The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
Open accessAbstract
Hypersensitive site 2 located in the beta-globin locus control region confers high levels of expression to the genes of the beta-globin cluster. A tandem repeat of the consensus sequence for the transcription factors AP1 and NF-E2 (activating protein 1 and nuclear factor erythroid 2, respectively) is present within hypersensitive site 2 and is absolutely required for strong enhancer activity. This sequence binds, in vitro and in vivo, to ubiquitous proteins of the AP1 family and to the recently cloned erythroid-specific transcription factor NF-E2. Using the tandem repeat as a recognition site probe to screen a lambda gt11 cDNA expression library from K562 cells, we isolated several DNA binding proteins. Here, we report the characterization of one of the clones isolated. The gene, which we named Nrf2 (NF-E2-related factor 2), is encoded within a 2.2-kb transcript and predicts a 66-kDa protein with a basic leucine zipper DNA binding domain highly homologous to that of NF-E2. Although Nrf2 is expressed ubiquitously, a role of this protein in mediating enhancer activity of hypersensitive site 2 in erythroid cells cannot be excluded. In this respect, Nrf2 contains a powerful acidic activation domain that may participate in the transcriptional stimulation of beta-globin genes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The text we found for this paper looks like another document, so the self-check wasn’t run.
Citations
Cites
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
Recombinant Genomes Which Express Chloramphenicol Acetyltransferase in Mammalian Cells
Gorman, C., Moffat, L. F., & Howard, B. H. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.9.1044 · Cited by 7,674
An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
Kozak, M. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.20.8125 · Cited by 5,090
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Firefly Luciferase Gene: Structure and Expression in Mammalian Cells
de Wet, J. R., Wood, K. V., DeLuca, M., Helinski, D. R., & Subramani, S. E. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.2.725 · Cited by 3,088
Transcriptional Regulation in Mammalian Cells by Sequence-Specific DNA Binding Proteins
Mitchell, P. J., & Tjian, R. (1989) · Science · doi:10.1126/science.2667136 · Cited by 3,046
Position-independent, high-level expression of the human β-globin gene in transgenic mice
Grosveld, F. G., van Assendelft, G. B., Greaves, D. R., & Kollias, G. A. (1987) · Cell · doi:10.1016/0092-8674(87)90584-8 · Cited by 1,908
GAL4-VP16 is an unusually potent transcriptional activator
Sadowski, I., Ma, J., Triezenberg, S., & Ptashne, M. (1988) · Nature · doi:10.1038/335563a0 · Cited by 1,298
Firefly Luciferase Gene: Structure and Expression in Mammalian Cells
de Wet, J. R., Wood, K. V., DeLuca, M. A., et al. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.2.725-737.1987 · Cited by 913
Tsai, S., Martin, D. I. K., Zon, L. I., D’Andrea, A. D., Wong, G. G., & Orkin, S. H. (1989) · Nature · doi:10.1038/339446a0 · Cited by 884
Cited by
Sorted by citations
Items 701–800 of 1,002
Discovery of a novel Nrf2 inhibitor that induces apoptosis of human acute myeloid leukemia cells
Zhang, J., Su, L., Ye, Q., Zhang, S., Kung, H., Jiang, F., Jiang, G., Miao, J., & Zhao, B. (2016) · Oncotarget · doi:10.18632/oncotarget.13825 · Cited by 48
Bresciani, A., Missineo, A., Gallo, M. L., Cerretani, M., Fezzardi, P., Tomei, L., Cicero, D. O., Altamura, S., Santoprete, A., Ingenito, R., et al. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.08.003 · Cited by 49
Zhao, X., Liu, L., WANG, Y., Wang, G., Zhao, Y.-X., & Zhang, Y. (2019) · Physiological Research · doi:10.33549/physiolres.934084 · Cited by 49
El‐Ghafar, O. A. M. A., Hassanein, E. H. M., Sayed, A. M. M., Rashwan, E. K., Shalkami, A. S., & Mahmoud, A. M. (2021) · Phytotherapy Research · doi:10.1002/ptr.7153 · Cited by 48
Reduced oxidative-stress response in red blood cells from p45NFE2-deficient mice
Chan, J. Y., Kwong, M., Lo, M. C., Emerson, R. K., & Kuypers, F. A. (2001) · Blood · doi:10.1182/blood.v97.7.2151 · Cited by 48
Amrolia, P. J., Cunningham, J. M., Ney, P. A., Nienhuis, A. W., & Jane, S. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12892 · Cited by 48
Modulation of Reactive Oxygen Species to Overcome 5-Fluorouracil Resistance
Chun, K., & Joo, S. H. (2022) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2022.017 · Cited by 52
Shukla, S. J., Huang, R., Simmons, S. O., Tice, R. R., Witt, K. L., VanLeer, D., Ramabhadran, R., Austin, C. P., & Xia, M. (2012) · Environmental Health Perspectives · doi:10.1289/ehp.1104709 · Cited by 47
Zhang, Y., & Hayes, J. D. (2010) · Biochemical Journal · doi:10.1042/bj20100471 · Cited by 47
Cortese-Krott, M. M., Suschek, C. V., Wetzel, W., Kröncke, K., & Kolb-Bachofen, V. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00643.2008 · Cited by 47
Nrf2 in aging – Focus on the cardiovascular system
Klóska, D., Kopacz, A., Piechota-Polańczyk, A., Nowak, W. N., Dulak, J., Józkowicz, A., & Grochot‐Przeczek, A. (2018) · Vascular Pharmacology · doi:10.1016/j.vph.2018.08.009 · Cited by 47
Role of thioredoxin in lung disease
Xu, J., Li, T., Wu, H., & Xu, T. (2012) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2012.01.002 · Cited by 50
Murphy, P., & Kolstø, A. (2000) · Mechanisms of Development · doi:10.1016/s0925-4773(00)00413-5 · Cited by 47
Forsberg, E. C., Johnson, K., Zaboikina, T. N., Mosser, E. A., & Bresnick, E. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.26850 · Cited by 46
Shen, X., Hu, B., Xu, G., Chen, F., Ma, R., Zhang, N., Liu, J., Ma, X., Zhu, J., Wu, Y., et al. (2017) · Kidney & Blood Pressure Research · doi:10.1159/000477947 · Cited by 46
A Novel Nrf2 Pathway Inhibitor Sensitizes Keap1-Mutant Lung Cancer Cells to Chemotherapy
Zhang, D., Hou, Z., Aldrich, K. E., Lockwood, L. R., Odom, A. L., & Liby, K. T. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0210 · Cited by 46
The Nrf2 in Obesity: A Friend or Foe?
Xia, Y., Zhai, X., Qiu, Y., Lu, X., & Jiao, Y. (2022) · Antioxidants · doi:10.3390/antiox11102067 · Cited by 46
Natural Allies for Heart Health: Nrf2 Activation and Cardiovascular Disease Management
Khan, S. U., Khan, S. U., Suleman, M., Khan, S. U., Suleman, M., Arbi, F. M., Hussain, T., Alsuhaibani, A. M., & Refat, M. S. E.-D. (2023) · Current Problems in Cardiology · doi:10.1016/j.cpcardiol.2023.102084 · Cited by 47
A state-of-the-art review on the NRF2 in Hepatitis virus-associated liver cancer
Kalantari, L., Ghotbabadi, Z. R., Gholipour, A., Ehymayed, H. M., Najafiyan, B., Amirlou, P., Yasamineh, S., Gholizadeh, O., & Emtiazi, N. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01351-6 · Cited by 47
Polymorphisms in the transcription factor NRF2 and forearm vasodilator responses in humans
Marczak, E. D., Marzec, J. M., Zeldin, D. C., Kleeberger, S. R., Brown, N., Pretorius, M., & Lee, C. R. (2012) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0b013e32835516e5 · Cited by 46
Dong, L., Dai, F., Sun, L., & Zhou, B. (2015) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500297 · Cited by 46
Ji, X., CHEN, S.-H., Zhu, L., Pan, H., Zhou, Y., Li, W., You, W., Gao, C.-C., Zhu, J., Jiang, K., et al. (2013) · Oncology Reports · doi:10.3892/or.2013.2476 · Cited by 46
Recent progress in the development of small molecule Nrf2 modulators: a patent review (2012-2016)
Sun, H., Zhu, J., Lin, H., Gu, K. X., & Feng, F. (2017) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1325464 · Cited by 47
Park, D.-D., Yum, H.-W., Zhong, X., Kim, S. H., Kim, S. H., Kim, D., Kim, S., Na, H., Sato, A., Miura, T., et al. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00482 · Cited by 46
Global Analysis of Enhancer Targets Reveals Convergent Enhancer-Driven Regulatory Modules
Xie, S., Armendariz, D. A., Zhou, P., Duan, J., & Hon, G. C. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.073 · Cited by 46
Aktepe, O. H., Şahin, T. K., Güner, G., Arık, Z., & Yalçın, Ş. (2020) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.3906/sag-2005-413 · Cited by 47
Panieri, E., & Saso, L. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8146 · Cited by 46
Redox activation of Ref-1 potentiates cell survival following myocardial ischemia reperfusion injury
Gurusamy, N., Malik, G., Gorbunov, N. V., & Das, D. K. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.04.025 · Cited by 46
Transcriptional control of globin gene switching during vertebrate development
Baron, M. H. (1997) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(96)00195-9 · Cited by 46
Manandhar, S., Choi, B.-H., Jung, K.-A., Ryoo, I.-G., Song, M., Kang, S. J., Choi, H.-G., Kim, J.-A., Park, P.-H., & Kwak, M.-K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.031 · Cited by 45
NRF2 in kidney physiology and disease
Bondi, C. D., Hartman, H. L., & Tan, R. J. (2024) · Physiological Reports · doi:10.14814/phy2.15961 · Cited by 46
Yu, Z. (2012) · World Journal of Diabetes · doi:10.4239/wjd.v3.i1.19 · Cited by 45
Li, Y., Zou, X., Cao, K. J., Xu, J., Yue, T., Dai, F., Zhou, B., Lu, W., Feng, Z., & Liu, J. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.07.029 · Cited by 45
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
Han, W., Ming, M., Zhao, R., Pi, J., Wu, C., & He, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.363614 · Cited by 45
Rajesh, Y., Biswas, A., Kumar, U., Das, S., Banerjee, I., Banik, P., Bharti, R., Nayak, S., Ghosh, S. K., & Mandal, M. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.03.025 · Cited by 45
Jingyuan, H., Yan, L., Wenjing, P., Jiang, W., Liu, B., Linghong, M., Qunlang, Z., Liang, H., & Xian-ping, G. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.03.041 · Cited by 45
Fu, Y., & Jia, J. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.638772 · Cited by 45
Hu, L., Johnston, L. J., Wang, F., & Ma, X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111411 · Cited by 45
Yuan, J.-H., Li, Y., & Yang, X. (2008) · Molecular Medicine · doi:10.2119/2007-00050.yuan · Cited by 45
Megherbi, R., Kiorpelidou, E., Foster, B. J., Rowe, C., Naisbitt, D. J., Goldring, C. E., & Park, B. K. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.05.001 · Cited by 50
Zhang, Y., & Hayes, J. D. (2013) · Scientific Reports · doi:10.1038/srep02006 · Cited by 45
Lee, J., Anderson, P. C., Padgitt, J. K., Hanson, J. M., Waters, C. M., & Johnson, J. A. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.08.006 · Cited by 45
Transgenic expression of BACH1 transcription factor results in megakaryocytic impairment
Toki, T. (2004) · Blood · doi:10.1182/blood-2004-07-2826 · Cited by 45
Role of the Nrf2 Signaling Pathway in Ovarian Aging: Potential Mechanism and Protective Strategies
Gao, X., Wang, B., Huang, Y., Wu, M., Li, Y., Li, Y., Zhu, X., & Wu, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713327 · Cited by 44
Oliveira, A. M., Cardoso, S. M., Ribeiro, M., Seixas, R. S. G. R., Silva, A. M. S., & Rego, A. C. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.10.004 · Cited by 44
NRF2-ome: An Integrated Web Resource to Discover Protein Interaction and Regulatory Networks of NRF2
Türei, D., Papp, D., Fazekas, D., Földvári-Nagy, L., Módos, D., Lenti, K., Csermely, P., & Korcsmaros, T. D. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/737591 · Cited by 44
Weerachayaphorn, J., Amaya, M. J., Spirlı̀, C., Chansela, P., Mitchell-Richards, K., Ananthanarayanan, M., & Nathanson, M. H. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.03.014 · Cited by 44
Phytochemical Regulation of UDP-Glucuronosyltransferases: Implications for Cancer Prevention
Saracino, M. R., & Lampe, J. W. (2007) · Nutrition and Cancer · doi:10.1080/01635580701458178 · Cited by 44
Qian, C., Wang, Y., Zhong, Y., Tang, J., Zhang, J., Li, Z., Wang, Q., & Hu, R. (2014) · Free Radical Research · doi:10.3109/10715762.2014.897342 · Cited by 44
Li, X., Chatterjee, N., Spirohn, K., Boutros, M., & Bohmann, D. (2016) · Scientific Reports · doi:10.1038/srep21455 · Cited by 44
CHAC2 is essential for self-renewal and glutathione maintenance in human embryonic stem cells
Wang, C., Yang, S., Hsu, S., Chang, F., Lin, Y., Chen, S., Cheng, C., Hsiao, M., Lu, F. L., & Lu, J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.345 · Cited by 44
Acute kidney injury to chronic kidney disease transition
Strausser, S. A., Nakano, D., & Souma, T. (2018) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0000000000000424 · Cited by 45
Can Nrf2 Modulate the Development of Intestinal Fibrosis and Cancer in Inflammatory Bowel Disease?
Pompili, S., Sferra, R., Gaudio, E., Viscido, A., Frieri, G., Vetuschi, A., & Latella, G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20164061 · Cited by 44
Rosa, P. L., Bertini, E., & Piemonte, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030916 · Cited by 45
Walters, T. S., McIntosh, D., Ingram, S., Tillery, L., Motley, E. D., Arinze, I., & Misra, S. (2021) · Cellular Physiology and Biochemistry · doi:10.33594/000000351 · Cited by 44
NRF2 as a therapeutic opportunity to impact in the molecular roadmap of ALS
Jiménez-Villegas, J., Ferraiuolo, L., Mead, R. J., Shaw, P. J., Cuadrado, A., & Rojo, A. I. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.022 · Cited by 44
Wu, L., Li, H., Wu, Q. E., Miao, S., Liu, Z., Wu, P., & Ye, D. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0525-6 · Cited by 44
Prieschl, E. E., Novotny, V., Csonga, R., Jaksche, D., Elbe‐Bürger, A., Thumb, W., Auer, M., Stingl, G., & Baumruker, T. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.10.2291 · Cited by 44
Nrf2: A promising therapeutic target in bone-related diseases
Che, J., Yang, X., Jin, Z., & Xu, C. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115748 · Cited by 45
Role of NRF2 in Pathogenesis of Alzheimer’s Disease
Chu, C., Uruno, A., Katsuoka, F., & Yamamoto, M. (2024) · Antioxidants · doi:10.3390/antiox13121529 · Cited by 43
Sugiyama, K., Ebinuma, H., Nakamoto, N., Sakasegawa, N., Murakami, Y., Chu, P., Usui∥, S., Ishibashi∥, Y., Wakayama, Y., Taniki, N., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094460 · Cited by 43
Choe, K. P., Leung, C. K., & Miyamoto, M. M. (2012) · Drug Metabolism Reviews · doi:10.3109/03602532.2012.684799 · Cited by 47
Lce1 Family Members Are Nrf2-Target Genes that Are Induced to Compensate for the Loss of Loricrin
Ishitsuka, Y., Huebner, A. J., Rice, R. H., Koch, P. J., Speransky, V. V., Steven, A. C., & Roop, D. R. (2016) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2016.04.022 · Cited by 43
Carneiro, C. C., Santos, S. C., Lino, R. D. S., Bara, M. T. F., Chaibub, B. A., Reis, P. R. D. M., Chaves, D. A., da Silva, A. J. R., Silva, L. S., Silva, D. D. M. E., et al. (2016) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2016.08.015 · Cited by 43
Regulation of Nrf2 Transactivation Domain Activity by p160 RAC3/SRC3 and Other Nuclear Co-Regulators
Lin, W., Shen, G., Yuan, X., Jain, M. R., Yu, S., Zhang, A., Chen, J. D., & Kong, A. T. (2006) · BMB Reports · doi:10.5483/bmbrep.2006.39.3.304 · Cited by 43
Endoplasmic reticulum association and N‐linked glycosylation of the human Nrf3 transcription factor
Nouhi, Z., Chevillard, G., Derjuga, A., & Blank, V. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.10.041 · Cited by 44
Thromboxane synthase: structure and function of protein and gene
Wang, L.-H., & Kulmacz, R. J. (2002) · Prostaglandins & Other Lipid Mediators · doi:10.1016/s0090-6980(02)00045-x · Cited by 43
Significance of NRF2 in physiological and pathological conditions an comprehensive review
Kryszczuk, M., & Kowalczuk, O. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109417 · Cited by 44
Liu, Y., Wang, Y., Miao, X., Zhou, S., Tan, Y., Liang, G., Zheng, Y., Liu, Q., Sun, J., & Cai, L. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12267 · Cited by 42
Zhao, J., Wu, J., Zhang, L., Chen, Y., Yu, S., & Zhao, Y. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.153700 · Cited by 42
Verma, A. K., Yadav, A., Singh, S. V., Mishra, P., & Rath, S. K. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.02.037 · Cited by 42
Li, G.-H., Li, Y., Jiao, P., Zhao, Y., Hu, H., Lou, H., & Shen, T. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7309073 · Cited by 42
Nrf2 regulates CD4+ T cell–induced acute graft-versus-host disease in mice
Tsai, J. J.-Y., Velardi, E., Shono, Y., Argyropoulos, K. V., Holland, A. M., Smith, O. M., Yim, N. L., Rao, U. K., Kreines, F. M., Lieberman, S. R., et al. (2018) · Blood · doi:10.1182/blood-2017-10-812941 · Cited by 42
Bevinakoppamath, S., Ramachandra, S. C., Yadav, A. K., Basavaraj, V., Vishwanath, P., & Prashant, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.719631 · Cited by 42
Lu, C., Day, C. H., Kuo, C., Wang, T., Ho, T., Lai, P., Chen, R., Yao, C., Viswanadha, V. P., Kuo, W., et al. (2022) · Environmental Toxicology · doi:10.1002/tox.23449 · Cited by 43
NRF2 and Key Transcriptional Targets in Melanoma Redox Manipulation
Carpenter, E. L., Becker, A. L., & Indra, A. K. (2022) · Cancers · doi:10.3390/cancers14061531 · Cited by 42
Multiple regions of p45 NF-E2 are required for -globin gene expression in erythroid cells
Bean, T. L., & Ney, P. A. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.12.2509 · Cited by 42
Iwasaki, K., Hailemariam, K., & Tsuji, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701477200 · Cited by 41
Exercise-induced Nrf2 activation increases antioxidant defenses in skeletal muscles
Powers, S. K., Lategan-Potgieter, R., & Goldstein, E. R. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.07.041 · Cited by 45
Thioredoxin system – a novel therapeutic target
Koháryová, M., & Kollárová, M. (2015) · General Physiology and Biophysics · doi:10.4149/gpb_2015006 · Cited by 41
Esakky, P., & Moley, K. H. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.07.015 · Cited by 41
NRF2 mediates γ-globin gene regulation and fetal hemoglobin induction in human erythroid progenitors
Zhu, X.-G., Li, B., & Pace, B. (2017) · Haematologica · doi:10.3324/haematol.2016.160788 · Cited by 37
Li, S. N., Li, W., Wang, C., Wu, R., Yin, R., Kuo, H. D., Wang, L., & Kong, A. T. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.06.014 · Cited by 41
MIAO, H., Xu, J., Xu, D., Ma, X., Zhao, X., & Liu, L. (2018) · Physiological Research · doi:10.33549/physiolres.933939 · Cited by 42
Comparison of human Nrf2 antibodies: A tale of two proteins
Kemmerer, Z. A., Ader, N. R., Mulroy, S. S., & Eggler, A. L. (2015) · Toxicology Letters · doi:10.1016/j.toxlet.2015.07.004 · Cited by 41
Wu, L., Liu, Z. J., Miao, S., Zou, L. B., Cai, L., Wu, P., Ye, D., Wu, Q., & Li, H. H. (2013) · Neurological Research · doi:10.1179/1743132813y.0000000242 · Cited by 41
Redox Regulation of Genes that Protect Against Carcinogens
Primiano, T., Sutter, T. R., & Kensler, T. W. (1997) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s0305-0491(97)00221-6 · Cited by 41
Feng, J., Read, O. J., & Dinkova‐Kostova, A. T. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.2183 · Cited by 42
The Nrf2 Pathway in Depressive Disorders: A Systematic Review of Animal and Human Studies
Sani, G., Margoni, S., Brugnami, A., Ferrara, O. M., Bernardi, E., Simonetti, A., Monti, L., Mazza, M., Janiri, D., Moccia, L., et al. (2023) · Antioxidants · doi:10.3390/antiox12040817 · Cited by 41
Association of nanoparticles and Nrf2 with various oxidative stress-mediated diseases
Thiruvengadam, R., Venkidasamy, B., Samynathan, R., Rajakumar, G., Thiruvengadam, M., & Kim, J. H. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110535 · Cited by 40
Macari, E. R., Schaeffer, E. K., West, R. J., & Lowrey, C. H. (2012) · Blood · doi:10.1182/blood-2012-07-443986 · Cited by 40
Redox Signaling and Its Impact on Skeletal and Vascular Responses to Spaceflight
Tahimic, C. G. T., & Globus, R. K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102153 · Cited by 40
Zhu, X., Xi, C., Thomas, B., & Pace, B. S. (2017) · Blood · doi:10.1182/blood-2017-10-810531 · Cited by 40
Transcriptional regulation of the 26S proteasome by Nrf1
Koizumi, S., Hamazaki, J., & Murata, S. (2018) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.94.021 · Cited by 43
Gao, L., Morine, Y., Yamada, S., Saito, Y., Ikemoto, T., Tokuda, K., Takasu, C., Miyazaki, K., & Shimada, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0256755 · Cited by 40
Terui, K., Takahashi, Y., Kitazawa, J., Toki, T., Yokoyama, M., & Ito, E. (2000) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.192.259 · Cited by 40
Repeated Nrf2 stimulation using sulforaphane protects fibroblasts from ionizing radiation
Mathew, S. T., Bergström, P., & Hammarsten, O. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.02.013 · Cited by 40
Signal Transduction, Ageing and Disease
Zhang, L. J., Yousefzadeh, M. J., Suh, Y., Niedernhofer, L. J., & Robbins, P. D. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-3681-2_9 · Cited by 40
Haque, E., Karim, M. R., Teeli, A. S., Śmiech, M., Leszczyński, P., Winiarczyk, D., Parvanov, E. D., Atanasov, A. G., & Taniguchi, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155378 · Cited by 40
Metadata
- Authors
- Moi, P., Chan, K., Asunis, I., Cao, A., & Kan, Y. W.
- Affiliations
- University of Cagliari (IT)
- Howard Hughes Medical Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1994-10-11
- Volume
- 91
- Issue
- 21
- Pages
- 9926-9930
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC44930
- OpenAlex
- W1991265255
- Cited by
- 1,607
- References
- 41
- Citations by year
- 2026: 38 · 2025: 71 · 2024: 102 · 2023: 96 · 2022: 111 · 2021: 89 · 2020: 89 · 2019: 87 · 2018: 61 · 2017: 65 · 2016: 59 · 2015: 68 · 2014: 77 · 2013: 65 · 2012: 72
- FWCI
- 10.89
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UNICA IRIS Institutional Research Information System (University of Cagliari) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- University of California, San Francisco
- National Institute of Diabetes and Digestive and Kidney Diseases (DK16666)
- Topics
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- Nrf2, NF-E2, beta-globin locus control region, AP-1, bZIP transcription factors, erythroid-specific transcription factors, acidic activation domain, transcriptional activation, beta-globin gene expression, K562 cells
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Cell Line, DNA-Binding Proteins, Leukemia, Erythroblastic, Acute, Genes, Regulator, Multigene Family, Globins, Humans, Molecular Sequence Data, Oligodeoxyribonucleotides, Repetitive Sequences, Nucleic Acid, RNA, Messenger, Transcription Factors, Tumor Cells, Cultured, Blotting, Northern, Trans-Activators, Gene Library, Gene Expression, Zinc Fingers, Leucine Zippers, Open Reading Frames, Consensus Sequence, Sequence Homology, Amino Acid, Transcription Factor AP-1, Erythroid-Specific DNA-Binding Factors, NF-E2 Transcription Factor, NF-E2 Transcription Factor, p45 Subunit, 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