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Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease
Open accessAbstract
Nuclear factor-erythroid 2 p45-related factor 2 (Nrf2) regulates the basal and stress-inducible expression of a battery of genes encoding key components of the glutathione-based and thioredoxin-based antioxidant systems, as well as aldo-keto reductase, glutathione S-transferase, and Nad(p)h quinone oxidoreductase-1 drug-metabolizing isoenzymes along with multidrug-resistance-associated efflux pumps. It therefore plays a pivotal role in both intrinsic resistance and cellular adaptation to reactive oxygen species (ROS) and xenobiotics. Activation of Nrf2 can, however, serve as a double-edged sword because some of the genes it induces may contribute to chemical carcinogenesis by promoting futile redox cycling of polycyclic aromatic hydrocarbon metabolites or confer resistance to chemotherapeutic drugs by increasing the expression of efflux pumps, suggesting its cytoprotective effects will vary in a context-specific fashion. In addition to cytoprotection, Nrf2 also controls genes involved in intermediary metabolism, positively regulating those involved in NADPH generation, purine biosynthesis, and the β-oxidation of fatty acids, while suppressing those involved in lipogenesis and gluconeogenesis. Nrf2 is subject to regulation at multiple levels. Its ability to orchestrate adaptation to oxidants and electrophiles is due principally to stress-stimulated modification of thiols within one of its repressors, the Kelch-like ECH-associated protein 1 (Keap1), which is present in the cullin-3 RING ubiquitin ligase (CRL) complex CRLKeap1. Thus modification of Cys residues in Keap1 blocks CRLKeap1 activity, allowing newly translated Nrf2 to accumulate rapidly and induce its target genes. The ability of Keap1 to repress Nrf2 can be attenuated by p62/sequestosome-1 in a mechanistic target of rapamycin complex 1 (mTORC1)-dependent manner, thereby allowing refeeding after fasting to increase Nrf2-target gene expression. In parallel with repression by Keap1, Nrf2 is also repressed by β-transducin repeat-containing protein (β-TrCP), present in the Skp1-cullin-1-F-box protein (SCF) ubiquitin ligase complex SCFβ-TrCP. The ability of SCFβ-TrCP to suppress Nrf2 activity is itself enhanced by prior phosphorylation of the transcription factor by glycogen synthase kinase-3 (GSK-3) through formation of a DSGIS-containing phosphodegron. However, formation of the phosphodegron in Nrf2 by GSK-3 is inhibited by stimuli that activate protein kinase B (PKB)/Akt. In particular, PKB/Akt activity can be increased by phosphoinositide 3-kinase and mTORC2, thereby providing an explanation of why antioxidant-responsive element-driven genes are induced by growth factors and nutrients. Thus Nrf2 activity is tightly controlled via CRLKeap1 and SCFβ-TrCP by oxidative stress and energy-based signals, allowing it to mediate adaptive responses that restore redox homeostasis and modulate intermediary metabolism. Based on the fact that Nrf2 influences multiple biochemical pathways in both positive and negative ways, it is likely its dose-response curve, in terms of susceptibility to certain degenerative disease, is U-shaped. Specifically, too little Nrf2 activity will lead to loss of cytoprotection, diminished antioxidant capacity, and lowered β-oxidation of fatty acids, while conversely also exhibiting heightened sensitivity to ROS-based signaling that involves receptor tyrosine kinases and apoptosis signal-regulating kinase-1. By contrast, too much Nrf2 activity disturbs the homeostatic balance in favor of reduction, and so may have deleterious consequences including overproduction of reduced glutathione and NADPH, the blunting of ROS-based signal transduction, epithelial cell hyperplasia, and failure of certain cell types to differentiate correctly. We discuss the basis of a putative U-shaped Nrf2 dose-response curve in terms of potentially competing processes relevant to different stages of tumorigenesis.
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“This interaction is mediated by a 349DPSTGE354 motif in p62’s Keap1-interacting region (KIR) that resembles the ETGE motif in the Keap1-binding domain of Nrf2 [79,80,81].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [79]
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“In response to elevated levels of reactive oxygen species (ROS) and environmental toxins or to nutrient and metabolic changes through mTOR signaling and insulin/IGF signaling, NRF/SKN-1 activates the expression of genes involved in cellular protection (Blackwell et al., 2015; Tebay et al., 2015).”
From The Aging Epigenome (2016) · cites this paper as Tebay et al., 2015
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Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Toxic potential of materials at the nanolevel
Nel, A., Xia, T., Mädler, L., & Li, N. (2006) · Science · doi:10.1126/science.1114397 · Cited by 9,324
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,897
Comprehensive molecular profiling of lung adenocarcinoma
The Cancer Genome Atlas Research Network (2014) · Nature · doi:10.1038/nature13385 · Cited by 5,732
Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,131
Comprehensive genomic characterization of head and neck squamous cell carcinomas
The Cancer Genome Atlas Network (2015) · Nature · doi:10.1038/nature14129 · Cited by 4,147
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Items 401–500 of 842
Esselun, C., Dieter, F., Sus, N., Frank, J., & Eckert, G. P. (2022) · Nutrients · doi:10.3390/nu14091694 · Cited by 24
Redox-Regulation in Cancer Stem Cells
Lendeckel, U., & Wolke, C. (2022) · Biomedicines · doi:10.3390/biomedicines10102413 · Cited by 24
Bernuzzi, F., Märtens, A., Saha, S., Troncoso‐Rey, P., Ludwig, T., Hiller, K., Mithen, R. F., Korcsmáros, T., & Τράκα, Μ. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102878 · Cited by 25
Galván-Álvarez, V., Gallego-Selles, Á., Martinez‐Canton, M., García-Gonzalez, E., Gelabert‐Rebato, M., Ponce‐González, J. G., Larsen, S., Morales‐Álamo, D., Losa‐Reyna, J., Pérez-Suárez, I., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.10.393 · Cited by 26
Han, X., Wang, H., Du, F., Zeng, X., & Guo, C. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115855 · Cited by 25
Li, Q., Karim, A. F., Ding, X., Das, B., Dobrowolski, C. N., Gibson, R. M., Quiñones‐Mateu, M. E., Karn, J., & Rojas, R. E. (2016) · Scientific Reports · doi:10.1038/srep27566 · Cited by 23
Tutakhail, A., Nazari, Q. A., Lebsir, D., Kerdine‐Römer, S., & Coudoré, F. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.08.004 · Cited by 24
Fu, J., Ni, C., Ni, H., Xu, L., He, Q., Pan, H., Huang, D., Sun, Y., Luo, G., Liu, M., et al. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15468 · Cited by 24
NFκB Regulates Muscle Development and Mitochondrial Function
Valentine, J. M., Li, M. E., Shoelson, S. E., Zhang, N., Reddick, R. L., & Musi, N. (2020) · The Journals of Gerontology: Series A · doi:10.1093/gerona/gly262 · Cited by 23
Hydrogen Sulfide: A Worthwhile Tool in the Design of New Multitarget Drugs
Sestito, S., Nesi, G., Pi, R., Macchia, M., & Rapposelli, S. (2017) · Frontiers in Chemistry · doi:10.3389/fchem.2017.00072 · Cited by 23
Shilovsky, G. A., Putyatina, T. S., Васильевна, М. Г., Селиверстов, А. В., Ashapkin, V. V., Сорокина, Е. В., Markov, A. V., & Skulachev, V. P. (2021) · Biochemistry (Moscow) · doi:10.1134/s0006297921040052 · Cited by 23
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van der Merwe, M., van Niekerk, G., Fourie, C., du Plessis, M., & Engelbrecht, A. (2021) · Cellular Oncology · doi:10.1007/s13402-021-00623-y · Cited by 24
Role of Nrf2 and HO-1 in intervertebral disc degeneration
Zhang, C., Hu, X., Zhang, G., Liu, M.-Q., Chen, H., & Kang, X. (2022) · Connective Tissue Research · doi:10.1080/03008207.2022.2089565 · Cited by 23
Muchtaridi, M., Amirah, S. R., Harmonis, J. A., & Ikram, E. H. K. (2022) · Antioxidants · doi:10.3390/antiox11081551 · Cited by 26
Kaziród, K., Myszka, M., Dulak, J., & Łoboda, A. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04636-0 · Cited by 24
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Puente-Cobacho, B., Varela‐López, A., Quiles, J. L., & Ramírez, L. V. (2023) · Cancer and Metastasis Reviews · doi:10.1007/s10555-022-10077-9 · Cited by 25
Smith, M. J., Yang, F., Griffiths, A., Morrell, A. P., Chapple, S. J., Siow, R. C. M., Stewart, T. J., Maret, W., & Mann, G. E. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102712 · Cited by 23
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Snow, W. M., Pahlavan, P. S., Djordjevic, J., McAllister, D., Platt, E. E., Alashmali, S. M., Bernstein, M. J., Suh, M., & Albensi, B. C. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00070 · Cited by 23
Yu, Q., Xia, Z., Liong, E. C., & Tipoe, G. L. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10787 · Cited by 23
Role of Nrf2 and exercise in alleviating COPD-induced skeletal muscle dysfunction
Jiang, M., Li, P., Wang, Y., Cao, Y., Han, X., Jiang, L., Liu, X., & Wu, W. (2023) · Therapeutic Advances in Respiratory Disease · doi:10.1177/17534666231208633 · Cited by 22
Xu, J., Tao, L., Jiang, L., Lai, J., Hu, J., & Tang, Z. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s491885 · Cited by 22
Choi, J.-I., Kim, J., & Choung, S.-Y. (2019) · Europe PMC (PubMed Central) · Cited by 22
Huang, X., Xu, S., Yu, L.-J., Zhou, Y., Zhou, Y., & Liu, Z. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6635080 · Cited by 22
Ruan, Q., Wen, C., Jin, G., Yuan, Z., Yang, X., Wen, Z., Huang, G., Li, G., Deng, J., & Bai, Y. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154990 · Cited by 22
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Li, H., Li, D., He, Z., Fan, J., Li, Q., Liu, X., Guo, P., Zhang, H., Chen, S., Li, Q., et al. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.09.002 · Cited by 22
Nabih, H. K. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108326 · Cited by 22
Lipid-derived reactive aldehydes link oxidative stress to cell senescence
Flor, A. C., & Kron, S. J. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.275 · Cited by 24
Modulating Nrf2 to control lipid peroxidation and ferroptosis: implications for cancer management
Tunc, R., Ateş, İ., Yılmaz, B., Medoro, A., Davinelli, S., Süzen, S., & Saso, L. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1701249 · Cited by 21
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Smith, R. E. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666190517113533 · Cited by 22
Effects of acute iron overload on Nrf2-related glutathione metabolism in rat brain
Piloni, N. E., Vargas, R., Fernández, V., Videla, L. A., & Puntarulo, S. (2021) · BioMetals · doi:10.1007/s10534-021-00324-x · Cited by 21
Proteomic profile of the effects of low-dose bisphenol A on zebrafish ovaries
Molina-López, A. M., Abril, N., Lora-Benítez, A. J., Huertas-Abril, P. V., Ayala-Soldado, N., Blanco, C., & Moyano, R. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112435 · Cited by 23
Ishii, T., Warabi, E., & Mann, G. E. (2023) · Antioxidants · doi:10.3390/antiox12020274 · Cited by 21
Ni, X., Ye, C., Xi, Y., Zhang, Y., Hou, Y., Zheng, Q., Chen, Z., Wang, L., Weng, X., Yang, C., et al. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176110 · Cited by 23
Stępniewski, J., Pacholczak, T., Skrzypczyk, A., Cieśla, M., Szade, A., Szade, K., Bidanel, R., Langrzyk, A., Grochowski, R., Vandermeeren, F., et al. (2018) · IUBMB Life · doi:10.1002/iub.1711 · Cited by 21
Tain, Y., Leu, S., Lee, W., Wu, K. L. H., & Chan, J. Y. H. (2018) · Molecules · doi:10.3390/molecules23040886 · Cited by 21
Giudice, A., Barbieri, A., Bimonte, S., Cascella, M., Cuomo, A., Crispo, A., D'Arena, G. F., Galdiero, M., Pepa, M. E. D., Botti, G., et al. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s183192 · Cited by 21
Murray, J. R., de la Vega, L., Hayes, J. D., Duan, L., & Penning, T. M. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00399 · Cited by 21
Self-citationSun, W., Zhang, W., Yu, J., Lu, Z., & Yu, J. (2020) · International Journal of Neuroscience · doi:10.1080/00207454.2020.1766458 · Cited by 22
Wang, Y., Wang, C., Xie, M., Tang, T., Wang, Z., & Nie, X. (2021) · Environmental Pollution · doi:10.1016/j.envpol.2021.117879 · Cited by 21
Zhang, J., Li, H., Yang, H., Lin, J., Wang, Y., Zhang, Q., Gao, W., & Xu, H. (2020) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-020-09969-w · Cited by 20
Chen, W., Su, J., Cai, S., & Shi, C. (2021) · Bioengineered · doi:10.1080/21655979.2021.1943603 · Cited by 20
Zhou, J., Fang, F., Qi, J., Li, T., Zhang, L., Liu, H., Lv, J., Xu, T., Wu, F., Song, C., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.10.274 · Cited by 20
Ding, Y., Fang, Y., Pan, Y., Lan, J., Xu, T., Zhang, W., Mao, H., Gu, Z., Chen, X., & Shen, Q. (2022) · Food & Function · doi:10.1039/d2fo02463b · Cited by 20
Mitochondrial Alterations in Prostate Cancer: Roles in Pathobiology and Racial Disparities
Vikramdeo, K. S., Sharma, A., Anand, S., Sudan, S. K., Singh, S., Singh, A. P., & Dasgupta, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054482 · Cited by 20
Qin, Y., Poulsen, C., Narayanan, D., Chan, C. B., Chen, X., Montes, B. R., Tran, K. T., Mukminova, E., Lin, C., Gajhede, M., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01221 · Cited by 23
Priftis, A., Soursou, V., Makiou, A.-S., Tekos, F., Veskoukis, A. S., Tsantarliotou, M. P., Taitzoglou, I., & Kouretas, D. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.01.012 · Cited by 21
Tsuneyoshi, T., Kunimura, K., & Morihara, N. (2019) · Nitric Oxide · doi:10.1016/j.niox.2019.01.003 · Cited by 20
Xiang, Y., Halin, J., Fan, Z., Hu, S., Wang, M., Qiu, L., Zhang, Z., Mattjus, P., & Zhang, Y. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.09.039 · Cited by 20
Baldwin, W. S. (2019) · Nuclear Receptor Research · doi:10.32527/2019/101447 · Cited by 20
Modulation of NRF2/ARE pathway- and cell death-related genes during drug-induced liver injury
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Zbinden‐Foncea, H., Castro‐Sepúlveda, M., Fuentes, J., & Speisky, H. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867329666211217100020 · Cited by 19
Streyczek, J., Apweiler, M., Sun, L., & Fiebich, B. L. (2022) · Molecules · doi:10.3390/molecules27030784 · Cited by 20
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Wolowczyk, C., Neckmann, U., Aure, M. R. R., Hall, M., Johannessen, B., Zhao, S., Skotheim, R. I., Andersen, S. B., Zwiggelaar, R. T., Steigedal, T. S., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.03.029 · Cited by 21
Galli, F., Bartolini, D., & Ronco, C. (2024) · European Journal of Clinical Investigation · doi:10.1111/eci.14229 · Cited by 21
Bayliak, M. M., Demianchuk, O., Gospodaryov, D. V., Abrat, O., Lylyk, M. P., Storey, K. B., & Lushchak, V. I. (2020) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2020.110746 · Cited by 19
Age-related alteration in HNE elimination enzymes
Zhang, H., Morgan, T. E., & Forman, H. J. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108749 · Cited by 20
Jiang, Z., Wang, W., Zhao, Y., Li, T., Xin, D., Gai, C., Liu, D., & Wang, Z. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.12.016 · Cited by 19
Dual NRF2 paralogs in Coho salmon and their antioxidant response element targets☆
Ramsden, R., & Gallagher, E. (2016) · Redox Biology · doi:10.1016/j.redox.2016.07.001 · Cited by 19
Regulation of the CNC-bZIP transcription factor Nrf2 by Keap1 and the axis between GSK-3 and β-TrCP
Hayes, J. D., Ebisine, K., Sharma, R. S., Chowdhry, S., Dinkova‐Kostova, A. T., & Sutherland, C. D. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.003 · Cited by 19
Self-citationDanielli, N. M., Trevisan, R., Mello, D. F., Fischer, K., Deconto, V. S., Bianchini, A., Bainy, A. C. D., & Dafré, A. L. (2017) · Marine Environmental Research · doi:10.1016/j.marenvres.2017.07.020 · Cited by 19
Simenauer, A., Assefa, B., Rios-Ochoa, J., Geraci, K. P., Hybertson, B. M., Gao, B., McCord, J. M., Elajaili, H. B., Nozik‐Grayck, E., & Cota‐Gomez, A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.06.015 · Cited by 19
Patra, U., Mukhopadhyay, U., Mukherjee, A., Sarkar, R., & Chawla‐Sarkar, M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7289120 · Cited by 19
Lim, J. C.-H., Jiang, L., Lust, N. G., & Donaldson, P. J. (2024) · Antioxidants · doi:10.3390/antiox13101193 · Cited by 21
Chu, X., Zhang, X., Gong, X., Zhou, H., & Cai, C. (2020) · Molecular and Cellular Probes · doi:10.1016/j.mcp.2020.101529 · Cited by 18
Kaseda, S., Sannomiya, Y., Horizono, J., Kuwazuru, J., Suico, M. A., Ogi, S., Sasaki, R., Sunamoto, H., Fukiya, H., Nishiyama, H., et al. (2021) · Kidney360 · doi:10.34067/kid.0004572021 · Cited by 18
da Costa, R. M., Dias, M. C., Alves, J. V., Silva, J. L. M., Rodrigues, D., da Silva, J. F., Francescato, H. D. C., Ramalho, L. N. Z., Coimbra, T. M., & Tostes, R. C. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115982 · Cited by 19
Antioxidants for Early Treatment of Type 2 Diabetes in Rodents and Humans: Lost in Translation?
Robertson, R. P. (2024) · Diabetes · doi:10.2337/db23-0901 · Cited by 18
Song, X., Ding, J., Zhang, Y., Zhu, M., Peng, Y., Wang, Z., Pan, G., & Zou, H. (2024) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2024.134047 · Cited by 20
Gregorio, J. D., Giuseppe, L. D., Terreri, S., Rossi, M., Battafarano, G., Pagliarosi, O., Flati, V., & Fattore, A. D. (2024) · Cells · doi:10.3390/cells13060537 · Cited by 18
Gajos‐Draus, A., Duda, M. K., & Berȩsewicz, A. (2017) · Physiological Reports · doi:10.14814/phy2.13474 · Cited by 18
Jang, D. E., Song, J., Park, J., Yoon, S.-H., & Bae, Y. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.5.044 · Cited by 18
Iñesta-Vaquera, F., Navasumrit, P., Henderson, C. J., Frangova, T. G., Honda, T., Dinkova‐Kostova, A. T., Ruchirawat, M., & Wolf, C. R. (2020) · Environmental Pollution · doi:10.1016/j.envpol.2020.116053 · Cited by 17
Self-citationGroh, I. A. M., Riva, A., Braun, D., Sutherland, H. G. E., Williams, O., Bakuradze, T., Pahlke, G., Richling, E., Haupt, L. M., Griffiths, L. R., et al. (2020) · Antioxidants · doi:10.3390/antiox10010027 · Cited by 18
Qin, Y., Zhang, H., Liu, Q., Jiang, B., Chen, J., & Zhang, T. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104460 · Cited by 18
Trinity, J. D., Drummond, M. J., Fermoyle, C. C., McKenzie, A. I., Supiano, M. A., & Richardson, R. S. (2022) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00607.2021 · Cited by 18
Fiorani, M., Guidarelli, A., Capellacci, V., Cerioni, L., Crinelli, R., & Cantoni, O. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.03.008 · Cited by 18
Choi, J.-W., Im, J. Y., & Balakrishnan, R. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118299 · Cited by 19
Role of STAT3 and NRF2 in Tumors: Potential Targets for Antitumor Therapy
Tian, Y., Liu, H., Wang, M., Wang, R., Yi, G., Zhang, M., & Chen, R. (2022) · Molecules · doi:10.3390/molecules27248768 · Cited by 18
Toyama, T., Kudryashova, T. V., 麻子, 市., Lenna, S., Looney, A. P., Shen, Y., Jiang, L., Teos, L., Avolio, T., Lin, D., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-33779-8 · Cited by 16
Biagiotti, S., Bianchi, M., Rossi, L., Chessa, L., & Magnani, M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0216668 · Cited by 17
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Metadata
- Authors
- Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D.
- Affiliations
- University of Dundee (GB)
- AstraZeneca (United Kingdom) (GB)
- University of Pennsylvania (US)
- Corresponding author
- Hayes, John D.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 88
- Issue
- Pt B
- Pages
- 108-146
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC4659505
- OpenAlex
- W1421415727
- Cited by
- 837
- References
- 514
- Citations by year
- 2026: 56 · 2025: 54 · 2024: 65 · 2023: 89 · 2022: 90 · 2021: 92 · 2020: 103 · 2019: 88 · 2018: 72 · 2017: 75 · 2016: 45 · 2015: 7
- FWCI
- 6.46
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Funders
- Cancer Research UK (C4909/A13786)
- MRC (MR/J001465/1)
- MRC ITTP (1313992)
- BBSRC Industrial CASE (BB/L01405X/1)
- BBSRC (BB/L01923X/1, P30-ES013508)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- Nrf2, redox stress, Keap1, mTORC1, p62/sequestosome 1, nutrient sensing, energy status, reactive oxygen species, xenobiotic metabolism, drug resistance, multidrug resistance, glutathione, thioredoxin, antioxidant defense, degenerative diseases
- MeSH terms
- Animals, Humans, Oxidation-Reduction, Signal Transduction, Oxidative Stress, NF-E2-Related Factor 2, Carcinogenesis
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