The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Keap1-dependent Proteasomal Degradation of Transcription Factor Nrf2 Contributes to the Negative Regulation of Antioxidant Response Element-driven Gene Expression
Open accessAbstract
Keap1 is a negative regulator of Nrf2, a bZIP transcription factor that mediates adaptation to oxidative stress. Previous studies suggested this negative regulation is a consequence of Keap1 controlling the subcellular distribution of Nrf2. We now report that Keap1 also controls the total cellular level of Nrf2 protein. In the RL34 non-transformed rat liver cell line, Nrf2 was found to accumulate rapidly in response to oxidative stress caused by treatment with sulforaphane, and the accumulation resulted from inhibition of proteasomal-mediated degradation of the bZIP protein. By heterologously expressing in COS1 cells epitope-tagged Nrf2 and an Nrf2DeltaETGE mutant lacking the Keap1-binding site, in both the presence and absence of Keap1 we demonstrate that Nrf2 is subject to ubiquitination and proteasomal degradation independently of both Keap1 and the redox environment of the cell. In oxidatively stressed cells, this is the sole mechanism responsible for Nrf2 degradation. However, under homeostatic conditions Nrf2 is subject to a substantially more rapid mode of proteasomal degradation than it is in oxidatively stressed cells, and this rapid turnover of Nrf2 requires it to interact with Keap1. Within Nrf2, the N-terminal Neh2 domain is identified as the redox-sensitive degron. These data suggest that Keap1 negatively regulates Nrf2 by both enhancing its rate of proteasomal degradation and altering its subcellular distribution.
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
“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 [52]
Citations
Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,296
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-citationDinkova-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
Hayes, J. D., & McLellan, L. I. (1999) · Free Radical Research · doi:10.1080/10715769900300851 · Cited by 1,528
The Proteasome: Paradigm of a Self-Compartmentalizing Protease
Baumeister, W. P., Walz, J., Zühl, F., & Seemüller, E. (1998) · Cell · doi:10.1016/s0092-8674(00)80929-0 · Cited by 1,497
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
The ubiquitin–proteasome pathway: on protein death and cell life
Ciechanover, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7151 · Cited by 1,419
Flagged first, then by citations
Research works printed but not linked: 4
- Kelly, 2000, Cancer Res., 60, 957
- McMahon, 2001, Cancer Res., 61, 3299
- Thimmulappa, 2002, Cancer Res., 62, 5196
- Bonneson, 2001, Cancer Res., 61, 6120
Cited by
Sorted by citations
Items 701–800 of 1,000
McMahon, M. J., Campbell, K. H., MacLeod, A. K., McLaughlin, L. A., Henderson, C. J., & Wolf, C. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114055 · Cited by 24
Limited expression of Nrf2 in neurons across the central nervous system
Levings, D. C., Pathak, S. S., Yang, Y., & Slattery, M. G. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102830 · Cited by 23
Kapuy, O., Holczer, M., Márton, M., & Korcsmáros, T. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03599-7 · Cited by 24
Snijders, K. E., Fehér, A., Táncos, Z., Bock, I., Téglási, A., van den Berk, L., Niemeijer, M., Bouwman, P., Dévédec, S. E. L., Moné, M. J., et al. (2021) · Archives of Toxicology · doi:10.1007/s00204-021-03127-8 · Cited by 23
Xie, D., Wei, H., Lee, J., & Wang, M. (2022) · Environmental Pollution · doi:10.1016/j.envpol.2022.119170 · Cited by 23
Şahin, D., Çağlar, E. Ş., Boran, T., Karadağ, A. E., Özhan, G., & Okur, N. Ü. (2023) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2023.104422 · Cited by 23
Tabei, Y., Abe, H., Suzuki, S., Takeda, N., Arai, J.-I., & Nakajima, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216532 · Cited by 23
Sobočanec, S., Šarić, A., Šafranko, Ž. M., Hadžija, M. P., Abramić, M., & Balog, T. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.03.014 · Cited by 23
Metabolic contribution of hepatic autophagic proteolysis: Old wine in new bottles
Ueno, T., Ezaki, J., & Kominami, E. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.019 · Cited by 23
Cytochrome P450 2A5 and bilirubin: Mechanisms of gene regulation and cytoprotection
Kim, S. D., Antenos, M., Squires, E. J., & Kirby, G. M. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.04.013 · Cited by 24
Yukitake, H., Takizawa, M., & Kimura, H. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8584930 · Cited by 23
McMahon, M. J., Ding, S., Acosta-Jimenez, L., Frangova, T. G., Henderson, C. J., & Wolf, C. R. (2017) · The Journal of Physiology · doi:10.1113/jp274915 · Cited by 21
Wang, J. (2018) · Phytotherapy Research · doi:10.1002/ptr.6067 · Cited by 23
Bousquet, M. S., Ratnayake, R., Pope, J. L., Chen, Q.-Y., Zhu, F., Chen, S., Carney, T. J., Gharaibeh, R. Z., Jobin, C., Paul, V. J., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.013 · Cited by 23
Liu, B., Chen, Z., Li, Z., Zhao, X., Zhang, W., Zhang, A., Wen, L., Wang, X., Zhou, S., & Qian, D. (2024) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2024138 · Cited by 25
Binding of Disordered Peptides to Kelch: Insights from Enhanced Sampling Simulations
Do, T. N., Choy, W., & Karttunen, M. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00868 · Cited by 22
Cykowiak, M., Krajka‐Kuźniak, V., & Baer‐Dubowska, W. (2021) · Nutrition and Cancer · doi:10.1080/01635581.2021.1933097 · Cited by 22
Adams, B., Mapanga, R. F., & Essop, M. F. (2015) · Cardiovascular Diabetology · doi:10.1186/s12933-015-0258-4 · Cited by 22
Alam, M. B., Kwon, K.-R., Lee, S.-H., & Lee, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020266 · Cited by 22
Li, C., Xin, H., Shi, Y., & Mu, J. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107428 · Cited by 22
Kim, K. C., Lee, I. K., Kang, K. A., Cha, J. W., Cho, S. J., Na, S. Y., Chae, S., Kim, H. S., Kim, S., & Hyun, J. W. (2013) · BioMed Research International · doi:10.1155/2013/863720 · Cited by 22
Emerging Therapeutic Targets in Oncologic Photodynamic Therapy
Manda, G., Hinescu, M. E., Neagoe, I. V., Ferreira, L. F. V., Boscencu, R., Vasos, P. R., Basaga, S. H., & Cuadrado, A. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190122163832 · Cited by 23
Role of 4-hydroxynonenal in chemopreventive activities of sulforaphane
Sharma, R., Sharma, A., Chaudhary, P., Sahu, M., Jaiswal, S., Awasthi, S., & Awasthi, Y. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.012 · Cited by 21
Balasubramanian, P., Asirvatham‐Jeyaraj, N., Monteiro, R., Sivasubramanian, M. K., Hall, D., & Subramanian, M. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00206.2019 · Cited by 21
Παπανικολάου, Κ., Veskoukis, A. S., Draganidis, D., Baloyiannis, I., Deli, C. K., Poulios, A., Jamurtas, A. Z., & Fatouros, I. G. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.10.001 · Cited by 22
Tang, Z., Chen, B.-J., & Niu, C.-J. (2021) · Cryobiology · doi:10.1016/j.cryobiol.2021.01.015 · Cited by 24
Qing, T.-L., Yan, L., Wang, S., Dai, X., Ren, L., Zhang, J., Shi, W., Zhang, X., Wang, M.-T., Chen, J., et al. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.114623 · Cited by 21
Lee, H. G., Li, M., Joung, E.-J., Na, H., Cha, Y., & Surh, Y. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3226 · Cited by 21
Hahn, M. E., Merson, R. R., & Karchner, S. I. (2005) · Biochemistry and molecular biology of fishes · doi:10.1016/s1873-0140(05)80010-4 · Cited by 21
Ting, K. K. Y. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1403915 · Cited by 20
Kim, J., Park, H., Lee, J., & Kang, T. (2020) · Cells · doi:10.3390/cells9051123 · Cited by 21
Nakada, E. M., Sun, R., Fujii, U., & Martin, J. G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.665622 · Cited by 22
Depleted uranium causes renal mitochondrial dysfunction through the ETHE1/Nrf2 pathway
Liu, S., Wang, S., Zhao, Y., Li, J., Shu, C., Li, Y., Li, J., Lu, B., Xu, Z., Ran, Y., et al. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110356 · Cited by 20
Redox-dependent signaling system Nrf2/ARE in inflammation
Брониславовна, М. Е., Tkachev, V., & Зенков, Н. К. (2010) · Molecular Biology · doi:10.1134/s0026893310030015 · Cited by 20
Edwards, M. R., & Basler, C. F. (2015) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiv050 · Cited by 21
Ano, S., Panariti, A., Allard, B., O’Sullivan, M. J., McGovern, T. K., Hamamoto, Y., Ishii, Y., Yamamoto, M. P., Powell, W. S., & Martin, J. G. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.017 · Cited by 20
Yoshizaki, Y., Mori, T., Ishigami‐Yuasa, M., Kikuchi, E., Takahashi, D., Zeniya, M., Nomura, N., Mori, Y., Araki, Y., Ando, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04233-3 · Cited by 20
Cardio- and reno-protective effects of dipeptidyl peptidase III in diabetic mice
Komeno, M., Pang, X., Shimizu, A., Molla, M. R., Yasuda‒Yamahara, M., Kume, S., Rahman, N. I. A., Soh, J. E. C., Nguyen, L. K. C., Amin, M. K. B. A., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100761 · Cited by 21
Ma, L., Li, C., Lian, S., Xu, B., Lv, H., Liu, Y., Lu, J., Ji, H. L., Li, S., Guo, J., et al. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16733 · Cited by 19
Wang, J., Wang, S., Sun, S., Lu, Y., Gao, K., Guo, C., Li, R., Li, W., Zhao, X., Tang, H., et al. (2020) · Aging · doi:10.18632/aging.104050 · Cited by 19
Wei, J., Zhao, J., Su, T., Li, S., Wenjun, S., Feng, L., & Bi, Y. (2023) · Antioxidants · doi:10.3390/antiox12030562 · Cited by 20
Transcription Factor NRF2 in Shaping Myeloid Cell Differentiation and Function
Pfefferlé, M., & Vallelian, F. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-62731-6_8 · Cited by 18
Regulation of the CNC-bZIP transcription factor Nrf2 by Keap1 and the axis between GSK-3 and β-TrCP
Hayes, J. D., Ebisine, K., Sharma, R. S., Chowdhry, S., Dinkova‐Kostova, A. T., & Sutherland, C. D. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.003 · Cited by 19
Nrf2 Activation as a Protective Feedback to Limit Cell Death in High Glucose‐Exposed Cardiomyocytes
Tsai, C., Wen, S., Cheng, S., Wang, C., Yang, Y., Viswanadha, V. P., Huang, C., & Kuo, W. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25785 · Cited by 19
Inhibition of Nrf2 promotes the antitumor effect of Pinelliae rhizome in papillary thyroid cancer
Du, Z., Wang, Q., Ma, G., Jiao, J., Jiang, D., Zheng, X., Qiu, M., & Liu, S. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28069 · Cited by 19
Simenauer, A., Assefa, B., Rios-Ochoa, J., Geraci, K. P., Hybertson, B. M., Gao, B., McCord, J. M., Elajaili, H. B., Nozik‐Grayck, E., & Cota‐Gomez, A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.06.015 · Cited by 19
Patra, U., Mukhopadhyay, U., Mukherjee, A., Sarkar, R., & Chawla‐Sarkar, M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7289120 · Cited by 19
Eslami, M., Esfandyari, S., Aghahosseini, M., Rashidi, Z., Hosseinishental, S. H., Brenjian, S., Sobhani, A., & Amidi, F. (2021) · PubMed Central · doi:10.22074/cellj.2021.7222 · Cited by 19
Dong, D., Qi, Y., Xu, L., Yin, L., Xu, Y., Han, X., Zhao, Y., & Peng, J. (2014) · Food & Function · doi:10.1039/c4fo00491d · 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
Lee, J., Seo, Y. J., & Roh, J. (2025) · Antioxidants · doi:10.3390/antiox14080993 · Cited by 18
Dysregulation of Transcription Factors: A Key Culprit Behind Neurodegenerative Disorders
Jin, W., Qazi, T. J., Quan, Z., Li, N., & Qing, H. (2018) · The Neuroscientist · doi:10.1177/1073858418811787 · Cited by 17
Zhao, Y. D., Wang, Y., Zhang, M., Gao, Y., & Yan, Z. (2021) · Chemistry & Biodiversity · doi:10.1002/cbdv.202001007 · Cited by 18
Dong, H., Liu, M., Wang, L., Liu, Y., Lu, X., Stagos, D., Lin, X., & Liu, M. (2021) · Antioxidants · doi:10.3390/antiox10091436 · Cited by 18
Redox Biology in Adipose Tissue Physiology and Obesity
Yu, J., Qiu, J., Zhang, Z., Cui, X., Guo, W., Sheng, M., Gao, M., Wang, D., Xu, L., & Ma, X. (2023) · Advanced Biology · doi:10.1002/adbi.202200234 · Cited by 20
Zhang, Z., Liu, Y., Feng, W., Mao, P., Yang, J., Zhao, Z., Zhou, S., Zhao, A. Z., Li, F., & Mu, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137457 · Cited by 20
Demasi, M., Simões, V., & Bonatto, D. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.10.031 · Cited by 20
Wang, F., Liu, P., An, H., & Zhang, Y. L. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4665 · Cited by 18
Song, N., Kim, D., Kim, E., Na, H., & Surh, Y. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04914.x · Cited by 19
Ghali, E. N. H. K., Kumar, S. S., Meriga, B., Maurya, D. K., & Kesavulu, M. M. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111801 · Cited by 18
Sutton, E. R., & Pekovic‐Vaughan, V. (2025) · Antioxidants · doi:10.3390/antiox14091132 · Cited by 20
A novel yeast model detects Nrf2 and Keap1 interactions with Hsp90
Ngo, V., Brickenden, A. M., Liu, H., Yeung, C., Choy, W., & Duennwald, M. L. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049258 · Cited by 16
Zhang, Y., Yu, W., Liu, Y., Chang, W., Wang, M., & Zhang, L. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.995518 · Cited by 17
Díaz, M. L., Valdés‐Baizabal, C., Pereda, D., & Marín, R. (2024) · Antioxidants · doi:10.3390/antiox13020206 · Cited by 17
Garnier, N. M., Petruccelli, L. A., Molina, M. F., Kourelis, M., Kwan, S., Diaz, Z., Schipper, H. M., Gupta, A., Rincon, S. V. D., Mann, K. K., et al. (2013) · Leukemia · doi:10.1038/leu.2013.54 · Cited by 17
Kong, L., Liu, B., Zhang, C., Wang, B., Wang, H., Song, X., Yang, Y., Ren, X. S., Yin, L., Kong, H., et al. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.08.011 · Cited by 17
Cai, M., Li, T., Dong, B., Hou, W., Shi, L., & Dong, H. (2016) · Anesthesiology · doi:10.1097/aln.0000000000001485 · Cited by 17
Targeting Autophagy In Disease: Recent Advances In Drug Discovery
Kim, D., Hwang, H., & Kwon, H. J. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1773429 · Cited by 17
Xu, Q., Zhang, Z., Tang, M., Xing, C., Chen, H., Zheng, K., Zhao, Z., Zhou, S., Zhao, A. Z., Li, F., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.03.005 · Cited by 16
Role of Protein Phosphorylation in the Regulation of NF-E2–Related Factor 2 Activity
Sherratt, P. J., Huang, H., Nguyen, T., & Pickett, C. B. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)78022-2 · Cited by 17
Li, K., Ji, X., Tian, S., Li, J., Tian, Y., Ma, X., Huan-ping, L., Zhang, H., Chen, C.-T., & Gu, W. (2025) · Cell and Tissue Research · doi:10.1007/s00441-025-03953-7 · Cited by 18
Role of oxeiptosis in disease mechanisms and therapeutic opportunities
Bhuvaneshwari, K., Harithpriya, K., Ganesan, K., Xu, B., & Ramkumar, K. M. (2025) · APOPTOSIS · doi:10.1007/s10495-025-02087-z · Cited by 16
Arisawa, K., Natori, M., Hiranuma, T., Shimizu, M., Yamazaki, Y., Miki, Y., Toyama, T., & Saito, Y. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103821 · Cited by 16
The Keap1-Nrf2 pathway: From mechanism to medical applications
Baird, L., & Yamamoto, M. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00009-2 · Cited by 16
Milosavljevic, I. M., Jakovljevic, V. L., Petrović, D., Draginic, N. D., Jeremic, J. N., Mitrović, M., Zivkovic, V. I., Srejovic, I. M., Stojić, V., Bolevich, S., et al. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04225-y · Cited by 16
Song, Y., Wang, M., Zhao, S., Tian, Y., & Zhang, C. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.936632 · Cited by 16
Wei, Y., Wang, H., Zhang, Y., Gu, J., Zhang, X., Gong, X.-H., & Hao, Z. (2022) · Antioxidants · doi:10.3390/antiox11112234 · Cited by 16
Ranasinghe, N., Chen, W., Hu, Y.-C., Gamage, L., Lee, T., & Ho, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216187 · Cited by 16
Gayatri, V., Prasad, M. K., Mohandas, S., Nagarajan, S., Kumaran, K., & Ramkumar, K. M. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176241 · Cited by 17
Dopaminergic REST/NRSF is protective against manganese-induced neurotoxicity in mice
Pajarillo, E. A. B., Kim, S. H., Digman, A., Ajayi, I., Nyarko‐Danquah, I., Son, D., Aschner, M., & Lee, E.-S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107707 · Cited by 16
Xie, W., Pao, C. S., Graham, T. L., Dul, E., Lu, Q., Sweitzer, T. D., Ames, R. S., & Li, H. (2012) · Assay and Drug Development Technologies · doi:10.1089/adt.2011.436 · Cited by 16
Baqader, N. O., Radulović, M., Crawford, M., Stoeber, K., & Godovac‐Zimmermann, J. (2014) · Journal of Proteome Research · doi:10.1021/pr500638h · Cited by 16
Zagorski, J. W., Maser, T. P., Liby, K. T., & Rockwell, C. E. (2017) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.116.238899 · Cited by 16
Phenethyl isothiocyanate protects against H2O2-induced insulin resistance in 3T3-L1 adipocytes
Nagami, M., Ito, Y., & Nagasawa, T. (2017) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2017.1372181 · Cited by 16
Inhibition of early T cell cytokine production by arsenic trioxide occurs independently of Nrf2
VanDenBerg, K. R., Freeborn, R. A., Liu, S., Kennedy, R. C. M., Zagorski, J. W., & Rockwell, C. E. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185579 · Cited by 16
Elshaer, M., ElManawy, A. I., Hammad, A., Namani, A., Wang, X. J., & Tang, X. (2020) · Aging · doi:10.18632/aging.103068 · Cited by 16
Extract of Ginkgo biloba induces glutathione-S-transferase subunit-P1 in vitro
Liu, X., Goldring, C. E., Wang, H.-Y., Copple, I. M., Kitteringham, N. R., & Park, B. K. (2009) · Phytomedicine · doi:10.1016/j.phymed.2008.11.001 · Cited by 16
Pin1 Plays Essential Roles in NASH Development by Modulating Multiple Target Proteins
Inoue, M.-K., Nakatsu, Y., Yamamotoya, T., Hasei, S., Kanamoto, M., Naitou, M., Matsunaga, Y., Sakoda, H., Fujishiro, M., Ono, H., et al. (2019) · Cells · doi:10.3390/cells8121545 · Cited by 16
Padmanabhan, B., Scharlock, M., Tong, K. I., Nakamura, Y., Kang, M.-I., Kobayashi, A., Matsumoto, T., Tanaka, A., Yamamoto, M., & Yokoyama, S. (2004) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309104032506 · Cited by 16
Effects of Cyclopentenone Prostaglandins on the Expression of Heme Oxygenase‐1 in MCF‐7 Cells
Kim, E. H., Kim, D., Na, H., & Surh, Y. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1329.061 · Cited by 16
Bates, D. J. P., Smitherman, P. K., Townsend, A. J., King, S. B., & Morrow, C. S. (2011) · Biochemistry · doi:10.1021/bi2005784 · Cited by 15
Das, A., Chowdhury, O., Gupta, P., Das, N., Mitra, A., Ghosh, S., Ghosh, S., Sarkar, S., Bandyopadhyay, D., & Chattopadhyay, S. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121290 · Cited by 15
Yamagishi, N., Yamamoto, Y., Nishi, T., Ito, T., & Kanai, Y. (2023) · PLoS ONE · doi:10.1371/journal.pone.0287788 · Cited by 16
Lee, Y. S., Kang, J. K., Jung, E. S., & Lee, A. (2023) · Journal of Breast Cancer · doi:10.4048/jbc.2023.26.e42 · Cited by 15
Toxicity and oxidative stress of HepG2 and HL-7702 cells induced by PAH4 using oil as a carrier
Liu, G., Zhou, W., Zhang, X., Zhu, J., Xu, X., Li, Y., Zhang, J., Wen, C., Liang, L., Liu, X., et al. (2024) · Food Research International · doi:10.1016/j.foodres.2024.113988 · Cited by 15
Physiological and molecular predictors of cycling sprint performance
Galván-Álvarez, V., Gallego-Selles, Á., Martinez‐Canton, M., Pérez-Suárez, I., García-Gonzalez, E., Martín-Rincón, M., & Calbet, J. A. L. (2024) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.14545 · Cited by 15
Rahtes, A., & Li, L. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01478 · Cited by 15
Prominent role of exopeptidase DPP III in estrogen-mediated protection against hyperoxia in vivo
Sobočanec, S., Filić, V., Matovina, M., Majhen, D., Šafranko, Ž. M., Hadžija, M. P., Krsnik, Ž., Kurilj, A. G., Šarić, A., Abramić, M., et al. (2016) · Redox Biology · doi:10.1016/j.redox.2016.01.003 · Cited by 15
Zhang, Z., Cheng, X., Ge, D., Wang, S., & Qi, B. (2018) · Medical Science Monitor · doi:10.12659/msm.911150 · Cited by 15
Dikovskaya, D., Appleton, P. L., Bento‐Pereira, C., & Dinkova‐Kostova, A. T. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00354 · Cited by 15
Metadata
- Authors
- McMahon, M., Itoh, K., Yamamoto, M., & Hayes, J. D.
- Affiliations
- University of Dundee (GB)
- University of Tsukuba (JP)
- Corresponding author
- McMahon, Michael
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 278
- Issue
- 24
- Pages
- 21592-21600
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2040114786
- Cited by
- 1,141
- References
- 54
- Citations by year
- 2026: 39 · 2025: 52 · 2024: 56 · 2023: 53 · 2022: 54 · 2021: 57 · 2020: 66 · 2019: 56 · 2018: 52 · 2017: 67 · 2016: 65 · 2015: 47 · 2014: 60 · 2013: 50 · 2012: 45
- FWCI
- 14.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- 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 › Ubiquitin and proteasome pathways
- Keywords
- Keap1, Nrf2, proteasomal degradation, ubiquitination, oxidative stress, antioxidant response element, bZIP transcription factors, subcellular localization, sulforaphane, hepatocytes
- MeSH terms
- Animals, Epitopes, Antioxidants, Binding Sites, Carrier Proteins, Cell Line, Cell Nucleus, Cysteine Endopeptidases, DNA-Binding Proteins, Escherichia coli, Gene Expression Regulation, Multienzyme Complexes, Oxidation-Reduction, Plasmids, Protein Binding, RNA, Messenger, Subcellular Fractions, Sulfoxides, Thiocyanates, Time Factors, Transcription, Genetic, Transfection, Immunoblotting, Trans-Activators, Protein Structure, Tertiary, Isothiocyanates, Genes, Reporter, Oxidative Stress, COS Cells, Response Elements, Ubiquitin, Proteasome Endopeptidase Complex, NF-E2-Related Factor 2, Rats
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