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A genomic screen for activators of the antioxidant response element
Open accessAbstract
The antioxidant response element (ARE) is a cis-acting regulatory enhancer element found in the 5′ flanking region of many phase II detoxification enzymes. Up-regulation of ARE-dependent target genes is known to have neuroprotective effects; yet, the mechanism of activation is largely unknown. By screening an arrayed collection of ≈15,000 full-length expression cDNAs in the human neuroblastoma cell line IMR-32 with an ARE-luciferase reporter, we have identified several cDNAs not previously associated with ARE activation. A subset of cDNAs, encoding sequestosome 1 (SQSTM1) and dipeptidylpeptidase 3 (DPP3), activated the ARE in primary mouse-derived cortical neurons. Overexpression of SQSTM1 and DPP3 in IMR-32 cells stimulated NF-E2-related factor 2 (NRF2) nuclear translocation and led to increased levels of NAD(P)H:quinone oxidoreductase 1, a protein which is transcriptionally regulated by the ARE. When transfected into IMR-32 neuroblastoma cells that were depleted of transcription factor NRF2 by RNA interference, SQSTM1 and DPP3 were unable to activate the ARE or induce NAD(P)H:quinone oxidoreductase 1 expression, indicating that the ARE activation upon ectopic expression of these cDNAs is mediated by NRF2. Studies with pharmacological inhibitors indicated that 1-phosphatidylinositol 3-kinase and protein kinase C signaling are essential for activity. Overexpression of these cDNAs conferred partial resistance to hydrogen peroxide or rotenone-induced toxicity, consistent with the induction of antioxidant and phase II detoxification enzymes, which can protect from oxidative stress. This work and other such studies may provide mechanisms for activating the ARE in the absence of general oxidative stress and a yet-unexploited therapeutic approach to degenerative diseases and aging.
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“One of these SNPs (rs242561) was located in the regulatory region of the microtubule-associated protein Tau gene, which induced a strong binding of the NRF2/sMAF complex, leading to increased transcription and a reduced risk of parkinsonian diseases61,62.”
From Key points for the development of antioxidant cocktails to prevent cellular stress and damage caused by reactive oxygen species (ROS) during manned space missions (2021) · cites this paper as [62]
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Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Rational siRNA design for RNA interference
Reynolds, A., Leake, D., Boese, Q., Scaringe, S., Marshall, W. S., & Khvorova, A. (2004) · Nature Biotechnology · doi:10.1038/nbt936 · Cited by 2,094
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
Regulatory Mechanisms Controlling Gene Expression Mediated by the Antioxidant Response Element
Nguyen, T., Sherratt, P. J., & Pickett, C. B. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140229 · Cited by 1,232
Ramos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102
Huang, H.-C., Nguyen, T., & Pickett, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206911200 · Cited by 1,070
Wakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M.-I., Kobayashi, A., Yamamoto, M., Kensler, T. W., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307301101 · Cited by 986
Lee, J., Calkins, M. J., Chan, K., Kan, Y. W., & Johnson, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211558200 · Cited by 783
Self-citationAn important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen
Chan, K., Han, X.-D., & Kan, Y. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081082098 · Cited by 766
Research works printed but not linked: 1
- M McMahon, K Itoh, M Yamamoto, SA Chanas, CJ Henderson, LI McLellan, CR Wolf, C Cavin, JD Hayes Cancer Res 61, 3299–3307 (2001).
Cited by
Sorted by citations
Redox regulation of cell survival
Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,788
The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway
Baird, L., & Yamamoto, M. P. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00099-20 · Cited by 1,671
Jain, A., Lamark, T., Sjøttem, E., Bowitz Larsen, K., Atesoh Awuh, J., Øvervatn, A., McMahon, M., Hayes, J. D., & Johansen, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.118976 · Cited by 1,472
Linker, R. A., Lee, D.-H., Ryan, S., van Dam, A. M., Conrad, R., Bista, P., Zeng, W., Hronowsky, X., Buko, A., Chollate, S., et al. (2011) · Brain · doi:10.1093/brain/awq386 · Cited by 1,155
Lau, A., Wang, X.-J., Zhao, F. L., Villeneuve, N. F., Wu, T., Jiang, T., Sun, Z., White, E., & Zhang, D. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00248-10 · Cited by 852
Oxidative stress response and Nrf2 signaling in aging
Zhang, H., Davies, K. J. A., & Forman, H. J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.036 · Cited by 804
Stress-activated cap’n’collar transcription factors in aging and human disease
Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776
p62 links autophagy and Nrf2 signaling
Jiang, T., Harder, B. G., de la Vega, M. R., Wong, P. K., Chapman, E., & Zhang, D. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.014 · Cited by 657
Cancer Chemoprevention Mechanisms Mediated Through the Keap1–Nrf2 Pathway
Hayes, J. D., McMahon, M. J., Chowdhry, S., & Dinkova‐Kostova, A. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3221 · Cited by 549
Gene Overexpression: Uses, Mechanisms, and Interpretation
Prelich, G. (2012) · Genetics · doi:10.1534/genetics.111.136911 · Cited by 480
Nrf2 Regulates Oxidative Stress and Its Role in Cerebral Ischemic Stroke
Wang, L., Zhang, X., Xiong, X., Zhu, H., Chen, R., Zhang, S., Chen, G., & Jian, Z. (2022) · Antioxidants · doi:10.3390/antiox11122377 · Cited by 367
Nrf2—a therapeutic target for the treatment of neurodegenerative diseases
Johnson, D. A., & Johnson, J. A. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.147 · Cited by 333
Self-citationKanninen, 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
Ng, C.-T., Yong, L., Hande, M. P., Ong, C. N., Yu, L. E., Bay, B., & Baeg, G. H. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s124403 · Cited by 270
Beyond repression of Nrf2: An update on Keap1
Kopacz, A., Klóska, D., Forman, H. J., Józkowicz, A., & Grochot‐Przeczek, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.023 · Cited by 269
Copple, I. M., Lister, A., Obeng, A. D., Kitteringham, N. R., Jenkins, R. E., Layfield, R., Foster, B. J., Goldring, C. E., & Park, B. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096545 · Cited by 260
Hast, B. E., Goldfarb, D., Mulvaney, K. M., Hast, M. A., Siesser, P. F., Yan, F., Hayes, D. N., & Major, M. B. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4400 · Cited by 259
Keap1 facilitates p62-mediated ubiquitin aggregate clearance via autophagy
Fan, W., Tang, Z., Chen, D., Moughon, D., Ding, X., Chen, S., Zhu, M., & Zhong, Q. (2010) · Autophagy · doi:10.4161/auto.6.5.12189 · Cited by 251
Regulation of Nrf2 signaling and longevity in naturally long-lived rodents
Lewis, K. N., Wason, E., Edrey, Y. H., Kristan, D. M., Nevo, E., & Buffenstein, R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417566112 · Cited by 249
Modulation of proteostasis by transcription factor NRF2 and impact in neurodegenerative diseases
Pajares, M., Cuadrado, A., & Rojo, A. I. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.006 · Cited by 226
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
Free radical biology and medicine
(2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00493-3 · Cited by 209
Ma, Y., Su, Q., Yue, C., Zou, H., Zhu, J., Zhao, H., Song, R., & Liu, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113491 · Cited by 214
Nrf2 targeting by sulforaphane: A potential therapy for cancer treatment
Russo, M., Spagnuolo, C., Russo, G. L., Skalicka‐Woźniak, K., Daglia, M., Sobarzo‐Sánchez, E., Nabavi, S. F., & Nabavi, S. M. (2016) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2016.1259983 · Cited by 199
Guise, C. P., Abbattista, M. R., Singleton, R. S., Holford, S. D., Connolly, J., Dachs, G. U., Fox, S. B., Pollock, R., Harvey, J., Guilford, P., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3237 · Cited by 187
Lu, K., Alcivar, A. L., Ma, J., Foo, T. K., Zywea, S., Mahdi, A., Huo, Y., Kensler, T. W., Gatza, M. L., & Xia, B. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2204 · Cited by 181
The Keap1–Nrf2 Cell Defense Pathway – A Promising Therapeutic Target?
Copple, I. M. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-398339-8.00002-1 · Cited by 174
Monitoring Keap1–Nrf2 interactions in single live cells
Baird, L., Swift, S., Llères, D., & Dinkova‐Kostova, A. T. (2014) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.03.004 · Cited by 179
Riley, B. E., Kaiser, S. E., Shaler, T. A., Ng, A., Hara, T., Hipp, M. S., Lage, K., Xavier, R. J., Ryu, K., Taguchi, K., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201005012 · Cited by 165
Lee, D.-H., Gold, R., & Linker, R. A. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130911783 · Cited by 163
Linker, R. A., & Gold, R. (2013) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-013-0394-8 · Cited by 148
Danilov, C. A., Chandrasekaran, K., Racz, J. L., Soane, L., Zielke, C. L., & Fiskum, G. M. (2008) · Glia · doi:10.1002/glia.20793 · Cited by 141
Sánchez-Ortega, M., Carrera, A. C., & Garrido, A. (2021) · Cells · doi:10.3390/cells10081879 · Cited by 130
Role of the K eap1/ N rf2 pathway in neurodegenerative diseases
Yamazaki, H., Tanji, K., Wakabayashi, K., Matsuura, S., & Itoh, K. (2015) · Pathology International · doi:10.1111/pin.12261 · Cited by 123
Wang, R., Paul, V. J., & Luesch, H. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.12.019 · Cited by 122
Self-citationDipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter
Prajapati, S. C., & Chauhan, S. S. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08275.x · Cited by 116
Yang, B., Zhou, Y., Wu, M., Li, X., Mai, K., & Ai, Q. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02750-0 · Cited by 117
Scuderi, S. A., Ardizzone, A., Paterniti, I., Esposito, E., & Campolo, M. (2020) · Antioxidants · doi:10.3390/antiox9070630 · Cited by 114
Current mechanistic insights into the CCCP-induced cell survival response
Kane, M. S., Paris, A., Codron, P., Cassereau, J., Procaccio, V., Lenaers, G., Reynier, P., & Chevrollier, A. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.12.018 · Cited by 115
Age-associated oxidative damage to the p62 promoter: implications for Alzheimer disease
Du, Y., Wooten, M. C., Gearing, M., & Wooten, M. W. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.11.003 · Cited by 108
Song, C., Mitter, S. K., Qi, X., Beli, E., Rao, H. V., Ding, J., Ip, C. S., Gu, H., Akin, D., Dunn, W. A., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171940 · Cited by 100
Oxidative damage to the promoter region of SQSTM1/p62 is common to neurodegenerative disease
Du, Y., Wooten, M. C., & Wooten, M. W. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.015 · Cited by 96
Role of Nrf2 and p62/ZIP in the neurite outgrowth by carnosic acid in PC12h cells
Kosaka, K., Mimura, J., Itoh, K., Satoh, T., Shimojo, Y., Kitajima, C., Maruyama, A., Yamamoto, M. P., & Shirasawa, T. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp149 · Cited by 95
Gómez, X., Sanon, S., Zambrano, K., Asquel, S., Bassantes, M., Morales, J. E., Otáñez, G., Pomaquero, C., Villarroel, S., Zurita, A., et al. (2021) · npj Microgravity · doi:10.1038/s41526-021-00162-8 · Cited by 92
Ehren, J. L., & Maher, P. A. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.04.010 · Cited by 86
Oxidative stress promotes exit from the stem cell state and spontaneous neuronal differentiation
Hu, Q., Khanna, P., Wong, B. S. E., Heng, Z. S., Subhramanyam, C. S., Thanga, L. Z., Tan, S. W. S., & Baeg, G. H. (2017) · Oncotarget · doi:10.18632/oncotarget.23786 · Cited by 84
Baral, P. K., Jajčanin-Jozić, N., Deller, S., Macheroux, P., Abramić, M., & Gruber, K. F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803522200 · Cited by 83
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Wang, L., Cano, M., & Handa, J. T. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.016 · Cited by 82
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Bezerra, G. A., Dobrovetsky, E., Viertlmayr, R., Dong, A., Binter, A., Abramić, M., Macheroux, P., Dhe‐Paganon, S., & Gruber, K. F. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118005109 · Cited by 73
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Jha, S., Taschler, U., Domenig, O., Poglitsch, M., Bourgeois, B. M. R., Pollheimer, M. J., Pusch, L. M., Malovan, G., Frank, S., Madl, T., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014183 · Cited by 72
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Yamamoto, S., Inoue, J., Kawano, T., Kozaki, K., Omura, K., & Inazawa, J. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0246-t · Cited by 72
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Franco, R., Navarro, G., & Martínez‐Pinilla, E. (2019) · Antioxidants · doi:10.3390/antiox8020046 · Cited by 70
Coe, K. J., Jia, Y., Ho, H. K., Rademacher, P. M., Bammler, T. K., Beyer, R. P., Farin, F. M., Woodke, L., Plymate, S. R., Fausto, N., et al. (2007) · Chemical Research in Toxicology · doi:10.1021/tx7001349 · Cited by 68
Zhang, Y., Shi, Z., Zhou, Y., Xiao, Q., Wang, H., & Peng, Y. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01865 · Cited by 67
Reactive oxygen species: the root cause of nanoparticle-induced toxicity in Drosophila melanogaster
Mishra, M., & Panda, M. (2021) · Free Radical Research · doi:10.1080/10715762.2021.1914335 · Cited by 61
Transcriptomic responses of European flounder (Platichthys flesus) to model toxicants
Williams, T., DIAB, A., Ortega, F. G., Sabine, V. S., Godfrey, R. E., Francesco Falciani, B., Chipman, J. K., & GEORGE, S. (2008) · Aquatic Toxicology · doi:10.1016/j.aquatox.2008.07.019 · Cited by 61
Li, H., Shang, Z., Liu, X., Qiao, Y., Wang, K., & Qiao, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.771826 · Cited by 62
Kanno, T., Tanaka, K., Yanagisawa, Y., Yasutake, K., Hadano, S., Yoshii, F., Hirayama, N., & Ikeda, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.010 · Cited by 59
Phosphorylation of serine 349 of p62 in Alzheimer’s disease brain
Tanji, K., Miki, Y., Ozaki, T., Maruyama, A., Yoshida, H., Mimura, J., Matsumiya, T., Mori, F., Imaizumi, T., Itoh, K., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-50 · Cited by 59
Halim, M., Yee, D. J., & Sameš, D. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801245y · Cited by 59
Iwadate, R., Inoue, J., Tsuda, H., Takano, M., Furuya, K., Hirasawa, A., Aoki, D., & Inazawa, J. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.05.008 · Cited by 59
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Kumar, P., Reithofer, V., Reisinger, M., Wallner, S., Pavkov‐Keller, T., Macheroux, P., & Gruber, K. F. (2016) · Scientific Reports · doi:10.1038/srep23787 · Cited by 56
Schriner, S. E., Avanesian, A., Liu, Y., Luesch, H., & Jafari, M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.025 · Cited by 54
Self-citationChen, Y., Li, Q., Li, Q., Xing, S., Liu, Y., Liu, Y., Chen, Y., Liu, W., Feng, F., & Sun, H. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b02038 · Cited by 56
Self-citationHigh Expression of SQSTM1/p62 Protein Is Associated with Poor Prognosis in Epithelial Ovarian Cancer
Iwadate, R., Inoue, J., Tsuda, H., Takano, M., Furuya, K., Hirasawa, A., Aoki, D., & Inazawa, J. (2014) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.14048 · Cited by 54
The emerging role of dipeptidyl peptidase 3 in pathophysiology
Malovan, G., Hierzberger, B., Suraci, S., Schaefer, M. M., Santos, K. F., Jha, S., & Macheroux, P. (2022) · FEBS Journal · doi:10.1111/febs.16429 · Cited by 55
Borneol alleviates oxidative stress via upregulation of Nrf2 and Bcl-2 in SH-SY5Y cells
Hur, J., Pak, S. C., Koo, B., & Jeon, S. (2012) · Pharmaceutical Biology · doi:10.3109/13880209.2012.700718 · Cited by 50
Oxidative stress and the multifaceted roles of ATM in maintaining cellular redox homeostasis
Lee, J. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103269 · Cited by 54
Cao, X., Xiao, H., Zhang, Y., Zou, L., Chu, Y., & Chu, X. (2010) · Brain Research · doi:10.1016/j.brainres.2010.05.072 · Cited by 48
A transcriptome signature distinguished sporadic from postradiotherapy radiation-induced sarcomas
Hadj-Hamou, N.-S., Ugolin, N., Ory, C., Britzen‐Laurent, N., Sastre‐Garau, X., Chevillard, S., & Malfoy, B. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr064 · Cited by 49
Activation of the antioxidant response element by specific oxidized metabolites of linoleic acid
Wang, R., Kern, J. T., Goodfriend, T. L., Ball, D. L., & Luesch, H. (2009) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2009.04.008 · Cited by 46
Self-citationMicroRNA Regulation of Human Protease Genes Essential for Influenza Virus Replication
Meliopoulos, V., Andersen, L. E., Brooks, P., Yan, X., Bakre, A. A., Coleman, J. K., Tompkins, S. M., & Tripp, R. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037169 · Cited by 46
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
Liu, Y., Zhong, W., Zhang, J., Chen, W., Lu, Y., Qiao, Y., Zeng, Z., Huang, H., Zou, F., 孟小晶, et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.739220 · Cited by 42
Self-citationMaino, B., Ciotti, M. T., Calissano, P., & Cavallaro, S. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15045596 · 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
Luo, M., Zheng, Y., Tang, S., Gu, L., Zhu, Y., Ying, R., Liu, Y., Ma, J., Guo, R., Gao, P., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1166178 · Cited by 41
Self-citationLi, M., Chen, L., Xiang, H.-X., Jiang, Y., Lv, B.-B., Xu, D., Zhao, H., & Fu, L. (2024) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2024.134560 · Cited by 41
Comprehensive proteomics analysis of autophagy-deficient mouse liver
Matsumoto, N., Ezaki, J., Komatsu, M., Takahashi, K., Mineki, R., Taka, H., Kikkawa, M., Fujimura, T., Takeda‐Ezaki, M., Ueno, T., et al. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.112 · Cited by 39
Pérez, Ó. C., Barrero, C. A., & Merali, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.770925 · Cited by 36
Jiang, Z., Yang, X., Han, Y., Li, J., Hu, C., Liu, C., & Xiao, W. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154337 · Cited by 35
Small Maf functions in the maintenance of germline stem cells in the Drosophila testis
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Metadata
- Authors
- Liu, Y., Kern, J. T., Walker, J. R., Johnson, J. A., Schultz, P. G., & Luesch, H.
- Affiliations
- University of Florida (US)
- University of Wisconsin–Madison (US)
- Genomics Institute of the Novartis Research Foundation (US)
- Scripps Research Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-03-20
- Volume
- 104
- Issue
- 12
- Pages
- 5205-5210
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1829287
- OpenAlex
- W2147984935
- Cited by
- 196
- References
- 53
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 8 · 2023: 6 · 2022: 11 · 2021: 15 · 2020: 15 · 2019: 5 · 2018: 7 · 2017: 13 · 2016: 12 · 2015: 14 · 2014: 11 · 2013: 12 · 2012: 12
- FWCI
- 4.91
- 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)
- Funders
- Ellison Medical Foundation
- American Heart Association
- McKnight Foundation
- National Institute of Environmental Health Sciences (ES10042, R01ES010042, ES08089, R01ES008089, R29ES008089)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- antioxidant response element, Nrf2, NAD(P)H:quinone oxidoreductase 1, p62, phase II enzymes, oxidative stress, neuroprotection, PI3K signaling, protein kinase C signaling, neuroblastoma cells, cortical neurons, neurodegenerative diseases
- MeSH terms
- Sequestosome-1 Protein, Animals, Antioxidants, Cell Nucleus, Cells, Cultured, Cerebral Cortex, Enzyme Induction, Heat-Shock Proteins, NADPH Dehydrogenase, Trans-Activators, Gene Library, Gene Expression, NAD(P)H Dehydrogenase (Quinone), Genome, DNA, Complementary, Oxidative Stress, Response Elements, Oligonucleotide Array Sequence Analysis, Protein Transport, Genomics, RNA, Small Interfering, Protein Kinase Inhibitors, Adaptor Proteins, Signal Transducing, NF-E2-Related Factor 2, Mice
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