The DOI matches its Crossref record; 84 of the 84 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“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]
Citations
Cites
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
Self-citationKomatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., Sou, Y.-S., Ueno, I., Sakamoto, A., Tong, K. I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2021 · Cited by 2,288
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
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
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 2,210
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
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
Self-citationZhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480
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
Self-citation
Cited by
Sorted by citations
Items 501–600 of 997
Effect of chlorogenic acid on lipid metabolism in 3T3-L1 cells induced by oxidative stress
Liu, L., Zhang, C., Zhai, M., Yu, T., Pei, M., Du, P., Li, A., Yan, J., Li, C., & Zhang, G. (2022) · Food Bioscience · doi:10.1016/j.fbio.2022.102330 · Cited by 22
The Xanthine Oxidase Inhibitor Febuxostat Suppresses Adipogenesis and Activates Nrf2
Higa, Y., Hiasa, M., Tenshin, H., Nakaue, E., Tanaka, M. H., Kim, S., Nakagawa, M., Shimizu, S., Tanimoto, K., Teramachi, J., et al. (2023) · Antioxidants · doi:10.3390/antiox12010133 · Cited by 22
Elbialy, Z. I., Salah, A. S., Elsheshtawy, A., Elkatatny, N. M., Fouad, A. M., & Abo‐Al‐Ela, H. G. (2023) · Aquaculture International · doi:10.1007/s10499-023-01175-8 · Cited by 22
Zheng, K., Zhang, Q., Sheng, Z.-Q., Li, Y., & Lu, H.-H. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000495711 · Cited by 22
Tavakoli, A., Akhgarjand, C., Ansar, H., Houjaghani, H., Khormani, A., Djafarian, K., Rostamian, A., Ranjbar, M., & Farsani, G. M. (2025) · Scientific Reports · doi:10.1038/s41598-025-86734-0 · Cited by 25
Heme oxygenase-1 as a potential therapeutic target in rheumatic diseases
Liu, Y., Lin, Z., He, S., & Zuo, J. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.12.033 · Cited by 21
Kövesi, B., Kulcsár, S., Zándoki, E., Szabó‐Fodor, J., Mézes, M., Balogh, K., Ancsin, Z., & Pelyhe, C. (2020) · Fish Physiology and Biochemistry · doi:10.1007/s10695-020-00845-1 · Cited by 21
Zhang, P., Wang, X., Peng, Q., Jin, Y., Shi, G., Fan, Z., & Zhou, Z. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2206167 · Cited by 21
Molecular mechanisms of autophagy and implications in liver diseases
Wu, Y., Tan, H. W. S., Lin, J.-Y., Shen, H., Wang, H., & Lu, G. X. (2023) · Liver Research · doi:10.1016/j.livres.2023.02.002 · Cited by 24
Cardamonin targets KEAP1/NRF2 signaling for protection against atherosclerosis
Fan, P., Meng, H., Hao, W., Zheng, Y., Li, H., Zhang, Z., Du, L., Guo, X., Wang, D., Wang, Y., et al. (2023) · Food & Function · doi:10.1039/d3fo00967j · Cited by 20
SIRT6 : A potential therapeutic target for diabetic cardiomyopathy
Wu, T., Qu, Y., Xu, S., Wang, Y., Liu, X., & Ma, D. (2023) · The FASEB Journal · doi:10.1096/fj.202301012r · Cited by 23
Ariffianto, A., Deng, L., Abe, T., Matsui, C., Ito, M., Ryo, A., Aly, H. H., Watashi, K., Suzuki, T., Mizokami, M., et al. (2023) · Journal of Virology · doi:10.1128/jvi.01287-23 · Cited by 22
Self-citationYang, F., & Smith, M. J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.11.013 · Cited by 25
Skoupá, N., Doležel, P., Ruzickova, E., & Mlejnek, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112289 · Cited by 21
PML nuclear bodies, membrane-less domains acting as ROS sensors?
Niwa‐Kawakita, M., Wu, H.-C., de Thé, H., & Lallemand-Breitenbach, V. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.11.007 · Cited by 21
Wang, C., Zhou, Y.-L., Zhu, Q.-H., Zhou, Z., Gu, W.-B., Liu, Z.-P., Wang, L.-Z., & Shu, M.-A. (2018) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2018.07.016 · Cited by 22
Liu, D., Xue, J., Liu, Y., Gu, H., Wei, X., Ma, W., Luo, W., Ma, L., Jia, S., Dong, N., et al. (2018) · NeuroToxicology · doi:10.1016/j.neuro.2018.09.005 · Cited by 23
Yang, J. H., Choi, M., Na, C.-S., Cho, S. S., Kim, J. H., Ku, S., Cho, I. J., Shin, H., & Ki, S. H. (2019) · Nutrients · doi:10.3390/nu11010114 · Cited by 21
Pro-caspase-3 protects cells from polymyxin B-induced cytotoxicity by preventing ROS accumulation
Yokosawa, T., Yamada, M., Noguchi, T., Suzuki, S., Hirata, Y., & Matsuzawa, A. (2019) · The Journal of Antibiotics · doi:10.1038/s41429-019-0216-6 · Cited by 21
FAM96B inhibits the senescence of dental pulp stem cells
Liang, H., Li, W., Yang, H., Cao, Y., Ge, L., Shi, R., Fan, Z., Dong, R., & Zhang, C. (2020) · Cell Biology International · doi:10.1002/cbin.11319 · Cited by 21
Rarison, R. H. G., Truong, V., Yoon, B.-H., Park, J., & Jeong, W. (2023) · Foods · doi:10.3390/foods12193643 · Cited by 20
Histone deacetylases and inhibitors in diabetes mellitus and its complications
Wang, L., Bai, Y., Cao, Z., Guo, Z., Lian, Y., Liu, P., Zeng, Y., Lyu, W., & Chen, Q. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117010 · Cited by 24
Sun, G., Huang, D. F., Li, K., & Jiang, Q. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.05.026 · Cited by 20
Chen, W., Su, J., Cai, S., & Shi, C. (2021) · Bioengineered · doi:10.1080/21655979.2021.1943603 · Cited by 20
Nrf2 in the Field of Dentistry with Special Attention to NLRP3
Schieffer, L., Manzl, C., Schatz, C., Haybaeck, J., & Crismani, A. G. (2022) · Antioxidants · doi:10.3390/antiox11010149 · Cited by 20
Gao, F., Chen, M., Yu, J., Xu, L., Yu, L., Jiang, H., & Gu, Z. (2022) · Journal of Functional Foods · doi:10.1016/j.jff.2022.104957 · Cited by 21
Xu, H., Wan, X., Zhu, R.-R., Liu, J., Liu, J., & Zhou, X. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.63297 · Cited by 20
Pectolinarigenin Induces Antioxidant Enzymes through Nrf2/ARE Pathway in HepG2 Cells
Shiraiwa, M., Kitakaze, T., Yamashita, Y., Ukawa, Y., Mukai, K., & Ashida, H. (2022) · Antioxidants · doi:10.3390/antiox11040675 · 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
Zhang, W., Xu, M., Wen, S., Wang, L., Zhang, K., Zhang, C., Zou, H., Gu, J., Liu, X., Bian, J., et al. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.114239 · Cited by 21
Alhaddad, L., Osipov, A. N., & Leonov, S. V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113577 · Cited by 21
Yu, Q., Lee, Y.-Y., Xia, Z., Liong, E. C., Xiao, J., & Tipoe, G. L. (2020) · European Journal of Nutrition · doi:10.1007/s00394-020-02305-1 · Cited by 20
Han, J., Shi, X., Zheng, Z., Zhang, B., Shi, F., Jiang, L., & Xu, J. (2018) · Drug Design Development and Therapy · doi:10.2147/dddt.s184245 · Cited by 20
Tawarayama, H., Suzuki, N., Inoue-Yanagimachi, M., Himori, N., Tsuda, S., Sato, K., Ida, T., Akaike, T., Kunikata, H., & Nakazawa, T. (2020) · Ocular Immunology and Inflammation · doi:10.1080/09273948.2020.1833224 · Cited by 19
Yao, H., Zhang, W., Yang, F., Ai, F., Du, D., & Li, Y. (2021) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2021.1998025 · Cited by 19
Micronutrients and Renal Outcomes: A Prospective Cohort Study
Chen, C., Chiu, C., Wu, I., Hsu, H.-J., Chen, Y.-T., Hsu, C.-K., Pan, H., Lee, C., & Sun, C. (2022) · Nutrients · doi:10.3390/nu14153063 · Cited by 19
Li, Y., Zhu, X., Wang, K., Zhu, L., Murray, M. T., & Zhou, F. (2022) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgac069 · Cited by 22
Oxymatrine ameliorates osteoarthritis via the Nrf2/NF-κB axis in vitro and in vivo
Zhou, K., Liu, D., Jin, Y., Xia, W., Zhang, P., & Zhou, Z. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110539 · Cited by 19
Muscle p62 stimulates the expression of antioxidant proteins alleviating cancer cachexia
Yamada, M., Warabi, E., Oishi, H., Lira, V. A., & Okutsu, M. (2023) · The FASEB Journal · doi:10.1096/fj.202300349r · 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
Karttunen, M., Choy, W., & Cino, E. A. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b03295 · Cited by 19
Protective effect of inducible aldo-keto reductases on 4-hydroxynonenal- induced hepatotoxicity
Li, D., Gu, Z., Zhang, J., & Ma, S. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.02.012 · Cited by 19
Chen, N., Li, Y., Huang, N. J., Yao, J., Luo, W., & Jiang, Q. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29619 · Cited by 19
Wang, Z., Zheng, N., Liang, J., Wang, Q., Xiujie, Z., Wang, H., Yuan, H., Zhang, R., Guo, S., Liu, Y., et al. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.109023 · Cited by 19
Jiang, T., & He, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.851257 · Cited by 19
Role of nuclear factor erythroid 2-related factor 2 (Nrf2) in female and male fertility
Valipour, J., Taghizadeh, F., Esfahani, R., Ramesh, M., & Rastegar, T. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e29752 · Cited by 19
Regulation of KCNMA1 transcription by Nrf2 in coronary arterial smooth muscle cells
Sun, X., Qian, L.-L., Li, Y., Pfiefer, T. M., Wang, X.-L., Lee, H.-C., & Lü, T. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.03.001 · Cited by 18
Wang, X.-M., She, C., Li, Q., Zhang, D., Xu, J., Li, M., Li, P., & Xu, H. (2020) · Aging · doi:10.18632/aging.103009 · Cited by 18
Coleman, D. N., Vailati-Riboni, M., Pate, R. T., Aboragah, A. A., Luchini, D. N., Cardoso, F. C., & Loor, J. J. (2022) · Journal of Animal Science · doi:10.1093/jas/skac175 · Cited by 18
Yang, S., Meng, L., Yunlong, D., He, T., Yao, S., & Li, P. (2022) · BioMed Research International · doi:10.1155/2022/8562795 · Cited by 19
Li, J., Li, T., Li, Z., Song, Z., & Gong, X. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1153297 · Cited by 18
Zhang, M.-J., Sun, W., Yang, J., Shi, D., Dai, X., & Li, X. (2023) · Antioxidants · doi:10.3390/antiox12091677 · Cited by 18
Therapeutic potentials of cannabidiol: Focus on the Nrf2 signaling pathway
Talebi, M., Sadoughi, M. M., Ayatollahi, S. A., Ainy, E., Kiani, R., Zali, A., & Miri, M. M. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115805 · Cited by 20
Zhao, L., Zhang, Z., Li, P., Gao, Y., & Shi, Y. (2023) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-023-02813-x · Cited by 18
Luo, Y., Châtre, L., Melhem, S., Al-Dahmani, Z. M., Homer, N. Z. M., Miedema, A., Deelman, L. E., Groves, M. R., Feelisch, M., Morton, N. M., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102965 · Cited by 18
Targeting Nrf2 to treat thyroid cancer
Gong, Z., Xue, L., Li, H., Fan, S., van Hasselt, C. A., Li, D., Zeng, X., Tong, M. C. F., & Chen, G. G. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116324 · Cited by 18
Alfardan, A. S., Nadeem, A., Ahmad, S. F., Al-Harbi, N. O., Alqinyah, M., Attia, S. M., El‐Sherbeeny, A. M., Al-Harbi, M. M., Al‐Shabanah, O. A., Ibrahim, K. E., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112503 · Cited by 18
Insights into the Pathogenic Secondary Symptoms Caused by the Primary Loss of Dystrophin
Forcina, L., Pelosi, L., Miano, C., & Musarò, A. (2017) · Journal of Functional Morphology and Kinesiology · doi:10.3390/jfmk2040044 · Cited by 18
Redox cell signaling and hepatic progenitor cells
di Bello, G., Vendemiale, G., & Bellanti, F. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.09.004 · Cited by 18
Chen, L., Wang, J., Cai, X., Chen, S., Zhang, J., Li, B., Chen, W., Guo, X., Luo, H., & Chen, J. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105516 · Cited by 19
Jung, Y.-S., Lee, S. H., Chun, S. Y., Kim, D. H., Jang, B. I., Han, M., & Lee, S. (2021) · Molecules · doi:10.3390/molecules27010059 · Cited by 18
Redox Homeostasis and Immune Alterations in Coronavirus Disease-19
Bellanti, F., Buglio, A. L., & Vendemiale, G. (2022) · Biology · doi:10.3390/biology11020159 · Cited by 18
Sun, Y., Zong, W., Wang, J., He, J., Zhang, J., & Han, T. (2025) · Frontiers in Marine Science · doi:10.3389/fmars.2025.1595039 · Cited by 17
Oral isoniazid causes oxidative stress, oocyte deterioration and infertility in mice
Qiao, P., Zhang, Y., Yang, Y., Meng, R., Xu, Z., Jiang, X., Zhang, Y., Zhang, C., & Su, J. (2021) · Toxicology · doi:10.1016/j.tox.2021.152749 · Cited by 17
The Role of Non-Coding RNAs in the Neuroprotective Effects of Glutathione
Kinoshita, C., & Aoyama, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084245 · Cited by 19
McCord, J. M., Hybertson, B. M., Cota‐Gomez, A., & Gao, B. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.033 · Cited by 18
Gao, Y., Liu, W., Su, X., Li, X., Yu, F., & Zhang, N. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/3959390 · Cited by 17
Kyriakaki, P., Zisis, F., Pappas, A. C., Mavrommatis, A., & Tsiplakou, E. (2022) · Metabolites · doi:10.3390/metabo13010044 · Cited by 17
Nita, M., & Grzybowski, A. E. (2023) · Antioxidants · doi:10.3390/antiox12071368 · Cited by 19
Xu, H., Deng, R., Li, E. T. S., Shen, J., & Wang, M. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.104019 · Cited by 17
Shimizu, S., Mimura, J., Hasegawa, T., Shimizu, E., Imoto, S., Tsushima, M., Kasai, S., Yamazaki, H., Ushida, Y., Suganuma, H., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0236834 · Cited by 17
Self-citationQiu, L.-J., Ma, Z., Li, X., Deng, Y., Duan, G., Zhao, L., Xu, X.-W., Xiao, L., Liu, H., Zhu, Z., et al. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa110 · Cited by 17
Chen, D., Wu, Z., Wu, L., Jiang, J., & Hu, G. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.830574 · Cited by 17
Activation of Nrf2 by MIND4-17 protects osteoblasts from hydrogen peroxide-induced oxidative stress
Guo, S., Fei, H., Ji, F., Chen, F., Xie, Y., & Wang, S. (2017) · Oncotarget · doi:10.18632/oncotarget.22360 · Cited by 17
Wen, M., Liu, M.-M., Zhang, Y., Qiao, B., Luo, T., Liu, G., Li, D., & Zhou, B. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144630 · Cited by 17
Lee, S. J., Kim, J. E., Choi, Y. J., Gong, J. E., Park, S. H., Douangdeuane, B., Souliya, O., Park, J. M., Lee, H. S., Kim, B.-H., et al. (2021) · Antioxidants · doi:10.3390/antiox10050791 · Cited by 16
Target Gene Diversity of the Nrf1-MafG Transcription Factor Revealed by a Tethered Heterodimer
Katsuoka, F., Otsuki, A., Hatanaka, N., Okuyama, H., & Yamamoto, M. P. (2022) · Molecular and Cellular Biology · doi:10.1128/mcb.00520-21 · Cited by 16
Self-citationNatural Products as Cancer Chemo Preventive Agents: Where We Stand
Boretti, A. A. (2022) · Natural Product Communications · doi:10.1177/1934578x221144579 · Cited by 16
Hu, B., Chen, R., Jiang, M., Xiong, S., Xie, A., Liu, X., & Fu, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087608 · Cited by 16
Li, T., Jin, M., Huang, L., Zhang, Y., Zong, J., Shan, H., Kang, H., Xu, M., Liu, H., Zhao, Y., et al. (2023) · Aquatic Toxicology · doi:10.1016/j.aquatox.2023.106616 · Cited by 17
Involvement of the Keap1-Nrf2-ARE pathway in the antioxidant activity of sinomenine
Guan, T., Li, N., Xu, X., Xiong, D., Wang, B., Xiao, L., Yang, W., Chu, G., Yusuf, A., Zhang, J., et al. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.109928 · Cited by 16
Protection against HEMA-Induced Mitochondrial Injury In Vitro by Nrf2 Activation
Jiao, Y., Niu, T., Liu, H., Tay, F. R., & Chen, J. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3501059 · Cited by 16
Mo, Y., Zhu, J., Jiang, A., Zhao, J., Ye, L., & Han, B. (2019) · Aging · doi:10.18632/aging.102534 · Cited by 15
The Potential Role of Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2) in Glaucoma: A Review
Wang, M., Li, J., & Zheng, Y. (2020) · Medical Science Monitor · doi:10.12659/msm.921514 · Cited by 16
Li, S., Cheng, W., Li, Y., Xu, H., Han, H., Li, P., & Zhang, D.-X. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-0526-0 · Cited by 16
Busceti, C. L., Cotugno, M., Bianchi, F., Forte, M., Stanzione, R., Marchitti, S., Battaglia, G., Nicoletti, F., Fornai, F., & Rubattu, S. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124289 · Cited by 16
Sun, Q., Shen, X., Ma, J., Lou, H., & Zhang, Q. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.07.026 · Cited by 16
Yang, Y., Li, J., Zhang, L., Lin, Z., Xiao, H., Sun, X., Zhang, M., Liu, P., & Huang, H. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105333 · Cited by 16
Hosohata, K., Jin, D., & Takai, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010446 · Cited by 16
Role of transcriptional factor Nrf2 in the acute lung injury of mice.
Kong, M., Mao, J., Luo, B., & Qin, Z. (2015) · PubMed Central · Cited by 16
Rui, W., Zou, Y., Lee, J., Nambiar, S. M., Lin, J., Zhang, L., Yang, Y., & Dai, G. (2016) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.231316 · Cited by 16
Interplay between Nrf2 and NF-κB in Neuroinflammatory Diseases
Liddell, J. R. (2017) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000489 · Cited by 16
Jung, J. Y., Park, S. M., Ko, H. L., Lee, J. R., Park, C. A., Byun, S. H., Ku, S., Cho, I. J., & Kim, S. C. (2018) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x18500246 · Cited by 16
Yamato, O., Tsuneyoshi, T., Ushijima, M., Jikihara, H., & Yabuki, A. (2018) · BMC Veterinary Research · doi:10.1186/s12917-018-1699-2 · Cited by 16
Kumar, A., Goel, H. L., Silva, C. A., Wang, T., Geng, Y., Wang, M., Goel, S., Hu, K., Li, R., Zhu, L. J., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci181368 · Cited by 16
Possible antidepressant mechanism of acupuncture: targeting neuroplasticity
Xu, N., He, Y., Wei, Y.-N., Bai, L., & Wang, L. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1512073 · Cited by 20
Park, H.-E., Lee, W., Shin, M., & Shin, S. J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.703060 · Cited by 16
Heme oxygenase-1, carbon monoxide, and malaria – The interplay of chemistry and biology
Pena, A. C., & Pamplona, A. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214285 · Cited by 17
Zhao, J., Tang, P., Zhou, Z., Xu, G., Li, Q., Li, K.-R., & Zheng, Y. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01146-7 · Cited by 15
Yang, F., Smith, M. J., 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.2023.102777 · Cited by 15
Metadata
- 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
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