Nrf2 in Cancer, Detoxifying Enzymes and Cell Death Programs

Ray, 2012, Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling, Cell. Signal., 24, 981, 10.1016/j.cellsig.2012.01.008

Paiva, 2014, Are Reactive Oxygen Species Always Detrimental to Pathogens?, Antioxid. Redox Signal., 20, 1000, 10.1089/ars.2013.5447

Trachootham, 2009, Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?, Nat. Rev. Drug Discov., 8, 579, 10.1038/nrd2803

Andersen, 2004, Oxidative stress in neurodegeneration: Cause or consequence?, Nat. Med., 10, S18, 10.1038/nrn1434

Haigis, 2010, The Aging Stress Response, Mol. Cell, 40, 333, 10.1016/j.molcel.2010.10.002

Maiorino, 2013, Glutathione peroxidases, Biochim. Biophys. Acta, 1830, 3289, 10.1016/j.bbagen.2012.11.020

Holmgren, 2010, Thioredoxin and thioredoxin reductase: Current research with special reference to human disease, Biochem. Biophys. Res. Commun., 396, 120, 10.1016/j.bbrc.2010.03.083

2011, Basic Principles and Emerging Concepts in the Redox Control of Transcription Factors, Antioxid. Redox Signal., 15, 2335, 10.1089/ars.2010.3534

Itoh, 2003, Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles, Genes Cells, 8, 379, 10.1046/j.1365-2443.2003.00640.x

Wu, 2014, Hrd1 suppresses Nrf2-mediated cellular protection during liver cirrhosis, Genes Dev., 28, 708, 10.1101/gad.238246.114

Rada, 2011, SCF/ -TrCP Promotes Glycogen Synthase Kinase 3-Dependent Degradation of the Nrf2 Transcription Factor in a Keap1-Independent Manner, Mol. Cell. Biol., 31, 1121, 10.1128/MCB.01204-10

Katsuragi, 2016, Regulation of the Keap1–Nrf2 pathway by p62/SQSTM1, Curr. Opin. Toxicol., 1, 54, 10.1016/j.cotox.2016.09.005

Chapman, 2018, NRF2 and the Hallmarks of Cancer, Cancer Cell, 34, 21, 10.1016/j.ccell.2018.03.022

Liu, 2021, Regulation of Nrf2 by phosphorylation: Consequences for biological function and therapeutic implications, Free. Radic. Biol. Med., 168, 129, 10.1016/j.freeradbiomed.2021.03.034

Walters, 2021, SUMO-Modification of Human Nrf2 at K110 and K533 Regulates Its Nucleocytoplasmic Localization, Stability and Transcriptional Activity, Cell. Physiol. Biochem., 55, 141, 10.33594/000000351

Baird, 2013, Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex, Proc. Natl. Acad. Sci. USA, 110, 15259, 10.1073/pnas.1305687110

Dancy, 2015, Protein Lysine Acetylation by p300/CBP, Chem. Rev., 115, 2419, 10.1021/cr500452k

Kawai, 2011, Acetylation-Deacetylation of the Transcription Factor Nrf2 (Nuclear Factor Erythroid 2-related Factor 2) Regulates Its Transcriptional Activity and Nucleocytoplasmic Localization, J. Biol. Chem., 286, 7629, 10.1074/jbc.M110.208173

Sun, 2009, Acetylation of Nrf2 by p300/CBP Augments Promoter-Specific DNA Binding of Nrf2 during the Antioxidant Response, Mol. Cell. Biol., 29, 2658, 10.1128/MCB.01639-08

Zhang, 2006, BRG1 Interacts with Nrf2 To Selectively Mediate HO-1 Induction in Response to Oxidative Stress, Mol. Cell. Biol., 26, 7942, 10.1128/MCB.00700-06

Sekine, 2016, The Mediator Subunit MED16 Transduces NRF2-Activating Signals into Antioxidant Gene Expression, Mol. Cell. Biol., 36, 407, 10.1128/MCB.00785-15

Menegon, 2016, The Dual Roles of NRF2 in Cancer, Trends Mol. Med., 22, 578, 10.1016/j.molmed.2016.05.002

Johansson, 2005, Selenocysteine in proteins—Properties and biotechnological use, Biochim. Biophys. Acta (BBA) Gen. Subj., 1726, 1, 10.1016/j.bbagen.2005.05.010

Kasaikina, 2012, Understanding selenoprotein function and regulation through the use of rodent models, Biochim. Biophys. Acta (BBA) Bioenerg., 1823, 1633, 10.1016/j.bbamcr.2012.02.018

Lu, 2014, The thioredoxin antioxidant system, Free Radic. Biol. Med., 66, 75, 10.1016/j.freeradbiomed.2013.07.036

Canning, 2015, Structural basis of Keap1 interactions with Nrf2, Free Radic. Biol. Med., 88, 101, 10.1016/j.freeradbiomed.2015.05.034

Zhang, 2004, Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex, Mol. Cell. Biol., 24, 10941, 10.1128/MCB.24.24.10941-10953.2004

Cullinan, 2004, The Keap1-BTB Protein Is an Adaptor That Bridges Nrf2 to a Cul3-Based E3 Ligase: Oxidative Stress Sensing by a Cul3-Keap1 Ligase, Mol. Cell Biol., 24, 8477, 10.1128/MCB.24.19.8477-8486.2004

Tong, 2007, Different Electrostatic Potentials Define ETGE and DLG Motifs as Hinge and Latch in Oxidative Stress Response, Mol. Cell. Biol., 27, 7511, 10.1128/MCB.00753-07

Tong, 2006, Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism, Biol. Chem., 387, 1311, 10.1515/BC.2006.164

Horie, 2021, Molecular basis for the disruption of Keap1–Nrf2 interaction via Hinge & Latch mechanism, Commun. Biol., 4, 1, 10.1038/s42003-021-02100-6

Iso, 2016, Absolute Amounts and Status of the Nrf2-Keap1-Cul3 Complex within Cells, Mol. Cell. Biol., 36, 3100, 10.1128/MCB.00389-16

Small, 2010, Development of an efficient E. coli expression and purification system for a catalytically active, human Cullin3–RINGBox1 protein complex and elucidation of its quaternary structure with Keap1, Biochem. Biophys. Res. Commun., 400, 471, 10.1016/j.bbrc.2010.08.062

Zhuang, 2009, Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases, Mol. Cell, 36, 39, 10.1016/j.molcel.2009.09.022

Choo, Y.Y., and Hagen, T. (2012). Mechanism of Cullin3 E3 Ubiquitin Ligase Dimerization. PLoS ONE, 7.

Villeneuve, 2010, Regulation of the Nrf2–Keap1 Antioxidant Response by the Ubiquitin Proteasome System: An Insight into Cullin-Ring Ubiquitin Ligases, Antioxid. Redox Signal., 13, 1699, 10.1089/ars.2010.3211

Varshavsky, 2019, N-degron and C-degron pathways of protein degradation, Proc. Natl. Acad. Sci. USA, 116, 358, 10.1073/pnas.1816596116

Tao, 2017, p97 Negatively Regulates NRF2 by Extracting Ubiquitylated NRF2 from the KEAP1-CUL3 E3 Complex, Mol. Cell. Biol., 37, e00660-16, 10.1128/MCB.00660-16

Lee, 2009, KEAP1 E3 Ligase-Mediated Downregulation of NF-κB Signaling by Targeting IKKβ, Mol. Cell, 36, 131, 10.1016/j.molcel.2009.07.025

Suzuki, 2019, Molecular Mechanism of Cellular Oxidative Stress Sensing by Keap1, Cell Rep., 28, 746, 10.1016/j.celrep.2019.06.047

Mills, 2018, Itaconate Is an Anti-Inflammatory Metabolite That Activates Nrf2 via Alkylation of KEAP1, Nature, 556, 113, 10.1038/nature25986

Sun, 2007, Keap1 Controls Postinduction Repression of the Nrf2-Mediated Antioxidant Response by Escorting Nuclear Export of Nrf2, Mol. Cell. Biol., 27, 6334, 10.1128/MCB.00630-07

Chowdhry, 2013, Nrf2 is controlled by two distinct β-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity, Oncogene, 32, 3765, 10.1038/onc.2012.388

Fuchs, 2004, The many faces of β-TrCP E3 ubiquitin ligases: Reflections in the magic mirror of cancer, Oncogene, 23, 2028, 10.1038/sj.onc.1207389

Niture, 2014, Regulation of Nrf2—An update, Free Radic. Biol. Med., 66, 36, 10.1016/j.freeradbiomed.2013.02.008

Newman, 2003, Comprehensive Identification of Human bZIP Interactions with Coiled-Coil Arrays, Science, 300, 2097, 10.1126/science.1084648

Malhotra, 2010, Global mapping of binding sites for Nrf2 identifies novel targets in cell survival response through ChIP-Seq profiling and network analysis, Nucleic Acids Res., 38, 5718, 10.1093/nar/gkq212

Chorley, 2012, Identification of novel NRF2-regulated genes by ChIP-Seq: Influence on retinoid X receptor alpha, Nucleic Acids Res., 40, 7416, 10.1093/nar/gks409

Namani, 2019, Genome-wide global identification of NRF2 binding sites in A549 non-small cell lung cancer cells by ChIP-Seq reveals NRF2 regulation of genes involved in focal adhesion pathways, Aging, 11, 12600, 10.18632/aging.102590

Okazaki, 2020, Enhancer remodeling promotes tumor-initiating activity in NRF2-activated non-small cell lung cancers, Nat. Commun., 11, 5911, 10.1038/s41467-020-19593-0

Otsuki, 2016, Unique cistrome defined as CsMBE is strictly required for Nrf2-sMaf heterodimer function in cytoprotection, Free Radic. Biol. Med., 91, 45, 10.1016/j.freeradbiomed.2015.12.005

Itoh, 1997, An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response Elements, Biochem. Biophys. Res. Commun., 236, 313, 10.1006/bbrc.1997.6943

Katsuoka, 2016, Small Maf proteins (MafF, MafG, MafK): History, structure and function, Gene, 586, 197, 10.1016/j.gene.2016.03.058

Katsuoka, F., Otsuki, A., Takahashi, M., Ito, S., and Yamamoto, M. (2019). Direct and Specific Functional Evaluation of the Nrf2 and MafG Heterodimer by Introducing a Tethered Dimer into Small Maf-Deficient Cells. Mol. Cell. Biol., 39.

Liu, 2018, RPA1 binding to NRF2 switches ARE-dependent transcriptional activation to ARE-NRE–dependent repression, Proc. Natl. Acad. Sci. USA, 115, E10352, 10.1073/pnas.1812125115

Ito, 2009, Crystal structure of the Bach1 BTB domain and its regulation of homodimerization, Genes Cells, 14, 167, 10.1111/j.1365-2443.2008.01259.x

Ogawa, 2001, Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1, EMBO J., 20, 2835, 10.1093/emboj/20.11.2835

Sun, 2002, Hemoprotein Bach1 regulates enhancer availability of heme oxygenase-1 gene, EMBO J., 21, 5216, 10.1093/emboj/cdf516

Cai, 2021, Crm1-Dependent Nuclear Export of Bach1 is Involved in the Protective Effect of Hyperoside on Oxidative Damage in Hepatocytes and CCl4-induced Acute Liver Injury, J. Inflamm. Res., 14, 551, 10.2147/JIR.S279249

Lignitto, 2019, Nrf2 Activation Promotes Lung Cancer Metastasis by Inhibiting the Degradation of Bach1, Cell, 178, 316, 10.1016/j.cell.2019.06.003

Wiel, 2019, BACH1 Stabilization by Antioxidants Stimulates Lung Cancer Metastasis, Cell, 178, 330, 10.1016/j.cell.2019.06.005

Hanahan, 2000, The Hallmarks of Cancer, Cell, 100, 57, 10.1016/S0092-8674(00)81683-9

Hanahan, 2011, Hallmarks of Cancer: The Next Generation, Cell, 144, 646, 10.1016/j.cell.2011.02.013

Nguyen, 2007, Genetic determinants of cancer metastasis, Nat. Rev. Genet., 8, 341, 10.1038/nrg2101

Paul, D. (2020). The systemic hallmarks of cancer. J. Cancer Metastasis Treat., 6.

Bhagwat, 2015, Targeting Transcription Factors in Cancer, Trends Cancer, 1, 53, 10.1016/j.trecan.2015.07.001

Nebert, 2002, Transcription factors and cancer: An overview, Toxicology, 181–182, 131, 10.1016/S0300-483X(02)00269-X

Vishnoi, K., Viswakarma, N., Rana, A., and Rana, B. (2020). Transcription Factors in Cancer Development and Therapy. Cancers, 12.

DeNicola, 2011, Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis, Nat. Cell Biol., 475, 106

Wei, 2013, Oncogenic functions of the transcription factor Nrf2, Free Radic. Biol. Med., 65, 750, 10.1016/j.freeradbiomed.2013.06.041

Ohta, 2008, Loss of Keap1 Function Activates Nrf2 and Provides Advantages for Lung Cancer Cell Growth, Cancer Res., 68, 1303, 10.1158/0008-5472.CAN-07-5003

Singh, A., Misra, V., Thimmulappa, R.K., Lee, H., Ames, S., Hoque, M.O., Herman, J.G., Baylin, S.B., Sidransky, D., and Gabrielson, E. (2006). Dysfunctional KEAP1–NRF2 Interaction in Non-Small-Cell Lung Cancer. PLoS Med., 3.

Shibata, 2008, Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy, Proc. Natl. Acad. Sci. USA, 105, 13568, 10.1073/pnas.0806268105

Siegel, 1998, Immunohistochemical detection of NAD(P)H:quinone oxidoreductase in human lung and lung tumors, Clin. Cancer Res., 4, 2065

Guichard, 2012, Integrated analysis of somatic mutations and focal copy-number changes identifies key genes and pathways in hepatocellular carcinoma, Nat. Genet., 44, 694, 10.1038/ng.2256

Kowalik, 2016, Metabolic reprogramming identifies the most aggressive lesions at early phases of hepatic carcinogenesis, Oncotarget, 7, 32375, 10.18632/oncotarget.8632

Sanghvi, 2019, The Oncogenic Action of NRF2 Depends on De-glycation by Fructosamine-3-Kinase, Cell, 178, 807, 10.1016/j.cell.2019.07.031

Wang, 2008, Hypermethylation of the Keap1 gene in human lung cancer cell lines and lung cancer tissues, Biochem. Biophys. Res. Commun., 373, 151, 10.1016/j.bbrc.2008.06.004

Muscarella, 2011, Frequent epigenetics inactivation of KEAP1 gene in non-small cell lung cancer, Epigenetics, 6, 710, 10.4161/epi.6.6.15773

2005, Redox Activation of p21Cip1/WAF1/Sdi1: A Multifunctional Regulator of Cell Survival and Death, Antioxid. Redox Signal., 7, 108, 10.1089/ars.2005.7.108

Chen, 2009, Direct Interaction between Nrf2 and p21Cip1/WAF1 Upregulates the Nrf2-Mediated Antioxidant Response, Mol. Cell, 34, 663, 10.1016/j.molcel.2009.04.029

Sakurai, 2005, Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: Role of NF-E2-related factor-2, J. Cell. Physiol., 203, 529, 10.1002/jcp.20246

Thimmulappa, 2002, Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray, Cancer Res., 62, 5196

Kwak, 2003, Modulation of Gene Expression by Cancer Chemopreventive Dithiolethiones through the Keap1-Nrf2 Pathway, J. Biol. Chem., 278, 8135, 10.1074/jbc.M211898200

Papp, 2007, From Selenium to Selenoproteins: Synthesis, Identity, and Their Role in Human Health, Antioxid. Redox Signal., 9, 775, 10.1089/ars.2007.1528

Flouda, 2016, Quantification of low molecular weight selenium metabolites in human plasma after treatment with selenite in pharmacological doses by LC-ICP-MS, Anal. Bioanal. Chem., 408, 2293, 10.1007/s00216-016-9325-2

Schomburg, 2009, Hierarchical regulation of selenoprotein expression and sex-specific effects of selenium, Biochim. Biophys. Acta (BBA) Gen. Subj., 1790, 1453, 10.1016/j.bbagen.2009.03.015

Legrain, 2014, Selective Up-regulation of Human Selenoproteins in Response to Oxidative Stress, J. Biol. Chem., 289, 14750, 10.1074/jbc.M114.551994

Muller, 2010, Nrf2 target genes are induced under marginal selenium-deficiency, Genes Nutr., 5, 297, 10.1007/s12263-010-0168-8

Tauber, S., Sieckmann, M., Erler, K., Stahl, W., Klotz, L.-O., and Steinbrenner, H. (2021). Activation of Nrf2 by Electrophiles Is Largely Independent of the Selenium Status of HepG2 Cells. Antioxidants, 10.

Cadenas, 2013, Chapter Four—Selenium in the Redox Regulation of the Nrf2 and the Wnt Pathway, Methods in Enzymology, Volume 527, 65, 10.1016/B978-0-12-405882-8.00004-0

Schmidt, H.H.H.W., Ghezzi, P., and Cuadrado, A. (2021). Effects of Mammalian Thioredoxin Reductase Inhibitors. Reactive Oxygen Species: Network Pharmacology and Therapeutic Applications, Springer International Publishing. Handbook of Experimental Pharmacology.

Selenius, 2010, Selenium and the Selenoprotein Thioredoxin Reductase in the Prevention, Treatment and Diagnostics of Cancer, Antioxid. Redox Signal., 12, 867, 10.1089/ars.2009.2884

Bhatia, 2016, The thioredoxin system in breast cancer cell invasion and migration, Redox Biol., 8, 68, 10.1016/j.redox.2015.12.004

Yoo, 2006, Thioredoxin Reductase 1 Deficiency Reverses Tumor Phenotype and Tumorigenicity of Lung Carcinoma Cells, J. Biol. Chem., 281, 13005, 10.1074/jbc.C600012200

Lubos, 2011, Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities, Antioxid. Redox Signal., 15, 1957, 10.1089/ars.2010.3586

Liu, 2004, Redox Regulation of Pancreatic Cancer Cell Growth: Role of Glutathione Peroxidase in the Suppression of the Malignant Phenotype, Hum. Gene Ther., 15, 239, 10.1089/104303404322886093

Krehl, 2011, Glutathione peroxidase-2 and selenium decreased inflammation and tumors in a mouse model of inflammation-associated carcinogenesis whereas sulforaphane effects differed with selenium supply, Carcinogenesis, 33, 620, 10.1093/carcin/bgr288

Banning, 2008, GPx2 Counteracts PGE2 Production by Dampening COX-2 and mPGES-1 Expression in Human Colon Cancer Cells, Antioxid. Redox Signal., 10, 1491, 10.1089/ars.2008.2047

Florian, 2001, Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue, Free Radic. Res., 35, 655, 10.1080/10715760100301181

Yu, 2007, Glutathione Peroxidase 3, Deleted or Methylated in Prostate Cancer, Suppresses Prostate Cancer Growth and Metastasis, Cancer Res., 67, 8043, 10.1158/0008-5472.CAN-07-0648

Yang, 2014, Regulation of Ferroptotic Cancer Cell Death by GPX4, Cell, 156, 317, 10.1016/j.cell.2013.12.010

Tew, 2017, Chapter Two—Selenoproteins in Tumorigenesis and Cancer Progression, Advances in Cancer Re-search, Volume 136, 49, 10.1016/bs.acr.2017.08.002

Tew, 2017, Chapter Three–Selenoproteins and Metastasis, Advances in Cancer Research, Volume 136, 85, 10.1016/bs.acr.2017.07.008

Stockwell, 2020, Emerging Mechanisms and Disease Relevance of Ferroptosis, Trends Cell Biol., 30, 478, 10.1016/j.tcb.2020.02.009

Gaschler, 2017, Lipid peroxidation in cell death, Biochem. Biophys. Res. Commun., 482, 419, 10.1016/j.bbrc.2016.10.086

Cao, 2016, Mechanisms of ferroptosis, Cell. Mol. Life Sci., 73, 2195, 10.1007/s00018-016-2194-1

Dodson, 2019, NRF2 plays a critical role in mitigating lipid peroxidation and ferroptosis, Redox Biol., 23, 101107, 10.1016/j.redox.2019.101107

Takahashi, 2020, 3D Culture Models with CRISPR Screens Reveal Hyperactive NRF2 as a Prerequisite for Spheroid Formation via Regulation of Proliferation and Ferroptosis, Mol. Cell, 80, 828, 10.1016/j.molcel.2020.10.010

Ota, 2013, Microtechnology-based three-dimensional spheroid formation, Front. Biosci., E5, 37, 10.2741/E594

Ubellacker, 2020, Lymph protects metastasizing melanoma cells from ferroptosis, Nat. Cell Biol., 585, 113

Sies, H. (2020). Chapter 31—Perspectives of TrxR1-based cancer therapies. Oxidative Stress, Academic Press.

Zheng, 2019, The antimetastatic effect and underlying mechanisms of thioredoxin reductase inhibitor ethaselen, Free Radic. Biol. Med., 131, 7, 10.1016/j.freeradbiomed.2018.11.030

Stafford, 2018, Irreversible inhibition of cytosolic thioredoxin reductase 1 as a mechanistic basis for anticancer therapy, Sci. Transl. Med., 10, eaaf7444, 10.1126/scitranslmed.aaf7444

2003, Rapid Induction of Cell Death by Selenium-compromised Thioredoxin Reductase 1 but Not by the Fully Active Enzyme Containing Selenocysteine, J. Biol. Chem., 278, 15966, 10.1074/jbc.M210733200

Anestål, K., Prast-Nielsen, S., Cenas, N., and Arnér, E.S.J. (2008). Cell Death by SecTRAPs: Thioredoxin Reductase as a Prooxidant Killer of Cells. PLoS ONE, 3.

Ingold, 2018, Selenium Utilization by GPX4 Is Required to Prevent Hydroperoxide-Induced Ferroptosis, Cell, 172, 409, 10.1016/j.cell.2017.11.048

Niture, 2012, Nrf2 Protein Up-regulates Antiapoptotic Protein Bcl-2 and Prevents Cellular Apoptosis, J. Biol. Chem., 287, 9873, 10.1074/jbc.M111.312694

Duhieu, 2012, The differential expression of glutathione peroxidase 1 and 4 depends on the nature of the SECIS element, RNA Biol., 9, 681, 10.4161/rna.20147

Papp, 2010, SECIS-Binding Protein 2 Promotes Cell Survival by Protecting Against Oxidative Stress, Antioxid. Redox Signal., 12, 797, 10.1089/ars.2009.2913

Gouge, 2015, Redox Signaling by the RNA Polymerase III TFIIB-Related Factor Brf2, Cell, 163, 1375, 10.1016/j.cell.2015.11.005

Faresse, N.J., Canella, D., Praz, V., Michaud, J., Romascano, D., and Hernandez, N. (2012). Genomic Study of RNA Polymerase II and III SNAPc-Bound Promoters Reveals a Gene Transcribed by Both Enzymes and a Broad Use of Common Activators. PLoS Genet., 8.

Schramm, 2002, Recruitment of RNA polymerase III to its target promoters, Genes Dev., 16, 2593, 10.1101/gad.1018902

Gouge, 2017, Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation, Nat. Commun., 8, 130, 10.1038/s41467-017-00126-1

Lockwood, W.W., Chari, R., Coe, B.P., Thu, K.L., Garnis, C., Malloff, C.A., Campbell, J., Williams, A.C., Hwang, D., and Zhu, C.-Q. (2010). Integrative Genomic Analyses Identify BRF2 as a Novel Lineage-Specific Oncogene in Lung Squamous Cell Carcinoma. PLoS Med., 7.

Bian, 2020, Silencing of BRF2 inhibits the growth and metastasis of lung cancer cells, Mol. Med. Rep., 22, 1767, 10.3892/mmr.2020.11285

Villagrasa, 2014, Integration of Genomic Data Enables Selective Discovery of Breast Cancer Drivers, Cell, 159, 1461, 10.1016/j.cell.2014.10.048

Meneses, 2020, A meta-analysis of BRF2 as a prognostic biomarker in invasive breast carcinoma, BMC Cancer, 20, 1

Jameson, 2002, Selenium Influences the Turnover of Selenocysteine tRNA[Ser]Sec in Chinese Hamster Ovary Cells, J. Nutr., 132, 1830, 10.1093/jn/132.7.1830

Gouge, 2018, New tricks for an old dog: Brf2-dependent RNA Polymerase III transcription in oxidative stress and cancer, Transcription, 9, 61, 10.1080/21541264.2017.1335269

Zucker, 2014, Nrf2 Amplifies Oxidative Stress via Induction of Klf9, Mol. Cell, 53, 916, 10.1016/j.molcel.2014.01.033

Yang, 2020, Auranofin mitigates systemic iron overload and induces ferroptosis via distinct mechanisms, Signal Transduct. Target. Ther., 5, 1

Panieri, E., Buha, A., Telkoparan-Akillilar, P., Cevik, D., Kouretas, D., Veskoukis, A., Skaperda, Z., Tsatsakis, A., Wallace, D., and Suzen, S. (2020). Potential Applications of NRF2 Modulators in Cancer Therapy. Antioxidants, 9.