The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Increased Protein Stability as a Mechanism That Enhances Nrf2-mediated Transcriptional Activation of the Antioxidant Response Element
Open accessAbstract
Nrf2 (NF-E2-related factor 2) is a central transcription factor involved in the transcriptional activation of many genes encoding phase II drug-metabolizing enzymes via the antioxidant response element. Nrf2 has previously been found to undergo nuclear translocation by a phosphorylation-dependent mechanism mediated by protein kinase C in HepG2 cells treated with tert-butylhydroquinone, beta-naphthoflavone, or 12-O-tetradecanoylphorbol-13-acetate. In the present report, we have found that the levels of Nrf2 were increased in cells treated with tert-butylhydroquinone or beta-naphthoflavone by a post-transcriptional mechanism. Treatment of HepG2 cells with cycloheximide resulted in the loss of Nrf2 within 30 min. By contrast, treatment with the proteasome inhibitors (lactacystin or MG-132) caused an accumulation of Nrf2 as well as an induction of reporter gene activity in cells transfected with the GSTA2 antioxidant response element-chloramphenicol acetyl transferase construct. Similarly, the protein phosphatase inhibitor okadaic acid also caused an accumulation of Nrf2, whereas the reverse effects were observed with PD 98059 and U 0126, two compounds that block the activation of the MAPK/ERK signaling cascade. These data suggest that Nrf2 is degraded by the ubiquitin-dependent pathway and that phosphorylation of Nrf2 leads to an increase in its stability and subsequent transactivation activity.
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
“Nrf2 regulates the expression of a multitude of antioxidant and phase II enzyme genes and is negatively regulated by Kelch-like ECH-associated protein (Keap1) [49], a substrate adaptor protein that binds to Nrf2 in the cytosol to facilitate its polyubiquitination by the Cullin 3 (Cul3) E3 ubiquitin ligase for proteasomal degradation [50,51,52].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [50]
In the citing paper
“Under basal conditions, Nrf2 has a short half-life of only 10–30 min [50,77].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [50]
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
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999
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
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312
Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947
Moi, P., Chan, K., Asunis, I., Cao, A., & Kan, Y. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.21.9926 · Cited by 1,607
Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., & Yamamoto, M. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.21.16023 · Cited by 1,473
Rushmore, T. H., Morton, M. R., & Pickett, C. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99004-6 · Cited by 1,464
Self-citationOkadaic acid: a new probe for the study of cellular regulation
Cohen, P., Holmes, C. F. B., & Tsukitani, Y. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90192-e · Cited by 1,373
Nrf2, a Cap'n'Collar Transcription Factor, Regulates Induction of the Heme Oxygenase-1 Gene
Alam, J., Stewart, D. P., Touchard, C. L., Boinapally, S., Choi, A. M. K., & Cook, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26071 · Cited by 1,284
Flagged first, then by citations
Research works printed but not linked: 1
- McMahon, 2001, Cancer Res., 61, 3299
Cited by
Sorted by citations
Items 101–200 of 617
Activation of hepatic Nrf2 in vivo by acetaminophen in CD-1 mice
Goldring, C. E., Kitteringham, N. R., Elsby, R., Randle, L. E., Clement, Y. N., Williams, D. P., McMahon, M. J., Hayes, J. D., Itoh, K., Yamamoto, M. P., et al. (2004) · Hepatology · doi:10.1002/hep.20183 · Cited by 207
Lv, H., Yu, Z., Zheng, Y., Wang, L., Qin, F. X.-F., Cheng, G., & Ci, X. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.13188 · Cited by 203
Oncogenic functions of the transcription factor Nrf2
Gañán‐Gómez, I., Wei, Y., Yang, H., Boyano-Adánez, M. C., & Garcia‐Manero, G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.041 · Cited by 203
Nrf2 as a target for cancer chemoprevention
Yu, X. Y., & Kensler, T. W. (2005) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.04.017 · Cited by 199
Nuclear Import and Export Signals in Control of Nrf2
Jain, A. K., Bloom, D. A., & Jaiswal, A. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502083200 · Cited by 195
RetractedRegulation of Nrf2 Transactivation Domain Activity
Shen, G., Hebbar, V., Nair, S., Xu, C., Li, W., Lin, W., Keum, Y.-S., Han, J., Gallo, M. A., & Kong, A.-N. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401368200 · Cited by 194
Pro-Oxidant Activity of Flavonoids Induces EpRE-Mediated Gene Expression
Lee-Hilz, Y. Y., Boerboom, A.-M. J. F., Westphal, A. H., van Berkel, W. J. H., Aarts, J. M. M. J. G., & Rietjens, I. M. C. M. (2006) · Chemical Research in Toxicology · doi:10.1021/tx060157q · Cited by 192
Multiple regulations of Keap1/Nrf2 system by dietary phytochemicals
Qin, S., & Hou, D. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201501017 · Cited by 191
Shen, G., & Kong, A. T. (2009) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.680 · Cited by 185
Hayes, J. D., Chowdhry, S., Dinkova‐Kostova, A. T., & Sutherland, C. D. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150011 · Cited by 187
Potential Applications of NRF2 Inhibitors in Cancer Therapy
Panieri, E., & Saso, L. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8592348 · Cited by 189
Vargas, M. R., Pehar, M., Cassina, P., Beckman, J. S., & Barbeito, L. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03742.x · Cited by 182
Zerumbone, a tropical ginger sesquiterpene, activates phase II drug metabolizing enzymes
Nakamura, Y., Yoshida, C., Murakami, A., Ohigashi, H., Osawa, T., & Uchida, K. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.042 · Cited by 182
Mitogen-Activated Protein Kinases in Mammalian Oxidative Stress Responses
Runchel, C., Matsuzawa, A., & Ichijo, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3733 · Cited by 179
Jian, Z., Li, K., Liu, L., Zhang, Y., Zhou, Z., Li, C., & Gao, T. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.56 · Cited by 175
The Keap1–Nrf2 Cell Defense Pathway – A Promising Therapeutic Target?
Copple, I. M. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-398339-8.00002-1 · Cited by 174
Liu, T., Lv, Y., Zhao, J., You, Q., & Jiang, Z. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.03.034 · Cited by 177
Varı́, R., D’Archivio, M., Filesi, C., Carotenuto, S., Scazzocchio, B., Santangelo, C., Giovannini, C., & Masella, R. (2010) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.03.008 · Cited by 174
The role of phytochemicals in inhibition of cancer and inflammation: New directions and perspectives
Issa, A., Volate, S. R., & Wargovich, M. J. (2006) · Journal of Food Composition and Analysis · doi:10.1016/j.jfca.2006.02.009 · Cited by 169
Nrf2 as regulator of innate immunity: A molecular Swiss army knife!
Battino, M. A., Giampieri, F., Pistollato, F., Sureda, A., de Oliveira, M. R., Pittalà, V., Fallarino, F., Nabavi, S. F., Atanasov, A. G., & Nabavi, S. M. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.12.012 · Cited by 170
Papaiahgari, S. R., Kleeberger, S. R., Cho, H., Kalvakolanu, D. V., & Reddy, S. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408275200 · Cited by 167
Giuliani, M. E., & Regoli, F. (2014) · Aquatic Toxicology · doi:10.1016/j.aquatox.2014.03.003 · Cited by 166
Warabi, E., Takabe, W., Minami, T., Inoue, K., Itoh, K., Yamamoto, M. P., Ishii, T., Kodama, T., & Noguchi, N. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.10.043 · Cited by 165
Nrf2 expression modifies influenza A entry and replication in nasal epithelial cells
Kesic, M. J., Simmons, S. O., Bauer, R. N., & Jaspers, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.027 · Cited by 171
Curcumin, Hormesis and the Nervous System
Scuto, M. C., Mancuso, C., Tomasello, B., Ontario, M. L., Cavallaro, A. S., Frasca, F., Maiolino, L., Salinaro, A. T., Calabrese, E. J., & Calabrese, V. (2019) · Nutrients · doi:10.3390/nu11102417 · Cited by 157
Expression of NAD(P)H:quinone oxidoreductase in the normal and Parkinsonian substantia nigra
Muiswinkel, F. L. V., de Vos, R. A. I., Bol, J. G. J. M., Andringa, G., Steur, E. N. H. J., Ross, D., Siegel, D. M., & Drukarch, B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.12.010 · Cited by 155
Emerging promise of sulforaphane-mediated Nrf2 signaling cascade against neurological disorders
Uddin, M. S., Mamun, A. A., Jakaria, M., Thangapandiyan, S., Ahmad, J., Rahman, M. A., Mathew, B., Abdel-Daim, M. M., & Aleya, L. (2020) · Science of The Total Environment · doi:10.1016/j.scitotenv.2019.135624 · Cited by 154
Antioxidant Functions of the Aryl Hydrocarbon Receptor
Dietrich, C. (2016) · Stem Cells International · doi:10.1155/2016/7943495 · Cited by 148
Wang, H., Sun, X.-B., Xu, Y.-X., Zhao, H., Zhu, Q.-Y., & Zhu, C.-Q. (2010) · Brain Research · doi:10.1016/j.brainres.2010.08.100 · Cited by 147
Reactive Oxygen Species and Oxidative Stress
Giulio, R. T. D., & Hinton, D. E. (2008) · CRC Press eBooks · doi:10.1201/9780203647295-12 · Cited by 145
Holtzclaw, W. D., Dinkova‐Kostova, A. T., & Talalay, P. (2004) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2003.11.013 · Cited by 145
Vargas, M. R., Pehar, M., Cassina, P., Palma, L. M., Thompson, J. A., Beckman, J. S., & Barbeito, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501920200 · Cited by 146
Danilov, C. A., Chandrasekaran, K., Racz, J. L., Soane, L., Zielke, C. L., & Fiskum, G. M. (2008) · Glia · doi:10.1002/glia.20793 · Cited by 141
Zhu, C., Dong, Y., Liu, H., Ren, H. N., & Cui, Z.-H. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.11.089 · Cited by 141
Bertinato, J., & L’Abbé, M. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302242200 · Cited by 143
Subcellular localization and cytoplasmic complex status of endogenous Keap1
Watai, Y., Kobayashi, A., Nagase, H., Mizukami, M., McEvoy, J. D., Singer, J. D., Itoh, K., & Yamamoto, M. P. (2007) · Genes to Cells · doi:10.1111/j.1365-2443.2007.01118.x · Cited by 141
Identification of polymorphisms in the promoter region of the human NRF2 gene
Yamamoto, T., Yoh, K., Kobayashi, A., Ishii, Y., Kure, S., Kôyama, A., Sakamoto, T., Sekizawa, K., Motohashi, H., & Yamamoto, M. P. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.112 · Cited by 140
Stacy, D., Ely, K., Massion, P. P., Yarbrough, W. G., Hallahan, D. E., Sekhar, K. R., & Freeman, M. L. (2006) · Head & Neck · doi:10.1002/hed.20430 · Cited by 136
Zhai, X., Lin, M., Zhang, F., Hu, Y. W., Xu, X., Li, Y., Liu, K., Ma, X., Tian, X., & Yao, J. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200536 · Cited by 134
Alves-Lopes, R., Neves, K. B., Tostes, R. C., Montezano, A. C. I., & Touyz, R. M. (2015) · Hypertension · doi:10.1161/hypertensionaha.115.06163 · Cited by 133
Chen, H., Chen, Y.-T., Huang, Y.-W., Tsai, H., & Kuo, C. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.012 · Cited by 133
Jeong, W., Keum, Y.-S., Chen, C., Jain, M. R., Shen, G., Kim, J. H., Li, W., & Kong, A. T. (2005) · BMB Reports · doi:10.5483/bmbrep.2005.38.2.167 · Cited by 133
Proteasome Inhibition Induces Glutathione Synthesis and Protects Cells from Oxidative Stress
Yamamoto, N., Sawada, H., Izumi, Y., Kume, T., Katsuki, H., Shimohama, S., & Akaike, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603712200 · Cited by 133
Kokot, A., Metze, D., Mouchet, N., Galibert, M.-D., Schiller, M., Luger, T. A., & Böhm, M. (2009) · Endocrinology · doi:10.1210/en.2008-1315 · Cited by 132
Antioxidant Responses and NRF2 in Synergistic Developmental Toxicity of PAHs in Zebrafish
Timme‐Laragy, A. R., Tiem, L. A. V., Linney, E. A., & Giulio, R. T. D. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp038 · Cited by 130
Liu, J., Hu, Y., Feng, Y., Jiang, Y., Guo, Y., Liu, Y., Chen, X., Yang, J., Chen, Y., Mao, Q.-S., et al. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01620-z · Cited by 130
Zhang, L., Xu, L.-Y., Tang, F., Liu, D., Zhao, X.-L., Zhang, J.-N., Xia, J., Wu, J.-J., Yang, Y., Peng, C. Y., et al. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2023.12.020 · Cited by 130
Kalthoff, S., Ehmer, U., Freiberg, N., Manns, M. P., & Strassburg, C. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.075770 · Cited by 129
NRF2, cancer and calorie restriction
Martín‐Montalvo, A., Villalba, J. M., Navas, P., & de Cabo, R. (2010) · Oncogene · doi:10.1038/onc.2010.492 · Cited by 129
Yuan, X., Xu, C., Pan, Z., Keum, Y., Kim, J. H., Shen, G., Yu, S., Oo, K. T., Ma, J., & Kong, A. T. (2006) · Molecular Carcinogenesis · doi:10.1002/mc.20234 · Cited by 128
Camp, N. D., James, R. G., Dawson, D. W., Yan, F., Davison, J. M., Houck, S. A., Tang, X., Zheng, N., Major, M. B., & Moon, R. T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316471 · Cited by 128
Liu, Y., Chan, F., Sun, H., Yan, J., Fan, D., Zhao, D., An, J., & Zhou, D. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.10.009 · Cited by 126
Truong, M., Kim, H. G., Khanal, T., Choi, J. H., Kim, D. H., Jeong, T. C., & Jeong, H. G. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.05.010 · Cited by 124
Merchant, A. A., Singh, A., Matsui, W. H., & Biswal, S. S. (2011) · Blood · doi:10.1182/blood-2011-05-355362 · Cited by 123
Active defense under oxidative stress. The antioxidant responsive element
Lyakhovich, V. V., Андреевич, В. В., Зенков, Н. К., & Брониславовна, М. Е. (2006) · Biochemistry (Moscow) · doi:10.1134/s0006297906090033 · Cited by 123
Utility of siRNA against Keap1 as a strategy to stimulate a cancer chemopreventive phenotype
Devling, T. W. P., LINDSAY, C. D., McLellan, L. I., McMahon, M. J., & Hayes, J. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501475102 · Cited by 122
Staurengo‐Ferrari, L., Badaro‐Garcia, S., Hohmann, M. S., Manchope, M. F., Zaninelli, T. H., Casagrande, R., & Verri, W. A., Jr. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01536 · Cited by 127
The Role of the Nrf2 Signaling in Obesity and Insulin Resistance
Li, S., Eguchi, N., Lau, H., & Ichii, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186973 · Cited by 120
Granado‐Serrano, A. B., Martín, M. Á., Haegeman, G., Goya, L., Bravo, L., & Ramos, S. (2009) · British Journal Of Nutrition · doi:10.1017/s0007114509991747 · Cited by 115
Regulation of Nrf2-Mediated Phase II Detoxification and Anti-oxidant Genes
Keum, Y. (2012) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2012.20.2.144 · Cited by 114
Costa, G., Francisco, V., Lopes, M. C., Cruz, M. T., & Batista, M. T. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712800672049 · Cited by 113
Kim, J.-H., Thimmulappa, R. K., Kumar, V., Cui, W., Kumar, S., Kombairaju, P., Zhang, H., Margolick, J. B., Matsui, W. H., MacVittie, T. J., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci70812 · Cited by 114
Ni, M., Li, X., Yin, Z., Jiang, H., Sidoryk‐Wȩgrzynowicz, M., Milatović, D., Cai, J., & Aschner, M. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq126 · Cited by 112
Myeloid-Derived Suppressor Cell Survival and Function Are Regulated by the Transcription Factor Nrf2
Beury, D. W., Carter, K. A., Nelson, C. E., Sinha, P., Hanson, E. M., Nyandjo, M., Fitzgerald, P., Majeed, A., Wali, N., & Ostrand‐Rosenberg, S. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501785 · Cited by 115
Lv, H., Liu, Q., Zhou, J., Tan, G., Deng, X., & Ci, X. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.016 · Cited by 111
Liu, Q., Lv, H., Wen, Z., Ci, X., & Peng, L. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01518 · Cited by 111
Gopalakrishnan, A., & Kong, A. T. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.09.082 · Cited by 110
Reuland, D. J., Khademi, S., Castle, C. J., Irwin, D. C., McCord, J. M., Miller, B. F., & Hamilton, K. L. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.016 · Cited by 110
Alaofi, A. L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01119 · Cited by 109
Kim, J.-H., Yu, S., Chen, J. D., & Kong, A.-N. T. (2012) · Oncogene · doi:10.1038/onc.2012.59 · Cited by 110
Redox regulation of the transcriptional repressor Bach1
Ishikawa, M., Numazawa, S., & Yoshida, T. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.01.021 · Cited by 112
Distinct roles of c-Abl and Atm in oxidative stress response are mediated by protein kinase C δPreprint
Li, B., Wang, X., Rasheed, N., Hu, Y., Boast, S., Ishii, T., Nakayama, K., Nakayama, K., & Goff, S. P. (2004) · Genes & Development · doi:10.1101/gad.1223504 · Cited by 109
Srisook, K., Kim, C., & Cha, Y. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1674 · Cited by 108
Pullikotil, P., Chen, H., Muniyappa, R., Greenberg, C. C., Yang, S., Reiter, C. E. N., Lee, J.-W., Chung, J. H., & Quon, M. J. (2011) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.06.007 · Cited by 106
Activation of transcription factor Nrf2 by hepatitis C virus induces the cell-survival pathway
Burdette, D. O., Olivarez, M., & Waris, G. (2009) · Journal of General Virology · doi:10.1099/vir.0.014340-0 · Cited by 105
RetractedFisetin alleviates oxidative stress after traumatic brain injury via the Nrf2-ARE pathway
Zhang, L., Wang, H., Zhou, Y., Zhu, Y., & Fei, M. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.05.011 · Cited by 104
Hahn, M. E., Timme‐Laragy, A. R., Karchner, S. I., & Stegeman, J. J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.022 · Cited by 106
Activation of the Nrf2/antioxidant response pathway increases IL-8 expression
Zhang, X., Chen, X., Song, H., Chen, H., & Rovin, B. H. (2005) · European Journal of Immunology · doi:10.1002/eji.200526116 · Cited by 103
Goldstone, J. V. (2008) · Cell Biology and Toxicology · doi:10.1007/s10565-008-9107-5 · Cited by 107
Du, Y., Villeneuve, N. F., Wang, X., Sun, Z., Chen, W., Li, J., Lou, H., Wong, P. K., & Zhang, D. D. (2008) · Environmental Health Perspectives · doi:10.1289/ehp.11464 · Cited by 99
Synthesis and anticancer activity of CDDO and CDDO-Me, two derivatives of natural triterpenoids
Borella, R., Forti, L., Gibellini, L., De Gaetano, A., De Biasi, S., Nasi, M., Cossarizza, A., & Pinti, M. (2019) · Molecules · doi:10.3390/molecules24224097 · Cited by 98
The KEAP1-NRF2 System in Healthy Aging and Longevity
Matsumaru, D., & Motohashi, H. (2021) · Antioxidants · doi:10.3390/antiox10121929 · Cited by 103
Cap-independent Nrf2 translation is part of a lipoic acid-stimulated detoxification stress response
Shay, K. P., Michels, A. J., Li, W., Kong, A. T., & Hagen, T. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.04.002 · Cited by 97
Nuclear Factor Erythroid 2-Related Factor 2 in Regulating Cancer Metabolism
Smolková, K., Mikó, E., Kovàcs, T., Leguina‐Ruzzi, A., Sipos, A., & Bai, P. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8024 · Cited by 101
Nrf2 Possesses a Redox-insensitive Nuclear Export Signal Overlapping with the Leucine Zipper Motif
Li, W., Jain, M. R., Chen, C., Yue, X., Hebbar, V., Zhou, R., & Kong, A.-N. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410601200 · Cited by 95
Venkatraman, G., Benesch, M. G. K., Tang, X., Dewald, J. W., McMullen, T. P. W., & Brindley, D. N. (2014) · The FASEB Journal · doi:10.1096/fj.14-262659 · Cited by 95
Ooi, B. K., Chan, K., Goh, B. H., & Yap, W. H. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01308 · Cited by 99
Regulating Nrf2 activity: ubiquitin ligases and signaling molecules in redox homeostasis
Hayes, J. D., Naidu, S. D., & Dinkova‐Kostova, A. T. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.12.010 · Cited by 103
Regulation of Nrf2, NF-κB, and AP-1 Signaling Pathways by Chemopreventive Agents
Shen, G., Jeong, W., Hu, R., & Kong, A. T. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1648 · Cited by 94
Copple, I. M., Goldring, C. E., Kitteringham, N. R., & Park, B. K. (2009) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-00663-0_9 · Cited by 98
Tanshinone IIA suppresses cholesterol accumulation in human macrophages: role of heme oxygenase-1
Liu, Z., Wang, J., Huang, E., Gao, S., Li, H., Lü, J., Tian, K., Little, P. J., Shen, X., Xu, S., et al. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m040394 · Cited by 92
Failure of protein quality control in amyotrophic lateral sclerosis
Kabashi, E., & Durham, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.006 · Cited by 90
Protection of vascular cells from oxidative stress by proteasome inhibition depends on Nrf2
Dreger, H., Westphal, K., Wilck, N., Baumann, G., Stangl, V., Stangl, K., & Meiners, S. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp279 · Cited by 92
The Generation, Detection, and Effects of Reactive Drug Metabolites
Stachulski, A. V., Baillie, T. A., Park, B. K., Obach, R. S., Dalvie, D., Williams, D. P., Srivastava, A., Regan, S., Antoine, D. J., Goldring, C. E., et al. (2012) · Medicinal Research Reviews · doi:10.1002/med.21273 · Cited by 89
Andrographolide induces Nrf2 and heme oxygenase 1 in astrocytes by activating p38 MAPK and ERK
Wong, S. Y., Tan, M. G. K., Wong, P. T. ‐., Herr, D. R., & Lai, M. K. P. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0723-3 · Cited by 86
Bahia, P. K., Rattray, M., & Williams, R. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05542.x · Cited by 86
Preventive and Protective Roles of Dietary Nrf2 Activators Against Central Nervous System Diseases
Sun, Y., Yang, T., Leak, R. K., Chen, J., & Zhang, F. (2017) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527316666170102120211 · Cited by 86
Gambari, L., Lisignoli, G., Cattini, L., Manferdini, C., Facchini, A., & Grassi, F. (2014) · Pharmacological Research · doi:10.1016/j.phrs.2014.06.014 · Cited by 86
Acrylamide-Responsive Genes in the Nematode Caenorhabditis elegans
Hasegawa, K., Miwa, S., Isomura, K., Tsutsumiuchi, K., Taniguchi, H., & Miwa, J. (2007) · Toxicological Sciences · doi:10.1093/toxsci/kfm276 · Cited by 85
Lv, H., Xiao, Q., Zhou, J., Feng, H., Liu, G., & Ci, X. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00147 · Cited by 83
Metadata
- Authors
- Nguyen, T., Sherratt, P. J., Huang, H.-C., Yang, C. S., & Pickett, C. B.
- Affiliations
- Rutgers, The State University of New Jersey (US)
- Corresponding author
- Pickett, Cecil B.
- ORCID
- Yang, Chung S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 278
- Issue
- 7
- Pages
- 4536-4541
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2080435498
- Cited by
- 615
- References
- 44
- Citations by year
- 2026: 15 · 2025: 13 · 2024: 24 · 2023: 25 · 2022: 29 · 2021: 25 · 2020: 24 · 2019: 31 · 2018: 23 · 2017: 24 · 2016: 29 · 2015: 31 · 2014: 21 · 2013: 31 · 2012: 36
- FWCI
- 12.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- Nrf2, antioxidant response element, protein stability, ubiquitin-mediated proteolysis, Nrf2 phosphorylation, phase II enzymes, tert-butylhydroquinone, beta-naphthoflavone, proteasome inhibitors, ERK signaling, protein phosphatase, transcriptional activation, HepG2 cells
- MeSH terms
- Antioxidants, Butadienes, Cell Line, DNA-Binding Proteins, Enzyme Inhibitors, Flavonoids, Humans, Hydroquinones, Nitriles, Peptide Hydrolases, Phosphorylation, RNA Processing, Post-Transcriptional, Transcriptional Activation, Trans-Activators, Leucine Zippers, Oxidative Stress, beta-Naphthoflavone, Protein Subunits, Proteasome Endopeptidase Complex, NF-E2-Related Factor 2
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