
Janssen-Heininger, Y. M. W., Persinger, R. L., Korn, S. H., Pantano, C., McElhinney, B., Reynaert, N. L., LANGEN, R. C. J., Ckless, K., Shrivastava, P., & Poynter, M. E. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206008 · Cited by 64
The Bad, the Good, and the Ugly about Oxidative Stress
Jiménez-Del-Río, M., & Velez‐Pardo, C. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/163913 · Cited by 65
Ethyl pyruvate: A novel anti-inflammatory agent
Fink, M. P. (2003) · Critical Care Medicine · doi:10.1097/00003246-200301001-00008 · Cited by 64
Proteolytic Response to Oxidative Stress in Mammalian Cells
Mehlhase, J., & Grune, T. (2002) · Biological Chemistry · doi:10.1515/bc.2002.057 · Cited by 61
Oxidative Stress Decreases G Protein-Coupled Receptor Kinase 2 in Lymphocytes via a Calpain-Dependent Mechanism
Lombardi, M. S., Kavelaars, A., Penela, P., Scholtens, E. J., Roccio, M., Schmidt, R. E., Schedlowski, M., Mayor, F., & Heijnen, C. J. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.2.379 · Cited by 63

Authors: Schoonbroodt, S., Ferreira, V., Best-Belpomme, M., Boelaert, J. R., Legrand-Poels, S., Korner, M., & Piette, J.
Affiliations: University of Liège (BE)
Oncogenesis, Differentiation, and Signal Transduction Laboratory, Institut de Recherche sur le Cancer-Centre Nationale de la Recherche Scientifique , Villejuif ,
Institut National de la Santé et de la Recherche Médicale, Unit 99, Hôpital Henri Mondor , Creteil ,
AZ Sint-Jan (BE)
Corresponding author: Schoonbroodt, Sonia
Piette, Jacques
ORCID: Schoonbroodt, Sonia
Piette, Jacques
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 2000-04
Volume: 164
Issue: 8
Pages: 4292-4300
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.164.8.4292
OpenAlex: W1557884422
Cited by: 263
References: 66
Citations by year: 2026: 8 · 2025: 8 · 2024: 8 · 2023: 6 · 2022: 9 · 2021: 9 · 2020: 13 · 2019: 6 · 2018: 9 · 2017: 7 · 2016: 5 · 2015: 7 · 2014: 7 · 2013: 13 · 2012: 10
FWCI: 8.40
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
ORBi (University of Liège) (submittedVersion)
Funders: Association pour la Recherche sur le Cancer
Sidaction
Fonds De La Recherche Scientifique - FNRS
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: NF-κB activation, IκBα, PEST domain, oxidative stress, hydrogen peroxide, IκBα phosphorylation, casein kinase 2, proteasomal degradation, IκB kinase, IL-1β, PMA/ionomycin, T cells, EL4 cells
MeSH terms: NF-KappaB Inhibitor alpha, Animals, Calpain, Cysteine Endopeptidases, DNA, DNA-Binding Proteins, Enzyme Activation, Humans, Hydrogen Peroxide, Multienzyme Complexes, Peptide Fragments, Phosphorylation, Protein Binding, Serine, Tumor Cells, Cultured, Tyrosine, NF-kappa B, Protein Tyrosine Phosphatases, Protein Serine-Threonine Kinases, Point Mutation, Protein Structure, Tertiary, Oxidative Stress, I-kappa B Proteins, Proteasome Endopeptidase Complex, Casein Kinase II, Mice, I-kappa B Kinase, Protein Tyrosine Phosphatase, Non-Receptor Type 12

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

Crucial Role of the Amino-Terminal Tyrosine Residue 42 and the Carboxyl-Terminal PEST Domain of IκBα in NF-κB Activation by an Oxidative Stress

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks