The DOI matches its Crossref record; 215 of the 217 references it cites were found in a registry or an index.
Glutathione peroxidases
Abstract
Background With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Scope of the review Since GPxs have recently been reviewed under various aspects, we here focus on novel findings considering their diverse physiological roles exceeding an antioxidant activity.Major conclusions GPxs are involved in balancing the H2O2 homeostasis in signalling cascades, e.g. in the insulin signalling pathway by GPx1; GPx2 plays a dual role in carcinogenesis depending on the mode of initiation and cancer stage; GPx3 is membrane associated possibly explaining a peroxidatic function despite low plasma concentrations of GSH; GPx4 has novel roles in the regulation of apoptosis and, together with GPx5, in male fertility. Functions of GPx6 are still unknown, and the proposed involvement of GPx7 and GPx8 in protein folding awaits elucidation.General significance Collectively, selenium-containing GPxs (GPx1-4 and 6) as well as their non-selenium congeners (GPx5, 7 and 8) became key players in important biological contexts far beyond the detoxification of hydroperoxides. This article is part of a Special Issue entitled Cellular functions of glutathione.
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In the citing paper
“the reduced glutathione (GSH)-dependent enzyme glutathione peroxidase 4 (GPX4)—which is directly targeted by RSL3—has emerged as the main endogenous inhibitor of ferroptosis by virtue of its ability to limit lipid peroxidation by catalyzing the GSH-dependent reduction of lipid hydroperoxides to lipid alcohols [547–550].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [549]
In the citing paper
“erastin triggers ferroptosis by (indirectly) affecting the catalytic cycle of GPX4 via a mechanism that involves the inhibition of the cystine/glutamate antiporter system xc− and consequent decrease in intracellular cysteine (which derives from cystine reduction in the cytoplasm) and GSH (which is synthesized from cysteine) [539, 548, 549, 551].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [549]
In the citing paper
“Glutathione depletion causes loss of cellular antioxidant capacity, as well as inhibition of glutathione-dependent enzymes, such as glutathione peroxidases [24, 25].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [25]
In the citing paper
“First, GPX4 is the only enzyme that can reduce lipid hydroperoxides within biological membranes [25].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [25]
In the citing paper
“Second, GPX4 uses glutathione as an essential cofactor for its enzymatic activity [25].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [25]
In the citing paper
“GPx-1 acts in the intracellular environment and maintains the physiological level of hydrogen peroxide, which is important in mitochondrial function, thiol redox homeostasis, and signal transduction (Brigelius-Flohé and Maiorino 2013).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Brigelius-Flohé and Maiorino 2013
Citations
Cites
1 retracted
Xu, X., Liu, T., Zhang, A., Huo, X., Luo, Q., Chen, Z., Yu, L., Li, Q., Liu, L., Lun, Z., et al. (2012) · Infection and Immunity · doi:10.1128/iai.06295-11 · Cited by 69
RetractedSelenium: Biochemical Role as a Component of Glutathione Peroxidase
Rotruck, J. T., Pope, A. L., Ganther, H. E., Swanson, A. B., Hafeman, D. G., & Hoekstra, W. G. (1973) · Science · doi:10.1126/science.179.4073.588 · Cited by 7,815
Association of reactive oxygen species levels and radioresistance in cancer stem cells
Diehn, M., Cho, R. W., Lobo, N. A., Kalisky, T., Dorie, M. J., Kulp, A. N., Qian, D., Lam, J. S., Ailles, L. E., Wong, M., et al. (2009) · Nature · doi:10.1038/nature07733 · Cited by 2,555
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
Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
DeNicola, G. M., Karreth, F. A., Humpton, T. J., Gopinathan, A., Wei, C., Frese, K., Mangal, D., Yu, K. H., Yeo, C. J., Calhoun, E. S., et al. (2011) · Nature · doi:10.1038/nature10189 · Cited by 2,277
Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470
Glutathione peroxidase: A selenoenzyme
Flohé, L., Günzler, W. A., & Schock, H. H. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80755-0 · Cited by 1,389
Keaney, J. F., Larson, M. G., Vasan, R. S., Wilson, P. W. F., Lipinska, I., Corey, D., Massaro, J. M., Sutherland, P., Vita, J. A., & Benjamin, E. J. (2003) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000058402.34138.11 · Cited by 1,304
Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114
Self-citationReversible 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
Canonical Wnt signals are essential for homeostasis of the intestinal epithelium
Pinto, D., Gregorieff, A., Begthel, H., & Clevers, H. (2003) · Genes & Development · doi:10.1101/gad.267103 · Cited by 1,026
A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation
Delaunay, A., Pflieger, D., Barrault, M., Vinh, J., & Tolédano, M. B. (2002) · Cell · doi:10.1016/s0092-8674(02)01048-6 · Cited by 902
Dual Function of the Selenoprotein PHGPx During Sperm Maturation
Ursini, F., Heim, S., Kieß, M., Maiorino, M., Roveri, A., Wissing, J. B., & Flohé, L. (1999) · Science · doi:10.1126/science.285.5432.1393 · Cited by 902
Self-citationUrsini, F., Maiorino, M., Valente, M., Ferri, L., & Gregolin, C. (1982) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(82)90150-3 · Cited by 884
[5] Diversity of glutathione peroxidases
Maiorino, F. M., Brigelius‐Flohé, R., Aumann, K. D., Roveri, A., Schomburg, D., & Flohé, L. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52007-4 · Cited by 854
Self-citationUnraveling the biological roles of reactive oxygen species
Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., Rhee, S. G., Thornalley, P. J., Partridge, L., Gems, D., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.010 · Cited by 836
Signaling Functions of Reactive Oxygen Species
Forman, H. J., Maiorino, M., & Ursini, F. (2010) · Biochemistry · doi:10.1021/bi9020378 · Cited by 827
Self-citationActivation of Nrf2-antioxidant signaling attenuates NFκB-inflammatory response and elicits apoptosis
Li, W., Khor, T. O., Xu, C., Shen, G., Jeong, W.-S., Yu, S., & Kong, A.-N. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.07.017 · Cited by 738
Koppers, A. J., Iuliis, G. N. D., Finnie, J. M., McLaughlin, E. A., & Aitken, R. J. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-2616 · Cited by 699
The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2‐nm Resolution
Epp, O., Ladenstein, R., & Wendel, A. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07429.x · Cited by 689
Chambers, I., Frampton, J., Goldfarb, P. S., Affara, N. A., McBain, W., & Harrison, P. R. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04350.x · Cited by 667
LAU, A., VILLENEUVE, N., Sun, Z., Wong, P. K., & Zhang, D. (2008) · Pharmacological Research · doi:10.1016/j.phrs.2008.09.003 · Cited by 653
"Selenium: Its Molecular Biology and Role in Human Health"
Hatfield, D. L. (2002) · Free Radical Research · doi:10.1080/10715760290006394 · Cited by 651
Hofmann, B., Hecht, H., & Flohé, L. (2002) · Biological Chemistry · doi:10.1515/bc.2002.040 · Cited by 620
Glutathione peroxidase family – an evolutionary overview
Margis, R., Dunand, C., Teixeira, F. K., & Margis-Pinheiro, M. M. A. N. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06542.x · Cited by 611
Basic Principles and Emerging Concepts in the Redox Control of Transcription Factors
Brigelius‐Flohé, R., & Flohé, L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3534 · Cited by 590
Self-citationReactive oxygen species enhance insulin sensitivity
Loh, K., Deng, H., Fukushima, A., Cai, X., Boivin, B., Galic, S., Bruce, C., Shields, B. J., Skiba, B., Ooms, L. M., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.009 · Cited by 581
Ho, Y., Magnenat, J.-L., Bronson, R. T., Cao, J., Gargano, M. D., Sugawara, M., & Funk, C. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16644 · Cited by 562
Chu, F., Doroshow, J. H., & Esworthy, R. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53812-6 · Cited by 560
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542
Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase
McClung, J. P., Roneker, C. A., Mu, W., Lisk, D. J., Langlais, P., Liu, F., & Lei, X. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308096101 · Cited by 536
Discovery of the Negative Regulator of Nrf2, Keap1: A Historical Overview
Itoh, K., Mimura, J., & Yamamoto, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3222 · Cited by 521
de Haan, J. B., Bladier, C., Griffiths, P., Kelner, M. J., O’Shea, R. D., Cheung, N. S., Bronson, R. T., Silvestro, M. J., Wild, S., Zheng, S. S., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22528 · Cited by 456
Miller, D., Brinkworth, M. H., & Iles, D. (2009) · Reproduction · doi:10.1530/rep-09-0281 · Cited by 416
Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme
Toppo, S., Flohé, L., Ursini, F., Vanin, S., & Maiorino, M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.007 · Cited by 368
Self-citationBjörnstedt, M., Xue, J., Huang, W., Åkesson, B., & Holmgren, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43889-6 · Cited by 364
The GI-GPx Gene Is a Target for Nrf2
Banning, A., Deubel, S., Kluth�, D., Zhou, Z., & Brigelius‐Flohé, R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.12.4914-4923.2005 · Cited by 344
Self-citationGlutathione Peroxidase, V. The kinetic mechanism
Flohé, L., Loschen, G., Günzler, W. A., & Eichele, E. (1972) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1972.353.1.987 · Cited by 340
Mitochondrial glutathione peroxidase 4 disruption causes male infertility
Schneider, M., Förster, H., Boersma, A., Seiler, A., Wehnes, H., Sinowatz, F., Neumüller, C., Deutsch, M. J., Walch, A. K., de Angelis, M. H., et al. (2009) · The FASEB Journal · doi:10.1096/fj.09-132795 · Cited by 328
Self-citationHuman kidney proximal tubules are the main source of plasma glutathione peroxidase
Avissar, N. E., Ornt, D. B., Yagil, Y., Horowitz, S., Watkins, R. H., Kerl, E. A., Takahashi, K., PALMER, I. S., & Cohen, H. J. (1994) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1994.266.2.c367 · Cited by 324
Takebe, G., Yarimizu, J., Saito, Y., Hayashi, T., Nakamura, H., Yodoi, J., Nagasawa, S., & Takahashi, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202773200 · Cited by 318
Glutathione peroxidases in different stages of carcinogenesis
Brigelius‐Flohé, R., & Kipp, A. P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.006 · Cited by 311
Self-citationBacteria-Induced Intestinal Cancer in Mice with DisruptedGpx1andGpx2Genes
Chu, F., Esworthy, R. S., Chu, P. G., Longmate, J., Huycke, M. M., Wilczynski, S. P., & Doroshow, J. H. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2272 · Cited by 310
Epididymosomes are involved in the acquisition of new sperm proteins during epididymal transit
Sullivan, R., Frenette, G., & Girouard, J. (2007) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2007.00281.x · Cited by 307
Biosynthesis of Selenocysteine on Its tRNA in Eukaryotes
Xu, X.-M., Carlson, B. A., Mix, H., Zhang, Y., Saira, K., Glass, R. S., Berry, M. J., Gladyshev, V. N., & Hatfield, D. L. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0050004 · Cited by 303
Mice with combined disruption of Gpx1 and Gpx2 genes have colitis
Esworthy, R. S., Aranda, R., Martı́n, M. G., Doroshow, J. H., Binder, S. W., & Chu, F. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.3.g848 · Cited by 299
Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation
Fagegaltier, D., Hubert, N., Yamada, K., Mizutani, T., Carbon, P., & Krol, A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4796 · Cited by 294
Analysis of an expression profile of genes in the human adipose tissue
Maeda, K., Okubo, K., Shimomura, I., Mizuno, K., Matsuzawa, Y., & Matsubara, K. (1997) · Gene · doi:10.1016/s0378-1119(96)00730-5 · Cited by 294
The antioxidant glutathione peroxidase family and spermatozoa: A complex story
Drevet, J. R. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.027 · Cited by 282
Pfeifer, H., Conrad, M., Roethlein, D., Kyriakopoulos, A., Brielmeier, M., Bornkamm, G. W., & BEHNE, D. (2001) · The FASEB Journal · doi:10.1096/fj.00-0655fje · Cited by 281
Schomburg, L., & Köhrle, J. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700465 · Cited by 278
The Lipoxygenase of Reticulocytes
Rapoport, S. M., SCHEWE, T., Wiesner, R., Halangk, W., Ludwig, P., JANICKE‐HÖHNE, M., Tannert, C., Hiebsch, C., & Klatt, D. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb13068.x · Cited by 277
Nguyen, V. D., Saaranen, M. J., Karala, A., Lappi, A., Wang, L., Raykhel, I. B., Alanen, H. I., Salo, K. E. H., Wang, C.-C., & Ruddock, L. W. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.12.039 · Cited by 275
Conrad, M., Moreno, S. G., Sinowatz, F., Ursini, F., Kölle, S., Roveri, A., Brielmeier, M., Wurst, W., Maiorino, M., & Bornkamm, G. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.17.7637-7644.2005 · Cited by 270
Self-citationMitochondrial regulation of cell death: Processing of apoptosis-inducing factor (AIF)
Norberg, E., Orrenius, S., & Zhivotovsky, B. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.02.163 · Cited by 270
Composition and Evolution of the Vertebrate and Mammalian Selenoproteomes
Mariotti, M., Ridge, P. G., Zhang, Y., Lobanov, A. V., Pringle, T. H., Guigó, R., Hatfield, D. L., & Gladyshev, V. N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033066 · Cited by 261
A Comparison of Thiol Peroxidase Mechanisms
Flohé, L., Toppo, S., Cozza, G., & Ursini, F. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3397 · Cited by 260
Protein disulfide isomerase in redox cell signaling and homeostasis
Laurindo, F. R. M., Pescatore, L. A., & Fernandes, D. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.037 · Cited by 258
Disulfide Formation in the ER and Mitochondria: Two Solutions to a Common Process
Riemer, J., Bulleid, N. J., & Herrmann, J. M. (2009) · Science · doi:10.1126/science.1170653 · Cited by 257
Agyeman, A. S., Chaerkady, R., Shaw, P. G., Davidson, N. E., Visvanathan, K., Pandey, A., & Kensler, T. W. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1536-9 · Cited by 256
Gpx4 ablation in adult mice results in a lethal phenotype accompanied by neuronal loss in brain
Yoo, S.-E., Chen, L., Na, R., Liu, Y., Rios, C. I., Remmen, H. V., Richardson, A. G., & Ran, Q. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.043 · Cited by 256
Evolutionary and Structural Insights Into the Multifaceted Glutathione Peroxidase (Gpx) Superfamily
Toppo, S., Vanin, S., Bosello-Travain, V., & Tosatto, S. C. E. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2057 · Cited by 255
Epididymis seleno-independent glutathione peroxidase 5 maintains sperm DNA integrity in mice
Chabory, E., Damon‐Soubeyrand, C., Lenoir, A., Kauselmann, G., Kern, H., Zevnik, B., Garrel, C., Saez, F., Cadet, R., Henry-Berger, J., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38940 · Cited by 250
Vitamin E: The shrew waiting to be tamed
Brigelius‐Flohé, R. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.12.007 · Cited by 249
Self-citationERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis
Zito, E., Chin, K., Blais, J. D., Harding, H. P., & Ron, D. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911086 · Cited by 249
Multiple ways to make disulfides
Bulleid, N. J., & Ellgaard, L. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.05.004 · Cited by 233
Seleno‐independent glutathione peroxidases
Herbette, S., Roeckel‐Drevet, P., & Drevet, J. R. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05774.x · Cited by 233
Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells
May, J. M., & de Haën, C. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30209-0 · Cited by 231
Yu, Y. P., Yu, G., Tseng, G. C., Cieply, K. M., Nelson, J. B., DeFrances, M. C., Zarnegar, R., Michalopoulos, G. K., & Luo, J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0648 · Cited by 231
Cheng, W., Ho, Y., Valentine, B. A., Ross, D. A., Combs, G. F., & Lei, X. G. (1998) · Journal of Nutrition · doi:10.1093/jn/128.7.1070 · Cited by 212
Czech, M., Lawrence, J. C., & Lynn, W. S. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.10.4173 · Cited by 208
Jaeschke, H., Ho, Y.-S., Fisher, M. A., Lawson, J. A., & Farhood, A. I. (1999) · Hepatology · doi:10.1002/hep.510290222 · Cited by 202
Brigelius‐Flohé, R., Aumann, K.-D., Blöcker, H., Gross, G., Kiess, M., Klöppel, K.-D., Maiorino, M., Roveri, A., Schuckelt, R., & Usani, F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37290-3 · Cited by 199
Self-citationSelenoproteins and human health: Insights from epidemiological data
Rayman, M. P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.014 · Cited by 199
Wingler, K., Böcher, M., Flohé, L., Kollmus, H., & Brigelius‐Flohé, R. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00012.x · Cited by 196
Self-citationRat Phospholipid-hydroperoxide Glutathione Peroxidase
Thimmalapura, P., Burdsall, A., Oleksa, L. M., Chisolm, G. M., & Driscoll, D. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26993 · Cited by 195
Structure of a bacterial homologue of vitamin K epoxide reductase
Li, W., Schulman, S., Dutton, R. J., Boyd, D. H., Beckwith, J., & Rapoport, T. A. (2010) · Nature · doi:10.1038/nature08720 · Cited by 189
Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes
Chavatte, L., Brown, B. A., & Driscoll, D. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb922 · Cited by 189
Selenoproteins and Cancer Prevention
Davis, C. D., Tsuji, P. A., & Milner, J. A. (2012) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071811-150740 · Cited by 189
Handy, D. E., Lubos, E., Yang, Y., Galbraith, J. D., Kelly, N., Zhang, Y.-Y., Leopold, J. A., & Loscalzo, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900392200 · Cited by 187
Glutathione Peroxidase-3 Deficiency Promotes Platelet-Dependent Thrombosis In Vivo
Jin, R. C., Mahoney, C. E., (Coleman) Anderson, L., Ottaviano, F., Croce, K., Leopold, J. A., Zhang, Y.-Y., Tang, S.-S., Handy, D. E., & Loscalzo, J. (2011) · Circulation · doi:10.1161/circulationaha.110.000034 · Cited by 186
Peng, D., Razvi, M. H., Chen, H., Washington, K., Roessner, A., Schneider-Stock, R., & El-Rifai, W. M. (2008) · Gut · doi:10.1136/gut.2007.146290 · Cited by 185
COMHAIR, S. A. A., Bhathena, P. R., Farver, C. F., Thunnissen, E., & ERZURUM, S. C. (2001) · The FASEB Journal · doi:10.1096/fj.00-0085com · Cited by 184
Lee, Y. S., Kim, A., Choi, J. W., Kim, M., Yasue, S., Son, H. J., Masuzaki, H., Park, K. S., & Kim, J. B. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0023 · Cited by 184
Harmon, J. S., Bogdani, M., Parazzoli, S. D., Mak, S. S. M., Oseid, E. A., Berghmans, M., LeBoeuf, R. C., & Robertson, R. P. (2009) · Endocrinology · doi:10.1210/en.2009-0708 · Cited by 183
The Catalytic Site of Glutathione Peroxidases
Tosatto, S. C. E., Bosello-Travain, V., Fogolari, F., Mauri, P., Roveri, A., Toppo, S., Flohé, L., Ursini, F., & Maiorino, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2055 · Cited by 181
Self-citationThomas, J. P., Geiger, P. G., Maiorino, M., Ursini, F., & Girotti, A. W. (1990) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(90)90128-k · Cited by 181
Self-citationChung, 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
Epididymosomes and Prostasomes: Their Roles in Posttesticular Maturation of the Sperm Cells
Saez, F., Frenette, G., & Sullivan, R. (2003) · Journal of Andrology · doi:10.1002/j.1939-4640.2003.tb02653.x · Cited by 175
Sengupta, T. K., Bandyopadhyay, S., Fernandes, D., & Spicer, E. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309111200 · Cited by 174
Nair, S., Doh, S. T., Chan, J. Y., Kong, A.-N., & Cai, L. (2008) · British Journal of Cancer · doi:10.1038/sj.bjc.6604703 · Cited by 167
GPX2, a Direct Target of p63, Inhibits Oxidative Stress-induced Apoptosis in a p53-dependent Manner
Yan, W., & Chen, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512655200 · Cited by 167
Selenium and the Control of Thyroid Hormone Metabolism
Köhrle, J. (2005) · Thyroid · doi:10.1089/thy.2005.15.841 · Cited by 164
γ-Glutamylcysteine detoxifies reactive oxygen species by acting as glutathione peroxidase-1 cofactor
Quintana–Cabrera, R., Fernández-Fernández, S., Bobo-Jiménez, V., Escobar, J., Sastre, J., Almeida, Á., & Bolaños, J. P. (2012) · Nature Communications · doi:10.1038/ncomms1722 · Cited by 163
Wang, X. D., Vatamaniuk, M. Z., Wang, S. K., Roneker, C. A., Simmons, R. A., & Lei, X. G. (2008) · Diabetologia · doi:10.1007/s00125-008-1055-3 · Cited by 159
Redox Regulation in the Extracellular Environment
Ottaviano, F. G., Handy, D. E., & Loscalzo, J. (2007) · Circulation Journal · doi:10.1253/circj.72.1 · Cited by 158
Olson, G. E., Whitin, J. C., Hill, K. E., Winfrey, V. P., Motley, A. K., Austin, L. M., Deal, J., Cohen, H. J., & Burk, R. F. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00662.2009 · Cited by 158
Maiorino, M., Coassin, M., Roveri, A., & Ursini, F. (1989) · Lipids · doi:10.1007/bf02535211 · Cited by 152
Self-citationSmoking and cancer‐related gene expression in bronchial epithelium and non‐small‐cell lung cancers
Woenckhaus, M., Klein‐Hitpaß, L., Grepmeier, U., Merk, J., Pfeifer, R., Wild, P. J., Bettstetter, M., Wuensch, P. H., Blaszyk, H., Hartmann, A., et al. (2006) · The Journal of Pathology · doi:10.1002/path.2039 · Cited by 149
Yoo, M., Gu, X., Xu, X.-M., Kim, J. Y., Carlson, B. A., Patterson, A. D., Cai, H., Gladyshev, V. N., & Hatfield, D. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2891 · 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
Self-citationNF-κB, Nrf2, and HO-1 Interplay in Redox-Regulated VCAM-1 Expression
Banning, A., & Brigelius‐Flohé, R. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.889 · Cited by 141
Self-citationInvolvement of fas antigen in ovarian follicular atresia and luteolysis
Sakamaki, K., Yoshida, H., Nishimura, Y., Nishikawa, S.-I., MANABE, N., & Yonehara, S. (1997) · Molecular Reproduction and Development · doi:10.1002/(sici)1098-2795(199705)47:1 · Cited by 137
Oxidative Protein Folding and the Quiescin–Sulfhydryl Oxidase Family of Flavoproteins
Kodali, V. K., & Thorpe, C. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3098 · Cited by 136
Pro-metastatic signaling by c-Met through RAC-1 and reactive oxygen species (ROS)
Ferraro, D. A., Corso, S., Fasano, E., Panieri, E., Santangelo, R., Borrello, S., Giordano, S., Pani, G., & Galeotti, T. (2006) · Oncogene · doi:10.1038/sj.onc.1209409 · Cited by 135
Two Tales of Antioxidant Enzymes on β Cells and Diabetes
Lei, X. G., & Vatamaniuk, M. Z. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3416 · Cited by 134
Budiman, M. E., Bubenik, J. L., Miniard, A. C., Middleton, L. M., Gerber, C. A., Cash, A., & Driscoll, D. M. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.026 · Cited by 130
Maiorino, M., Ursini, F., Bosello-Travain, V., Toppo, S., Tosatto, S. C. E., Mauri, P., Becker, K., Roveri, A., Bulato, C., Benazzi, L., et al. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.033 · Cited by 129
Self-citationMaiorino, M., Scapin, M., Ursini, F., Biasolo, M. A., Bosello-Travain, V., & Flohé, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305327200 · Cited by 128
Self-citationAnalysis of Reactive Oxygen Species Generating Systems in Rat Epididymal Spermatozoa1
Vernet, P., Fulton, N., Wallace, C. A., & Aitken, R. J. (2001) · Biology of Reproduction · doi:10.1095/biolreprod65.4.1102 · Cited by 127
Krehl, S., Löwinger, M., Florian, S., Kipp, A. P., Banning, A., Wessjohann, L. A., Brauer, M. N., Iori, R., Esworthy, R. S., Chu, F., et al. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr288 · Cited by 125
Self-citationShen, Q., Chu, F., & Newburger, P. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82146-9 · Cited by 123
Al‐Taie, O., Üçeyler, N., Eubner, U., Jakob, F. J., Mörk, H., Scheurlen, M., Brigelius‐Flohé, R., Schöttker, K., Abel, J., Thalheimer, A., et al. (2004) · Nutrition and Cancer · doi:10.1207/s15327914nc4801_2 · Cited by 123
Self-citationUtomo, A. R. H., Jiang, X., Furuta, S., Yun, J., Levin, D. S., Wang, Y.-C. J., Desai, K. V., Green, J. E., Chen, P., & Lee, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407141200 · Cited by 123
A role for GPx3 in activity of normal and leukemia stem cells
Hérault, O., Hope, K. J., Deneault, É., Mayotte, N., Chagraoui, J., Wilhelm, B. T., Cellot, S., Sauvageau, M., Andrade-Navarro, M. A., Hébert, J., et al. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20102386 · Cited by 123
Esworthy, R. S., Yang, L., Frankel, P. H., & Chu, F. (2005) · Journal of Nutrition · doi:10.1093/jn/135.4.740 · Cited by 120
Hypermethylation, Loss of Expression of Glutathione Peroxidase-3 in Barrett's Tumorigenesis
Lee, O., Schneider‐Stock, R., McChesney, P. A., Kuester, D., Roessner, A., Vieth, M. W., Moskaluk, C. A., & El-Rifai, W. M. (2005) · Neoplasia · doi:10.1593/neo.05328 · Cited by 118
Florian, S., Wingler, K., Schmehl, K., Jacobasch, G., Kreuzer, O. J., Meyerhof, W., & Brigelius‐Flohé, R. (2001) · Free Radical Research · doi:10.1080/10715760100301181 · Cited by 117
Self-citationMolecular cloning of putative odorant-binding and odorant-metabolizing proteins
Dear, T. N., Campbell, K., & Rabbitts, T. H. (1991) · Biochemistry · doi:10.1021/bi00107a003 · Cited by 113
Extracellular glutathione peroxidase is secreted basolaterally by human renal proximal tubule cells
Whitin, J. C., Bhamre, S., Tham, D. M., & Cohen, H. J. (2002) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00014.2001 · Cited by 113
Aumann, K.-D., Bedorf, N., Brigelius‐Flohé, R., Schomburg, D., & Flohé, L. (1997) · PubMed · Cited by 112
Self-citationLu, Y., Lou, Y. R., Yen, P., Newmark, H. L., Mirochnitchenko, O., Inouye, M., & Huang, M. (1997) · PubMed · Cited by 111
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
Self-citationVibet, S., Goupille, C., Bougnoux, P., Steghens, J., Goré, J., & Mahéo, K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.009 · Cited by 110
Liu, J., Hinkhouse, M. M., Sun, W., Weydert, C. J. D., Ritchie, J. M., Oberley, L. W., & Cullen, J. J. (2004) · Human Gene Therapy · doi:10.1089/104303404322886093 · Cited by 109
Selenium and GPx-1 overexpression protect mammalian cells against UV-induced DNA damage
Baliga, M. S., Wang, H., Zhuo, P., Schwartz, J. L., & Diamond, A. M. (2007) · Biological Trace Element Research · doi:10.1007/bf02685998 · Cited by 106
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
Alterations in gene expression and activity during squamous cell carcinoma development.
Serewko-Auret, M. M., Popa, C., Dahler, A. L., Smith, L., Strutton, G. M., Coman, W. B., Dicker, T., & Saunders, N. A. (2002) · PubMed · Cited by 105
Perry, A. C. F., Jones, R., Niang, L., Jackson, R. M., & Hall, L. N. (1992) · Biochemical Journal · doi:10.1042/bj2850863 · Cited by 103
Conrad, M., Sandin, Å., Förster, H., Seiler, A., Frijhoff, J., Dagnell, M., Bornkamm, G. W., Rådmark, O., van Huijsduijnen, R. H., Aspenström, P., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007909107 · Cited by 101
Changing Paradigms in Thiology
Flohé, L. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)73001-9 · Cited by 100
Glutathione peroxidase 7 protects against oxidative DNA damage in oesophageal cells
Peng, D., Belkhiri, A., Hu, T., Chaturvedi, R., Asim, M., Wilson, K. T., Zaika, A. I., & El-Rifai, W. M. (2011) · Gut · doi:10.1136/gutjnl-2011-301078 · Cited by 99
Physiological functions of GPx2 and its role in inflammation‐triggered carcinogenesis
Brigelius‐Flohé, R., & Kipp, A. P. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06574.x · Cited by 98
Self-citationGPX5 is present in the mouse caput and cauda epididymidis lumen at three different locations
Pons‐Rejraji, H., Vernet, P., & Drevet, J. R. (2002) · Molecular Reproduction and Development · doi:10.1002/mrd.10136 · Cited by 98
Huang, C. Z., Ding, G., Gu, C., Zhou, J., Kuang, M., Ji, Y., He, Y., Kondo, T., & Fan, J. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-0183 · Cited by 97
Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury
Zmijewski, J. W., Lorne, E., Zhao, X., Tsuruta, Y., Sha, Y., Liu, G., & Abraham, E. H. (2009) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200806-851oc · Cited by 96
Yang, K., Popova, N. V., Yang, W., Lozonschi, I., Tadesse, S., Kent, S., Bancroft, L. K., Matise, I., Cormier, R. T., Scherer, S. J., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0598 · Cited by 96
Nrf2 target genes are induced under marginal selenium-deficiency
Müller, M. F., Banning, A., Brigelius‐Flohé, R., & Kipp, A. P. (2010) · Genes & Nutrition · doi:10.1007/s12263-010-0168-8 · Cited by 95
Self-citationRole of nucleolin in posttranscriptional control of MMP-9 expression
Fähling, M., Steege, A., Perlewitz, A., Nafz, B., Mrowka, R., Persson, P. B., & Thiele, B. J. (2005) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2005.08.005 · Cited by 93
Maiorino, M., Roveri, A., Benazzi, L., Bosello-Travain, V., Mauri, P., Toppo, S., Tosatto, S. C. E., & Ursini, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505983200 · Cited by 93
Self-citationKarunasinghe, N., Han, D. Y., Zhu, S., Yu, J., Lange, K., Duan, H., Medhora, R., Singh, N., Kan, J., Alzaher, W., et al. (2011) · Genes & Nutrition · doi:10.1007/s12263-011-0259-1 · Cited by 92
Fang, W., Goldberg, M. L., Pohl, N. M., Bi, X., Tong, C., Xiong, B., Koh, T. J., Diamond, A. M., & Yang, W. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq114 · Cited by 91
Li, T., Yang, W., Li, M., Byun, D., Tong, C., Nasser, S., Zhuang, M., Arango, D., Mariadason, J. M., & Augenlicht, L. H. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700331 · Cited by 90
Hall, L., Williams, K., Perry, A. C. F., Frayne, J., & JURY, J. A. (1998) · Biochemical Journal · doi:10.1042/bj3330005 · Cited by 89
Banning, A., Kipp, A. P., Schmitmeier, S., Löwinger, M., Florian, S., Krehl, S., Thalmann, S., Thierbach, R., Steinberg, P., & Brigelius‐Flohé, R. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1321 · Cited by 89
Self-citationVelde, A. A. T., Pronk, I., de Kort, F., & Stokkers, P. C. F. (2008) · European Journal of Gastroenterology & Hepatology · doi:10.1097/meg.0b013e3282f45751 · Cited by 88
Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than an antioxidant enzyme?
Ursini, F., Maiorino, M., & Roveri, A. (1997) · PubMed · Cited by 88
Self-citationGhyselinck, N. B., Dufaure, I., Lareyre, J., Rigaudière, N., Mattéi, M., & Dufaure, J. P. (1993) · Molecular Endocrinology · doi:10.1210/me.7.2.258 · Cited by 87
Burk, R. F., Olson, G. E., Winfrey, V. P., Hill, K. E., & Yin, D. (2011) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00064.2011 · Cited by 84
Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) in Rat Testis Nuclei Is Bound to Chromatin
Godeas, C., Tramer, F., Micali, F., Roveri, A., Maiorino, M., Nisii, C., Sandri, G., & Panfili, E. (1996) · Biochemical and Molecular Medicine · doi:10.1006/bmme.1996.0076 · Cited by 83
Self-citationNucleolin binds to a subset of selenoprotein mRNAs and regulates their expression
Miniard, A. C., Middleton, L. M., Budiman, M. E., Gerber, C. A., & Driscoll, D. M. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq247 · Cited by 82
Banning, A., Florian, S., Deubel, S., Thalmann, S., Schmehl, K., Jacobasch, G., & Brigelius‐Flohé, R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2047 · Cited by 80
Self-citationChiu, S. T., Hsieh, F., Chen, S., Chen, C.-L., Shu, H.-F., & Li, H. (2005) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-04-0396 · Cited by 79
Kakihana, T., Nagata, K., & Sitia, R. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4238 · Cited by 78
The influence of selenium and selenoprotein gene variants on colorectal cancer risk
Méplan, C., & Hesketh, J. E. (2012) · Mutagenesis · doi:10.1093/mutage/ger058 · Cited by 78
Won, H. Y., Sohn, J.-H., Min, H. J., Lee, K., Woo, H. A., Ho, Y.-S., Park, J., Rhee, S.-G., & Hwang, E. S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2989 · Cited by 77
Müller, C., Wingler, K., & Brigelius‐Flohé, R. (2003) · Biological Chemistry · doi:10.1515/bc.2003.002 · Cited by 72
Self-citationCirculating antioxidant concentrations in children with inflammatory bowel disease
Hoffenberg, E. J., Deutsch, J., Smith, S. M., & Sokol, R. (1997) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/65.5.1482 · Cited by 72
Esworthy, R. S., Mann, J. R., Sam, M., & Chu, F. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.279.2.g426 · Cited by 69
Norberg, E., Gogvadze, V. G., Vakifahmetoglu, H., Orrenius, S., & Zhivotovsky, B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.020 · Cited by 69
Britan, A., Maffre, V., Toné, S., & Drevet, J. R. (2006) · Cell and Tissue Research · doi:10.1007/s00441-005-0151-7 · Cited by 69
The Yin and Yang of Nrf2-Regulated Selenoproteins in Carcinogenesis
Brigelius‐Flohé, R., Müller, M. F., Lippmann, D., & Kipp, A. P. (2012) · International Journal of Cell Biology · doi:10.1155/2012/486147 · Cited by 68
Self-citationMörk, H., Al‐Taie, O., Bahr, K., Zierer, A., Beck, C., Scheurlen, M., Jacob, F., & Köhrle, J. (2000) · Nutrition and Cancer · doi:10.1207/s15327914nc3701_14 · Cited by 67
Kipp, A. P., Müller, M. F., Göken, E. M., Deubel, S., & Brigelius‐Flohé, R. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.05.016 · Cited by 67
Self-citationNOX4 Pathway as a Source of Selective Insulin Resistance and Responsiveness
Wu, X., & Williams, K. J. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.244525 · Cited by 67
Puglisi, R., Maccari, I., Pipolo, S., Conrad, M., Mangia, F., & Boitani, C. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22857 · Cited by 67
A mouse cDNA sequence for epididymal androgen regulated proteins related to glutathione peroxidase
Ghyselinck, N. B., & Dufaure, J. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.23.7144 · Cited by 65
Yamada, Y., Limmon, G. V., Zheng, D., Li, N., Li, L., Yin, L., Chow, V. T. K., Chen, J., & Engelward, B. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031494 · Cited by 64
p53-induced Gene 3 Mediates Cell Death Induced by Glutathione Peroxidase 3
Wang, H., Luo, K. L., Tan, L., Ren, B., Gu, L., Michalopoulos, G. K., Luo, J., & Yu, Y. P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322636 · Cited by 64
Donovan, J., Caban, K., Ranaweera, R. S., González-Flores, J., & Copeland, P. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806008200 · Cited by 64
Jrad-Lamine, A., Henry-Berger, J., Gourbeyre, P., Damon‐Soubeyrand, C., Lenoir, A., Combaret, L., Saez, F., Kocer, A., Toné, S., Fuchs, D., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172114 · Cited by 63
The Role of Dehydroascorbate in Disulfide Bond Formation
Saaranen, M. J., Karala, A., Lappi, A., & Ruddock, L. W. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2674 · Cited by 63
Vitamin E: A vitamin still awaiting the detection of its biological function
Brigelius‐Flohé, R., & Galli, F. (2010) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000091 · Cited by 61
Self-citationMarinho, H. S., Antunes, F., & Pinto, R. E. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00468-6 · Cited by 59
Baker, M. A., Krutskikh, A., Curry, B. J., Hetherington, L., & Aitken, R. J. (2005) · Biology of Reproduction · doi:10.1095/biolreprod.104.037960 · Cited by 59
Met degradation: more than one stone to shoot a receptor down
Lefebvre, J., Ancot, F., Leroy, C., Muharram, G., Lemière, A., & Tulasne, D. (2012) · The FASEB Journal · doi:10.1096/fj.11-197723 · Cited by 59
Estimation of Individual Types of Glutathione Peroxidases
Brigelius‐Flohé, R., Wingler, K., & Müller, C. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)47011-5 · Cited by 58
Self-citationFalck, E., Karlsson, S., Carlsson, J., Helenius, G., Karlsson, M. G., & Klinga‐Levan, K. (2010) · Cancer Cell International · doi:10.1186/1475-2867-10-46 · Cited by 57
He, Y., Wang, Y., Li, P., Zhu, S., Wang, J., & Zhang, S. (2010) · Digestive Diseases and Sciences · doi:10.1007/s10620-010-1369-0 · Cited by 56
Mörk, H., Scheurlen, M., Al‐Taie, O., Zierer, A., Kraus, M. R., Schöttker, K., Jakob, F. J., & Köhrle, J. (2003) · International Journal of Cancer · doi:10.1002/ijc.11087 · Cited by 56
Mueller, A. S., Bosse, A., Most, E., Klomann, S. D., Schneider, S., & Pallauf, J. (2008) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2008.02.007 · Cited by 56
Activation of the glutathione peroxidase 2 (GPx2) promoter by β-catenin
Kipp, A. P., Banning, A., & Brigelius‐Flohé, R. (2007) · Biological Chemistry · doi:10.1515/bc.2007.137 · Cited by 55
Self-citationGlutathione peroxidase-2 protects from allergen-induced airway inflammation in mice
Dittrich, A., Meyer, H., Krokowski, M., Quarcoo, D., Ahrens, B., Kube, S., Witzenrath, M., Esworthy, R. S., Chu, F., & Hamelmann, E. H. (2009) · European Respiratory Journal · doi:10.1183/09031936.00026108 · Cited by 55
Okamura, N., Iwaki, Y., Hiramoto, S., Tamba, M., Bannai, S., Sugita, Y., Syntin, P., Dacheux, F., & Dacheux, J. (1997) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(97)00016-0 · Cited by 51
Mannes, A. M., Seiler, A., Bosello-Travain, V., Maiorino, M., & Conrad, M. (2011) · The FASEB Journal · doi:10.1096/fj.10-177147 · Cited by 51
Self-citationSelenoprotein deficiency enhances radiation‐induced micronuclei formation
Baliga, M. S., Diwadkar‐Navsariwala, V., Koh, T. J., Fayad, R., Fantuzzi, G., & Diamond, A. M. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200800020 · Cited by 51
Noblanc, A., Peltier, M., Damon‐Soubeyrand, C., Kerchkove, N., Chabory, E., Vernet, P., Saez, F., Cadet, R., Janny, L., Pons‐Rejraji, H., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038565 · Cited by 50
Selenoproteins of the glutathione system
Flohé, L., & Brigelius‐Flohé, R. (2007) · Springer eBooks · doi:10.1007/0-387-33827-6_15 · Cited by 48
Self-citationTham, D. M., Whitin, J. C., & Cohen, H. J. (2002) · Pediatric Research · doi:10.1203/00006450-200205000-00016 · Cited by 47
Malinouski, M., Kehr, S., Finney, L. A., Vogt, S., Carlson, B. A., Seravalli, J., Jin, R. C., Handy, D. E., Park, T. J., Loscalzo, J., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3997 · Cited by 47
Alterations in gene expression and activity during squamous cell carcinoma development
Serewko-Auret, M. M. (2002) · The University of Queensland · doi:10.14264/106364 · Cited by 46
Ding, F. H., & Grabowski, P. J. (1999) · RNA · doi:10.1017/s1355838299991598 · Cited by 44
Jerome‐Morais, A., Wright, M. E., Liu, R., Yang, W., Jackson, M. I., Combs, G. F., & Diamond, A. M. (2011) · The Prostate · doi:10.1002/pros.21506 · Cited by 44
Rigaudière, N., Ghyselinck, N. B., Faure, J., & Dufaure, J. P. (1992) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(92)90212-o · Cited by 42
Lubos, E., Mahoney, C. E., Leopold, J. A., Zhang, Y., Loscalzo, J., & Handy, D. E. (2010) · The FASEB Journal · doi:10.1096/fj.09-147421 · Cited by 40
Seligman, J., Newton, G. L., Fahey, R. C., Shalgi, R., & Kosower, N. S. (2005) · Journal of Andrology · doi:10.2164/jandrol.05040 · Cited by 40
Endotoxemia in Transgenic Mice Overexpressing Human Glutathione Peroxidases
Mirochnitchenko, O., Prokopenko, O., Palnitkar, U., Kister, I., Powell, W. S., & Inouye, M. (2000) · Circulation Research · doi:10.1161/01.res.87.4.289 · Cited by 40
Hesketh, J. E., & Méplan, C. (2011) · Proceedings of The Nutrition Society · doi:10.1017/s0029665111000115 · Cited by 34
Tanaka, C., Coling, D., Manohar, S., Chen, G., Hu, B. H., Salvi, R., & Henderson, D. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.12.027 · Cited by 34
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2 of the 217 references couldn’t be matched to a known paper.
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Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,837
Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732
Ferroptosis: Death by Lipid Peroxidation
Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088
Metadata
- Authors
- Brigelius-Flohé, R., & Maiorino, M.
- Affiliations
- University of Padua (IT)
- ORCID
- Maiorino, Matilde
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 1830
- Issue
- 5
- Pages
- 3289-3303
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W4211158689
- Cited by
- 1,904
- References
- 217
- Citations by year
- 2026: 162 · 2025: 179 · 2024: 181 · 2023: 191 · 2022: 220 · 2021: 196 · 2020: 154 · 2019: 123 · 2018: 112 · 2017: 106 · 2016: 86 · 2015: 91 · 2014: 75 · 2013: 25
- FWCI
- 7.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- German Research Council (BR778/8-1)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione peroxidase, glutathione peroxidase 1, GPX2, glutathione peroxidase 3, GPX4, GPX5, GPX7, GPX8, hydrogen peroxide homeostasis, hydroperoxide detoxification, insulin signaling, carcinogenesis, apoptosis, male fertility, protein folding, glutathione
- MeSH terms
- Animals, Antioxidants, Glutathione, Glutathione Peroxidase, Humans, Hydrogen Peroxide, Oxidation-Reduction
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