The DOI matches its Crossref record; 73 of the 77 references it cites were found in a registry or an index.
NF-κB/p65 antagonizes Nrf2-ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK
Open accessAbstract
Constitutively activated NF-kappaB occurs in many inflammatory and tumor tissues. Does it interfere with anti-inflammatory or anti-tumor signaling pathway? Here, we report that NF-kappaB p65 subunit repressed the Nrf2-antioxidant response element (ARE) pathway at transcriptional level. In the cells where NF-kappaB and Nrf2 were simultaneously activated, p65 unidirectionally antagonized the transcriptional activity of Nrf2. In the p65-overexpressing cells, the ARE-dependent expression of heme oxygenase-1 was strongly suppressed. However, p65 inhibited the ARE-driven gene transcription in a way that was independent of its own transcriptional activity. Two mechanisms were found to coordinate the p65-mediated repression of ARE: (1) p65 selectively deprives CREB binding protein (CBP) from Nrf2 by competitive interaction with the CH1-KIX domain of CBP, which results in inactivation of Nrf2. The inactivation depends on PKA catalytic subunit-mediated phosphorylation of p65 at S276. (2) p65 promotes recruitment of histone deacetylase 3 (HDAC3), the corepressor, to ARE by facilitating the interaction of HDAC3 with either CBP or MafK, leading to local histone hypoacetylation. This investigation revealed the participation of NF-kappaB p65 in the negative regulation of Nrf2-ARE signaling, and might provide a new insight into a possible role of NF-kappaB in suppressing the expression of anti-inflammatory or anti-tumor genes.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In addition, decreased levels of Nrf2, a transcription factor negatively regulated by NF-κB (Liu et al., 2008) that is involved in antioxidants response mechanisms (Nair et al., 2008), have been reported in the brains of AD patients (Ramsey et al., 2007).”
From Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes (2022) · cites this paper as Liu et al., 2008
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Cytokines suppress adipogenesis and PPAR-γ function through the TAK1/TAB1/NIK cascade
Suzawa, M., Takada, I., Yanagisawa, J., Ohtake, F., Ogawa, S., Yamauchi, T., Kadowaki, T., Takeuchi, Y., Shibuyà, H., Gotoh, Y., et al. (2003) · Nature Cell Biology · doi:10.1038/ncb942 · Cited by 292
RetractedHayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
NF-κB: linking inflammation and immunity to cancer development and progression
Karin, M., & Greten, F. R. (2005) · Nature reviews. Immunology · doi:10.1038/nri1703 · Cited by 3,175
Cancer chemoprevention with dietary phytochemicals
Surh, Y.-J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1189 · Cited by 2,955
Nrf2–Keap1 defines a physiologically important stress response mechanism
Motohashi, H., & Yamamoto, M. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.09.003 · Cited by 1,725 · cited 1×
“Nrf2 is amember of theCNC-basic leucine zipper (CNC-bZIP) family of transcription factors, which coordinately regulates the constitutive and inducible expression of antioxidant and phase 2 detoxification enzymes, such as heme oxygenase-1 (HO-1) and NAD(P)H:quinone oxidoreductase 1 (NQO1), via a cis-acting DNA element…”
BackgroundNF-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
Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex
Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,284
Duration of Nuclear NF-κB Action Regulated by Reversible Acetylation
Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231
Persistent oxidative stress in cancer
Toyokuni, S., Okamoto, K., Yodoi, J., & Hiai, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01368-b · Cited by 1,219
Cited by
Sorted by citations
Items 601–699 of 699
Shi, Y., Xu, Z., Li, F., Liu, Q., Zhan, Y., Wu, F., Li, Q., He, F., Fan, P., Zhang, H., et al. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.09.002 · Cited by 2
“This epigenetic repression ultimately attenuates the transcriptional activity of Nrf2 [33].”
He, Y., Wang, J., Ying, C., Liang, W., Yin, Z., Gao, J., Wang, B., Zhao, X., & Zhang, Y. (2025) · Medicine · doi:10.1097/md.0000000000044392 · Cited by 2
Fermented Yeast Complex Extract Promotes Hair Regrowth by Decreasing Oxidative Stress
Byun, K.-A., Choi, C. H., Oh, S., Hyun, J., Son, K. H., & Byun, K. (2025) · Antioxidants · doi:10.3390/antiox14121503 · Cited by 2
“ARE pathway at the transcriptional level by competing with NRF2 for the co-activator CBP and by recruiting HDAC3 to NRF2 target promoters, leading to reduced NRF2-dependent gene expression [40].”
Dalaka, E., Gidari, D. L. S., Filintas, C. S., Bantola, V., Kavallieratos, N. G., & Θεοδώρου, Γ. (2026) · Antioxidants · doi:10.3390/antiox15020262 · Cited by 2
Škrbić, R., Milivojac, T., Grabež, M., Amidžić, L., Bajić, Z., Šobot, T., Mandić-Kovačević, N., Uletilović, S., Đukanović, Đ., Bojić, M. G., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27062843 · Cited by 2
Gu, X., Luo, Y., Zhang, J., Ouyang, H., 孔紫靖, Wang, T., Huang, Z., & Ji, L. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.117989 · Cited by 2
Hou, J., Duan, X., Shi, H., Zhang, J., Jiang, Z., Tan, Z., Tian, Z., Li, X., & Wang, Q. (2026) · Food & Function · doi:10.1039/d5fo05215g · Cited by 2
Kang, D. (2026) · Antioxidants · doi:10.3390/antiox15060782 · Cited by 2
Oxidative stress and its biological significance
Uyeda, M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90905-1.00003-1 · Cited by 2
Skrzydlewska, E., Łuczaj, W., Biernacki, M., Wójcik, P., Jarocka-Karpowicz, I., Orehovec, B., Baršić, B., Tarle, M., Kmet, M., Lukšić, I., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713574 · Cited by 2
“However, NFκB may also modify the expression of ARE-regulated genes, as the canonical subunit of NFκB-p65 antagonizes the formation of the Nrf2-ARE adduct, which reduces the transcription of AREdependent genes, including antioxidant proteins [30].”
BackgroundNuciferine ameliorates osteoarthritis: An in vitro and in vivo study
Peng, M., Shen, G., Tu, Q., Zhang, W., & Wang, J. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113098 · Cited by 2
Zhu, X., Zhang, L., Cui, W., Wang, L., Xu, F., Liu, M., Chen, S., Jiang, H., He, Z., Peng, C., et al. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1567639 · Cited by 2
Ding, L.-L., Li, X., Guo, Y., Zhou, F., & Deng, D. Y. B. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01488-z · Cited by 2
Vervaecke, L. S. (2017) · NC Digital Online Collection of Knowledge and Scholarship (The University of North Carolina at Greensboro) · Cited by 3
Relation of signal in mononuclear cell with endotoxin response and clinical outcome after trauma
Shih, H., Huang, M., & Lee, C. (2011) · The American Journal of Emergency Medicine · doi:10.1016/j.ajem.2010.12.025 · Cited by 2
Feed-Forward and Feed-Back Circuits of the NRF2/AP-1 Composite Pathway
Zolotukhin, P. V., & Belanova, A. A. (2016) · InTech eBooks · doi:10.5772/65216 · Cited by 2
Biochemical Mechanisms of Vascular Complications in Diabetes
Flores, M. D., Ginez, M. D. C. C., & Baiza-Gutman, L. A. (2023) · Springer eBooks · doi:10.1007/978-3-031-25519-9_49 · Cited by 2
Fu, Y., Zeng, Z., Feng, S., Chen, Y., Ding, Q., & Shi, Y. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105782 · Cited by 2
Tao, T., Ye, B., Xu, Y., Wang, Y., Zhu, Y., & Tian, Y. (2022) · Journal of Surgical Research · doi:10.1016/j.jss.2022.02.001 · Cited by 2
Gaastra, B., & Galea, I. (2019) · medRxiv · doi:10.1101/19004853 · Cited by 2
Wang, C., Zhao, X., Wang, K., Liang, H., Chen, S., Liu, Y., Yao, H., & Jiang, J. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s467158 · Cited by 1
“113 Research indicates that Nrf2 facilitates the polarization of M2 macrophages while inhibiting the polarization of M1 macrophages, thus exerting an anti-inflammatory effect.”
Melatonin’s role in redox homeostasis: A preclinical and clinical perspective
Torres, F. F., Bernardo, V. S., Zucão, A. C. A., Gazarini, L., Reiter, R. J., & da Silva, D. G. H. (2025) · Pharmacological Research - Natural Products · doi:10.1016/j.prenap.2025.100147 · Cited by 2
Li, M., Chen, L., Xu, H., Li, J., Liu, Y., Chen, X., Luo, M., Xie, X., Yin, M., & He, J. (2025) · Pharmaceuticals · doi:10.3390/ph18091363 · Cited by 1
“Conversely, sustained NF-κ B activation impairs Nrf2-driven transcriptional responses, highlighting their reciprocal interplay [90].”
The role of Nrf2 in anoikis resistance and metastasis in anaplastic thyroid carcinoma
Fan, S., Li, H., Li, K., Gong, Z., Zeng, X., Wang, S., Li, Y., Nie, C., van Hasselt, C. A., Chan, J. Y. K., et al. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00355-7 · Cited by 1
“Concurrent KRAS suppression indicates disruption of a KRAS–Nrf2– BCL-2 loop, while the parallel decline of Nrf2 and NF-κB suggests pathway crosstalk in the metastatic niche [51].”
Xue, H., Wen, Y., Yang, J., Zhang, Y., Jin, C. H., Li, B., Ai, Y., Zheng, M., Wen, B., & Song, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311446 · Cited by 1
“…mitochondrial apoptosis by decreasing cleaved Caspase-3 and restoring the Bcl-2/Bax ratio a It also suppressed TLR4 and p-NF-κ B expression, while enhancing NRF2 nuclear translocation, increasing HO-1 expression, and decreasing KEAP1 levels [17,28], with effects comparable to those of Edaravone.”
InfluentialMo, S., Chen, T., Shen, M., Wang, C., Yu, Q., Chen, Y., Jiang, S., Wen, H., & Xie, J. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.108262 · Cited by 1
Ewees, M. G., Abdelzaher, L. A., El‐Shoura, E. A. M., Rahman, F. E.-Z. S. A., Shabaan, A. M., Embaby, M. A., Abdelmenem, A. M., & Ahmed, Y. M. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116267 · Cited by 1
Abduljabbar, H., Jamal, M., & Esmat, A. (2026) · Current Pharmaceutical Biotechnology · doi:10.2174/0113892010433981251031050335 · Cited by 1
Sun, D., Bao, Y., Fan, Q., Zhao, L., 付志方, Li, H., Zhao, L., & Jiao, H. (2026) · Nutrients · doi:10.3390/nu18060992 · Cited by 2
“Meanwhile, previous studies have indicated that Nrf2 directly competes with p65 for the essential transcriptional coactivators CBP/p300, thereby physically inhibiting NF-κ B’s transcriptional activity [37,38].”
Nama, L., Abubakar, M., Daksh, R., Goel, G., Gajbhiye, R. L., Kumar, P., Rai, A., Murti, K., Ravichandiran, V., & Kumar, N. (2026) · Journal of Molecular Histology · doi:10.1007/s10735-026-10781-8 · Cited by 1
Wang, J., Cai, X., & Liang, Q. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1808772 · Cited by 1
“For instance, curcumin, a hydrophobic polyphenol, has been demonstrated to modify cysteine residues on the Keap1 protein through electrophilic reactions, thereby relieving its inhibition of Nrf2 and activating the Nrf2/HO-1 antioxidant pathway (Xu et al., 2019).”
InfluentialTang, Q., Wang, Y., Wang, Y., Qi, H., Jia, H., Xu, L., & Li, J. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.142151 · Cited by 3
Romero-Durán, M. A., Maldonado-Pichardo, M. C., Perez‐Aguilar, J. M., & Aguirre, V. M. B. (2026) · F1000Research · doi:10.12688/f1000research.177148.3 · Cited by 1
Martins, T., Rei, N., & Machado-Carvalho, L. (2026) · Nutraceuticals · doi:10.3390/nutraceuticals6030050 · Cited by 1
Redox Regulation of Differentiation in Neuroblastoma
Silvis, A. M. (2012) · Cited by 1
Multiple Modes of Nrf2 Regulation and Transcriptional Response
Mathew, S. T., & Hammarsten, O. (2016) · InTech eBooks · doi:10.5772/65295 · Cited by 1
“NF‐κB blocks Nrf2 transcriptional activation of target genes [41].”
BackgroundGong, X., Hu, F., Hu, J., Bao, Z., & Wang, M. (2024) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2024.105157 · Cited by 1
Hassan, E. A., Abdelnaser, A., Ibrahim, S., Yousef, E. H., Mosallam, A. M., & Zayed, S. E. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140859 · Cited by 1
Anti-inflammatory action of the transcription factor Nrf2
Izumi, Y. (2018) · Folia Pharmacologica Japonica · doi:10.1254/fpj.152.209 · Cited by 1
Regulation of NRF2 signaling pathway and the hallmarks of aging: An overview
Medoro, A., Scapagnini, G., & Davinelli, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-19247-0.00004-7 · Cited by 1
Targeting Nrf2 in inflammation and cancer
Cowan, J. (2014) · UEA Digital Repository (University of East Anglia) · Cited by 1
Cellular and molecular aspects of the anti-inflammatory effects of low-dose radiation therapy
Large, M. (2015) · Technischen Universität Darmstadt · doi:10.26083/tuprints-00004977 · Cited by 1
Regulation of oxidoreductase enzymes during inflammation
Ingram, S. (2018) · Cited by 1
Cordell, W. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3721693 · Cited by 1
Konkin, D. J. F. (2013) · University Library - University of Saskatchewan (University of Saskatchewan)
Cancer Chemopreventive Phytochemicals Targeting NF‐κB and Nrf2 Signaling Pathways
Na, H., & Surh, Y. (2015) · doi:10.1002/9781118930458.ch9
Chemopreventive activity of tocopherols in mammary tumorigenesis
Smolarek, A. K. (2013) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t3f47mtc
“competing for the transcription co-activator CREB binding protein and by recruiting histone deacetylase 3 to cause local hypoacetylation to hamper Nrf2 signaling [258].”
BackgroundMolecular and pharmacological study of transcription factor Nrf2
Lin, W. (2009) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t34x5819
Characterisation of glyoxalase 1 mutant mouse and glyoxalase 1 copy number alteration
Shafie, A. (2026) · Warwick Research Archive Portal (University of Warwick) · doi:10.82444/warw.33721561
Lipoic Acid in the Prevention and Treatment of Inflammatory Disease and Cancer
Shay, K. P., Moreau, R. F., & Hagen, T. M. (2013) · CRC Press eBooks · doi:10.1201/b15323-39
Ramkissoon, A. (2012) · TSpace (University of Toronto)
Oxidative Status Pathways: Systemic Biomarkers
Zolotukhin, P. V., Чмыхало, В. К., Belanova, A. A., Dybushkin, A., Fedoseev, V., & Smirnov, D. (2018) · InTech eBooks · doi:10.5772/intechopen.75543
Investigation of renal ischemia-reperfusion induced liver injury
Shang, Y. (2018) · Mspace (University of Manitoba)
Interplay between HSP90 and Nrf2 pathways in diabetes-associated atherosclerosis
Lázaro, I., Oguiza, A., Recio, C., Lopez‐Sanz, L., Bernal, S., Egido, J., & Gómez‐Guerrero, C. (2017) · Clínica e Investigación en Arteriosclerosis (English Edition) · doi:10.1016/j.artere.2017.03.001
Bhandari, R., & Kuhad, A. (2022) · Springer eBooks · doi:10.1007/978-981-16-6760-2_5
KUMAR, S., & Singh, S. (2019) · The Indian Journal of Animal Sciences · doi:10.56093/ijans.v89i11.95862
“Heat stress suppresses the transcriptional activity of Nrf2 by promoting the localisation of transcription repressors, histone deacetylases with Nrf2/ARE and sequestering coactivators like CREB binding protein (CBP) (Liu et al. 2008).”
BackgroundDay, M., Daley, C., Wu, Y., Pathmaraj, M., Verner, M.-A., & Caron-Beaudoin, É. (2024) · Toxicological Sciences · doi:10.1093/toxsci/kfae080
“…enzymes, responds to moderate levels of oxidative stress but beyond a threshold, high ROS concentrations overwhelm the antioxidant capacity resulting in the consumption of antioxidants and the downregulation of Nrf2 (Xiao et al. 2003; Myatt and Cui 2004; Faraonio et al. 2006; Liu et al. 2008).”
BackgroundEpigenetic Modulation by Isothiocyanates
Ross, I. A. (2024) · Springer eBooks · doi:10.1007/978-3-031-63681-3_7
Gu, X.-N., Zhang, J., Ouyang, H., Wang, T., Huang, Z., & Ji, L. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5114053
Transcription factor NRF2: New therapeutic approach to modify Parkinson's disease progression
Rojo, A. I., Esteras, N., Cuadrado, A., & Lastres‐Becker, I. (2025) · Handbook of behavioral neuroscience · doi:10.1016/b978-0-443-21992-4.00025-7
Kinetic and Conformational Characterization of Transcriptional Activator-Coactivator Interactions.
Wang, N. (2013) · Deep Blue (University of Michigan)
Romero-Durán, M. A., Maldonado-Pichardo, M. C., Perez‐Aguilar, J. M., & Aguirre, V. M. B. (2026) · F1000Research · doi:10.12688/f1000research.177148.1
Romero-Durán, M. A., Maldonado-Pichardo, M. C., Perez‐Aguilar, J. M., & Aguirre, V. M. B. (2026) · F1000Research · doi:10.12688/f1000research.177148.2
Das, S., Roy, A., Bhattacharya, P., & Borah, A. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.178988
Impaired NF ‐ κB /Nrf2 Crosstalk in Rett Syndrome
Cordone, V., Vallese, A., Bianchi, A., Guiotto, A., Pecorelli, A., & Valacchi, G. (2026) · The FASEB Journal · doi:10.1096/fj.202601117r
“The acetyl-transferase complex CBP/p300 is known to target transcription factors, such as NF-κB p65 and Nrf2, enhancing their DNA-binding and transcriptional activity in response to physiological stress [9, 10].”
Hassen, H., Tarko, T., & Franczyk‐Żarów, M. (2026) · Applied Sciences · doi:10.3390/app16115254
Ramkumar, K. M., Ganesh, G. V., Gopinath, V., & Paulmurugan, R. (2026) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70949
“Conventionally, the signaling networks connecting Nrf2 and NF‐κB pathways mediated by small molecule drugs occur through the suppression of NF‐κB via the activation of Nrf2 [45].”
Sanjaya, B. R. L., Wahyudia, L. D., & Cho, M. K. (2026) · Journal of Ginseng Research · doi:10.1016/j.jgr.2026.101079
“In addition, p65 can promote histone deacetylase 3 (HDAC3) association with MafK, leading to dissociation of heterodimer formation with Nrf2 [59].”
Ajackson, M., Monteiro, E. B., Martins, F. F., Júnior, J. X. D. N., Neto, E. S. C., do Nascimento, M. D. S. M. A., Camillo, C. D. S., Vieira, J. R. C., Lisboa, P. C., Tavares, D. A. G., et al. (2026) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2026.112849
Computational approaches to pleiotropic drug design for intestinal ischemia-reperfusion injury
Hezekiah, O. S., Afolabi, O. A., Ajike, R. A., Oyekunle, O. S., Ezekiel Oladele, O. J. O., & KOMOLAFE, A. I. (2026) · In Silico Research in Biomedicine · doi:10.1016/j.insi.2026.100511
Nutraceuticals in Uro-Oncology: A Structured Expert Review and Precision-Oriented Framework
Erten, F., Kalemoglu, E., Küçük, Ö., & Şahin, K. (2026) · Nutrients · doi:10.3390/nu18152411
Roy, S. S., Hajra, S., Basu, A., & Bhattacharya, S. (2026) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2026.503951
Romero-Durán, M. A., Maldonado-Pichardo, M. C., Perez‐Aguilar, J. M., & Aguirre, V. M. B. (2026) · F1000Research · doi:10.12688/f1000research.177148.4
Zhou, J., Xu, C., Gu, C., Zhou, Q., Wang, H., Su, H., Zhou, M., Zhu, Q., Huang, G., & Xu, W. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1893871
“Mechanistically, Nrf2 and NF-k B competitively bind to the transcriptional coactivator CBP (35), thereby mutually inhibiting each other.”
Gu, Y., Miao, X., Fan, L., Cai, G., Song, R., Zou, H., Gu, J., Yuan, Y., Liu, X., Liu, Z., et al. (2026) · Food Research International · doi:10.1016/j.foodres.2026.120573
Gu, Y., Miao, X., Fan, L., Cai, G., Song, R., Zou, H., Gu, J., Yuan, Y., Liu, X., Liu, Z., et al. (2026) · Redox Report · doi:10.1080/13510002.2026.2724639
“Activation of the NF-κB subunit p65 can negatively regulate Nrf2 activation, participate in the negative regulation of the Nrf2 antioxidant pathway, and trigger ferroptosis [62,63].”
Reactive Oxygen Species in Breast Cancer: From Redox Dysregulation to ROS‐Responsive Therapeutics
Nikolovska, M., Stojchevski, R., Eftimov, A., Mladenov, M. I., Avtanski, D. B., & Hadzi‐Petrushev, N. (2026) · Cell Biochemistry and Function · doi:10.1002/cbf.70301
Oxidative Stress in Animals: A Systematic Analysis from Signaling Pathways to Biological Effects
Chang, L., Liu, C., & Huang, G. (2026) · Life · doi:10.3390/life16091516
“Conversely, persistent NF-κ B activation may attenuate the antioxidant capacity of Nrf2 either through competing for transcriptional cofactors [73].”
Dzhalilova, D. S., Fokichev, N., & Makarova, O. V. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1922856
“On the other hand, NF-k B reduces free CBP levels, which is an NRF2 transcriptional coactivator, by competing with the CBP CH1-KIX domain, and in addition prevents NRF2 binding to ARE by recruiting the corepressor histone deacetylase 3 (HDAC3) (128).”
Üstündağ, H., & Doğanay, S. (2026) · Purinergic Signalling · doi:10.1007/s11302-026-10185-z
“NF-κB activation suppresses Nrf2 transcriptional activity through competitive binding of the co-activator CREB-binding protein (CBP) [14]; NLRP3 inflammasome-derived reactive oxygen species (ROS) inhibit Nrf2 nuclear translocation [15]; and conversely, Nrf2/HO-1 activation exerts anti-inflammatory…”
A matter of balance: Heme oxygenase-1 at the crossroads of healthy and pathological aging
Wahba, S., & Stec, D. E. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.111006
Molecular Mechanisms of Obesity-Associated Oxidative Stress and Therapeutic Strategies
Wang, R., Luo, Y., Liu, L., Zhang, J., Li, R., & Zhang, N. (2026) · Antioxidants · doi:10.3390/antiox15091193
Tognarelli, E. I., Cornejo, D. A., del Campo, E. J., Reyes-Ramírez, R., Ortiz, G. E., Gaete-Argel, A., Kalergis, A. M., Bueno, S. M., Carreño, L. J., Soto‐Rifo, R., et al. (2026) · Antiviral Research · doi:10.1016/j.antiviral.2026.106545
Yang, Z., Chen, Y., Wen, C., Chang, Y., & Zhang, H. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.122476
Cysteine-based molecular switches: a focus on KEAP1 and BACH1 in regulating the antioxidant response
Feng, J., & Dinkova‐Kostova, A. T. (2026) · Archives of Toxicology · doi:10.1007/s00204-026-04562-1
Ferrer, B., Tinkov, A. A., Santamaria, A., Rocha, J. B., Skalny, A. V., Bowman, A. B., & Aschner, M. (2026) · Neurochemical Research · doi:10.1007/s11064-026-04898-1
Silencing without clearing: pharmacological modulation of the SASP in aging and disease
Fresser, L., Chrienová, Ž., Gebrt, J., Olekšák, P., Kuča, K., & Nepovimová, E. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1911529
“Mechanistically, resveratrol inhibits NF-κ B signaling (Lilja et al., 2020) and activates Nrf2, a negative regulator of NF-κ B, reinforcing anti-inflammatory effects (Liu et al., 2008).”
Keap1 Deficiency Promotes Macrophage M2 Polarization and Protects β Cells
Huang, B., Mou, L., Huang, X., Su, S., Hong, Z., & Zhang, Y. (2026) · Journal of Diabetes Research · doi:10.1155/jdr/6786708
“On the one hand, Nrf2 activation may attenuate upstream NF-κ B–activating signals by scavenging ROS [29, 30]; on the other, p65 may competitively bind CBP/ p300 or interact with Keap1 to repress Nrf2 activity [31, 32].”
Kong, E., Sánchez‐Taltavull, D., Rizzo, C. O., Suspitsyna, A., Stroka, D., & Polacek, N. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104439
“While the direct regulatory mechanism remains to be elucidated, our observations that vtRNA1-1 plays a key role in attenuating cellular ROS accumulation by modulating pivotal transcription factors, NF-κ B and NRF2, align with their well-known antagonistic crosstalk [58,59].”
NRF2: sensing stress, shaping immunity - keeping inflammation quiet and antigens out of sight
Benatzy, Y., & Brüne, B. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1974746
“Moreover, these data indicate that in contrast to Liu et al. (2008), who reported that p65 competes with NRF2 for CBP binding and promotes histone deacetylase 3-dependent hypoacetylation at ARE-containing gene loci, repression of pro-inflammatory genes can occur independently of p65-mediated CBP…”
Campbell, S., O’Reilly, R., Ahmed, O., McElheron, M., Chapman, W. C., & O’Farrelly, C. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.10.038
Geng, S., Guo, H., Tian, S., Miao, Q., Diao, Y., & Wang, X. (2026) · Biomedicines · doi:10.3390/biomedicines14102397
NRF2 in hypertrophic scarring: A stage-dependent redox hub poised between resolution and persistence
Thangboonjit, W., Pluempreecha, M., Soingam, T., & Panich, U. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104460
The Origins of Allergy: An Outside‐In, Bioenergetic Hypothesis
Smith, P. K., West, N. P., Preez, S. D., Sampson, H. A., Hellings, P. W., Price, D. B., O’Mahony, L., Venter, C., Akdiş, C. A., & Yosipovitch, G. (2026) · Allergy · doi:10.1111/all.70532
Metadata
- Authors
- Liu, G.-H., Qu, J., & Shen, X.
- Affiliations
- Chinese Academy of Sciences (CN)
- Corresponding author
- Shen, Xun
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 1783
- Issue
- 5
- Pages
- 713-727
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2113024198
- Cited by
- 697
- References
- 77
- Citations by year
- 2026: 54 · 2025: 45 · 2024: 51 · 2023: 47 · 2022: 68 · 2021: 51 · 2020: 59 · 2019: 59 · 2018: 47 · 2017: 38 · 2016: 32 · 2015: 33 · 2014: 15 · 2013: 28 · 2012: 13
- FWCI
- 7.82
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1904 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (30330250, 30570462)
- Shanghai Municipal Education Commission (E-04010)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- NF-κB p65, Nrf2, antioxidant response element, CBP, HDAC3, MafK, heme oxygenase-1, transcriptional repression, histone deacetylation, histone hypoacetylation, PKA phosphorylation, corepressor recruitment, anti-inflammatory signaling
- MeSH terms
- Histone Deacetylase 3, Antioxidants, Cell Line, Gene Expression Regulation, Histone Deacetylases, Humans, Transcription, Genetic, Trans-Activators, NF-kappa B, Response Elements, CREB-Binding Protein, MafK Transcription Factor, NF-E2-Related Factor 2, Transcription Factor RelA
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
