Molecular basis of the Keap1–Nrf2 system
Open accessAbstract
Nrf2 (NF-E2-related factor 2) is a master regulator of cellular responses against environmental stresses. Nrf2 induces the expression of detoxification and antioxidant enzymes, and Keap1 (Kelch-like ECH-associated protein 1), an adaptor subunit of Cullin 3-based E3 ubiquitin ligase, regulates Nrf2 activity. Keap1 also acts as a sensor for oxidative and electrophilic stresses. Keap1 retains multiple sensor cysteine residues that detect various stress stimuli. Increasing attention has been paid to the roles that Nrf2 plays in the protection of our bodies against drug toxicity and stress-induced diseases. On the other hand, Nrf2 is found to promote both oncogenesis and cancer cell resistance against chemotherapeutic drugs. Thus, although Nrf2 acts to protect our body from deleterious stresses, cancer cells hijack the Nrf2 activity to support their malignant growth. Nrf2 has emerged as a new therapeutic target, and both inducers and inhibitors of Nrf2 are awaited. Studies challenging the molecular basis of the Keap1-Nrf2 system functions are now critically important to improve translational studies of the system. Indeed, recent studies identified cross talk between Nrf2 and other signaling pathways, which provides new insights into the mechanisms by which the Keap1-Nrf2 system serves as a potent regulator of our health and disease.
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The transcription factor Nrf2 is a redox switch regulating the expression of antioxidant enzymes, GSH-synthesizing enzymes, and detoxifying Phase 2 enzymes.
“The transcription factor Nrf2 is considered as a redox switch regulating the expression of antioxidant enzymes, GSH-synthesizing enzymes, and detoxifying Phase 2 enzymes (175), while the specific selenocysteine tRNA is needed for the synthesis of selenoproteins such as GPx or Trx reductase, which reduces oxidized Trx (133) (Fig. 2).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [175]
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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 · see citing works
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 · see citing works
Self-citationKomatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., Sou, Y., Ueno, I., Sakamoto, A., Tong, K. I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2021 · Cited by 2,422 · see citing works
Self-citationOncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
DeNicola, G. M., Karreth, F. A., Humpton, T. J., Gopinathan, A., Wei, C., Frese, K., Mangal, D., Yu, K. H., Yeo, C. J., Calhoun, E. S., et al. (2011) · Nature · doi:10.1038/nature10189 · Cited by 2,277 · see citing works
Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224 · see citing works
The Nrf2 regulatory network provides an interface between redox and intermediary metabolism
Hayes, J. D., & Dinkova‐Kostova, A. T. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.002 · Cited by 2,158 · see citing works
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 · see citing works
Self-citationNrf2–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 · see citing works
Self-citationZhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480 · see citing works
Nrf2 Redirects Glucose and Glutamine into Anabolic Pathways in Metabolic Reprogramming
Mitsuishi, Y., Taguchi, K., Kawatani, Y., Shibata, T., Nukiwa, T., Aburatani, H., Yamamoto, M., & Motohashi, H. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.016 · Cited by 1,395 · see citing works
Self-citationKeap1 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 1,262 · see citing works
Phosphorylation of p62 Activates the Keap1-Nrf2 Pathway during Selective Autophagy
Ichimura, Y., Waguri, S., Sou, Y., Kageyama, S., Hasegawa, J., Ishimura, R., Saito, T., Yang, Y., Kouno, T., Fukutomi, T., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.003 · Cited by 1,205 · see citing works
Self-citationRamos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102 · see citing works
Self-citationBardoxolone Methyl in Type 2 Diabetes and Stage 4 Chronic Kidney Disease
de Zeeuw, D., Akizawa, T., Audhya, P., Bakris, G. L., Chin, M. P., Christ‐Schmidt, H., Goldsberry, A., Houser, M. T., Krauth, M., Heerspink, H. J. L., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1306033 · Cited by 1,041 · see citing works
Bardoxolone Methyl and Kidney Function in CKD with Type 2 Diabetes
Pergola, P. E., Raskin, P., Toto, R. D., Meyer, C. J., Huff, J. W., Grossman, E. B., Krauth, M., Ruiz, S., Audhya, P., Christ-Schmidt, H., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1105351 · Cited by 890 · see citing works
Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation
Wakabayashi, N., Itoh, K., Wakabayashi, J., Motohashi, H., Noda, S., Takahashi, S., Imakado, S., KOTSUJI, T., Otsuka, F., Roop, D. R., et al. (2003) · Nature Genetics · doi:10.1038/ng1248 · Cited by 881 · see citing works
Self-citationRada, P., Rojo, A. I., Chowdhry, S., McMahon, M., Hayes, J. D., & Cuadrado, A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01204-10 · Cited by 759 · see citing works
Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer
Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735 · see citing works
Self-citationShibata, T., Ohta, T., Tong, K. I., Kokubu, A., Odogawa, R., Tsuta, K., Asamura, H., Yamamoto, M., & Hirohashi, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806268105 · Cited by 728 · see citing works
Self-citationToward clinical application of the Keap1-Nrf2 pathway
Suzuki, T., Motohashi, H., & Yamamoto, M. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.005 · Cited by 680 · see citing works
Self-citationChowdhry, S., Zhang, Y., McMahon, M., Sutherland, C., Cuadrado, A., & Hayes, J. D. (2013) · Oncogene · doi:10.1038/onc.2012.388 · Cited by 657 · see citing works
Kobayashi, M., Li, L., Iwamoto, N., Nakajima‐Takagi, Y., Kaneko, H., Nakayama, Y., Eguchi, M., Wada, Y., Kumagai, Y., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01080-08 · Cited by 641 · see citing works
Self-citationLoss of Keap1 Function Activates Nrf2 and Provides Advantages for Lung Cancer Cell Growth
Ohta, T., Iijima, K., Miyamoto, M., Nakahara, I., Tanaka, H., Ohtsuji, M., Suzuki, T., Kobayashi, A., Yokota, J., Sakiyama, T., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5003 · Cited by 630 · see citing works
Self-citationGlucosinolates and isothiocyanates in health and disease
Dinkova‐Kostova, A. T., & Kostov, R. V. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.04.003 · Cited by 607 · see citing works
Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells
Inami, Y., Waguri, S., Sakamoto, A., Kouno, T., Nakada, K., Hino, O., Watanabe, S., Ando, J., Iwadate, M., Yamamoto, M. P., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201102031 · Cited by 602 · see citing works
Self-citationAdam, J., Hatipoglu, E., O'Flaherty, L., Ternette, N., Sahgal, N., Lockstone, H., Baban, D., Nye, E., Stamp, G. W., Wolhuter, K., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.006 · Cited by 585 · see citing works
Direct and indirect antioxidant properties of inducers of cytoprotective proteins
Dinkova‐Kostova, A. T., & Talalay, P. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700195 · Cited by 535 · see citing works
Physiological Significance of Reactive Cysteine Residues of Keap1 in Determining Nrf2 Activity
Yamamoto, T., Suzuki, T., Kobayashi, A., Wakabayashi, J., Maher, J. M., Motohashi, H., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01704-07 · Cited by 515 · see citing works
Self-citationNrf2: friend or foe for chemoprevention?
Kensler, T. W., & Wakabayashi, N. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp231 · Cited by 487 · see citing works
Keap1 degradation by autophagy for the maintenance of redox homeostasis
Taguchi, K., Fujikawa, N., Komatsu, M., Ishii, T., Unno, M., Akaike, T., Motohashi, H., & Yamamoto, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121572109 · Cited by 482 · see citing works
Self-citationTwo-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
Tong, K. I., Kobayashi, A., Katsuoka, F., & Yamamoto, M. (2006) · Biological Chemistry · doi:10.1515/bc.2006.164 · Cited by 473 · see citing works
Self-citationShibata, T., Kokubu, A., Gotoh, M., Ojima, H., Ohta, T., Yamamoto, M. P., & Hirohashi, S. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.06.082 · Cited by 468 · see citing works
Self-citationTong, K. I., Padmanabhan, B., Kobayashi, A., Shang, C., Hirotsu, Y., Yokoyama, S., & Yamamoto, M. P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00753-07 · Cited by 447 · see citing works
Self-citationLiby, K. T., & Sporn, M. B. (2012) · Pharmacological Reviews · doi:10.1124/pr.111.004846 · Cited by 410 · see citing works
Ooi, A., Wong, J.-C., Petillo, D., Roossien, D., Perrier-Trudova, V., Whitten, D., Min, B. W. H., Tan, M.-H., Zhang, Z., Yang, X. J., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.08.024 · Cited by 401 · see citing works
Baird, L., Llères, D., Swift, S., & Dinkova‐Kostova, A. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305687110 · Cited by 386 · see citing works
Xu, C., Huang, M., Shen, G., Yuan, X., Lin, W., Khor, T. O., Conney, A. H., & Kong, A. T. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0300 · Cited by 379 · see citing works
Iida, K., Itoh, K., Kumagai, Y., Oyasu, R., Hattori, K., Kawai, K., Shimazui, T., Akaza, H., & Yamamoto, M. P. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1906 · Cited by 372 · see citing works
Self-citationOncogenic NRF2 mutations in squamous cell carcinomas of oesophagus and skin
Kim, Y. R., Oh, J. E., Kim, M. S., Kang, M. R., Park, S. W., Han, J. Y., Eom, H., Yoo, N. J., & Lee, S. H. (2009) · The Journal of Pathology · doi:10.1002/path.2653 · Cited by 357 · see citing works
Regulatory mechanisms of cellular response to oxidative stress
Itoh, K., Ishii, T., Wakabayashi, N., & Yamamoto, M. P. (1999) · Free Radical Research · doi:10.1080/10715769900300881 · Cited by 349 · see citing works
Self-citationMarzec, J. M., Christie, J. D., Reddy, S. P., Jedlicka, A., Vuong, H., Lanken, P. N., Aplenc, R., Yamamoto, T., Yamamoto, M. P., Cho, H., et al. (2007) · The FASEB Journal · doi:10.1096/fj.06-7759com · Cited by 340 · see citing works
Self-citationThe Keap1-Nrf2 System Prevents Onset of Diabetes Mellitus
Uruno, A., Furusawa, Y., Yagishita, Y., Fukutomi, T., Muramatsu, H., Negishi, T., Sugawara, A., Kensler, T. W., & Yamamoto, M. P. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00225-13 · Cited by 330 · see citing works
Self-citationIncreased susceptibility of Nrf2 knockout mice to colitis-associated colorectal cancer
Khor, T. O., Huang, M.-T., Prawan, A., Liu, Y., Hao, X., Yu, S., Cheung, W. K. L., Chan, J. Y., Reddy, B. S., Yang, C. S., et al. (2008) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-08-0028 · Cited by 306 · see citing works
4-Nitroquinoline-1-oxide induced experimental oral carcinogenesis
Kanojia, D., & Vaidya, M. M. (2006) · Oral Oncology · doi:10.1016/j.oraloncology.2005.10.013 · Cited by 291 · see citing works
Nagaraj, S., Youn, J., Weber, H., Iclozan, C., Lu, L. D., Cotter, M. J., Meyer, C. J., Becerra, C. R., Fishman, M., Antonia, S. J., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-3272 · Cited by 286 · see citing works
Gao, L., Wang, J., Sekhar, K. R., Yin, H., Yared, N. F., Schneider, S. N., Sasi, S., Dalton, T. P., Anderson, M. E., Chan, J. Y., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607622200 · Cited by 278 · see citing works
Validation of the multiple sensor mechanism of the Keap1-Nrf2 system
Takaya, K., Suzuki, T., Motohashi, H., Onodera, K., Satomi, S., Kensler, T. W., & Yamamoto, M. P. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.06.023 · Cited by 277 · see citing works
Self-citationFukutomi, T., Takagi, K., Mizushima, T., Ohuchi, N., & Yamamoto, M. P. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01191-13 · Cited by 265 · see citing works
Self-citationSatoh, H., Moriguchi, T., Takai, J., Ebina, M., & Yamamoto, M. P. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4499 · Cited by 251 · see citing works
Self-citationRegulation of Nrf2 signaling and longevity in naturally long-lived rodents
Lewis, K. N., Wason, E., Edrey, Y. H., Kristan, D. M., Nevo, E., & Buffenstein, R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417566112 · Cited by 248 · see citing works
Marcotte, D. J., Zeng, W., Hus, J., McKenzie, A., Hession, C., Jin, P., Bergeron, C., Lugovskoy, A. A., Enyedy, I. J., Cuervo, H., et al. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.04.019 · Cited by 245 · see citing works
Hong, D. S., Kurzrock, R., Supko, J. G., He, X., Naing, A., Wheler, J., Lawrence, D., Eder, J. P., Meyer, C. J., Ferguson, D. A., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-2703 · Cited by 236 · see citing works
Ogura, T., Tong, K. I., Mio, K., Maruyama, Y., Kurokawa, H., Sato, C., & Yamamoto, M. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914036107 · Cited by 232 · see citing works
Self-citationThe Keap1-Nrf2 system and diabetes mellitus
Uruno, A., Yagishita, Y., & Yamamoto, M. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.12.012 · Cited by 231 · see citing works
Self-citationZhou, S.-F., Wang, Y., Zhe, H., Yang, Y., & He, Z. (2014) · Drug Design Development and Therapy · doi:10.2147/dddt.s68872 · Cited by 230 · see citing works
Meakin, P. J., Chowdhry, S., Sharma, R. S., Ashford, F. B., Walsh, S. V., McCrimmon, R. J., Dinkova‐Kostova, A. T., Dillon, J. F., Hayes, J. D., & Ashford, M. L. J. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00677-14 · Cited by 229 · see citing works
Genetic Analysis of Cytoprotective Functions Supported by Graded Expression of Keap1
Taguchi, K., Maher, J. M., Suzuki, T., Kawatani, Y., Motohashi, H., & Yamamoto, M. P. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01591-09 · Cited by 225 · see citing works
Self-citationNrf2: control of sensitivity to carcinogens
Slocum, S. L., & Kensler, T. W. (2011) · Archives of Toxicology · doi:10.1007/s00204-011-0675-4 · Cited by 219 · see citing works
Rachakonda, G., Xiong, Y., Sekhar, K. R., Stamer, S. L., Liebler, D. C., & Freeman, M. L. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700302s · Cited by 210 · see citing works
Discovery of a small-molecule inhibitor and cellular probe of Keap1–Nrf2 protein–protein interaction
Hu, L., Magesh, S., Chen, L., Wang, L., Lewis, T. A., Chen, Y., Khodier, C., Inoyama, D., Beamer, L. J., Emge, T. J., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.03.013 · Cited by 206 · see citing works
Nrf2 Protects Pancreatic β-Cells From Oxidative and Nitrosative Stress in Diabetic Model Mice
Yagishita, Y., Fukutomi, T., Sugawara, A., Kawamura, H., Takahashi, T., Pi, J., Uruno, A., & Yamamoto, M. P. (2013) · Diabetes · doi:10.2337/db13-0909 · Cited by 205 · see citing works
Self-citationNrf2-deficiency creates a responsive microenvironment for metastasis to the lung
Satoh, H., Moriguchi, T., Taguchi, K., Takai, J., Maher, J. M., Suzuki, T., Winnard, P. T., Raman, V., Ebina, M., Nukiwa, T., et al. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq105 · Cited by 197 · see citing works
Self-citationMorrow, C. S., Smitherman, P. K., Diah, S. K., Schneider, E., & Townsend, A. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20114 · Cited by 139 · see citing works
Cancer-Derived Mutations in KEAP1 Impair NRF2 Degradation but not Ubiquitination
Hast, B. E., Cloer, E. W., Goldfarb, D., Li, H., Siesser, P. F., Yan, F., Walter, V., Zheng, N., Hayes, D. N., & Major, M. B. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-1655 · Cited by 138 · see citing works
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 137 · see citing works
Self-citationThe PTEN/NRF2 Axis Promotes Human Carcinogenesis
Rojo, A. I., Rada, P., Mendiola, M., Ortega-Molina, A., Wojdyła, K., Rogowska-Wrzesińska, A., Hardisson, D., Serrano, M., & Cuadrado, A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5843 · Cited by 135 · see citing works
Frequent epigenetics inactivation of KEAP1 gene in non-small cell lung cancer
Muscarella, L. A., Parrella, P., D’Alessandro, V., la Torre, A., Barbano, R., Fontana, A., Tancredi, A., Guarnieri, V., Balsamo, T., Coco, M., et al. (2011) · Epigenetics · doi:10.4161/epi.6.6.15773 · Cited by 134 · see citing works
Regulatory Nexus of Synthesis and Degradation Deciphers Cellular Nrf2 Expression Levels
Suzuki, T., Shibata, T., Takaya, K., Shiraishi, K., Kohno, T., Kunitoh, H., Tsuta, K., Furuta, K., Goto, K., Hosoda, F., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00065-13 · Cited by 123 · see citing works
Self-citation(2014) · Dove Medical Press (Taylor and Francis Group) · Cited by 118 · see citing works
Saha, P., Reddy, V. T., Konopleva, M. Y., Andreeff, M., & Chan, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.176545 · Cited by 107 · see citing works
Nrf2 Enhances Cholangiocyte Expansion in Pten-Deficient Livers
Taguchi, K., Hirano, I., Itoh, T., Tanaka, M., Miyajima, A., Suzuki, A., Motohashi, H., & Yamamoto, M. P. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01384-13 · Cited by 98 · see citing works
Self-citationTargeted Deletion of Nrf2 Reduces Urethane-Induced Lung Tumor Development in Mice
Bauer, A. K., Cho, H., Miller‐DeGraff, L., Walker, C., Helms, K. L., Fostel, J. M., Yamamoto, M. P., & Kleeberger, S. R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026590 · Cited by 95 · see citing works
Self-citationMyeloid Lineage–Specific Deletion of Antioxidant System Enhances Tumor Metastasis
Hiramoto, K., Satoh, H., Suzuki, T., Moriguchi, T., Pi, J., Shimosegawa, T., & Yamamoto, M. P. (2014) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-14-0094 · Cited by 94 · see citing works
Self-citationNrf2 deficiency improves glucose tolerance in mice fed a high-fat diet
Zhang, Y.-K. J., Wu, K. C., Liu, J., & Klaassen, C. D. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.09.014 · Cited by 93 · see citing works
Becks, L., Prince, M., Burson, H. C., Christophe, C., Broadway, M., Itoh, K., Yamamoto, M. P., Mathis, J. M., Orchard, E. A., Shi, R., et al. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-540 · Cited by 71 · see citing works
Self-citationKitamura, Y., Umemura, T., Kanki, K., Kodama, Y., Kitamoto, S., Saito, K., Itoh, K., Yamamoto, M. P., Masegi, T., Nishikawa, A., et al. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00352.x · Cited by 70 · see citing works
Self-citationRoles of Keap1–Nrf2 System in Upper Aerodigestive Tract Carcinogenesis
Ohkoshi, A., Suzuki, T., Ono, M., Kobayashi, T., & Yamamoto, M. P. (2012) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-12-0401-t · Cited by 69 · see citing works
Self-citationNrf2 induces fibroblast growth factor 21 in diabetic mice
Furusawa, Y., Uruno, A., Yagishita, Y., Higashi, C., & Yamamoto, M. P. (2014) · Genes to Cells · doi:10.1111/gtc.12186 · Cited by 62 · see citing works
Self-citationXu, J., Donepudi, A. C., Moscovitz, J. E., & Slitt, A. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079841 · Cited by 56 · see citing works
Meher, A. K., Sharma, P. R., Lira, V. A., Yamamoto, M. P., Kensler, T. W., Yan, Z., & Leitinger, N. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.022 · Cited by 51 · see citing works
Self-citationTran, K., Risingsong, R., Royce, D. B., Williams, C. R., Sporn, M. B., & Liby, K. T. (2012) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-11-0404 · Cited by 47 · see citing works
Okano, Y., Nezu, U., Enokida, Y., Lee, M. T. M., Hiroko, K., Lezhava, A., Hayashizaki, Y., Morita, S., Taguri, M., Ichikawa, Y., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073794 · Cited by 45 · see citing works
Deeb, D., Gao, X., Liu, Y., Jiang, D., Divine, G., Arbab, A. S., Dulchavsky, S. A., & Gautam, S. C. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr030 · Cited by 38 · see citing works
Gao, X., Deeb, D., Liu, Y., Arbab, A. S., Divine, G., Dulchavsky, S. A., & Gautam, S. C. (2011) · Cancers · doi:10.3390/cancers3033353 · Cited by 34 · see citing works
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Nrf2-Keap1 signaling in oxidative and reductive stress
Bellezza, I., Giambanco, I., Minelli, A., & Donato, R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.02.010 · Cited by 2,096 · see citing works
Kurutas, E. B. (2015) · Nutrition Journal · doi:10.1186/s12937-016-0186-5 · Cited by 2,152 · see citing works
Ubiquitin ligases: structure, function, and regulation
Zheng, N., & Shabek, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014922 · Cited by 1,499 · see citing works
Cragg, G. M. L., & Pezzuto, J. M. (2015) · Medical Principles and Practice · doi:10.1159/000443404 · Cited by 807 · see citing works
The Keap1–Nrf2–ARE Pathway As a Potential Preventive and Therapeutic Target: An Update
Lu, M., Ji, J., Jiang, Z., & You, Q. (2016) · Medicinal Research Reviews · doi:10.1002/med.21396 · Cited by 807 · see citing works
Nrf2 Activation Promotes Lung Cancer Metastasis by Inhibiting the Degradation of Bach1
Lignitto, L., LeBoeuf, S. E., Homer, H., Jiang, S., Askenazi, M., Karakousi, T. R., Pass, H. I., Bhutkar, A. J., Tsirigos, A., Ueberheide, B., et al. (2019) · Cell · doi:10.1016/j.cell.2019.06.003 · Cited by 573 · see citing works
Formation and Biological Targets of Quinones: Cytotoxic versus Cytoprotective Effects
Bolton, J. L., & Dunlap, T. L. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00256 · Cited by 528 · see citing works
Nrf2/Keap1/ARE signaling: Towards specific regulation
Ulasov, A. V., Rosenkranz, A. A., Georgiev, G. P., & Sobolev, A. S. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.120111 · Cited by 520 · see citing works
ROS: Basic Concepts, Sources, Cellular Signaling, and its Implications in Aging Pathways
de Almeida, A. J. P. O., de Oliveira, J. C. P. L., Pontes, L. V. D. S., Júnior, J. F. D. S., Gonçalves, T. A. F., Dantas, S. H., Feitosa, M. S. D. A., Silva, A. O., & de Medeiros, I. A. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1225578 · Cited by 521 · see citing works
Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
Kuhn, V., Diederich, L., Keller, T. C. S., Kramer, C. M., Lückstädt, W., Panknin, C., Suvorava, T., Isakson, B. E., Kelm, M., & Cortese-Krott, M. M. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6954 · Cited by 469 · see citing works
Inhibition and induction of CYP enzymes in humans: an update
Hakkola, J., Hukkanen, J., Turpeinen, M., & Pelkonen, O. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02936-7 · Cited by 422 · see citing works
Transcription factor NFE2L2/NRF2 is a regulator of macroautophagy genes
Pajares, M., Jiménez-Moreno, N., García‐Yagüe, Á. J., Escoll, M., CEBALLOS, M. L. D., LEUVEN, F. V., Rábano, A., Yamamoto, M. P., Rojo, A. I., & Cuadrado, A. (2016) · Autophagy · doi:10.1080/15548627.2016.1208889 · Cited by 405 · see citing works
Self-citationSuzuki, T., & Yamamoto, M. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.800169 · Cited by 402 · see citing works
Self-citationLin, X., Bai, D.-P., Wei, Z., Zhang, Y., Huang, Y., Deng, H., & Huang, X. (2019) · PLoS ONE · doi:10.1371/journal.pone.0216711 · Cited by 332 · see citing works
Molecular Basis of the KEAP1-NRF2 Signaling Pathway
Suzuki, T., Takahashi, J. A., & Yamamoto, M. P. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.0028 · Cited by 309 · see citing works
Self-citationGeorgiou‐Siafis, S. K., & Tsiftsoglou, A. S. (2023) · Antioxidants · doi:10.3390/antiox12111953 · Cited by 298 · see citing works
Characterizations of Three Major Cysteine Sensors of Keap1 in Stress Response
Saito, R., Suzuki, T., Hiramoto, K., Asami, S., Naganuma, E., Suda, H., Iso, T., Yamamoto, H., Morita, M., Baird, L., et al. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00868-15 · Cited by 294 · see citing works
Self-citationSpeisky, H., Shahidi, F., de Camargo, A. C., & Fuentes, J. (2022) · Antioxidants · doi:10.3390/antiox11010133 · Cited by 288 · see citing works
Insulin signaling pathway and related molecules: Role in neurodegeneration and Alzheimer's disease
Akhtar, A., & Sah, S. P. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104707 · Cited by 290 · see citing works
Sun, Y., Zhu, H.-J., Zhao, R., Zhou, S., Wang, M., Yang, Y., & Guo, Z. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102852 · Cited by 284 · see citing works
Short-chain fatty acids as modulators of redox signaling in health and disease
González‐Bosch, C., Boorman, E., Zunszain, P. A., & Mann, G. E. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102165 · Cited by 285 · see citing works
Liang, M., Wang, Z., Li, H., Cai, L., Pan, J., He, H., Wu, Q., Tang, Y., Ma, J., & Yang, L. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.03.029 · Cited by 272 · see citing works
Advances and challenges in therapeutic targeting of NRF2
Dinkova‐Kostova, A. T., & Copple, I. M. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.12.003 · Cited by 272 · see citing works
Role of Nrf2 and Its Activators in Respiratory Diseases
Liu, Q., Gao, Y., & Ci, X. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7090534 · Cited by 273 · see citing works
Amodio, N., Stamato, M. A., Juli, G., Morelli, E., Fulciniti, M., Manzoni, M., Taìana, E., Agnelli, L., Cantafio, M. E. G., Romeo, E., et al. (2018) · Leukemia · doi:10.1038/s41375-018-0067-3 · Cited by 263 · see citing works
The Crosstalk between Nrf2 and Inflammasomes
Hennig, P., Garstkiewicz, M., Grossi, S., Filippo, M. D., French, L. E., & Beer, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020562 · Cited by 256 · see citing works
Small Maf proteins (MafF, MafG, MafK): History, structure and function
Katsuoka, F., & Yamamoto, M. P. (2016) · Gene · doi:10.1016/j.gene.2016.03.058 · Cited by 253 · see citing works
Self-citationGai, C., Liu, C., Wu, X., Yu, M., Zheng, J., Zhang, W., Lv, S., & Li, W. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02939-3 · Cited by 243 · see citing works
Kubo, E., Chhunchha, B., Singh, P., Sasaki, H., & Singh, D. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-14520-8 · Cited by 231 · see citing works
Transcriptional regulation of xenobiotic detoxification genes in insects - An overview
Amezian, D., Nauen, R., & Goff, G. L. (2021) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2021.104822 · Cited by 231 · see citing works
Cao, H., Cheng, Y., Gao, H., Zhuang, J., Zhang, W., Bian, Q., Wang, F., Du, Y., Li, Z., Kong, D., et al. (2020) · ACS Nano · doi:10.1021/acsnano.9b08207 · Cited by 217 · see citing works
Role of Nrf2 in aging, Alzheimer’s and other neurodegenerative diseases
George, M., Tharakan, M., Culberson, J. W., Reddy, A. P., & Reddy, P. H. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101756 · Cited by 212 · see citing works
Saha, S., Buttari, B., Profumo, E., Tucci, P., & Saso, L. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.787258 · Cited by 206 · see citing works
Cysteine sulfenylation directs IRE-1 to activate the SKN-1/Nrf2 antioxidant response
Hourihan, J. M., Mazzeo, L. E. M., Fernández-Cárdenas, L. P., & Blackwell, T. (2016) · Molecules and Cells · doi:10.1016/j.molcel.2016.07.019 · Cited by 195 · see citing works
Fetoni, A. R., Paciello, F., Rolesi, R., Paludetti, G., & Troiani, D. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.02.022 · Cited by 201 · see citing works
Shen, K., Jia, Y., Wang, X., Zhang, J., Liu, K., Wang, J., Cai, W., Li, J., Li, S., Zhao, M., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.023 · Cited by 194 · see citing works
Interactions between reactive oxygen species and autophagy
Redza-Dutordoir, M., & Averill‐Bates, D. A. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119041 · Cited by 192 · see citing works
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 190 · see citing works
Sun, J., Zhou, C., Zhao, Y., Zhang, X.-F., Chen, W., Zhou, Q., Hu, B., Gao, D., Raatz, L., Wang, Z., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101942 · Cited by 190 · see citing works
Targeting the KEAP1-NRF2 system to prevent kidney disease progression
Nezu, M., Suzuki, N., & Yamamoto, M. (2017) · American Journal of Nephrology · doi:10.1159/000475890 · Cited by 3,447 · see citing works
Self-citationGe, W., Zhao, K., Wang, X., Li, H., Yu, M., He, M., Xue, X., Zhu, Y., Zhang, C. L., Cheng, Y., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.09.008 · Cited by 189 · see citing works
Lutein as a Modulator of Oxidative Stress-Mediated Inflammatory Diseases
Ahn, Y. J., & Kim, H. (2021) · Antioxidants · doi:10.3390/antiox10091448 · Cited by 190 · see citing works
Lu, K., Alcivar, A. L., Ma, J., Foo, T. K., Zywea, S., Mahdi, A., Huo, Y., Kensler, T. W., Gatza, M. L., & Xia, B. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2204 · Cited by 178 · see citing works
Jin, X., Tang, J., Qiu, X., Nie, X., Ou, S., Wu, G., Zhang, R., & Zhu, J. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01825-7 · Cited by 182 · see citing works
Anticancer Activity of Sulforaphane: The Epigenetic Mechanisms and the Nrf2 Signaling Pathway
Su, X., Jiang, X. M., Meng, L., Dong, X., Shen, Y., & Xin, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/5438179 · Cited by 172 · see citing works
Regulation of the Keap1–Nrf2 pathway by p62/SQSTM1
Katsuragi, Y., Ichimura, Y., & Komatsu, M. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.09.005 · Cited by 166 · see citing works
Conservation of the Keap1-Nrf2 System: An Evolutionary Journey through Stressful Space and Time
Fuse, Y., & Kobayashi, M. (2017) · Molecules · doi:10.3390/molecules22030436 · Cited by 168 · see citing works
Are Astrocytes the Predominant Cell Type for Activation of Nrf2 in Aging and Neurodegeneration?
Liddell, J. R. (2017) · Antioxidants · doi:10.3390/antiox6030065 · Cited by 167 · see citing works
Potential Applications of NRF2 Modulators in Cancer Therapy
Panieri, E., Djordjević, A. B., Telkoparan‐Akillilar, P., Cevik, D., Kouretas, D., Veskoukis, A. S., Skaperda, Z., Tsatsakis, A. M., Wallace, D., Süzen, S., et al. (2020) · Antioxidants · doi:10.3390/antiox9030193 · Cited by 165 · see citing works
Zhu, J., Wang, H., Chen, F., Fu, J., Xu, Y., Hou, Y., Kou, H. H., Zhai, C., Nelson, M. B., Zhang, Q., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.010 · Cited by 162 · see citing works
Critical Role of Nrf2 in Experimental Ischemic Stroke
Liu, L., Locascio, L. M., & Doré, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00153 · Cited by 157 · see citing works
NRF2 activation induces NADH-reductive stress, providing a metabolic vulnerability in lung cancer
Weiss‐Sadan, T., Ge, M., Hayashi, M., Gohar, M., Yao, C.-H., de Groot, A., Harry, S. A., Carlin, A. D., Fischer, H., Shi, L., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.01.012 · Cited by 156 · see citing works
Yao, W., Zhang, J.-C., Ishima, T., Dong, C., Yang, C., Ren, Q., Ma, M., Han, M., Wu, J., Suganuma, H., et al. (2016) · Scientific Reports · doi:10.1038/srep30659 · Cited by 154 · see citing works
Self-citationLi, Y., Jongberg, S., Andersen, M. L., Davies, M. J., & Lund, M. N. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.05.019 · Cited by 151 · see citing works
Habtemariam, S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/4724920 · Cited by 148 · see citing works
A catalogue of somatic NRF2 gain-of-function mutations in cancer
Kerins, M. J., & Ooi, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-31281-0 · Cited by 140 · see citing works
Redox Paradox: A Novel Approach to Therapeutics-Resistant Cancer
Chaiswing, L., Clair, W. H. S., & Clair, D. K. S. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7485 · Cited by 147 · see citing works
Nrf2 controls iron homoeostasis in haemochromatosis and thalassaemia via Bmp6 and hepcidin
Lim, P. J., Duarte, T. L., Arezes, J., Garcia-Santos, D., Hamdi, A., Pasricha, S.-R., Armitage, A. E., Mehta, H., Wideman, S., Santos, A. G., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0063-6 · Cited by 147 · see citing works
Xu, X., Lu, Z., Lin, V., May, A., Shaw, D. H., Wang, Z., Che, B., Tran, K., Du, H., & Shaw, P. X. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7042105 · Cited by 141 · see citing works
Ferroptosis in colorectal cancer: Potential mechanisms and effective therapeutic targets
Wang, Y., Zhang, Z., Sun, W., Zhang, J., Xu, Q., Zhou, X., & Mao, L. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113524 · Cited by 141 · see citing works
Tao, S., de la Vega, M. R., Chapman, E., Ooi, A., & Zhang, D. D. (2017) · Molecular Carcinogenesis · doi:10.1002/mc.22745 · Cited by 136 · see citing works
A Protective Role of the NRF2-Keap1 Pathway in Maintaining Intestinal Barrier Function
Wen, Z., Liu, W., Li, X., Chen, W., Liu, Z., Wen, J., & Liu, Z. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/1759149 · Cited by 136 · see citing works
Heme Oxygenase-1 in Kidney Health and Disease
Lever, J. M., Boddu, R., George, J. F., & Agarwal, A. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6659 · Cited by 134 · see citing works
Shen, B., Feng, H., Cheng, J., Li, Z., Jin, M., Zhao, L., Wang, Q., Qin, H., & Liu, G. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15139 · Cited by 133 · see citing works
Perspectives of the Nrf-2 signaling pathway in cancer progression and therapy
Basak, P., Sadhukhan, P., Sarkar, P., & Sil, P. C. (2017) · Toxicology Reports · doi:10.1016/j.toxrep.2017.06.002 · Cited by 134 · see citing works
Mycosporine-Like Amino Acids: Making the Foundation for Organic Personalised Sunscreens
Rosic, N. N. (2019) · Marine Drugs · doi:10.3390/md17110638 · Cited by 133 · see citing works
Wible, R. S., Ramanathan, C., Sutter, T. R., Olesen, K. M., Kensler, T. W., Liu, A. C., & Sutter, T. R. (2018) · eLife · doi:10.7554/elife.31656 · Cited by 126 · see citing works
The Role of the Nrf2/ARE Antioxidant System in Preventing Cardiovascular Diseases
Smith, R., Tran, K., Smith, C. C., McDonald, M., Shejwalkar, P., & Hara, K. (2016) · Diseases · doi:10.3390/diseases4040034 · Cited by 125 · see citing works
Bardoxolone ameliorates TGF-β1-associated renal fibrosis through Nrf2/Smad7 elevation
Song, M., Lee, J., Ryoo, I.-G., Lee, S.-H., Ku, S., & Kwak, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.04.033 · Cited by 124 · see citing works
Gao, G., Xie, Z., Li, E.-W., Yuan, Y., Fu, Y., Wang, P., Zhang, X., Qiao, Y., Xu, J., Hölscher, C., et al. (2021) · Journal of Natural Medicines · doi:10.1007/s11418-021-01491-4 · Cited by 124 · see citing works
Zhang, Y.-B., Yan, T., Sun, D., Xie, C., Wang, T., Liu, X., Wang, J., Wang, Q., Luo, Y., Wang, P., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.12.012 · Cited by 120 · see citing works
On the Effects of Reactive Oxygen Species and Nitric Oxide on Red Blood Cell Deformability
Diederich, L., Suvorava, T., Sansone, R., Keller, T. C. S., Barbarino, F., Sutton, T. R., Kramer, C. M., Lückstädt, W., Isakson, B. E., Gohlke, H., et al. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00332 · Cited by 119 · see citing works
The homeostatic role of hydrogen peroxide, superoxide anion and nitric oxide in the vasculature
Costa, T. J. D., Barros, P. R., Arce, C., Santos, J. D., da Silva-Neto, J., Egea, G., Dantas, A. P., Tostes, R. C., & Jiménez‐Altayó, F. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.11.021 · Cited by 115 · see citing works
The role of natural products in revealing NRF2 function
Zhang, D. D., & Chapman, E. (2020) · Natural Product Reports · doi:10.1039/c9np00061e · Cited by 120 · see citing works
Targeting aging for disease modification in osteoarthritis
Collins, J. A., Diekman, B. O., & Loeser, R. F. (2017) · Current Opinion in Rheumatology · doi:10.1097/bor.0000000000000456 · Cited by 117 · see citing works
Zhou, Y., Men, L., Sun, Y., Wei, M., & Fan, X. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173796 · Cited by 117 · see citing works
Circadian Control of Mitochondria in Reactive Oxygen Species Homeostasis
Mezhnina, V., Ebeigbe, O. P., Poe, A., & Kondratov, R. V. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0274 · Cited by 117 · see citing works
Choi, E.-J., Jung, B.-J., Lee, S.-H., Yoo, H.-S., Shin, E.-A., Ko, H., Chang, S., Kim, S.-Y., & Jeon, S.-M. (2017) · Oncogene · doi:10.1038/onc.2017.153 · Cited by 115 · see citing works
The Pathways Underlying the Multiple Roles of p62 in Inflammation and Cancer
Hennig, P., Fenini, G., Filippo, M. D., Karakaya, T., & Beer, H. (2021) · Biomedicines · doi:10.3390/biomedicines9070707 · Cited by 117 · see citing works
p62/ SQSTM 1—Dr. Jekyll and Mr. Hyde that prevents oxidative stress but promotes liver cancer
Taniguchi, K., Yamachika, S., He, F., & Karin, M. (2016) · FEBS Letters · doi:10.1002/1873-3468.12301 · Cited by 112 · see citing works
Srivastava, S., Blower, P. J., Aubdool, A. A., Hider, R. C., Mann, G. E., & Siow, R. C. M. (2016) · Scientific Reports · doi:10.1038/s41598-016-0012-5 · Cited by 112 · see citing works
WDR23 regulates NRF2 independently of KEAP1
Lo, J. Y., Spatola, B. N., & Curran, S. P. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006762 · Cited by 109 · see citing works
Uddin, M. J., Kim, E. H., Hannan, M. A., & Ha, H. (2021) · Antioxidants · doi:10.3390/antiox10020258 · Cited by 112 · see citing works
Ya, B., Liu, Q., Li, H., Cheng, H.-J., Yu, T., Chen, L., Wang, Y., Yuan, L., Li, W., Liu, W., et al. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6069150 · Cited by 110 · see citing works
The KEAP1-NRF2 System and Neurodegenerative Diseases
Uruno, A., & Yamamoto, M. P. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0234 · Cited by 111 · see citing works
Self-citationErkens, R., Kramer, C. M., Lückstädt, W., Panknin, C., Krause, L., Weidenbach, M., Dirzka, J., Krenz, T., Mergia, E., Suvorava, T., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.409 · Cited by 108 · see citing works
Yao, W., Lin, S., Su, J. Y., Cao, Q., Chen, Y., Chen, J., Zhang, Z., Hashimoto, K., Qi, Q., & Zhang, J. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01261-6 · Cited by 106 · see citing works
Wang, Y., Liu, Z., Ma, J., Xv, Q., Gao, H., Yin, H., Ge, Y. H., Jiang, X., & Yu, W. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102494 · Cited by 105 · see citing works
Li, Q., Yin, X., Chen, Y., Tang, Y. M., & Zhang, Y. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000484578 · Cited by 104 · see citing works
The NRF2/Keap1 pathway as a therapeutic target in inflammatory bowel disease
Geertsema, S., Bourgonje, A. R., Fagundes, R. R., Gaćeša, R., Weersma, R. K., van Goor, H., Mann, G. E., Dijkstra, G. D. H., & Faber, K. N. (2023) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2023.07.008 · Cited by 101 · see citing works
Essential Role of Keap1-Nrf2 Signaling in Mood Disorders: Overview and Future Perspective
Hashimoto, K. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01182 · Cited by 98 · see citing works
Four-octyl itaconate activates Keap1-Nrf2 signaling to protect neuronal cells from hydrogen peroxide
Liu, H., Feng, Y. Y., Xu, M., Yang, J., Wang, Z., & Di, G. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0294-2 · Cited by 98 · see citing works
Alport Syndrome Classification and Management
Warady, B. A., Agarwal, R., Bangalore, S., Chapman, A. B., Levin, A., Stenvinkel, P., Toto, R. D., & Chertow, G. M. (2020) · Kidney Medicine · doi:10.1016/j.xkme.2020.05.014 · Cited by 98 · see citing works
Toward improved human health: Nrf2 plays a critical role in regulating ferroptosis
Lu, J., Zhao, Y., Liu, M., Lu, J., & Guan, S. (2021) · Food & Function · doi:10.1039/d1fo01036k · Cited by 96 · see citing works
Crossed Pathways for Radiation-Induced and Immunotherapy-Related Lung Injury
Zhang, Z., Zhou, J., Verma, V., Liu, X., Wu, M., Yu, J., & Chen, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.774807 · Cited by 95 · see citing works
Recognition of the Diglycine C-End Degron by CRL2KLHDC2 Ubiquitin Ligase
Rusnac, D.-V., Lin, H.-C., Canzani, D., Tien, K. X., Hinds, T. R., Tsue, A. F., Bush, M. F., Yen, H.-C. S., & Zheng, N. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.021 · Cited by 93 · see citing works
“The most striking difference lies in the affinity of the two classes of degrons toward their cognate E3s.”
Negative Regulation of the Keap1-Nrf2 Pathway by a p62/Sqstm1 Splicing Variant
Kageyama, S., Saito, T., Obata, M., Koide, R.-H., Ichimura, Y., & Komatsu, M. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00642-17 · Cited by 95 · see citing works
A Bibliometric Review of the Keap1/Nrf2 Pathway and its Related Antioxidant Compounds
Paunkov, A., Chartoumpekis, D. V., Ziros, P. G., & Sykiotis, G. P. (2019) · Antioxidants · doi:10.3390/antiox8090353 · Cited by 93 · see citing works
Feng, X., Guan, W., Zhao, Y., Wang, C., Song, M., Yao, Y., Yang, T., & Fan, H. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28539 · Cited by 94 · see citing works
Peng, S., Hou, Y., Yao, J., & Fang, J. (2017) · Food & Function · doi:10.1039/c7fo00054e · Cited by 93 · see citing works
- Authors
- Suzuki, T., & Yamamoto, M.
- Affiliations
- Tohoku University (JP)
- Corresponding author
- Yamamoto, Masayuki
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 88
- Issue
- Pt B
- Pages
- 93-100
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W952491933
- Cited by
- 995
- References
- 84
- Citations by year
- 2026: 62 · 2025: 89 · 2024: 83 · 2023: 102 · 2022: 116 · 2021: 104 · 2020: 118 · 2019: 88 · 2018: 78 · 2017: 82 · 2016: 62 · 2015: 10
- FWCI
- 7.53
- 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/ (am, 360 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
- Free Radical Biology and Medicine (acceptedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Japan Science and Technology Agency
- Japan Society for the Promotion of Science (26460354, 2611010, 24249015, 25112502)
- Takeda Science Foundation
- Naito Foundation
- Core Research for Evolutional Science and Technology
- 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
- Keap1, Nrf2, oxidative stress sensing, electrophilic stress, chemoresistance, carcinogenesis, Nrf2 inhibitors, Nrf2 inducers, therapeutic target
- MeSH terms
- Animals, Humans, Signal Transduction, Intracellular Signaling Peptides and Proteins, NF-E2-Related Factor 2
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