A genomic screen for activators of the antioxidant response element

Liu, Yanxia; Kern, Jonathan T.; Walker, John R.; Johnson, Jeffrey A.; Schultz, Peter G.; Luesch, Hendrik

doi:10.1073/pnas.0700898104

Cited by 199Genomics, phytochemicals, and oxidative stressGlutathione Transferases and PolymorphismsRedox biology and oxidative stress

A genomic screen for activators of the antioxidant response element

Open access

Liu, Yanxia, Kern, Jonathan T., Walker, John R., Johnson, Jeffrey A., Schultz, Peter G., Luesch, Hendrik·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0700898104PMC PMC1829287

Open this paper in CoChat — free account

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1073/pnas.0700898104

Cites

53 of 53 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

One SNP (rs242561) located in the regulatory region of the microtubule-associated protein Tau gene induced a strong binding of the NRF2/sMAF complex, leading to increased transcription and a reduced risk of parkinsonian diseases.
“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]
The Results and Discussion describe SQSTM1- and DPP3-driven NRF2 activation and increased expression of an antioxidant-response gene, not an effect of a Tau variant. Searches for rs242561, NRF2/sMAF binding at the Tau regulatory region, and reduced parkinsonian-disease risk found no passage addressing those claims. (LLM, conf=0.76)
Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
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 · see citing works
Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178 · see citing works
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 · see citing works
Transcription Factor Nrf2 Coordinately Regulates a Group of Oxidative Stress-inducible Genes in Macrophages
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 1,460 · see citing works
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 · see citing works
Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice
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 · see citing works
Phosphorylation of Nrf2 at Ser-40 by Protein Kinase C Regulates Antioxidant Response Element-mediated Transcription*
Huang, H.-C., Nguyen, T., & Pickett, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206911200 · Cited by 1,070 · see citing works
Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers
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 · see citing works
Identification of the NF-E2-related Factor-2-dependent Genes Conferring Protection against Oxidative Stress in Primary Cortical Astrocytes Using Oligonucleotide Microarray Analysis
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 · see citing works
Self-citation
An 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 · see citing works
The Cap'n'Collar basic leucine zipper transcription factor Nrf2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes.
McMahon, M. J., Itoh, K., Yamamoto, M. P., Chanas, S. A., Henderson, C. J., McLellan, L. I., Wolf, C. R., Cavin, C., & Hayes, J. D. (2001) · PubMed · Cited by 657 · see citing works
Ras-Dependent Induction of Cellular Responses by Constitutively Active Phosphatidylinositol-3 Kinase
Hu, Q., Klippel, A., Muslin, A. J., Fantl, W. J., & Williams, L. T. (1995) · Science · doi:10.1126/science.7701328 · Cited by 548 · see citing works
Nuclear Factor E2-Related Factor 2-Dependent Antioxidant Response Element Activation by tert -Butylhydroquinone and Sulforaphane Occurring Preferentially in Astrocytes Conditions Neurons against Oxidative Insult
Kraft, A. D., Johnson, D. A., & Johnson, J. A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3817-03.2004 · Cited by 541 · see citing works
Self-citation
Nrf2, a multi‐organ protector?
Lee, J., Li, J., Johnson, D. A., Stein, T. D., Kraft, A. D., Calkins, M. J., Jakel, R. J., & Johnson, J. A. (2005) · The FASEB Journal · doi:10.1096/fj.04-2591hyp · Cited by 532 · see citing works
Self-citation
Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice
CHANAS, S. A., JIANG, Q., McMAHON, M., McWALTER, G. K., McLELLAN, L. I., ELCOMBE, C. R., HENDERSON, C. J., WOLF, C. R., MOFFAT, G. J., ITOH, K., et al. (2002) · Biochemical Journal · doi:10.1042/bj20020320 · Cited by 460 · see citing works
The atypical PKC‐interacting protein p62 channels NF‐κB activation by the IL‐1–TRAF6 pathway
Sanz, L., Diaz‐Meco, M. T., Nakano, H., & Moscat, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.7.1576 · Cited by 436 · see citing works
Induction of Cytoprotective Genes Through Nrf2 / Antioxidant Response Element Pathway: A New Therapeutic Approach for the Treatment of Inflammatory Diseases
Chen, X., & KUNSCH, C. A. (2004) · Current Pharmaceutical Design · doi:10.2174/1381612043452901 · Cited by 387 · see citing works
Atypical protein kinase C mediates activation of NF-E2-related factor 2 in response to oxidative stress
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 316 · see citing works
Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation
Babu, J. R., Geetha, T., & Wooten, M. W. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03181.x · Cited by 315 · see citing works
NF-E2-related Factor-2 Mediates Neuroprotection against Mitochondrial Complex I Inhibitors and Increased Concentrations of Intracellular Calcium in Primary Cortical Neurons
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 · see citing works
Self-citation
Role of a Mitogen-activated Protein Kinase Pathway in the Induction of Phase II Detoxifying Enzymes by Chemicals
Yu, R., Lei, W., Mandlekar, S., Weber, M. J., Der, C. J., Wu, J., & Kong, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27545 · Cited by 281 · see citing works
Protection from mitochondrial complex II inhibition in vitro and in vivo by Nrf2-mediated transcription
Calkins, M. J., Jakel, R. J., Johnson, D. A., Chan, K., Kan, Y. W., & Johnson, J. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408487101 · Cited by 247 · see citing works
Self-citation
Stabilization of Nrf2 by tBHQ Confers Protection against Oxidative Stress-Induced Cell Death in Human Neural Stem Cells
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 227 · see citing works
Self-citation
Phosphatidylinositol 3-Kinase, Not Extracellular Signal-regulated Kinase, Regulates Activation of the Antioxidant-Responsive Element in IMR-32 Human Neuroblastoma Cells
Lee, J., Hanson, J. M., Chu, W. A., & Johnson, J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100734200 · Cited by 227 · see citing works
Self-citation
Structure and functional properties of the ubiquitin binding protein p62
Geetha, T., & Wooten, M. W. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02286-x · Cited by 223 · see citing works
The Nrf2-ARE Signalling Pathway: Promising Drug Target to Combat Oxidative Stress in Neurodegenerative Disorders
Muiswinkel, F. L. V., & Kuiperij, H. B. (2005) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1568007054038238 · Cited by 207 · see citing works
Microarray Analysis Reveals an Antioxidant Responsive Element-driven Gene Set Involved in Conferring Protection from an Oxidative Stress-induced Apoptosis in IMR-32 Cells
Li, J., Lee, J., & Johnson, J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109380200 · Cited by 193 · see citing works
Self-citation
In vivo modulation of the Parkinsonian phenotype by Nrf2
Burton, N. C., Kensler, T. W., & Guilarte, T. R. (2006) · NeuroToxicology · doi:10.1016/j.neuro.2006.07.019 · Cited by 187 · see citing works
Activation of the antioxidant response element in primary cortical neuronal cultures derived from transgenic reporter mice
Johnson, D. A., Andrews, G. K., Xu, W., & Johnson, J. A. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00913.x · Cited by 156 · see citing works
Self-citation
The alternative splicing of tau exon 10 and its regulatory proteins CLK2 and TRA2‐BETA1 changes in sporadic Alzheimer's disease
Glatz, D. C., Rujescu, D., Tang, Y., Berendt, F. J., Hartmann, A. M., Faltraco, F., Rosenberg, C. K., Hulette, C., Jellinger, K., Hampel, H. J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03552.x · Cited by 145 · see citing works
Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson's disease
Nakaso, K., Yoshimoto, Y., Nakano, T., Takeshima, T., Fukuhara, Y., Yasui, K., Araga, S., Yanagawa, T., Ishii, T., & Nakashima, K. (2004) · Brain Research · doi:10.1016/j.brainres.2004.03.029 · Cited by 139 · see citing works
Transforming activity of MECT1‐MAML2 fusion oncoprotein is mediated by constitutive CREB activation
Wu, L., Liu, J., Gao, P., Nakamura, M., Cao, Y., Shen, H., & Griffin, J. D. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600719 · Cited by 135 · see citing works
Nrf2-Dependent Activation of the Antioxidant Responsive Element by tert-Butylhydroquinone Is Independent of Oxidative Stress in IMR-32 Human Neuroblastoma Cells
Lee, J., Moehlenkamp, J. D., Hanson, J. M., & Johnson, J. A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4106 · Cited by 124 · see citing works
Self-citation
Differential Gene Expression Patterns Revealed by Oligonucleotide Versus Long cDNA Arrays
Li, J. (2002) · Toxicological Sciences · doi:10.1093/toxsci/69.2.383 · Cited by 121 · see citing works
Bcl‐xL blocks mitochondrial multiple conductance channel activation and inhibits 6‐OHDA‐induced death in SH‐SY5Y cells
Jordán, J., Galindo, M. F., Tornero, D., Gonzalez-Garcia, C., & Ceña, V. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02299.x · Cited by 118 · see citing works
Regional NAD(P)H:quinone oxidoreductase activity in Alzheimer’s disease
SantaCruz, K. S., Yazlovitskaya, E., Collins, J., Johnson, J., & DeCarli, C. (2004) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00117-9 · Cited by 116 · see citing works
Self-citation
Genome-scale functional profiling of the mammalian AP-1 signaling pathway
Chanda, S. K., White, S. M., Orth, A. P., Reisdorph, R. M., Miraglia, L. J., Thomas, R. S., DeJesus, P., Mason, D. E., Huang, Q., Vega, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934839100 · Cited by 109 · see citing works
Self-citation
Activation of Antioxidant/Electrophile-Responsive Elements in IMR-32 Human Neuroblastoma Cells
Moehlenkamp, J. D., & Johnson, J. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1046 · Cited by 80 · see citing works
Self-citation
Sustained expression of Mect1-Maml2 is essential for tumor cell growth in salivary gland cancers carrying the t(11;19) translocation
Komiya, T., Park, Y., Modi, S., Coxon, A. B., Oh, H., & Kaye, F. J. (2006) · Oncogene · doi:10.1038/sj.onc.1209627 · Cited by 79 · see citing works
The Anti-apoptotic Protein Mcl-1 Inhibits Mitochondrial Ca2+ Signals
Minagawa, N., Kruglov, E. A., Dranoff, J. A., Robert, M. E., Gores, G. J., & Nathanson, M. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503210200 · Cited by 72 · see citing works
Dipeptidyl peptidase III is a zinc metallo-exopeptidase: Molecular cloning and expression
Fukasawa, K., FUKASAWA, M. K., Kanai, M., Fujii, S., Hirose, J., & Harada, M. (1998) · Biochemical Journal · doi:10.1042/bj3290275 · Cited by 64 · see citing works
Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas
Šimaga, Š., Babić, D., Osmak, M., Šprem, M., & Abramić, M. (2003) · Gynecologic Oncology · doi:10.1016/s0090-8258(03)00462-1 · Cited by 59 · see citing works
Evidence for p62 aggregate formation: Role in cell survival
Paine, M. G., Babu, J. R., Seibenhener, M. L., & Wooten, M. W. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.010 · Cited by 55 · see citing works
Arginine/Serine-rich Protein Interaction Domain-dependent Modulation of a Tau Exon 10 Splicing Enhancer
D’Souza, I., & Schellenberg, G. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505809200 · Cited by 49 · see citing works
High-throughput Functional Genomics Identifies Genes That Ameliorate Toxicity Due to Oxidative Stress in Neuronal HT-22 Cells
Zitzler, J., Link, D., Schäfer, R., Liebetrau, W., Kazinski, M., Bonin-Debs, A. L., Behl, C., Buckel, P., & Brinkmann, U. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400054-mcp200 · Cited by 36 · see citing works
Targeting of p300/CREB Binding Protein Coactivators by Simian Virus 40 Is Mediated through p53
Borger, D. R., & DeCaprio, J. A. (2006) · Journal of Virology · doi:10.1128/jvi.80.9.4292-4303.2006 · Cited by 34 · see citing works
p62 modulates Akt activity via association with PKCζ in neuronal survival and differentiation
Joung, I., Kim, H. J., & Kwon, Y. K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.06.138 · Cited by 33 · see citing works
Chromosomal Localization and cDNA Cloning of the Human DBP and TEF Genes
Khatib, Z. A., Inaba, T., Valentine, M. B., & Look, A. T. (1994) · Genomics · doi:10.1006/geno.1994.1510 · Cited by 31 · see citing works
Towards high-throughput characterization of small molecule mechanisms of action
Luesch, H. (2006) · Molecular BioSystems · doi:10.1039/b609384a · Cited by 29 · see citing works
Self-citation
Oxidative stress-related proteins A170 and heme oxygenase-1 are differently induced in the rat cerebellum under kainate-mediated excitotoxicity
Nakaso, K., Kitayama, M., Fukuda, H., Kimura, K., Yanagawa, T., Ishii, T., Nakashima, K., & Yamada, K. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)00836-3 · Cited by 26 · see citing works
Identification of Dipeptidyl Peptidase III in Human Neutrophils
Hashimoto, J., Yamamoto, Y., Kurosawa, H., Nishimura, K., & Hazato, T. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2827 · Cited by 24 · see citing works
An enhancer-trap LacZ transgene reveals a distinct expression pattern of Kinesin family 26B in mouse embryos
Marikawa, Y., Fujita, T. C., & Alarcón, V. B. (2004) · Development Genes and Evolution · doi:10.1007/s00427-003-0377-x · Cited by 20 · see citing works
Angiotensin II Inactivation Process in Cultured Mouse Spinal Cord Cells
Michèle Allard, A., Simonnet, G., Dupouy, B., & Vincent, J. D. (1987) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1987.tb05700.x · Cited by 13 · see citing works

Flagged first, then by citations

Research works printed but not linked: 1

[6]McMahon M, Itoh K, Yamamoto M, Chanas SA, Henderson CJ, McLellan LI, Wolf CR, Cavin C, Hayes JD. Cancer Res. 2001;61:3299–3307. [PubMed] [Google Scholar]

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 · see citing works
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730 · see citing works
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 1,600 · see citing works
p62/SQSTM1 Is a Target Gene for Transcription Factor NRF2 and Creates a Positive Feedback Loop by Inducing Antioxidant Response Element-driven Gene Transcription
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 · see citing works
Fumaric acid esters exert neuroprotective effects in neuroinflammation via activation of the Nrf2 antioxidant pathway
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 · see citing works
A Noncanonical Mechanism of Nrf2 Activation by Autophagy Deficiency: Direct Interaction between Keap1 and p62
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 851 · see citing works
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 · see citing works
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 · see citing works
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 642 · see citing works
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 540 · see citing works
Gene Overexpression: Uses, Mechanisms, and Interpretation
Prelich, G. (2012) · Genetics · doi:10.1534/genetics.111.136911 · Cited by 480 · see citing works
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 361 · see citing works
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 328 · see citing works
Self-citation
Intrahippocampal injection of a lentiviral vector expressing Nrf2 improves spatial learning in a mouse model of Alzheimer's disease
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 293 · see citing works
Zinc oxide nanoparticles exhibit cytotoxicity and genotoxicity through oxidative stress responses in human lung fibroblasts and Drosophila melanogaster
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 · see citing works
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 262 · see citing works
Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway
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 · see citing works
Proteomic Analysis of Ubiquitin Ligase KEAP1 Reveals Associated Proteins That Inhibit NRF2 Ubiquitination
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 · see citing works
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 · see citing works
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 248 · see citing works
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 219 · see citing works
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 · see citing works
Free radical biology and medicine
(2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00493-3 · Cited by 209 · see citing works
The Effect of Oxidative Stress-Induced Autophagy by Cadmium Exposure in Kidney, Liver, and Bone Damage, and Neurotoxicity
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 209 · see citing works
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 · see citing works
The Bioreductive Prodrug PR-104A Is Activated under Aerobic Conditions by Human Aldo-Keto Reductase 1C3
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 186 · see citing works
NRF2 Induction Supporting Breast Cancer Cell Survival Is Enabled by Oxidative Stress–Induced DPP3–KEAP1 Interaction
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 178 · see citing works
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 172 · see citing works
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 171 · see citing works
Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection
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 162 · see citing works
Mechanisms of Oxidative Damage in Multiple Sclerosis and Neurodegenerative Diseases: Therapeutic Modulation via Fumaric Acid Esters
Lee, D.-H., Gold, R., & Linker, R. A. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130911783 · Cited by 161 · see citing works
Dimethyl Fumarate for Treatment of Multiple Sclerosis: Mechanism of Action, Effectiveness, and Side Effects
Linker, R. A., & Gold, R. (2013) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-013-0394-8 · Cited by 148 · see citing works
Sulforaphane protects astrocytes against oxidative stress and delayed death caused by oxygen and glucose deprivation
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 · see citing works
Role of NRF2 in Lung Cancer
Sánchez-Ortega, M., Carrera, A. C., & Garrido, A. (2021) · Cells · doi:10.3390/cells10081879 · Cited by 124 · see citing works
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 121 · see citing works
Seaweed extracts and unsaturated fatty acid constituents from the green alga Ulva lactuca as activators of the cytoprotective Nrf2–ARE pathway
Wang, R., Paul, V. J., & Luesch, H. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.12.019 · Cited by 120 · see citing works
Self-citation
Dipeptidyl 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 · see citing works
ω-6 Polyunsaturated fatty acids (linoleic acid) activate both autophagy and antioxidation in a synergistic feedback loop via TOR-dependent and TOR-independent signaling pathways
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 · see citing works
Antioxidant and Anti-inflammatory Effect of Nrf2 Inducer Dimethyl Fumarate in Neurodegenerative Diseases
Scuderi, S. A., Ardizzone, A., Paterniti, I., Esposito, E., & Campolo, M. (2020) · Antioxidants · doi:10.3390/antiox9070630 · Cited by 114 · see citing works
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 109 · see citing works
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 104 · see citing works
Oxidative stress-mediated NFκB phosphorylation upregulates p62/SQSTM1 and promotes retinal pigmented epithelial cell survival through increased autophagy
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 · see citing works
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 · see citing works
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 · see citing works
Key points for the development of antioxidant cocktails to prevent cellular stress and damage caused by reactive oxygen species (ROS) during manned space missions
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 · see citing works
Concurrent regulation of the transcription factors Nrf2 and ATF4 mediates the enhancement of glutathione levels by the flavonoid fisetin
Ehren, J. L., & Maher, P. A. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.04.010 · Cited by 84 · see citing works
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 82 · see citing works
The First Structure of Dipeptidyl-peptidase III Provides Insight into the Catalytic Mechanism and Mode of Substrate Binding
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 · see citing works
p62 provides dual cytoprotection against oxidative stress in the retinal pigment epithelium.
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 · see citing works
p62 as a therapeutic target for tumor
Tao, M., Liu, T., You, Q., & Jiang, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112231 · Cited by 78 · see citing works
Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III
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 · see citing works
Dipeptidyl peptidase 3 modulates the renin–angiotensin system in mice
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 · see citing works
The Impact of miRNA-Based Molecular Diagnostics and Treatment of NRF2-Stabilized Tumors
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 · see citing works
Antioxidant Defense Mechanisms in Erythrocytes and in the Central Nervous System
Franco, R., Navarro, G., & Martínez‐Pinilla, E. (2019) · Antioxidants · doi:10.3390/antiox8020046 · Cited by 70 · see citing works
Comparison of the Cytotoxicity of the Nitroaromatic Drug Flutamide to Its Cyano Analogue in the Hepatocyte Cell Line TAMH: Evidence for Complex I Inhibition and Mitochondrial Dysfunction Using Toxicogenomic Screening
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 · see citing works
Emerging Substrate Proteins of Kelch-like ECH Associated Protein 1 (Keap1) and Potential Challenges for the Development of Small-Molecule Inhibitors of the Keap1-Nuclear Factor Erythroid 2‑Related Factor 2 (Nrf2) Protein–Protein Interaction
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 · see citing works
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 · see citing works
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 · see citing works
Clostridium butyricum Alleviates Enterotoxigenic Escherichia coli K88-Induced Oxidative Damage Through Regulating the p62-Keap1-Nrf2 Signaling Pathway and Remodeling the Cecal Microbial Community
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 · see citing works
A novel small molecule, N-(4-(2-pyridyl)(1,3-thiazol-2-yl))-2-(2,4,6-trimethylphenoxy) acetamide, selectively protects against oxidative stress-induced cell death by activating the Nrf2–ARE pathway: Therapeutic implications for ALS
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 · see citing works
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 60 · see citing works
Imaging Induction of Cytoprotective Enzymes in Intact Human Cells: Coumberone, a Metabolic Reporter for Human AKR1C Enzymes Reveals Activation by Panaxytriol, an Active Component of Red Ginseng
Halim, M., Yee, D. J., & Sameš, D. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801245y · Cited by 59 · see citing works
High Expression of p62 Protein Is Associated with Poor Prognosis and Aggressive Phenotypes in Endometrial Cancer
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 56 · see citing works
Substrate complexes of human dipeptidyl peptidase III reveal the mechanism of enzyme inhibition
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 · see citing works
Protection of human cultured cells against oxidative stress by Rhodiola rosea without activation of antioxidant defenses
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 · see citing works
Self-citation
p62/SQSTM1, a Central but Unexploited Target: Advances in Its Physiological/Pathogenic Functions and Small Molecular Modulators
Chen, 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 58 · see citing works
Self-citation
High 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 52 · see citing works
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 50 · see citing works
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 · see citing works
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 50 · see citing works
1,5-Dicaffeoylquinic acid-mediated glutathione synthesis through activation of Nrf2 protects against OGD/reperfusion-induced oxidative stress in astrocytes
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 · see citing works
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 47 · see citing works
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 · see citing works
Self-citation
MicroRNA 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 · see citing works
Lipoxin A4 Activates Nrf2 Pathway and Ameliorates Cell Damage in Cultured Cortical Astrocytes Exposed to Oxygen-Glucose Deprivation/Reperfusion Insults
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 · see citing works
Tetrandrine Modulates Rheb-mTOR Signaling-Mediated Selective Autophagy and Protects Pulmonary Fibrosis
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 · see citing works
Self-citation
Transcriptional Analysis of Apoptotic Cerebellar Granule Neurons Following Rescue by Gastric Inhibitory Polypeptide
Maino, B., Ciotti, M. T., Calissano, P., & Cavallaro, S. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15045596 · Cited by 41 · see citing works
Lipoxin A4 ameliorates cerebral ischaemia/reperfusion injury through upregulation of nuclear factor erythroid 2-related factor 2
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 · see citing works
Radical oxygen species: an important breakthrough point for botanical drugs to regulate oxidative stress and treat the disorder of glycolipid metabolism
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 40 · see citing works
Self-citation
Benzo[a]pyrene evokes epithelial-mesenchymal transition and pulmonary fibrosis through AhR-mediated Nrf2-p62 signaling
Li, 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 · see citing works
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 · see citing works
Pharmacological stimulation of nuclear factor (erythroid-derived 2)-like 2 translation activates antioxidant responses
Pérez, Ó. C., Barrero, C. A., & Merali, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.770925 · Cited by 36 · see citing works
Sarmentosin promotes USP17 and regulates Nrf2-mediated mitophagy and cellular oxidative stress to alleviate APAP-induced acute liver failure
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 · see citing works
Small Maf functions in the maintenance of germline stem cells in the Drosophila testis
Tan, S. W. S., Yip, G. W. C., Suda, T., & Baeg, G. H. (2017) · Redox Biology · doi:10.1016/j.redox.2017.12.002 · Cited by 35 · see citing works
GBP3 promotes glioblastoma resistance to temozolomide by enhancing DNA damage repair
Xu, H., Jin, J., Chen, Y., Wu, G., Zhu, H., Wang, Q., Wang, J., Li, S., Grigore, F., Ma, J., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02397-5 · Cited by 35 · see citing works
Marine Natural Product Honaucin A Attenuates Inflammation by Activating the Nrf2-ARE Pathway
Mascuch, S. J., Boudreau, P. D., Carland, T. M., Pierce‐Ward, N. T., Olson, J., Hensler, M. E., Choi, H., Campanale, J. P., Hamdoun, A. M., Nizet, V., et al. (2017) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00734 · Cited by 34 · see citing works
The Activity of SN33638, an Inhibitor of AKR1C3, on Testosterone and 17β-Estradiol Production and Function in Castration-Resistant Prostate Cancer and ER-Positive Breast Cancer
Yin, Y. D., Fu, M., Brooke, D. G., Heinrich, D. M., Denny, W. A., & Jamieson, S. M. F. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00159 · Cited by 33 · see citing works
A Complementary Chemical and Genomic Screening Approach for Druggable Targets in the Nrf2 Pathway and Small Molecule Inhibitors to Overcome Cancer Cell Drug Resistance
Matthews, J., Liang, X., Paul, V. J., & Luesch, H. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b01025 · Cited by 33 · see citing works
Self-citation
The mechanistic insights of the antioxidant Keap1-Nrf2 pathway in oncogenesis: a deadly scenario
Mukherjee, A. G., & Gopalakrishnan, A. V. (2023) · Medical Oncology · doi:10.1007/s12032-023-02124-4 · Cited by 32 · see citing works
Mode of action and clinical studies with fumarates in multiple sclerosis
Salmen, A., & Gold, R. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.02.015 · Cited by 32 · see citing works
Rb1 Protects Endothelial Cells from Hydrogen Peroxide-Induced Cell Senescence by Modulating Redox Status
Liu, D., Chen, Y., Liu, Y., Hao, B., Zhou, B., Wu, L., Wang, M., Chen, L., Wu, W.-K., & Qian, X. (2011) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.34.1072 · Cited by 32 · see citing works
Self-citation
PPEF/PP7 protein Ser/Thr phosphatases
Andreeva, A. V., & Kutuzov, M. A. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0110-7 · Cited by 32 · see citing works
Benefits of Structural Genomics for Drug Discovery Research
Grabowski, M., Chruszcz, M., Zimmerman, M. D., Kirillova, O., & Minor, W. (2009) · Infectious Disorders - Drug Targets · doi:10.2174/187152609789105704 · Cited by 31 · see citing works
Regulated protein expression for in vivo gene therapy for neurological disorders: Progress, strategies, and issues
Manfredsson, F. P., Bloom, D. C., & Mandel, R. J. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.001 · Cited by 29 · see citing works
Identification of Candidate Genes and Gene Networks Specifically Associated with Analgesic Tolerance to Morphine
Tapocik, J. D., Letwin, N. E., Mayo, C. L., Frank, B. C., Luu, T., Oduaran, O. H., House, C. D., Williams, R., Elmer, G. I., & Lee, N. H. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4020-08.2009 · Cited by 29 · see citing works
Miconazole Contributes to NRF2 Activation by Noncanonical P62-KEAP1 Pathway in Bladder Cancer Cells
Tsai, T., Chen, P., Lin, Y., Chou, K., Chen, H., Ho, C., Lin, J., & Hwang, T. I. (2020) · Drug Design Development and Therapy · doi:10.2147/dddt.s227892 · Cited by 28 · see citing works
A global survey identifies novel upstream components of the Ath5 neurogenic network
Souren, M., Martínez‐Morales, J. R., Makri, P., Wittbrodt, B., & Wittbrodt, J. (2009) · Genome biology · doi:10.1186/gb-2009-10-9-r92 · Cited by 28 · see citing works
The Large Scale Conformational Change of the Human DPP III–Substrate Prefers the “Closed” Form
Tomić, A., González, M., & Tomić, S. (2012) · Journal of Chemical Information and Modeling · doi:10.1021/ci300141k · Cited by 27 · see citing works
Absolutely conserved tryptophan in M49 family of peptidases contributes to catalysis and binding of competitive inhibitors
Špoljarić, J., Salopek‐Sondi, B., Makarević, J., Vukelić, B., Agić, D., Šimaga, Š., Jajčanin-Jozić, N., & Abramić, M. (2009) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2009.03.002 · Cited by 27 · see citing works
Artemisinin Protects Human Retinal Pigmented Epithelial Cells Against Hydrogen Peroxide-induced Oxidative Damage by Enhancing the Activation of AMP-active Protein Kinase
Li, S., Chaudhary, S. C., Zhao, X., Gaur, U., Fang, J., Yan, F., & Zheng, W. (2019) · International Journal of Biological Sciences · doi:10.7150/ijbs.30536 · Cited by 27 · see citing works

Discovery and Characterization of Small Molecule Activators of the Antioxidant Response Element
Wang, R. (2012) · University of Florida Digital Collections (University of Florida)
Nrf2-Dependent Activation of the Antioxidant Responsive Element by tert-Butylhydroquinone Is Independent of Oxidative Stress in IMR-32 Human Neuroblastoma Cells
Lee, J., Moehlenkamp, J. D., Hanson, J. M., & Johnson, J. A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4106 · Cited by 124 · see citing works
Self-citation
Antioxidant Responsive Element Activation by Quinones: Antioxidant Responsive Element Target Genes, Role of PI3 Kinase in Activation
Li, J., Lee, J., Johnson, D. A., & Johnson, J. A. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)78019-2 · Cited by 10 · see citing works
Self-citation
Genome-Wide Overexpression Screen for Activators of Antioxidant Gene Transcription
Luesch, H., & Liu, Y. (2008) · Methods in molecular biology · doi:10.1007/978-1-60327-517-0_26 · Cited by 2 · see citing works
Self-citation
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 · see citing works

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)
ORCID: Liu, Yanxia
Kern, Jonathan T.
Walker, John R.
Johnson, Jeffrey A.
Schultz, Peter G.
Luesch, Hendrik
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
DOI: 10.1073/pnas.0700898104
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

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

A genomic screen for activators of the antioxidant response element

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks