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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.
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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
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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
Transcriptional Regulation of the Antioxidant Response Element
Nguyen, T., Huang, H.-C., & Pickett, C. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000361200 · Cited by 375
The multifaceted role of Nrf2 in mitochondrial function
Holmström, K. M., Kostov, R. V., & Dinkova-Kostova, A. T. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.10.002 · Cited by 368
Redox regulation: mechanisms, biology and therapeutic targets in diseases
Li, B., Ming, H., Qin, S., Nice, E. C., Dong, J., Du, Z., & Huang, C. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02095-6 · Cited by 389
Oncogenic 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
Kwak, M., Itoh, K., Yamamoto, M. P., Sutter, T. R., & Kensler, T. W. (2001) · Molecular Medicine · doi:10.1007/bf03401947 · Cited by 357
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
Yoh, K., Itoh, K., Enomoto, A., Hirayama, A., Yamaguchi, N., Kobayashi, M., Morito, N., Kôyama, A., Yamamoto, M. P., & Takahashi, S. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.00939.x · Cited by 345
Nguyen, T., Sherratt, P. J., Nioi, P., Yang, C. S., & Pickett, C. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503074200 · Cited by 345
Natural product-derived pharmacological modulators of Nrf2/ARE pathway for chronic diseases
Kumar, H., Kim, I., More, S. V., Kim, B.-W., & Choi, D. (2013) · Natural Product Reports · doi:10.1039/c3np70065h · Cited by 338
Wang, L., & He, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.967193 · Cited by 334
Abed, D. A., Goldstein, M., Albanyan, H., Jin, H., & Hu, L. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.05.008 · Cited by 336
The 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 339
The Nrf2–Keap1 defence pathway: Role in protection against drug-induced toxicity
Copple, I. M., Goldring, C. E., Kitteringham, N. R., & Park, B. K. (2007) · Toxicology · doi:10.1016/j.tox.2007.10.029 · Cited by 336
Colín-González, A. L., Santana-Martínez, R. A., Silva‐Islas, C. A., Chánez‐Cárdenas, M. E., Santamarı́a, A., & Maldonado, P. D. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/907162 · Cited by 329
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Hayes, J. D. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00695-4 · Cited by 323
Kong, A., Owuor, E. D., Yu, R., Hebbar, V., Chen, C., Hu, R., & Mandlekar, S. (2001) · Drug Metabolism Reviews · doi:10.1081/dmr-120000652 · Cited by 321
Molecular Basis of Electrophilic and Oxidative Defense: Promises and Perils of Nrf2
Ma, Q., & He, X. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.004333 · Cited by 317
Chan, J. Y., & Kwong, M. (2000) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00238-4 · Cited by 317
Specific Patterns of Electrophile Adduction Trigger Keap1 Ubiquitination and Nrf2 Activation
Hong, F., Sekhar, K. R., Freeman, M. L., & Liebler, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503346200 · Cited by 316
Numazawa, S., Ishikawa, M., Yoshida, A., Tanaka, S., & Yoshida, T. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00043.2003 · Cited by 319
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Rojo, A. I., McBean, G. J., Cindrić, M., Egea, J., López, M. G., Rada, P., Žarković, N., & Cuadrado, A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5745 · Cited by 323
Hemin-induced Activation of the Thioredoxin Gene by Nrf2
Kim, Y. C., Masutani, H., Yamaguchi, Y., Itoh, K., Yamamoto, M. P., & Yodoi, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100103200 · Cited by 313
Chemoprevention through the Keap1–Nrf2 signaling pathway by phase 2 enzyme inducers
Kwak, M.-K., Wakabayashi, N., & Kensler, T. W. (2004) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2004.06.041 · Cited by 312
Lee, J.-M., Shih, A. Y., Murphy, T. H., & Johnson, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305204200 · Cited by 308
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David, J. A., Rifkin, W. J., Rabbani, P. S., & Ceradini, D. J. (2017) · Journal of Diabetes Research · doi:10.1155/2017/4826724 · Cited by 311
Houghton, C. A., Fassett, R. G., & Coombes, J. S. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7857186 · Cited by 311
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Biasi, F., Leonarduzzi, G., Oteiza, P. I., & Poli, G. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4530 · Cited by 311
Leung, L., Kwong, M., Hou, S., Lee, C., & Chan, J. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308439200 · Cited by 299
Kobayashi, A., Ito, E., Toki, T., Kogame, K., Takahashi, S., Igarashi, K., Hayashi, N., & Yamamoto, M. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6443 · Cited by 299
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Satta, S., Mahmoud, A. M., Wilkinson, F. L., Alexander, M. Y., & White, S. J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9237263 · Cited by 306
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Zimța, A., Cenariu, D., Irimie, A., Magdo, L., Nabavi, S. M., Atanasov, A. G., & Berindan‐Neagoe, I. (2019) · Cancers · doi:10.3390/cancers11111755 · Cited by 309
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Brandes, M. S., & Gray, N. E. (2020) · ASN Neuro · doi:10.1177/1759091419899782 · Cited by 297
Accelerated DNA adduct formation in the lung of the Nrf2 knockout mouse exposed to diesel exhaust
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Furfaro, A. L., Traverso, N., Domenicotti, C., Piras, S., Moretta, L., Marinari, U. M., Pronzato, M. A., & Nitti, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1958174 · Cited by 303
Kanninen, K. M., Heikkinen, R., Malm, T., Rõlova, T., Kemppainen, S., Leinonen, H. M., Ylä‐Herttuala, S., Tanila, H., Levonen, A., Koistinaho, M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908397106 · Cited by 296
Singh, S., Vrishni, S., Singh, B. K., Rahman, I., & Kakkar, P. (2010) · Free Radical Research · doi:10.3109/10715762.2010.507670 · Cited by 305
Fuchs endothelial corneal dystrophy: The vicious cycle of Fuchs pathogenesis
Tone, S. O., Kocaba, V., Böhm, M., Wylęgała, A., White, T. L., & Jurkunas, U. V. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100863 · Cited by 306
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Dhakshinamoorthy, S., & Jaiswal, A. K. (2001) · Oncogene · doi:10.1038/sj.onc.1204506 · Cited by 290
The Nrf2–ARE cytoprotective pathway in astrocytes
Vargas, M. R., & Johnson, J. A. (2009) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001094 · Cited by 295
Oxidative damage and the Nrf2-ARE pathway in neurodegenerative diseases
Gan, L., & Johnson, J. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.12.011 · Cited by 288
Emerging Role of Nrf2 in Protecting Against Hepatic and Gastrointestinal Disease
Aleksunes, L. M., & Manautou, J. E. (2007) · Toxicologic Pathology · doi:10.1080/01926230701311344 · Cited by 288
NRF2 promotes neuronal survival in neurodegeneration and acute nerve damage
Xiong, W., Garfinkel, A. M., Li, Y., Benowitz, L. I., & Cepko, C. L. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79735 · Cited by 290
Katsuoka, F., Motohashi, H., Ishii, T., Aburatani, H., Engel, J. D., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.8044-8051.2005 · Cited by 289
Thirty years of NRF2: advances and therapeutic challenges.
Zhang, D. D. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01145-0 · Cited by 282
Motohashi, H. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.15.2953 · Cited by 282
Pickering, A. M., Linder, R. A., Zhang, H., Forman, H. J., & Davies, K. J. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277145 · Cited by 284
Chan, J. Y., Kwong, M., Lu, R., Chang, J., Wang, B., Yen, T. S. B., & Kan, Y. W. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1779 · Cited by 277
Self-citationCrisman, E., Duarte, P., Daudén, E., Cuadrado, A., Rodríguez-Franco, M. I., López, M. G., & Leon, R. M. (2022) · Medicinal Research Reviews · doi:10.1002/med.21925 · Cited by 289
Kang, K. W., Lee, S. J., Park, J. W., & Kim, S. G. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.5.1001 · Cited by 273
Kong, A. T., Yu, R., Chen, C., Mandlekar, S., & Primiano, T. (2000) · Archives of Pharmacal Research · doi:10.1007/bf02976458 · Cited by 272
Chen, C., & Kong, A. T. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.04.004 · Cited by 269
Nrf2 for protection against oxidant generation and mitochondrial damage in cardiac injury
Chen, Q. M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.12.001 · Cited by 283
Calabrese, V., Cornelius, C., Mancuso, C., Pennisi, G., Calafato, S., Bellia, F., Bates, T. E., Stella, A. M. G., Schapira, T., Dinkova‐Kostova, A. T., et al. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9775-9 · Cited by 273
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Broekgaarden, M., Weijer, R., van Gulik, T. M., Hamblin, M. R., & Heger, M. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9588-7 · Cited by 266
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Was, H., Dulak, J., & Jozkowicz, A. (2010) · Current Drug Targets · doi:10.2174/1389450111009011551 · Cited by 259
Biswas, C., Shah, N., Muthu, M., La, P., Fernando, A. P., Sengupta, S., Yang, G., & Dennery, P. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.567685 · Cited by 259
Involvement of Nrf2 in myocardial ischemia and reperfusion injury
Shen, Y., Liu, X., Shi, J., & Xiang, W. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.11.190 · Cited by 257
Nuclear factor erythroid 2-related factor 2 protects against beta amyloid
Kanninen, K. M., Malm, T., Jyrkkänen, H.-K., Goldsteins, G., Keksa-Goldsteine, V., Tanila, H., Yamamoto, M. P., Ylä‐Herttuala, S., Levonen, A., & Koıstınaho, J. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.07.010 · Cited by 259
Giudice, A., Arra, C., & Turco, M. C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-738-9_3 · Cited by 254
Iron and thiol redox signaling in cancer: an exquisite balance to escape ferroptosis
Toyokuni, S., Ito, F., Yamashita, K., Okazaki, Y., & Akatsuka, S. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.024 · Cited by 252
Nrf2-mediated protection against 6-hydroxydopamine
Jakel, R. J., Townsend, J. A., Kraft, A. D., & Johnson, J. A. (2007) · Brain Research · doi:10.1016/j.brainres.2007.01.131 · Cited by 252
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Prattichizzo, F., Nigris, V. D., Spiga, R., Mancuso, E., Sala, L. L., Antonicelli, R., Testa, R., Procopio, A. D., Olivieri, F., & Ceriello, A. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.10.003 · Cited by 255
Transcriptional responses to oxidative stress: Pathological and toxicological implications
Ma, Q. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.11.004 · Cited by 252
Ma, Q., Battelli, L. A., & Hubbs, A. F. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051113 · Cited by 246
Hammad, M., Raftari, M., Cesário, R., Salma, R., Godoy, P. R. D. V., Emami, S. N., & Haghdoost, S. (2023) · Antioxidants · doi:10.3390/antiox12071371 · Cited by 258
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Kobayashi, A., Ohta, T., & Yamamoto, M. P. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)78021-0 · Cited by 243
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Chen, C., & Kong, A. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.03.015 · Cited by 241
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Kwak, M.-K., Egner, P. A., Dolan, P. M., Ramos‐Gómez, M., Groopman, J. D., Itoh, K., Yamamoto, M. P., & Kensler, T. W. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00190-7 · Cited by 241
The story so far: molecular regulation of the heme oxygenase-1 gene in renal injury
Sikorski, E. M., Hock, T., Hill‐Kapturczak, N., & Agarwal, A. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00297.2003 · Cited by 236
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Bataille, A. M., & Manautou, J. E. (2012) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2012.110 · Cited by 230
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Tang, W. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i36.13079 · Cited by 228
Pi, J., Qu, W., Reece, J. M., Kumagai, Y., & Waalkes, M. P. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00341-0 · Cited by 231
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Jones, R. M., Mercante, J. W., & Neish, A. S. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712799828283 · Cited by 232
Li, J., Johnson, D. A., Calkins, M. J., Wright, L. S., Svendsen, C. N., & Johnson, J. A. (2004) · Toxicological Sciences · doi:10.1093/toxsci/kfi027 · Cited by 229
Lee, J., Hanson, J. M., Chu, W. A., & Johnson, J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100734200 · Cited by 229
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Orkin, S. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.4955 · Cited by 225
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Dinkova‐Kostova, A. T., Holtzclaw, W. D., & Wakabayashi, N. (2005) · Biochemistry · doi:10.1021/bi047434h · Cited by 220
Kataoka, K., Igarashi, K., Itoh, K., Fujiwara, K. T., Noda, M., Yamamoto, M. P., & Nishizawa, M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.4.2180 · Cited by 217
Somatic mutations of the KEAP1 gene in common solid cancers
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Nrf2 and NF-κB and Their Concerted Modulation in Cancer Pathogenesis and Progression
Bellezza, I., Mierla, A. L., & Minelli, A. (2010) · Cancers · doi:10.3390/cancers2020483 · Cited by 220
Adaptation to Oxidative Stress, Chemoresistance, and Cell Survival
Landriscina, M., Maddalena, F., Laudiero, G., & Esposito, F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2692 · Cited by 219
The Role of Reactive Oxygen Species in Regulating T Cell-mediated Immunity and Disease
Yarosz, E. L., & Chang, C.-H. (2018) · Immune Network · doi:10.4110/in.2018.18.e14 · Cited by 214
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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
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