Cited by 267Selenium in Biological SystemsOrganoselenium and organotellurium chemistryRedox biology and oxidative stress

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Role of Selenoproteins in Redox Regulation of Signaling and the Antioxidant System: A Review

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Zhang, Ying, Roh, Yeon Jin, Han, Seong-Jeong, Park, Iha, Lee, Hae Min, Ok, Yong Sik, Lee, Byung Cheon, Lee, Seung-Rock·2020·Antioxidants

DOI 10.3390/antiox9050383PMC PMC7278666

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Abstract

Selenium is a vital trace element present as selenocysteine (Sec) in proteins that are, thus, known as selenoproteins. Humans have 25 selenoproteins, most of which are functionally characterized as oxidoreductases, where the Sec residue plays a catalytic role in redox regulation and antioxidant activity. Glutathione peroxidase plays a pivotal role in scavenging and inactivating hydrogen and lipid peroxides, whereas thioredoxin reductase reduces oxidized thioredoxins as well as non-disulfide substrates, such as lipid hydroperoxides and hydrogen peroxide. Selenoprotein R protects the cell against oxidative damage by reducing methionine-R-sulfoxide back to methionine. Selenoprotein O regulates redox homeostasis with catalytic activity of protein AMPylation. Moreover, endoplasmic reticulum (ER) membrane selenoproteins (SelI, K, N, S, and Sel15) are involved in ER membrane stress regulation. Selenoproteins containing the CXXU motif (SelH, M, T, V, and W) are putative oxidoreductases that participate in various cellular processes depending on redox regulation. Herein, we review the recent studies on the role of selenoproteins in redox regulation and their physiological functions in humans, as well as their role in various diseases.

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Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269
Aging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695
Free radicals, metals and antioxidants in oxidative stress-induced cancer
Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680
Reactive oxygen species, antioxidants, and the mammalian thioredoxin system1 1This review is based on the licentiate thesis “Thioredoxin reductase—interactions with the redox active compounds 1-chloro-2,4-dinitrobenzene and lipoic acid” by Jonas Nordberg, 2001, Karolinska Institute, Stockholm, ISBN 91-631-1064-4.
Nordberg, J., & Arnér, E. S. J. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00724-9 · Cited by 2,720
Physiological functions of thioredoxin and thioredoxin reductase
Arnér, E. S. J., & Holmgren, A. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01701.x · Cited by 2,535
Characterization of Mammalian Selenoproteomes
Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigó, R., & Gladyshev, V. N. (2003) · Science · doi:10.1126/science.1083516 · Cited by 2,385
Oxidative stress in Parkinson's disease
Jenner, P. (2003) · Annals of Neurology · doi:10.1002/ana.10483 · Cited by 2,053
Biomarkers of Oxidative Damage in Human Disease
Dalle-Donne, I., Rossi, R., Colombo, R., Giustarini, D., & Milzani, A. (2006) · Clinical Chemistry · doi:10.1373/clinchem.2005.061408 · Cited by 1,703
Selenium Utilization by GPX4 Is Required to Prevent Hydroperoxide-Induced Ferroptosis
Ingold, I., Berndt, C., Schmitt, S., Doll, S. G., Poschmann, G., Buday, K., Roveri, A., Peng, X., Freitas, F. P., Seibt, T., et al. (2017) · Cell · doi:10.1016/j.cell.2017.11.048 · Cited by 1,701
Role of oxidative stress in cardiovascular diseases
Dhalla, N. S., Temsah, R. M., & Netticadan, T. (2000) · Journal of Hypertension · doi:10.1097/00004872-200018060-00002 · Cited by 1,467
From Selenium to Selenoproteins: Synthesis, Identity, and Their Role in Human Health
Papp, L. V., Lu, J., Holmgren, A., & Khanna, K. K. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1528 · Cited by 1,357
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061
Self-citation
Selenium, Selenoproteins, and Immunity
Avery, J., & Hoffmann, P. R. (2018) · Nutrients · doi:10.3390/nu10091203 · Cited by 948
Ablation of ferroptosis regulator glutathione peroxidase 4 in forebrain neurons promotes cognitive impairment and neurodegeneration
Hambright, W. S., Fonseca, R. S., Chen, L., Na, R., & Ran, Q. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.021 · Cited by 851
Thioredoxin reductase
Mustacich, D. J., & Powis, G. (2000) · Biochemical Journal · doi:10.1042/bj3460001 · Cited by 838
Selenium biochemistry and its role for human health
Roman, M., Jitaru, P., & Barbante, C. (2014) · Metallomics · doi:10.1039/c3mt00185g · Cited by 823
Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions
Arnér, E. S. J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.01.014 · Cited by 696
How Selenium Has Altered Our Understanding of the Genetic Code
Hatfield, D. L., & Gladyshev, V. N. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3565-3576.2002 · Cited by 681
T cell lipid peroxidation induces ferroptosis and prevents immunity to infection
Matsushita, M., Freigang, S., Schneider, C., Conrad, M., Bornkamm, G. W., & Kopf, M. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20140857 · Cited by 672 · cited 1×
“It has also been reported that GPx dysfunction is associated with the incidence of various types of cancer [40,41], muscle disorders [42], CVDs [43,44], hepatopathies [45], renal failure [46,47], neurological disorders (such as Alzheimer’s disease (AD) and Parkinson’s disease (PD)) [48–50], immune defense dysfunction…”
Background
Recognition of UGA as a selenocysteine codon in Type I deiodinase requires sequences in the 3′ untranslated region
Berry, M. J., Banu, L., Chen, Y., Mandel, S. J., Kieffer, J. D., Harney, J. W., & Larsen, P. R. (1991) · Nature · doi:10.1038/353273a0 · Cited by 652
Road to Ruin: Targeting Proteins for Degradation in the Endoplasmic Reticulum
Smith, M. H., Ploegh, H. L., & Weissman, J. S. (2011) · Science · doi:10.1126/science.1209235 · Cited by 648
Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631
Self-citation
Selenoproteins
Lu, J., & Holmgren, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800045200 · Cited by 618
Chemistry and Biochemistry of Oxidative Stress in Neurodegenerative Disease
Sayre, L. M., Smith, M. A., & Perry, G. L. (2001) · Current Medicinal Chemistry · doi:10.2174/0929867013372922 · Cited by 614
Selenoprotein P: an extracellular protein with unique physical characteristics and a role in selenium homeostasis.
Burk, R. F., & Hill, K. (2005) · Annual review of nutrition · doi:10.1146/annurev.nutr.24.012003.132120 · Cited by 591
The role of methionine on metabolism, oxidative stress, and diseases
Martínez, Y., Li, X., Liu, G., Bin, P., Yan, W., Más, D., Valdivié, M., Hu, C.-A. A., Ren, W., & Yin, Y. (2017) · Amino Acids · doi:10.1007/s00726-017-2494-2 · Cited by 583
Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
Holmgren, A., & Lu, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.083 · Cited by 577
The human selenoproteome: recent insights into functions and regulation
Reeves, M. A., & Hoffmann, P. R. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0032-4 · Cited by 540
Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide
Lu, J., Chew, E.-H., & Holmgren, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701549104 · Cited by 526
Thioredoxin Reductase Is Irreversibly Modified by Curcumin
Fang, J., Lu, J., & Holmgren, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414645200 · Cited by 521
Ablation of the Ferroptosis Inhibitor Glutathione Peroxidase 4 in Neurons Results in Rapid Motor Neuron Degeneration and Paralysis
Chen, L., Hambright, W. S., Na, R., & Ran, Q. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.680090 · Cited by 498
The role of the redox protein thioredoxin in cell growth and cancer
Powis, G., Mustacich, D. J., & Coon, A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00313-0 · Cited by 442
Selenium bioavailability: current knowledge and future research requirements
Fairweather‐Tait, S. J., Collings, R., & Hurst, R. (2010) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.28674j · Cited by 436
Essential Role of Selenium in the Catalytic Activities of Mammalian Thioredoxin Reductase Revealed by Characterization of Recombinant Enzymes with Selenocysteine Mutations
Zhong, L., & Holmgren, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000690200 · Cited by 430
The Biochemistry of the Complications of Diabetes Mellitus
Brownlee, M., & Cerami, A. (1981) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.50.070181.002125 · Cited by 416
Selenium: Significance, and outlook for supplementation
Kieliszek, M., & Błażejak, S. (2013) · Nutrition · doi:10.1016/j.nut.2012.11.012 · Cited by 393
Regulation and function of selenoproteins in human disease
Bellinger, F. P., Raman, A. V., Reeves, M. A., & Berry, M. J. (2009) · Biochemical Journal · doi:10.1042/bj20090219 · Cited by 393
Genetic variation in selenoprotein S influences inflammatory response
Curran, J. E., Jowett, J. B. M., Elliott, K., Gao, Y., Gluschenko, K., Wang, J., Azim, D. M. A., Cai, G., Mahaney, M. C., Comuzzie, A. G., et al. (2005) · Nature Genetics · doi:10.1038/ng1655 · Cited by 375
Eukaryotic selenoproteins and selenoproteomes
Lobanov, A. V., Hatfield, D. L., & Gladyshev, V. N. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.05.014 · Cited by 364
Selenocysteine in proteins—properties and biotechnological use
Johansson, L., Gafvelin, G., & Arnér, E. S. J. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.05.010 · Cited by 353
Reduction of Dehydroascorbate to Ascorbate by the Selenoenzyme Thioredoxin Reductase
May, J. M., Mendiratta, S. S., Hill, K. E., & Burk, R. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22607 · Cited by 344
Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme
Sandalova, T., Zhong, L., Lindqvist, Y., Holmgren, A., & Schneider, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171178698 · Cited by 343
On the potential of thioredoxin reductase inhibitors for cancer therapy
Urig, S., & Becker, K. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.09.004 · Cited by 338
The thioredoxin-thioredoxin reductase system: over-expression in human cancer.
Lincoln, D. T., Emadi, E. M. A., Tonissen, K. F., & Clarke, F. M. (2003) · PubMed · Cited by 337
Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene ( Trsp )
Bösl, M. R., Takaku, K., Oshima, M., Nishimura, S., & Taketo, M. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5531 · Cited by 337
Inhibition of Mammalian Thioredoxin Reductase by Some Flavonoids: Implications for Myricetin and Quercetin Anticancer Activity
Lu, J., Papp, L. V., Fang, J., Rodriguez-Nieto, S., Zhivotovsky, B., & Holmgren, A. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3310 · Cited by 326
Glutathione peroxidase 4 and vitamin E cooperatively prevent hepatocellular degeneration
Carlson, B. A., Tobe, R., Yefremova, E., Tsuji, P. A., Hoffmann, V. J., Schweizer, U., Gladyshev, V. N., Hatfield, D. L., & Conrad, M. (2016) · Redox Biology · doi:10.1016/j.redox.2016.05.003 · Cited by 316
Role of glutathione peroxidase 1 in breast cancer: loss of heterozygosity and allelic differences in the response to selenium.
Hu, Y. J., & Diamond, A. M. (2003) · PubMed · Cited by 314
Selenium in chemistry and biochemistry in comparison to sulfur
Wessjohann, L. A., Schneider, A. R., Abbas, M., & Brandt, W. (2007) · Biological Chemistry · doi:10.1515/bc.2007.138 · Cited by 308
Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia.
Berggren, M. I., Gallegos, A. C., Gasdaska, J. R., Gasdaska, P. Y., Warneke, J. A., & Powis, G. (1996) · PubMed · Cited by 306
Supplementation of Micronutrient Selenium in Metabolic Diseases: Its Role as an Antioxidant
Wang, N., Tan, H., Li, S., Xu, Y., Guo, W., & Feng, Y. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7478523 · Cited by 302
Thioredoxin reductase.
Mustacich, D. J., & Powis, G. (2000) · PubMed Central · Cited by 290
Glutathione peroxidase 4: a new player in neurodegeneration?
Cardoso, B. R., Hare, D. J., Bush, A. I., & Roberts, B. R. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.196 · Cited by 287
Oxidation Resistance of the Sulfur Amino Acids: Methionine and Cysteine
Bin, P., Huang, R., & Zhou, X. (2017) · BioMed Research International · doi:10.1155/2017/9584932 · Cited by 270
Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity
Lee, S.-R., Barnoy, S., Kwon, J., Levine, R. L., Stadtman, T. C., & Rhee, S. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.050579797 · Cited by 269
Self-citation
The CXXC Motif: A Rheostat in the Active Site
Chivers, P. T., Prehoda, K. E., & Raines, R. T. (1997) · Biochemistry · doi:10.1021/bi9628580 · Cited by 259
Novel Selenoproteins Identified in Silico andin Vivo by Using a Conserved RNA Structural Motif
Lescure, A., Gautheret, D., Carbon, P., & Krol, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38147 · Cited by 258
MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation
Lee, B. C., Péterfi, Z., Hoffmann, F. W., Moore, R. E., Kaya, A., Avanesov, A. S., Tarrago, L., Zhou, Y., Weerapana, E., Fomenko, D. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.019 · Cited by 255
Self-citation
Human selenoproteins at a glance
Gromer, S., Eubel, J., Lee, B. L., & Jacob, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5143-y · Cited by 250
Self-citation
Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non‐stoichiometric oxidation of NADPH in the presence of oxygen
Kumar, S., Björnstedt, M., & Holmgren, A. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17068.x · Cited by 248
The thioredoxin reductase/thioredoxin system: Novel redox targets for cancer therapy
Biaglow, J. E., & Miller, R. A. (2005) · Cancer Biology & Therapy · doi:10.4161/cbt.4.1.1434 · Cited by 245
Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1
Cheng, Q., Sandalova, T., Lindqvist, Y., & Arnér, E. S. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807068200 · Cited by 227
Inhibition of thioredoxin reductase but not of glutathione reductase by the major classes of alkylating and platinum-containing anticancer compounds
Witte, A.-B., Anestål, K., Jerremalm, E., Ehrsson, H., & Arnér, E. S. J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.04.025 · Cited by 225
Thioredoxin and Cancer: A Role for Thioredoxin in all States of Tumor Oxygenation
Karlenius, T., & Tonissen, K. F. (2010) · Cancers · doi:10.3390/cancers2020209 · Cited by 215
The Mammalian Cytosolic Selenoenzyme Thioredoxin Reductase Reduces Ubiquinone
Xia, L., Nordman, T., Olsson, J. M., Damdimopoulos, A. E., Björkhem‐Bergman, L., Nalvarte, I., Eriksson, L. C., Arnér, E. S. J., Spyrou, G., & Björnstedt, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210456200 · Cited by 209
Selenium status highly regulates selenoprotein mRNA levels for only a subset of the selenoproteins in the selenoproteome
Sunde, R. A., Raines, A. M., Barnes, K. M., & Evenson, J. K. (2008) · Bioscience Reports · doi:10.1042/bsr20080146 · Cited by 204
Mammalian Thioredoxin Reductase Is Irreversibly Inhibited by Dinitrohalobenzenes by Alkylation of Both the Redox Active Selenocysteine and Its Neighboring Cysteine Residue
Nordberg, J., Zhong, L., Holmgren, A., & Arnér, E. S. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.10835 · Cited by 200
Selenium and GPX4, a vital symbiosis
Angeli, J. P. F., & Conrad, M. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.001 · Cited by 197
Tumor Suppressor Function of the Plasma Glutathione Peroxidase Gpx3 in Colitis-Associated Carcinoma
Barrett, C. W., Wei, N., Chen, X., Smith, J. J., Washington, M. K., Hill, K. E., Coburn, L. A., Peek, R. M., Chaturvedi, R., Wilson, K. T., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-3150 · Cited by 196
Selenoprotein N: an endoplasmic reticulum glycoprotein with an early developmental expression pattern
Petit, N. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg115 · Cited by 193
Thioredoxin-1 binds to the C2 domain of PTEN inhibiting PTEN's lipid phosphatase activity and membrane binding: a mechanism for the functional loss of PTEN's tumor suppressor activity
Meuillet, E. J., Mahadevan, D., Berggren, M. I., Coon, A., & Powis, G. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.04.020 · Cited by 192
Protein AMPylation by an Evolutionarily Conserved Pseudokinase
Sreelatha, A., Yee, S. S., Lopez, V. A., Park, B. C., Kinch, L. N., Pilch, S., Servage, K. A., Zhang, J., Jiou, J., Karasiewicz-Urbańska, M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.08.046 · Cited by 192
Glutathione Peroxidase 3 Mediates the Antioxidant Effect of Peroxisome Proliferator-Activated Receptor γ in Human Skeletal Muscle Cells
Chung, S. S., Kim, M., Youn, B. S., Lee, N. S., Park, J. W., Lee, I. K., Lee, Y. S., Kim, J. B., Cho, Y. M., Lee, H. K., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00544-08 · Cited by 181
Self-citation
The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.
Chivers, P. T., Laboissière, M. C. A., & Raines, R. T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00626.x · Cited by 180
Crystal structure of the human thioredoxin reductase–thioredoxin complex
Fritz‐Wolf, K., Kehr, S., Stumpf, M., Rahlfs, S., & Becker, K. (2011) · Nature Communications · doi:10.1038/ncomms1382 · Cited by 173
Redox Regulation of Human Thioredoxin Network
Kondo, N., Nakamura, H., Masutani, H., & Yodoi, J. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1881 · Cited by 171
Motexafin Gadolinium, a Tumor-selective Drug Targeting Thioredoxin Reductase and Ribonucleotide Reductase
Hashemy, S. I., Ungerstedt, J. S., Avval, F. Z., & Holmgren, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511373200 · Cited by 164
Oxidative stress in SEPN1‐related myopathy: From pathophysiology to treatment
Arbogast, S., Beuvin, M., Fraysse, B., Zhou, H., Francesco Muntoni, A., & Ferreiro, A. (2009) · Annals of Neurology · doi:10.1002/ana.21644 · Cited by 161
SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics
Hung, R., Spaeth, C. S., Yesilyurt, H. G., & Terman, J. R. (2013) · Nature Cell Biology · doi:10.1038/ncb2871 · Cited by 155
Regulation of Redox Signaling by Selenoproteins
Hawkes, W. C., & Alkan, Z. (2010) · Biological Trace Element Research · doi:10.1007/s12011-010-8656-7 · Cited by 151
INCREASED RISK OF BLADDER CANCER ASSOCIATED WITH A GLUTATHIONE PEROXIDASE 1 CODON 198 VARIANT
Ichimura, Y., Habuchi, T., Tsuchiya, N., Wang, L., Oyama, C., Sato, K., Nishiyama, H., Ogawa, O., & Kato, T. (2004) · The Journal of Urology · doi:10.1097/01.ju.0000130942.40597.9d · Cited by 149
Selenoprotein T is a PACAP‐regulated gene involved in intracellular Ca 2+ mobilization and neuroendocrine secretion
Grumolato, L., Ghzili, H., Montero‐Hadjadje, M., Gasman, S., Lésage, J., Tanguy, Y., Galas, L., Aït‐Ali, D., Leprince, J., Guérineau, N. C., et al. (2008) · The FASEB Journal · doi:10.1096/fj.06-075820 · Cited by 149
The CXXC Motif Is More than a Redox Rheostat
Quan, S., Schneider, I., Pan, J. L., von Hacht, A., & Bardwell, J. C. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705291200 · Cited by 148
Loss of GPx2 increases apoptosis, mitosis, and GPx1 expression in the intestine of mice
Florian, S., Krehl, S., Löwinger, M., Kipp, A. P., Banning, A., Esworthy, R. S., Chu, F., & Brigelius‐Flohé, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.08.029 · Cited by 144
Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins
Leinweber, B. D., Leavis, P. C., Grabarek, Z., WANG, C.-L. A., & Morgan, K. G. (1999) · Biochemical Journal · doi:10.1042/bj3440117 · Cited by 139
Filopodia and their links with membrane traffic and cell adhesion
Gallop, J. L. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.11.017 · Cited by 135
Loss of heterozygosity of the human cytosolic glutathione peroxidase I gene in lung cancer
Moscow, J. A., Schmidt, L. S., Ingram, D. T., Gnarra, J. R., Johnson, B. E., & Cowan, K. H. (1994) · Carcinogenesis · doi:10.1093/carcin/15.12.2769 · Cited by 129
MsrB1 (Methionine-R-sulfoxide Reductase 1) Knock-out Mice
Fomenko, D. E., Novoselov, S. V., Natarajan, S. K., Lee, B. C., Koç, A., Carlson, B. A., Lee, T.-H., Kim, H.-Y., Hatfield, D. L., & Gladyshev, V. N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805770200 · Cited by 129
Self-citation
NK-lysin, a Disulfide-containing Effector Peptide of T-lymphocytes, Is Reduced and Inactivated by Human Thioredoxin Reductase
Andersson, M., Holmgren, A., & Spyrou, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.10116 · Cited by 126
Selenite protects human endothelial cells from oxidative damage and induces thioredoxin reductase
MILLER, S., Walker, S. W., Arthur, J. R., Nicol, F., Pickard, K. M., Lewin, M., Howie, A. F., & Beckett, G. J. (2001) · Clinical Science · doi:10.1042/cs1000543 · Cited by 126
Targeting Thioredoxin Reductase by Parthenolide Contributes to Inducing Apoptosis of HeLa Cells
Duan, D., Zhang, J., Yao, J., Liu, Y., & Fang, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700591 · Cited by 125
Effect of selenium on rat thioredoxin reductase activity
Berggren, M. I., Mangin, J., Gasdaska, J. R., & Powis, G. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00283-4 · Cited by 124
Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism
Biterova, E. I., Turanov, A. A., Gladyshev, V. N., & Barycki, J. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504218102 · Cited by 120
Study of the oxidative stress in a rat model of chronic brain hypoperfusion
Kašparová, S., Brezová, V., Valko, M., Horecký, J., Mlynárik, V., Liptaj, T., Vančová, O., Uličná, O., & Dobrota, D. (2005) · Neurochemistry International · doi:10.1016/j.neuint.2005.02.006 · Cited by 119
Selenoprotein T Exerts an Essential Oxidoreductase Activity That Protects Dopaminergic Neurons in Mouse Models of Parkinson's Disease
Boukhzar, L., Hamieh, A., Cartier, D., Tanguy, Y., Alsharif, I., Castex, M., Arabo, A., Hajji, S. E., Bonnet, J., Errami, M., et al. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6478 · Cited by 119
Thioredoxin Reductase as a Potential Molecular Target for Anticancer Agents That Induce Oxidative Stress
Smart, D. D., Ortiz, K. L., Mattson, D., Bradbury, C. M., Bisht, K. S., Sieck, L., Brechbiel, M. W., & Gius, D. R. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3990 · Cited by 117
Versatility of Selenium Catalysis in PHGPx Unraveled by LC/ESI-MS/MS
Mauri, P., Benazzi, L., Flohé, L., Maiorino, M., Pietta, P. G., Pilawa, S., Roveri, A., & Ursini, F. (2003) · Biological Chemistry · doi:10.1515/bc.2003.065 · Cited by 110
The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function
Lourenço dos Santos, S., Petropoulos, I., & Friguet, B. (2018) · Antioxidants · doi:10.3390/antiox7120191 · Cited by 109
Metabolism of selenium compounds catalyzed by the mammalian selenoprotein thioredoxin reductase
Lu, J., Berndt, C., & Holmgren, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.013 · Cited by 108
Levels of major selenoproteins in T cells decrease during HIV infection and low molecular mass selenium compounds increase
Gladyshev, V. N., Stadtman, T. C., Hatfield, D. L., & Jeang, K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.835 · Cited by 107
Selective Removal of the Selenocysteine tRNA[Ser]Sec Gene (Trsp) in Mouse Mammary Epithelium
Kumaraswamy, E., Carlson, B. A., Morgan, F., Miyoshi, K., Robinson, G. W., Su, D., Wang, S., Southon, E. A., Tessarollo, L., Lee, B. J., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1477-1488.2003 · Cited by 106
Self-citation
GPx3 promoter hypermethylation is a frequent event in human cancer and is associated with tumorigenesis and chemotherapy response
Chen, B., Rao, X., House, M. G., Nephew, K. P., Cullen, K. J., & Guo, Z. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.05.013 · Cited by 105
A hypothesis on the catalytic mechanism of the selenoenzyme thioredoxin reductase
Gromer, S., Wissing, J. B., BEHNE, D., Ashman, K., Schirmer, R. H., Floh�, L., & Becker, K. (1998) · Biochemical Journal · doi:10.1042/bj3320591 · Cited by 103
Structural classification of thioredoxin‐like fold proteins
Qi, Y., & Grishin, N. V. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20329 · Cited by 102
Regulation of inflammation by selenium and selenoproteins: impact on eicosanoid biosynthesis
Mattmiller, S. A., Carlson, B. A., & Sordillo, L. M. (2013) · Journal of Nutritional Science · doi:10.1017/jns.2013.17 · Cited by 102
Regulation of Protein Function by Reversible Methionine Oxidation and the Role of Selenoprotein MsrB1
Kaya, A., Lee, B. C., & Gladyshev, V. N. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6385 · Cited by 96
Self-citation
Thioredoxin and ventricular remodeling
Ago, T., & Sadoshima, J. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.08.006 · Cited by 92
Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation
Hansel, A., Heinemann, S. H., & Hoshi, T. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.010 · Cited by 90
Gastrointestinal glutathione peroxidase prevents transport of lipid hydroperoxides in CaCo-2 cells
Wingler, K., Müller, C., Schmehl, K., Florian, S., & Brigelius‐Flohé, R. (2000) · Gastroenterology · doi:10.1053/gast.2000.9521 · Cited by 89
Characterization of Mammalian Selenoprotein O: A Redox-Active Mitochondrial Protein
Han, S.-J., Lee, B. C., Yim, S. H., Gladyshev, V. N., & Lee, S.-R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095518 · Cited by 88
Self-citation
A Novel Protein Kinase-Like Domain in a Selenoprotein, Widespread in the Tree of Life
Dudkiewicz, M., Szczepińska, T., Grynberg, M., & Pawłowski, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032138 · Cited by 75
Allelic Loss of the Gene for the GPX1 Selenium-Containing Protein Is a Common Event in Cancer
Hu, Y., Benya, R. V., Carroll, R. E., & Diamond, A. M. (2005) · Journal of Nutrition · doi:10.1093/jn/135.12.3021s · Cited by 74
Selenoprotein MsrB1 promotes anti-inflammatory cytokine gene expression in macrophages and controls immune response in vivo
Lee, B. C., Lee, S., Choo, M., Kim, J. H., Lee, H. M., Kim, S., Fomenko, D. E., Kim, H.-Y., Park, J. M., & Gladyshev, V. N. (2017) · Scientific Reports · doi:10.1038/s41598-017-05230-2 · Cited by 74
Self-citation
The Dynamic Actin Cytoskeleton in Smooth Muscle
Tang, D. D. (2017) · Advances in pharmacology · doi:10.1016/bs.apha.2017.06.001 · Cited by 74
Glutathione peroxidase 3, a new retinoid target gene, is crucial for human skeletal muscle precursor cell survival
Haddad, M. E., Jean, E., Turki, A., Hugon, G., Vernus, B., Bonnieu, A., Passerieux, E., Hamadé, A., Mercier, J. G., Laoudj‐Chenivesse, D., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.115220 · Cited by 72
Effects of Weight Loss on Glutathione Peroxidase 3 Serum Concentrations and Adipose Tissue Expression in Human Obesity
Langhardt, J., Flehmig, G., Klöting, N., Lehmann, S., Ebert, T., Kern, M., Schön, M. R., Gärtner, D., Lohmann, T., Dreßler, M., et al. (2018) · Obesity Facts · doi:10.1159/000494295 · Cited by 71
Regulation of Selenoproteins and Methionine Sulfoxide Reductases A and B1 by Age, Calorie Restriction, and Dietary Selenium in Mice
Novoselov, S. V., Kim, H.-Y., Hua, D., Lee, B. C., Astle, C. M., Harrison, D. E., Friguet, B., Moustafa, M. E., Carlson, B. A., Hatfield, D. L., et al. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2895 · Cited by 67
Self-citation
Selenoprotein T deficiency alters cell adhesion and elevates selenoprotein W expression in murine fibroblast cells
Sengupta, A., Carlson, B. A., Labunskyy, V. M., Gladyshev, V. N., & Hatfield, D. L. (2009) · Biochemistry and Cell Biology · doi:10.1139/o09-064 · Cited by 67
Selenoprotein S expression in reactive astrocytes following brain injury
Fradejas‐Villar, N., Serrano‐Pérez, M. C., Tranque, P., & Calvo, S. (2011) · Glia · doi:10.1002/glia.21168 · Cited by 64
The 58 kDa mouse selenoprotein is a BCNU‐sensitive thioredoxin reductase
Gromer, S., Schirmer, R. H., & Becker, K. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00816-8 · Cited by 62
Thioredoxin expression in primary T-cell acute lymphoblastic leukemia and its therapeutic implication.
Shao, L., Diccianni, M. B., Tanaka, T. S., Gribi, R., Yu, A. L.-T., Pullen, J., Camitta, B. M., & Yu, A. L.-T. (2001) · PubMed · Cited by 60
Knockout of Mitochondrial Thioredoxin Reductase Stabilizes Prolyl Hydroxylase 2 and Inhibits Tumor Growth and Tumor-Derived Angiogenesis
Hellfritsch, J., Kirsch, J., Schneider, M., Fluege, T., Wortmann, M., Frijhoff, J., Dagnell, M., Fey, T., Esposito, I., Kölle, P., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5889 · Cited by 57
The Intrinsically Disordered Membrane Protein Selenoprotein S Is a Reductase in Vitro
Liu, J., Li, F., & Rozovsky, S. (2013) · Biochemistry · doi:10.1021/bi4001358 · Cited by 57
Cyclophosphamide as a potent inhibitor of tumor thioredoxin reductase in vivo
Wang, X., Zhang, J., & Xu, T. (2006) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2006.10.029 · Cited by 56
The Functions of the Mammalian Methionine Sulfoxide Reductase System and Related Diseases
Jiang, B., & Moskovitz, J. (2018) · Antioxidants · doi:10.3390/antiox7090122 · Cited by 56
Promoter Hypermethylation and Suppression of Glutathione Peroxidase 3 Are Associated with Inflammatory Breast Carcinogenesis
Mohamed, M. M., Sabet, S., Peng, D., Nouh, M. A., El‐Shinawi, M., & El-Rifai, W. M. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/787195 · Cited by 54
Influence of SelS gene silence on β-Mercaptoethanol-mediated endoplasmic reticulum stress and cell apoptosis in HepG2 cells
Du, S., Liu, H., & Huang, K. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.01.005 · Cited by 53
EF24 induces ROS-mediated apoptosis via targeting thioredoxin reductase 1 in gastric cancer cells
Zou, P., Xia, Y., Chen, W., Chen, X., Ying, S., Feng, Z., Chen, T., Ye, Q., Wang, Z., Qiu, C., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7633 · Cited by 52
Specific antioxidant selenoproteins are induced in the heart during hypertrophy
Hoffmann, F. W., Hashimoto, A. S., Lee, B. C., Rose, A. H., Shohet, R. V., & Hoffmann, P. R. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.05.007 · Cited by 47
Self-citation
Levels of selenium in plasma and glutathione peroxidase in erythrocytes in patients with prostate cancer or benign hyperplasia
Hardell, L., Degerman, A., Tomić, R., Marklund, S. L., & Bergfors, M. (1995) · European Journal of Cancer Prevention · doi:10.1097/00008469-199502000-00009 · Cited by 47
Selenoprotein S Is Highly Expressed in the Blood Vessels and Prevents Vascular Smooth Muscle Cells From Apoptosis
Ye, Y., Fu, F., Li, X., Yang, J., & Liu, H. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25254 · Cited by 47
Human mitochondrial thioredoxin reductase reduces cytochrome c and confers resistance to complex III inhibition
Nalvarte, I., Damdimopoulos, A. E., & Spyrou, G. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.072 · Cited by 46
Analyses of Selenotranscriptomes and Selenium Concentrations in Response to Dietary Selenium Deficiency and Age Reveal Common and Distinct Patterns by Tissue and Sex in Telomere-Dysfunctional Mice
Cao, L., Zhang, L., Zeng, H., Wu, R. T. Y., Wu, T.-L., & Cheng, W. (2017) · Journal of Nutrition · doi:10.3945/jn.117.247775 · Cited by 44
Synthetic lethal screening in the mammalian central nervous system identifies Gpx6 as a modulator of Huntington’s disease
Shema, R., Kulicke, R., Cowley, G. S., Stein, R., Root, D. E., & Heiman, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417231112 · Cited by 41
Possible regulation of the in vitro assembly of bovine brain tubulin by the bovine thioredoxin system
KHAN, I. A., & ̃a, R. F. L. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90280-d · Cited by 38
Extracellular ATP counteracts the ERK1/2‐mediated death‐promoting signaling cascades in astrocytes
Shinozaki, Y., Koizumi, S., Ohno, Y., Nagao, T., & Inoue, K. (2006) · Glia · doi:10.1002/glia.20408 · Cited by 38
Multiple roles of the actin and microtubule-regulating formins in the developing brain
Galbraith, K. K., & Kengaku, M. (2018) · Neuroscience Research · doi:10.1016/j.neures.2018.09.008 · Cited by 38
Thioredoxin reductase inactivation as a pivotal mechanism of ifosfamide in cancer therapy
Wang, X., Zhang, J., & Xu, T. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.10.012 · Cited by 37
Dietary selenium intake influences Cx43 dephosphorylation, TNF‐α expression and cardiac remodeling after reperfused infarction
Tanguy, S., Rakotovao, A., Jouan, M.-G., Ghezzi, C., de Leiris, J., & Boucher, F. R. (2010) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000393 · Cited by 36
Selenium supplementation to chronic kidney disease patients on hemodialysis does not induce the synthesis of plasma glutathione peroxidase.
Zachara, B., Gromadzińska, J., Zbróg, Z., Swiech, R., Wąsowicz, W., Twardowska, E., Jabłońska, E., & Sobala, W. (2009) · Acta Biochimica Polonica · doi:10.18388/abp.2009_2531 · Cited by 36
Epigenetic and Glucocorticoid Receptor-Mediated Regulation of Glutathione Peroxidase 3 in Lung Cancer Cells
An, B. C., Jung, N.-K., Park, C. Y., Oh, I., Choi, Y. D., Park, J., & Lee, S.-W. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.0164 · Cited by 34
Self-citation
Chronic treatment with statins increases the availability of selenium in the antioxidant defence systems of hemodialysis patients
TACCONE-GALLUCCI, M., Noce, A., Bertucci, P., Fabbri, C., di Villahermosa, S. M., Della-Rovere, F. R., Francesco, M. D., Lonzi, M., Federici, G., Scaccia, F., et al. (2009) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2009.06.005 · Cited by 33
A Bioinformatics Approach to Characterize Mammalian Selenoprotein T
Moustafa, M. E., & Antar, H. A. (2012) · Biochemical Genetics · doi:10.1007/s10528-012-9516-2 · Cited by 29
Selenoprotein R Protects Human Lens Epithelial Cells against D-Galactose-Induced Apoptosis by Regulating Oxidative Stress and Endoplasmic Reticulum Stress
Dai, J., Liu, H., Zhou, J., & Huang, K. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17020231 · Cited by 28
Berberine alleviates pulmonary hypertension through Trx1 and β-catenin signaling pathways in pulmonary artery smooth muscle cells
Yu, W., Luo, J., aikai, Z., yaguo, Z., linlin, Z., Gu, Y., & hang, Z. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.111910 · Cited by 28
Methionine Sulfoxide Reductase B1 Regulates Hepatocellular Carcinoma Cell Proliferation and Invasion via the Mitogen‐Activated Protein Kinase Pathway and Epithelial‐Mesenchymal Transition
He, Q., Li, H., Meng, F., Sun, X., Xu, F., Chen, J., Li, L., & Liu, J. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/5287971 · Cited by 27
Characterization of the Amino Acids from Neisseria meningitidis Methionine Sulfoxide Reductase B Involved in the Chemical Catalysis and Substrate Specificity of the Reductase Step
Neiers, F., Sonkaria, S., Olry, A., Boschi‐Müller, S., & Branlant, G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704730200 · Cited by 26
Selenomethionine and Methioninase: Selenium Free Radical Anticancer Activity
Spallholz, J. E. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-8796-2_15 · Cited by 26
Selenoprotein O deficiencies suppress chondrogenic differentiation of ATDC5 cells
Yan, J., Fei, Y., Han, Y., & Lu, S. (2016) · Cell Biology International · doi:10.1002/cbin.10644 · Cited by 22
Brain, immune system and selenium: a starting point for a new diagnostic marker for Alzheimer’s disease?
Achilli, C., Ciana, A., & Minetti, G. (2018) · Perspectives in Public Health · doi:10.1177/1757913918778707 · Cited by 21
A trienone analog of curcumin, 1,7-bis(3-hydroxyphenyl)-1,4,6-heptatrien-3-one, possesses ROS- and caspase-mediated apoptosis in human oral squamous cell carcinoma cells in vitro
Utaipan, T., Boonyanuphong, P., Chuprajob, T., Suksamrarn, A., & Chunglok, W. (2020) · Applied Biological Chemistry · doi:10.1186/s13765-020-0491-8 · Cited by 21
Molecular characterization and NF-κB-regulated transcription of selenoprotein S from the Bama mini-pig
Zhang, N., Jing, W., Cheng, J., Cui, W., Mu, Y., Li, K., & Lei, X. G. (2010) · Molecular Biology Reports · doi:10.1007/s11033-010-0551-y · Cited by 20
Prostate Epithelium-Specific Deletion of the Selenocysteine tRNA Gene Trsp Leads to Early Onset Intraepithelial Neoplasia
Luchman, H. A., Villemaire, M. L., Bismar, T. A., Carlson, B. A., & Jirik, F. R. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.11.025 · Cited by 18
Redox regulation of the tumor suppressor PTEN by the thioredoxin system and cumene hydroperoxide
Han, S.-J., Zhang, Y., Kim, I., Chay, K.-O., Yoon, H. J., Jang, D. I., Yang, S. Y., Park, J., Woo, H. A., Park, I., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.07.029 · Cited by 18
Self-citation
Selenoprotein MsrB1 deficiency exacerbates acetaminophen-induced hepatotoxicity via increased oxidative damage
Kim, K. Y., Kwak, G., Singh, M. P., Gladyshev, V. N., & Kim, H. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.09.020 · Cited by 18
Carnosol induces apoptotic cell death through ROS-dependent inactivation of STAT3 in human melanoma G361 cells
Choi, S. M., Kim, D., Chun, K., & Choi, J. (2019) · Applied Biological Chemistry · doi:10.1186/s13765-019-0463-z · Cited by 18
Human Selenium-Dependent Thioredoxin Reductase from HeLa Cells: Properties of Forms with Differing Heparin Affinities
Gorlatov, S. N., & Stadtman, T. C. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1356 · Cited by 16
Mammalian thioredoxin reductase alters cytolytic activity of an antibacterial peptide
Björkhem‐Bergman, L., Jönsson‐Videsäter, K., Paul, C., Björnstedt, M., & Andersson, M. (2004) · Peptides · doi:10.1016/j.peptides.2004.06.012 · Cited by 16
Effect of methionine sulfoxide reductase B1 (SelR) gene silencing on peroxynitrite-induced F-actin disruption in human lens epithelial cells
Jia, Y., Zhou, J., Liu, H., & Huang, K. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.12.055 · Cited by 13
Methionine sulfoxide reductase B1 regulates proliferation and invasion by affecting mitogen-activated protein kinase pathway and epithelial–mesenchymal transition in u2os cells
Li, H., He, Q., Meng, F., Xu, F., Chen, J., Li, L., & Liu, J. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.01.151 · Cited by 13

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Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638
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Sies, H., Mailloux, R. J., & Jakob, U. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00730-2 · Cited by 561
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Radomska, D., Czarnomysy, R., Radomski, D., & Bielawski, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031009 · Cited by 468
The relationship between nutrition and the immune system
Munteanu, C., & Schwartz, B. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1082500 · Cited by 346
Signaling pathways in vascular function and hypertension: molecular mechanisms and therapeutic interventions
Ma, J., Li, Y., Yang, X., Liu, K., Zhang, X., Zuo, X., Ye, R., Wang, Z., Shi, R., Meng, Q., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01430-7 · Cited by 265

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Authors: Zhang, Y., Roh, Y. J., Han, S.-J., Park, I., Lee, H. M., Ok, Y. S., Lee, B. C., & Lee, S.-R.
Affiliations: Chonnam National University (KR)
Korea University (KR)
COTDE Inc. 19-3, Ugakgol-gil, Susin-myeon, Cheonan-si, Chungcheongnam-do 330-882, Korea
Corresponding author: Lee, Byung Cheon
Lee, Seung-Rock
ORCID: Zhang, Ying
Roh, Yeon Jin
Han, Seong-Jeong
Park, Iha
Ok, Yong Sik
Lee, Byung Cheon
Lee, Seung-Rock
Venue: Antioxidants
Publisher: MDPI AG
Published: 2020-05-05
Volume: 9
Issue: 5
Pages: 383
ISSN: 2076-3921 (ISSN-L)
DOI: 10.3390/antiox9050383
PMC: PMC7278666
OpenAlex: W3022351363
Cited by: 267
References: 162
Citations by year: 2026: 52 · 2025: 55 · 2024: 51 · 2023: 40 · 2022: 43 · 2021: 16 · 2020: 9
FWCI: 3.31
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Antioxidants (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: National Research Foundation of Korea (2018R1D1A1B06051438, 2018M3A9F3055925, 2018R1A1A1A05079386)
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
Physical Sciences › Chemistry › Organic Chemistry › Organoselenium and organotellurium chemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: selenoproteins, selenocysteine, redox regulation, antioxidant defense, glutathione peroxidase, thioredoxin reductase, oxidative enzymes, redox homeostasis, oxidative stress

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Role of Selenoproteins in Redox Regulation of Signaling and the Antioxidant System: A Review

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