JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress

The ferritins: molecular properties, iron storage function and cellular regulation

Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667 · see citing works

Balancing Acts

Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736 · see citing works

The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity

Rushmore, T. H., Morton, M. R., & Pickett, C. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99004-6 · Cited by 1,464 · see citing works

Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress.

Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292 · 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

Regulation of ferritin genes and protein

Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173 · see citing works

REDOX REGULATION OF CELLULAR ACTIVATION

Nakamura, H., Nakamura, K., & Yodoi, J. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.351 · Cited by 1,106 · see citing works

AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1

Hirota, K., Matsui, M., Iwata, S., Nishiyama, A., Mori, K., & Yodoi, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3633 · Cited by 845 · see citing works

Identification and characterization of Ref‐1, a nuclear protein that facilitates AP‐1 DNA‐binding activity.

Xanthoudakis, S., & Curran, T. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05097.x · Cited by 708 · see citing works

The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells

Richardson, D. R., & Ponka, P. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(96)00014-7 · Cited by 706 · see citing works

Functional antioxidant responsive elements

Wasserman, W. W., & Fahl, W. E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5361 · Cited by 705 · see citing works

Ferritin heavy chain upregulation by NF-κB inhibits TNFα-induced apoptosis by suppressing reactive oxygen species

Pham, C. G., Bubici, C., Zazzeroni, F., Papa, S., Jones, J., Alvarez, K., Jayawardena, S., De Smaele, E., Cong, R., Beaumont, C., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.017 · Cited by 663 · see citing works

Regulation of γ-Glutamylcysteine Synthetase Subunit Gene Expression by the Transcription Factor Nrf2

Wild, A. C., Moinova, H., & Mulcahy, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33627 · Cited by 595 · see citing works

JunD Reduces Tumor Angiogenesis by Protecting Cells from Oxidative Stress

Gerald, D., Berra, E., Frapart, Y. M., Chan, D. A., Giaccia, A. J., Mansuy, D., Pouysségur, J., Yaniv, M., & Mechta-Grigoriou, F. (2004) · Cell · doi:10.1016/j.cell.2004.08.025 · Cited by 588 · see citing works

Iron Homeostasis, Oxidative Stress, and DNA Damage

Meneghini, R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00016-6 · Cited by 578 · see citing works

Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes

Radjendirane, V., & Jaiswal, A. K. (1998) · Oncogene · doi:10.1038/sj.onc.1202237 · Cited by 566 · see citing works

Ferritin, iron homeostasis, and oxidative damage1,2 1Guest Editor: Mario Comporti 2This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.

Arosio, P., & Levi, S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00842-0 · Cited by 543 · see citing works

Ferritin and the response to oxidative stress

Orino, K., Lehman, L. J., Tsuji, Y., Ayaki, H., Torti, S. V., & Torti, F. M. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570241 · Cited by 535 · see citing works

Ferritin and the response to oxidative stress

ORINO, K., LEHMAN, L., TSUJI, Y., AYAKI, H., TORTI, S. V., & TORTI, F. M. (2001) · Biochemical Journal · doi:10.1042/bj3570241 · Cited by 535 · see citing works

Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants.

Rushmore, T. H., & Pickett, C. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77351-1 · Cited by 522 · see citing works

Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence

Nioi, P., McMahon, M. J., Itoh, K., Yamamoto, M. P., & Hayes, J. D. (2003) · Biochemical Journal · doi:10.1042/bj20030754 · Cited by 508 · see citing works

Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element.

Friling, R. S., Bensimon, A., Tichauer, Y., & Daniel, V. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.16.6258 · Cited by 475 · see citing works

Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors

Motohashi, H., O'Connor, T., Katsuoka, F., Engel, J. D., & Yamamoto, M. P. (2002) · Gene · doi:10.1016/s0378-1119(02)00788-6 · Cited by 456 · see citing works

Regulation of glutathione S-transferase Ya subunit gene expression: identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds.

Rushmore, T. H., King, R. G., Paulson, K. E., & Pickett, C. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3826 · Cited by 423 · see citing works

Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site. A study of iron uptake and ferro-oxidase activity of human liver, recombinant H-chain ferritins, and of two H-chain deletion mutants.

Levi, S., Luzzago, A., Cesareni, G., Cozzi, A., Franceschinelli, F., Albertini, A., & Arosio, P. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81326-1 · Cited by 378 · see citing works

Role of Transcription Factor Nrf2 in the Induction of Hepatic Phase 2 and Antioxidative Enzymes in vivo by the Cancer Chemoprotective Agent, 3H-1, 2-Dithiole-3-thione

Kwak, M., Itoh, K., Yamamoto, M. P., Sutter, T. R., & Kensler, T. W. (2001) · Molecular Medicine · doi:10.1007/bf03401947 · Cited by 357 · see citing works

Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element.

Li, Y., & Jaiswal, A. K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42151-5 · Cited by 353 · see citing works

Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione.

Kwak, M.-K., Itoh, K., Yamamoto, M. P., Sutter, T. R., & Kensler, T. W. (2001) · PubMed Central · Cited by 330 · see citing works

Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention

Hayes, J. D. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00695-4 · Cited by 323 · see citing works

Induction of Ferritin Synthesis by Oxidative Stress

Cairo, G., Tacchini, L., Pogliaghi, G., Anzon, E., Tomasi, A., & Bernelli‐Zazzera, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.700 · Cited by 322 · see citing works

The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene.

Torti, S. V., Kwak, E. L., Miller, S. C., Miller, L. L., Ringold, G. M., Myambo, K. B., Young, A. P., & Torti, F. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37801-3 · Cited by 295 · see citing works

Coordinate Transcriptional and Translational Regulation of Ferritin in Response to Oxidative Stress

Tsuji, Y., Ayaki, H., Whitman, S. P., Morrow, C. S., Torti, S. V., & Torti, F. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5818-5827.2000 · Cited by 285 · see citing works

Nrf2 Mediates the Induction of Ferritin H in Response to Xenobiotics and Cancer Chemopreventive Dithiolethiones

Pietsch, E. C., Chan, J. Y., Torti, F. M., & Torti, S. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210664200 · Cited by 284 · see citing works

JunD Protects Cells from p53-Dependent Senescence and Apoptosis

Weitzman, J. B., Fiette, L., Matsuo, K., & Yaniv, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00109-x · Cited by 269 · see citing works

Evidence of H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin

Levi, S., Yewdall, S. J., Harrison, P. M., Santambrogio, P., Cozzi, A., Rovida, E., Albertini, A., & Arosio, P. (1992) · Biochemical Journal · doi:10.1042/bj2880591 · Cited by 268 · see citing works

JunD Mediates Survival Signaling by the JNK Signal Transduction Pathway

Lamb, J. A., Ventura, J., Hess, P., Flavell, R. A., & Davis, R. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00203-x · Cited by 261 · see citing works

Overexpression of Wild Type and Mutated Human Ferritin H-chain in HeLa Cells

Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Albertini, A., & Arosio, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003797200 · Cited by 242 · see citing works

Ferritin: At the Crossroads of Iron and Oxygen Metabolism

Theil, E. C. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1549s · Cited by 240 · see citing works

Antioxidant response element

Jaiswal, A. K. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90272-0 · Cited by 240 · see citing works

Iron-sulfur clusters as biosensors of oxidants and iron.

Rouault, T. A., & Klausner, R. D. (1996) · PubMed · Cited by 238 · see citing works

Iron-independent induction of ferritin H chain by tumor necrosis factor

Miller, L. L., Miller, S. C., Torti, S. V., Tsuji, Y., & Torti, F. M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4946 · Cited by 213 · see citing works

H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties

Epsztejn, S., Glickstein, H., Picard, V., Slotki, I. N., Breuer, W., Beaumont, C., & Cabantchik, Z. I. (1999) · Blood · doi:10.1182/blood.v94.10.3593.422k26_3593_3603 · Cited by 209 · see citing works

Iron-sulfur clusters as biosensors of oxidants and iron

Rouault, T. A., & Klausner, R. D. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10024-4 · Cited by 207 · see citing works

Small Maf (MafG and MafK) Proteins Negatively Regulate Antioxidant Response Element-mediated Expression and Antioxidant Induction of the NAD(P)H:Quinone Oxidoreductase1 Gene

Dhakshinamoorthy, S., & Jaiswal, A. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003531200 · Cited by 205 · see citing works

The Heme-Responsive Element of the Mouse Heme Oxygenase-1 Gene Is an Extended AP-1 Binding Site That Resembles the Recognition Sequences for MAF and NF-E2 Transcription Factors

Inamdar, N. M., Ahn, Y. I., & Alam, J. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0637 · Cited by 194 · see citing works

Role for NF-κB in the regulation of ferritin H by tumor necrosis factor-α

Kwak, E. L., Larochelle, D. A., Beaumont, C., Torti, S. V., & Torti, F. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.15285 · Cited by 189 · see citing works

The Role of the L-Chain in Ferritin Iron Incorporation

Levi, S., Santambrogio, P., Cozzi, A., Rovida, E., Corsi, B., Tamborini, E., Spada, S., Albertini, A., & Arosio, P. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1325 · Cited by 180 · see citing works

Evidence that a salt bridge in the light chain contributes to the physical stability difference between heavy and light human ferritins.

Santambrogio, P., Levi, S., Arosio, P., Palagi, L., Vecchio, G., Lawson, D. M., Yewdall, S. J., Artymiuk, P. J., Harrison, P. M., & Jappelli, R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49681-6 · Cited by 143 · see citing works

Properties of human tissue isoferritins

Wagstaff, M., Worwood, M., & Jacobs, A. J. (1978) · Biochemical Journal · doi:10.1042/bj1730969 · Cited by 132 · see citing works

Adaptive responses of rat tissue isoferritins to iron administration. Changes in subunit synthesis, isoferritin abundance, and capacity for iron storage.

Bomford, A. B., Conlon-Hollingshead, C., & Munro, H. N. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70071-4 · Cited by 129 · see citing works

Tumor necrosis factor-alpha and interleukin 1-alpha regulate transferrin receptor in human diploid fibroblasts. Relationship to the induction of ferritin heavy chain.

Tsuji, Y., Miller, L. L., Miller, S. C., Torti, S. V., & Torti, F. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89638-0 · Cited by 103 · see citing works

Structure and Expression of Ferritin Genes in a Human Promyelocytic Cell Line That Differentiates in Vitro

Chou, C. C., Gatti, R. A., Fuller, M. L., CONCANNON, P. J., Wong, A., Chada, S., Davis, R. C., & Salser, W. A. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.2.566 · Cited by 103 · see citing works

Menin uncouples Elk-1, JunD and c-Jun phosphorylation from MAP kinase activation

Gallo, A., Cuozzo, C., Esposito, I., Maggiolini, M., Bonofiglio, D., Vivacqua, A., Garramone, M., Weiß, C., Bohmann, D., & Musti, A. M. (2002) · Oncogene · doi:10.1038/sj.onc.1205822 · Cited by 101 · see citing works

Transcriptional Regulation of the Ferritin Heavy-Chain Gene: the Activity of the CCAAT Binding Factor NF-Y Is Modulated in Heme-Treated Friend Leukemia Cells and during Monocyte-to-Macrophage Differentiation

Marziali, G., Perrotti, E., Ilari, R., Testa, U., Coccia, E. M., & Battistini, A. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1387 · Cited by 91 · see citing works

The B Subunit of the CAAT-binding Factor NFY Binds the Central Segment of the Co-activator p300

Faniello, M. C., Bevilacqua, M. A., Condorelli, G., Crombrugghe, B. D., Maity, S. N., Avvedimento, V. E., Cimino, F., & Costanzo, F. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7623 · Cited by 90 · see citing works

Redox regulation of AP-1: a link between transcription factor signaling and DNA repair.

Xanthoudakis, S., & Curran, T. (1996) · PubMed · Cited by 80 · see citing works

Induction of c-fos and c-jun gene expression by phenolic antioxidants

Choi, H.-S., & Moore, D. D. (1993) · Molecular Endocrinology · doi:10.1210/mend.7.12.8145765 · Cited by 72 · see citing works

Redox Regulation of Ap-1

Xanthoudakis, S., & Curran, T. (1996) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4757-9480-9_10 · Cited by 63 · see citing works

Comprehensive Analysis of Proteins Which Interact with the Antioxidant Responsive Element: Correlation of ARE-BP-1 with the Chemoprotective Induction Response

Wasserman, W. W., & Fahl, W. E. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0215 · Cited by 62 · see citing works

Interaction between the Ah receptor and proteins binding to the AP-1-like electrophile response element (EpRE) during murine phase II [Ah] battery gene expression

Vasiliou, V., Puga, A., Chang, C., Tabor, M. W., & Nebert, D. W. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)02108-6 · Cited by 60 · see citing works

Coactivator MBF1 preserves the redox‐dependent AP‐1 activity during oxidative stress in Drosophila

Jindra, M., Gažiová, I., Uhlířová, M., Okabe, M., Hiromi, Y., & Hirose, S. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600356 · Cited by 58 · see citing works

Regulation of Two JunD Isoforms by Jun N-terminal Kinases

Yazgan, O., & Pfarr, C. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204552200 · Cited by 56 · see citing works

FER-1, an Enhancer of the Ferritin H Gene and a Target of E1A-Mediated Transcriptional Repression

Tsuji, Y., Akebi, N., Lam, T. K., Nakabeppu, Y., Torti, S. V., & Torti, F. M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.9.5152 · Cited by 54 · see citing works

Ferritin synthesis in differentiating Friend erythroleukemic cells.

Beaumont, C., Jain, S. K., Bogard, M., NORDMANN, Y., & Drysdale, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61008-7 · Cited by 53 · see citing works

Differential Phosphorylation of c-Jun and JunD in Response to the Epidermal Growth Factor Is Determined by the Structure of MAPK Targeting Sequences

Vinciguerra, M., Vivacqua, A., Fasanella, G., Gallo, A., Cuozzo, C., Morano, A., Maggiolini, M., & Musti, A. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308721200 · Cited by 51 · see citing works

Targeting mRNA to regulate iron and oxygen metabolism

Theil, E. C. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00300-7 · Cited by 45 · see citing works

The Rat Liver Glutathione S-Transferase Ya Subunit Gene: Characterization of the Binding Properties of a Nuclear Protein from HepG2 Cells That Has High Affinity for the Antioxidant Response Element

Liu, S., & Pickett, C. B. (1996) · Biochemistry · doi:10.1021/bi960572p · Cited by 43 · see citing works

Regulatory Mechanisms Involved in Activator‐Protein‐1 (AP‐1)‐Mediated Activation of Glutathione‐S‐Transferase Gene Expression by Chemical Agents

Ainbinder, E., Bergelson, S., Pinkus, R., & Daniel, V. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.0049a.x · Cited by 43 · see citing works

A Common Mechanism Underlying the E1A Repression and the cAMP Stimulation of the H Ferritin Transcription

Bevilacqua, M. A., Faniello, M. C., Quaresima, B., Tiano, M. T., Giuliano, P., Feliciello, A., Avvedimento, V. E., Cimino, F., & Costanzo, F. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20736 · Cited by 39 · see citing works

Transcriptional Regulation of the Mouse Ferritin H Gene

Tsuji, Y., Moran, E., Torti, S. V., & Torti, F. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.7501 · Cited by 37 · see citing works

Adenovirus E1A blocks oxidant‐dependent ferritin induction and sensitizes cells to pro‐oxidant cytotoxicity

Orino, K., Tsuji, Y., Torti, F. M., & Torti, S. V. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01443-x · Cited by 36 · see citing works

Mouse ferritin H subunit gene. Functional analysis of the promoter and identification of an upstream regulatory element active in erythroid cells.

Beaumont, C., Seyhan, A., Yachou, A. K., Grandchamp, B., & Jones, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31988-9 · Cited by 33 · see citing works

Regulation of Antioxidant Response Element–Dependent Induction of Detoxifying Enzyme Synthesis

Jaiswal, A. K. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)78018-0 · Cited by 33 · see citing works

P/CAF/p300 complex binds the promoter for the heavy subunit of ferritin and contributes to its tissue-specific expression

Bevilacqua, M. A., Faniello, M. C., Russo, T., Cimino, F., & Costanzo, F. S. (1998) · Biochemical Journal · doi:10.1042/bj3350521 · Cited by 22 · see citing works

Structure and Expression of Ferritin Genes in a Human Promyelocytic Cell Line That Differentiates in Vitro

Chou, C., Gatti, R. A., Fuller, M. L., et al. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.2.566-573.1986 · Cited by 20 · see citing works

Augmentation by IL-1 alpha of tumor necrosis factor-alpha cytotoxicity in cells transfected with adenovirus E1A

Tsuji, Y., Ninomiya‐Tsuji, J., Torti, S. V., & Torti, F. M. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.150.5.1897 · Cited by 13 · see citing works

Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling

Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373 · see citing works

The cytoprotective role of the Keap1–Nrf2 pathway

Baird, L., & Dinkova‐Kostova, A. T. (2011) · Archives of Toxicology · doi:10.1007/s00204-011-0674-5 · Cited by 1,029 · see citing works

Ferritins: A family of molecules for iron storage, antioxidation and more

Arosio, P., Ingrassia, R., & Cavadini, P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.004 · Cited by 886 · 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

Identification of novel NRF2-regulated genes by ChIP-Seq: influence on retinoid X receptor alpha

Chorley, B. N., Campbell, M. R., Wang, X., Karaca, M., Sambandan, D., Bangura, F., Xue, P., Pi, J., Kleeberger, S. R., & Bell, D. A. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks409 · Cited by 557 · 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

Intracellular iron transport and storage: from molecular mechanisms to health implications

Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526 · see citing works

Antioxidant response elements: Discovery, classes, regulation and potential applications

Raghunath, A., Sundarraj, K., Raju, N., Arfuso, F., Bian, J., Kumar, A. P., Sethi, G., & Perumal, E. (2018) · Redox Biology · doi:10.1016/j.redox.2018.05.002 · Cited by 470 · see citing works

Tumor and its microenvironment: A synergistic interplay

Catalano, V., Turdo, A., Franco, S. D., Dieli, F., Todaro, M., & Stassi, G. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.08.007 · Cited by 436 · see citing works

Redox control of inflammation in macrophages

Brüne, B., Dehne, N., Grossmann, N., Jung, M., Namgaladze, D., Schmid, T., von Knethen, A., & Weigert, A. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4785 · Cited by 377 · see citing works

Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage

Arosio, P., & Levi, S. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.02.005 · Cited by 320 · see citing works

Generation of a Stable Antioxidant Response Element–Driven Reporter Gene Cell Line and Its Use to Show Redox-Dependent Activation of Nrf2 by Cancer Chemotherapeutic Agents

Wang, X. J., Hayes, J. D., & Wolf, C. R. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-2298 · Cited by 317 · see citing works

Emerging Role of Nrf2 in Protecting Against Hepatic and Gastrointestinal Disease

Aleksunes, L. M., & Manautou, J. E. (2007) · Toxicologic Pathology · doi:10.1080/01926230701311344 · Cited by 285 · see citing works

Oxidative Stress and the Homeodynamics of Iron Metabolism

Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247 · see citing works

Molecular mechanism of endothelial and vascular aging: implications for cardiovascular disease

Camici, G. G., Savarese, G., Akhmedov, A., & Lüscher, T. F. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv587 · Cited by 223 · see citing works

Multiple regulations of Keap1/Nrf2 system by dietary phytochemicals

Qin, S., & Hou, D. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201501017 · Cited by 190 · see citing works

Chronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients

Gruosso, T., Mieulet, V., Cardon, M., Bourachot, B., Kieffer, Y., Devun, F., Dubois, T., Dutreix, M., Vincent‐Salomon, A., Miller, K. M., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505891 · Cited by 179 · see citing works

Multiple facets of junD gene expression are atypical among AP-1 family members

Hernandez, J. M., Floyd, D. H., Weilbaecher, K. N., Green, P. L., & Boris‐Lawrie, K. (2008) · Oncogene · doi:10.1038/onc.2008.120 · Cited by 139 · see citing works

Transcriptional profiling of MnSOD-mediated lifespan extension in Drosophilareveals a species-general network of aging and metabolic genes

Curtis, C. N., Landis, G. N., Folk, D. G., Wehr, N. B., Hoe, N., Waskar, M., Abdueva, D. A., Skvortsov, D., Ford, D., Luu, A., et al. (2007) · Genome biology · doi:10.1186/gb-2007-8-12-r262 · Cited by 135 · see citing works

NRF2 Oxidative Stress Induced by Heavy Metals is Cell Type Dependent

Simmons, S. O., Fan, C., Yeoman, K., Wakefield, J., & Ramabhadran, R. (2011) · Current Chemical Genomics · doi:10.2174/1875397301105010001 · Cited by 117 · see citing works

Hemin-Mediated Regulation of an Antioxidant-Responsive Element of the Human Ferritin H Gene and Role of Ref-1 during Erythroid Differentiation of K562 Cells

Iwasaki, K., MacKenzie, E. L., Hailemariam, K., Sakamoto, K., & Tsuji, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2845-2856.2006 · Cited by 112 · see citing works

Mobilization of Stored Iron in Mammals: A Review

Linder, M. C. (2013) · Nutrients · doi:10.3390/nu5104022 · Cited by 111 · see citing works

Regulation of iron pathways in response to hypoxia

Chepelev, N. L., & Willmore, W. G. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.023 · Cited by 102 · see citing works

Vascular ageing: Underlying mechanisms and clinical implications

Laina, A., Stellos, K., & Stamatelopoulos, K. S. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.06.007 · Cited by 103 · see citing works

The iron-regulatory hormone hepcidin: A possible therapeutic target?

Rochette, L., Gudjoncik, A., Guénancia, C., Zeller, M., Cottin, Y., & Vergely, C. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.09.004 · Cited by 99 · see citing works

The NRF2/KEAP1 Axis in the Regulation of Tumor Metabolism: Mechanisms and Therapeutic Perspectives

Panieri, E., Telkoparan‐Akillilar, P., Süzen, S., & Saso, L. (2020) · Biomolecules · doi:10.3390/biom10050791 · Cited by 96 · see citing works

Nuclear Factor Erythroid 2-Related Factor 2 in Regulating Cancer Metabolism

Smolková, K., Mikó, E., Kovàcs, T., Leguina‐Ruzzi, A., Sipos, A., & Bai, P. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8024 · Cited by 96 · see citing works

Sulforaphane Protects Rodent Retinas against Ischemia-Reperfusion Injury through the Activation of the Nrf2/HO-1 Antioxidant Pathway

Pan, H., He, M., Liu, R., Brecha, N. C., Yu, A. C., & Pu, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114186 · Cited by 94 · see citing works

Role of the Tumor Suppressor PTEN in Antioxidant Responsive Element-mediated Transcription and Associated Histone Modifications

Sakamoto, K., Iwasaki, K., Sugiyama, H., & Tsuji, Y. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0762 · Cited by 92 · see citing works

Decoding the endometrial niche of Asherman’s Syndrome at single-cell resolution

Santamaría, X., Rosón, B., Pérez-Moraga, R., Venkatesan, N., Pardo‐Figuerez, M., González-Fernández, J., Llera-Oyola, J., Fernández, E., Moreno, I., Salumets, A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41656-1 · Cited by 86 · see citing works

The Antioxidant Response Element and Oxidative Stress Modifiers in Airway Diseases

Reddy, S. P. (2008) · Current Molecular Medicine · doi:10.2174/156652408785160925 · Cited by 84 · see citing works

JunD Represses Transcription and Translation of the Tight Junction Protein Zona Occludens-1 Modulating Intestinal Epithelial Barrier Function

Chen, J., Xiao, L., Rao, J. N., Zou, T., Liu, L., Bellavance, E. C., Gorospe, M., & Wang, J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0175 · Cited by 80 · see citing works

Evidence for a Role of Oxidative Stress in the Carcinogenicity of Ochratoxin A

Marin‐Kuan, M., Ehrlich, V. A., Delatour, T., Cavin, C., & Schilter, B. (2011) · Journal of Toxicology · doi:10.1155/2011/645361 · Cited by 76 · see citing works

Discovery of the gene signature for acute lung injury in patients with sepsis

Howrylak, J. A., Dolinay, T., Lucht, L. A., Wang, Z., Christiani, D. C., Sethi, J. M., Xing, E. P., Donahoe, M. P., & Choi, A. M. K. (2009) · Physiological Genomics · doi:10.1152/physiolgenomics.90275.2008 · Cited by 74 · see citing works

Polyamines Regulate the Stability of JunD mRNA by Modulating the Competitive Binding of Its 3′ Untranslated Region to HuR and AUF1

Zou, T., Rao, J. N., Liu, L., Xiao, L., Yu, T., Jiang, P., Gorospe, M., & Wang, J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00807-10 · Cited by 74 · see citing works

A novel view of ferritin in cancer

Pandya, B., & Connor, J. R. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188917 · Cited by 72 · see citing works

Perturbation of Iron Metabolism by Cisplatin through Inhibition of Iron Regulatory Protein 2

Miyazawa, M., Bogdan, A. R., & Tsuji, Y. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.10.009 · Cited by 70 · see citing works

Iron homeostasis: new players, newer insights

Edison, E. S., Bajel, A. R., & Chandy, M. (2008) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2008.01143.x · Cited by 67 · see citing works

Ferritin heavy chain mediates the protective effect of heme oxygenase-1 against oxidative stress

Cheng, H., Yen, C., Chang, C.-C., Huang, K.-T., Chen, K.-H., Zhang, R.-Y., Lee, P.-Y., Miaw, S., Huang, J., Chiang, C., et al. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.09.018 · Cited by 62 · see citing works

TGF-β–Activated Kinase 1 Signaling Maintains Intestinal Integrity by Preventing Accumulation of Reactive Oxygen Species in the Intestinal Epithelium

Kajino‐Sakamoto, R., Omori, E., Nighot, P. K., Blikslager, A. T., Matsumoto, K., & Ninomiya‐Tsuji, J. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903587 · Cited by 58 · see citing works

Epigenetic Control of Cytomegalovirus Latency and Reactivation

Liu, X.-F., Wang, X., Yan, S., Zhang, Z., Abecassis, M. M., & Hummel, M. (2013) · Viruses · doi:10.3390/v5051325 · Cited by 57 · see citing works

Epithelial transforming growth factor β-activated kinase 1 (TAK1) is activated through two independent mechanisms and regulates reactive oxygen species

Omori, E., Inagaki, M., Mishina, Y. M., Matsumoto, K., & Ninomiya‐Tsuji, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116188109 · Cited by 55 · see citing works

Transcription Factors Bind Negatively Selected Sites within Human mtDNA Genes

Blumberg, A., Sailaja, B. S., Kundaje, A. B., Levin, L., Dadon, S., Shmorak, S., Shaulian, E., Meshorer, E., & Mishmar, D. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu210 · Cited by 55 · see citing works

The Antioxidant/electrophile Response Element Motif

Nerland, D. E. (2007) · Drug Metabolism Reviews · doi:10.1080/03602530601125000 · Cited by 55 · see citing works

Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress

Mackenzie, E. L., Ray, P. D., & Tsuji, Y. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.031 · Cited by 53 · see citing works

Transcriptional regulation of the human ferritin gene by coordinated regulation of Nrf2 and protein arginine methyltransferases PRMT1 and PRMT4

Huang, B., Ray, P. D., Iwasaki, K., & Tsuji, Y. (2013) · The FASEB Journal · doi:10.1096/fj.12-226043 · Cited by 52 · see citing works

Induced JunD in intestinal epithelial cells represses CDK4 transcription through its proximal promoter region following polyamine depletion

Xiao, L., Rao, J. N., Zou, T., Liu, L., Marasa, B. S., Chen, J., Turner, D. J., Passaniti, A., & Wang, J. (2007) · Biochemical Journal · doi:10.1042/bj20061436 · Cited by 50 · see citing works

JunD mediates androgen‐induced oxidative stress in androgen dependent LNCaP human prostate cancer cells

Mehraein‐Ghomi, F., Lee, E., Church, D. R., Thompson, T. A., Basu, H. S., & Wilding, G. (2008) · The Prostate · doi:10.1002/pros.20737 · Cited by 48 · see citing works

Role of extracellular Hydrogen peroxide in regulation of iron homeostasis genes in neuronal cells: Implication in iron accumulation

Dev, S., Kumari, S., Singh, N., Bal, S. K., Seth, P., & Mukhopadhyay, C. K. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.025 · Cited by 46 · see citing works

Ferritin couples iron and fatty acid metabolism

Bu, W., Liu, R., Cheung‐Lau, J. C., Dmochowski, I. J., Loll, P. J., & Eckenhoff, R. G. (2012) · The FASEB Journal · doi:10.1096/fj.11-198853 · Cited by 46 · see citing works

Distinct regulatory mechanisms of the human ferritin gene by hypoxia and hypoxia mimetic cobalt chloride at the transcriptional and post-transcriptional levels

Huang, B., Miyazawa, M., & Tsuji, Y. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.08.018 · Cited by 45 · see citing works

The good Samaritan glutathione-S-transferase P1: An evolving relationship in nitric oxide metabolism mediated by the direct interactions between multiple effector molecules

Russell, T. M., & Richardson, D. R. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102568 · Cited by 43 · see citing works

PIAS3 Interacts with ATF1 and Regulates the Human Ferritin H Gene through an Antioxidant-responsive Element

Iwasaki, K., Hailemariam, K., & Tsuji, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701477200 · Cited by 41 · see citing works

Transcriptional regulation of ferritin and antioxidant genes by HIPK2 under genotoxic stress

Hailemariam, K., Iwasaki, K., Huang, B., Sakamoto, K., & Tsuji, Y. (2010) · Journal of Cell Science · doi:10.1242/jcs.073627 · Cited by 38 · see citing works

Evidence for a novel antioxidant function and isoform-specific regulation of the human p66Shc gene

Miyazawa, M., & Tsuji, Y. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-11-0666 · Cited by 36 · see citing works

Androgen Receptor Requires JunD as a Coactivator to Switch on an Oxidative Stress Generation Pathway in Prostate Cancer Cells

Mehraein‐Ghomi, F., Basu, H. S., Church, D. R., Hoffmann, F. M., & Wilding, G. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3596 · Cited by 35 · see citing works

Significance of HLA class I antibody-induced antioxidant gene expression for endothelial cell protection against complement attack

Iwasaki, K., Miwa, Y., Haneda, M., Uchida, K., Nakao, A., & Kobayashi, T. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.042 · Cited by 33 · see citing works

Expression of MRP1 and GSTP1-1 modulate the acute cellular response to treatment with the chemopreventive isothiocyanate, sulforaphane

Sibhatu, M. B., Smitherman, P. K., Townsend, A. J., & Morrow, C. S. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn013 · Cited by 32 · see citing works

Proteomic mining in the dysplastic liver of WHV/c‐ myc mice – insights and indicators for early hepatocarcinogenesis

Liu, Y., Li, C., Xing, Z., Yuan, X., Wu, Y. C., Xu, M., Tu, K., Li, Q., Wu, C., Zhao, M., et al. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07795.x · Cited by 31 · see citing works

Three ferritin subunits involved in immune defense from bay scallop Argopecten irradians

Li, J., Li, L., Zhang, S., Li, J., & Zhang, G. (2011) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2011.10.030 · Cited by 31 · see citing works

Multiple functions of the histone chaperone Jun dimerization protein 2

Tsai, M.-H., Wuputra, K., Lin, Y., Lin, C., & Yokoyama, K. K. (2016) · Gene · doi:10.1016/j.gene.2016.03.048 · Cited by 30 · see citing works

Role of AMP-Activated Protein Kinase in Ferritin H Gene Expression by Resveratrol in Human T Cells

Iwasaki, K., Ray, P. D., Huang, B., Sakamoto, K., Kobayashi, T., & Tsuji, Y. (2013) · Biochemistry · doi:10.1021/bi400399f · Cited by 28 · see citing works

Transcriptomic and Histopathological Effects of Bifenthrin to the Brain of Juvenile Rainbow Trout (Oncorhynchus mykiss)

Magnuson, J. T., Hartz, K. E. H., Fulton, C. A., Lydy, M. J., & Schlenk, D. (2021) · Toxics · doi:10.3390/toxics9030048 · Cited by 27 · see citing works

JunD enhances miR-29b levels transcriptionally and posttranscriptionally to inhibit proliferation of intestinal epithelial cells

Zou, T., Rao, J. N., Liu, L., Xiao, L., Chung, H. K., Li, Y., Chen, G., Gorospe, M., & Wang, J. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00027.2015 · Cited by 25 · see citing works

Proteomic analyses of monocyte-derived macrophages infected with human immunodeficiency virus type 1 primary isolates from Hispanic women with and without cognitive impairment

Toro-Nieves, D., Rodriguez, Y., Plaud, M., Ciborowski, P. S., Duan, F., Laspiur, J. P., Wojna, V., & Melendez, L. M. (2009) · Journal of NeuroVirology · doi:10.1080/13550280802385505 · Cited by 24 · see citing works

Optimization of Biotinylated RNA or DNA Pull-Down Assays for Detection of Binding Proteins: Examples of IRP1, IRP2, HuR, AUF1, and Nrf2

Tsuji, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043604 · Cited by 22 · see citing works

Ferritin as an Effective Prognostic Factor and Potential Cancer Biomarker

Szymulewska-Konopko, K., Reszeć-Giełażyn, J., & Małeczek, M. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47010060 · Cited by 20 · see citing works

Cytoprotective responses in HaCaT keratinocytes exposed to high doses of curcumin

Lundvig, D. M. S., Pennings, S. W. C., Brouwer, K. M., Mtaya, M., Mugonzibwa, E. A., Kuijpers‐Jagtman, A. M., Wagener, F. A. D. T. G., & den Hoff, J. W. V. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.06.002 · Cited by 19 · see citing works

Update on Acute Lung Injury and Critical Care Medicine 2009

Matthay, M. A., & Idell, S. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201001-0074up · Cited by 18 · see citing works

Alternative ferritin mRNA translation via internal initiation

Daba, A., Koromilas, A. E., & Pantopoulos, K. (2012) · RNA · doi:10.1261/rna.029322.111 · Cited by 17 · see citing works

Aldo-keto reductase 1 family B7 is the gene induced in response to oxidative stress in the livers of Long-Evans Cinnamon rats

Jia, G., Takahashi, R., Zhang, Z., Tsuji, Y., & Sone, H. (2006) · International Journal of Oncology · doi:10.3892/ijo.29.4.829 · Cited by 17 · see citing works

Hypoxia induced changes in expression of proteins involved in iron uptake and storage in cultured lens epithelial cells

Goralska, M., Fleisher, L. N., & McGahan, M. C. (2014) · Experimental Eye Research · doi:10.1016/j.exer.2014.05.010 · Cited by 17 · see citing works

Induction of Glutathione Synthesis Explains Pharmacodynamics of High-Dose Busulfan in Mice and Highlights Putative Mechanisms of Drug Interaction

Bouligand, J., Deroussent, A., Simonnard, N., Opolon, P., Morizet, J., Connault, E., Daudigeos‐Dubus, E., Ré, M., Paci, A., & Vassal, G. (2006) · Drug Metabolism and Disposition · doi:10.1124/dmd.106.012880 · Cited by 17 · see citing works

Transplant-induced reactivation of murine cytomegalovirus immediate early gene expression is associated with recruitment of NF-κB and AP-1 to the major immediate early promoter

Liu, X.-F., Jie, C., Zhang, Z., Yan, S., Wang, J.-J., Wang, X., Kurian, S. M., Salomon, D. R., Abecassis, M. M., & Hummel, M. (2016) · Journal of General Virology · doi:10.1099/jgv.0.000407 · Cited by 17 · see citing works

The Role of Vascular Aging in Atherosclerotic Plaque Development and Vulnerability

Liberale, L., & Camici, G. G. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190830175424 · Cited by 17 · see citing works

Differential gene expression in rainbow trout (Oncorhynchus mykiss) liver and ovary after exposure to zearalenone

Woźny, M., Brzuzan, P., Wolińska‐Nizioł, L., Góra, M., & Łuczyński, M. K. (2012) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2012.05.005 · Cited by 16 · see citing works

Activator Protein-1 Regulation of Murine Aldehyde Dehydrogenase 1a1

Makia, N. L., Amunom, I., Falkner, K. C., Conklin, D. J., Surapureddi, S., Goldstein, J. A., & Prough, R. A. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.078147 · Cited by 16 · see citing works

Cadmium increases ferroportin-1 gene expression in J774 macrophage cells via the production of reactive oxygen species

Park, B.-Y., & Chung, J. (2009) · Nutrition Research and Practice · doi:10.4162/nrp.2009.3.3.192 · Cited by 16 · see citing works

Solving the Problem of Assessing Synergy and Antagonism for Non-Traditional Dosing Curve Compounds Using the DE/ZI Method: Application to Nrf2 Activators

Repash, E. M., Pensabene, K. M., Palenchar, P. M., & Eggler, A. L. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.686201 · Cited by 15 · see citing works

Oxidative status interactome map: towards novel approaches in experiment planning, data analysis, diagnostics and therapy

Zolotukhin, P. V., Kozlova, Y., Dovzhik, A. D., Коваленко, К. А., Kutsyn, K., Александрова, А. А., & Shkurat, T. P. (2013) · Molecular BioSystems · doi:10.1039/c3mb70096h · Cited by 15 · see citing works

Cord blood genomic analysis highlights the role of redox balance

Maron, J. L., Johnson, K. L., Parkin, C. D., Iyer, L., Davis, J. M., & Bianchi, D. W. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.026 · Cited by 14 · see citing works

Regulation of Human CYP2C9 Expression by Electrophilic Stress Involves Activator Protein 1 Activation and DNA Looping

Makia, N. L., Surapureddi, S., Monostory, K., Prough, R. A., & Goldstein, J. A. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.092585 · Cited by 14 · see citing works

Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization

Mackenzie, E. L., & Tsuji, Y. (2008) · Biochemical Journal · doi:10.1042/bj20071544 · Cited by 13 · see citing works

Regulation of Neuronal Ferritin Heavy Chain, A New Player in Opiate-Induced Chemokine Dysfunction

Abt, A., & Meucci, O. (2011) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-011-9278-3 · Cited by 13 · see citing works

Ferritin Heavy Chain (FHC) is Up-regulated in Papillomavirus-Associated Urothelial Tumours of the Urinary Bladder in Cattle

Roperto, S., Borzacchiello, G., Brun, R., Costanzo, F. S., Faniello, M. C., Raso, C. A., Rosati, A., Russo, V., Leonardi, L., Saracino, D., et al. (2009) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2009.05.009 · Cited by 13 · see citing works

Ferritin Genes Overexpression in PBMC and a Rise in Exercise Performance as an Adaptive Response to Ischaemic Preconditioning in Young Men

Mieszkowski, J., Kochanowicz, M., Żychowska, M., Kochanowicz, A., Grzybkowska, A., Anczykowska, K., Sawicki, P., Borkowska, A., Niespodziński, B., & Antosiewicz, J. (2019) · BioMed Research International · doi:10.1155/2019/9576876 · Cited by 11 · see citing works

Nuclear lamins and progerin are dispensable for antioxidant Nrf2 response to arsenic and cadmium

Hashimoto, K., Majumdar, R., & Tsuji, Y. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.02.012 · Cited by 10 · see citing works

An iron metabolism and immune related gene signature for the prediction of clinical outcome and molecular characteristics of triple-negative breast cancer

Li, X., Fu, W., Zhang, J., & Song, C. (2022) · BMC Cancer · doi:10.1186/s12885-022-09679-x · Cited by 9 · see citing works

Interferon-Inducible Stat2 Activation of JUND and CLDN4: Mediators of IFN Responses

Jia, D., Rahbar, R., & Fish, E. N. (2007) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2007.0014 · Cited by 9 · see citing works

Effects of Oxidative Stress Caused by tert-Butylhydroquinone on Cytotoxicity in MDCK Cells

Shibuya, N., Kobayashi, S., Yoshikawa, Y., Watanabe, K., & Orino, K. (2011) · Journal of Veterinary Medical Science · doi:10.1292/jvms.11-0412 · Cited by 9 · see citing works

Immunological function and antibacterial activity of two ferritin proteins from the freshwater pearl mussel Hyriopsis schlegelii

Sheng, J., Shu, Q. C., Shi, J., Wang, J. H., Peng, K., Yuan, S., & Hong, Y. (2016) · Genetics and Molecular Research · doi:10.4238/gmr.15038533 · Cited by 9 · see citing works

The Effect of tert-Butylhydroquinone-Induced Oxidative Stress in MDBK Cells using XTT Assay: Implication of tert-Butylhydroquinone-Induced NADPH Generating Enzymes

Tomoo, N. A. O. I., Shibuya, N., INOUE, H., Mita, S., Kobayashi, S., Watanabe, K., & Orino, K. (2010) · Journal of Veterinary Medical Science · doi:10.1292/jvms.09-0346 · Cited by 9 · see citing works

Evolution of the ferritin family in vertebrates

Lee, J.-H., Wan, K., Mohd-Adnan, A., & Gabaldón, T. (2012) · Trends in Evolutionary Biology · doi:10.4081/eb.2012.e3 · Cited by 9 · see citing works

REVIEW PAPER Do changes in iron metabolism contribute to the acceleration of the atherosclerosis process?

Formanowicz, D. (2014) · Biotechnologia · doi:10.5114/bta.2011.46533 · Cited by 8 · see citing works

JunD/AP-1 Antagonizes the Induction ofDAPK1To Promote the Survival of v-Src-Transformed Cells

Maślikowski, B. M., Wang, L., Wu, Y., Fielding, B. D., & Bédard, P. (2016) · Journal of Virology · doi:10.1128/jvi.01925-16 · Cited by 8 · see citing works

Liver iron overload induced by tamoxifen in diabetic and non-diabetic female Wistar rats

Jatobá, C. A. N., de Rezende, A. A., Rodrigues, S. J. D. P., Câmara, M. M. D. A., Almeida, M. D. G., Freire‐Neto, F. P., da Rocha, L. R. M., Medeiros, A. C., Brandão‐Neto, J., Formiga, M. C. D. C., et al. (2007) · BioMetals · doi:10.1007/s10534-007-9105-8 · Cited by 8 · see citing works

Comparative analysis on the immunoregulatory roles of ferritin M in hybrid fish (Carassius cuvieri ♀ × Carassius auratus red var ♂) and its parental species after bacterial infection

Xiong, N., Huang, J., Li, K.-X., Li, S., Zhao, J.-H., Wang, R., Ou, J., Fan, L., Luo, S., & Liu, S. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.05.039 · Cited by 7 · see citing works

Ferritin from the Pacific abalone Haliotis discus hannai: Analysis of cDNA sequence, expression, and activity

Qiu, R., Kan, Y., & Li, D. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.12.048 · Cited by 7 · see citing works

Nuclear Factor Kappa B Promotes Ferritin Heavy Chain Expression in Bombyx mori in Response to B. mori Nucleopolyhedrovirus Infection

Zhu, L., Liu, Y., Wang, A., Chen, X., Zhu, H.-D., Huang, Z., Cao, H., Liu, S., & Xu, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810380 · Cited by 6 · see citing works

Effects of JUN and NFE2L2 knockdown on oxidative status and NFE2L2/AP-1 targets expression in HeLa cells in basal conditions and upon sub-lethal hydrogen peroxide treatment

Belanova, A. A., Chmykhalo, V. K., Makarenko, M., Lyangasova, O. V., Belousova, M. M., Александрова, А. А., & Zolotukhin, P. V. (2018) · Molecular Biology Reports · doi:10.1007/s11033-018-4412-4 · Cited by 6 · see citing works

Hemin-Mediated Regulation of an Antioxidant-Responsive Element of the Human Ferritin H Gene and Role of Ref-1 during Erythroid Differentiation of K562 Cells

Iwasaki, K., MacKenzie, E. L., Hailemariam, K., Sakamoto, K., & Tsuji, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2845-2856.2006 · Cited by 112 · see citing works

Coordinate Transcriptional and Translational Regulation of Ferritin in Response to Oxidative Stress

Tsuji, Y., Ayaki, H., Whitman, S. P., Morrow, C. S., Torti, S. V., & Torti, F. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5818-5827.2000 · Cited by 285 · see citing works

Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress

Mackenzie, E. L., Ray, P. D., & Tsuji, Y. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.031 · Cited by 53 · see citing works

Nrf2 Mediates the Induction of Ferritin H in Response to Xenobiotics and Cancer Chemopreventive Dithiolethiones

Pietsch, E. C., Chan, J. Y., Torti, F. M., & Torti, S. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210664200 · Cited by 284 · see citing works

Adenovirus E1A blocks oxidant‐dependent ferritin induction and sensitizes cells to pro‐oxidant cytotoxicity

Orino, K., Tsuji, Y., Torti, F. M., & Torti, S. V. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01443-x · Cited by 36 · see citing works