Trends in selenium biochemistry

Synthesis of selenocysteine by cysteine synthases from selenium accumulator and non-accumulator plants

Ng, B. H., & Anderson, J. W. (1978) · Phytochemistry · doi:10.1016/s0031-9422(00)89282-1 · Cited by 86

Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme.

Gladyshev, V. N., Khangulov, S. V., & Stadtman, T. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.232 · Cited by 85

Expression of selenium-dependent glutathione peroxidase in human breast tumor cell lines.

Esworthy, R. S., Baker, M., & Chu, F. (1995) · PubMed · Cited by 85

Speciation of seleno compounds in yeast aqueous extracts by three-dimensional liquid chromatography with inductively coupled plasma mass spectrometric and electrospray mass spectrometric detection

McSheehy, S., Pannier, F., Szpunar, J., Potin‐Gautier, M., & Łobiński, R. (2002) · The Analyst · doi:10.1039/b108680b · Cited by 84

Expression of the Type II Iodothyronine Deiodinase in Cultured Rat Astrocytes Is Selenium-dependent

Pallud, S., Lennon, A., Ramaugé, M., Gavaret, J., Croteau, W., Pierre, M., Courtin, F., & Germain, D. L. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.18104 · Cited by 83

Methylseleninate Is a Substrate Rather Than an Inhibitor of Mammalian Thioredoxin Reductase

Gromer, S., & Gross, J. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109234200 · Cited by 83

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

Mitochondrial thioredoxin reductase in bovine adrenal cortex: Its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine

Watabe, S., Makino, Y., Ogawa, K., Hiroi, T., Yamamoto, Y., & TAKAHASHI, S. Y. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00578.x · Cited by 81

Selenocompounds Induce a Redox Modulation of Protein Kinase C in the Cell, Compartmentally Independent from Cytosolic Glutathione: Its Role in Inhibition of Tumor Promotion

Gopalakrishna, R., Chen, Z.-H., & Gundimeda, U. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0335 · Cited by 81

Heparin-binding Histidine and Lysine Residues of Rat Selenoprotein P

Hondal, R. J., Ma, S., Caprioli, R. M., Hill, K. E., & Burk, R. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010405200 · Cited by 81

A New Toxicant Occurring Naturally in Certain Samples of Plant Foodstuffs

Franke, K. W., & Potter, V. R. (1935) · Journal of Nutrition · doi:10.1093/jn/10.2.213 · Cited by 80

A novel very small subunit of a selenium containing [NiFe] hydrogenease of Methanococcus voltae is postranslationally processed by cleavage at a defined position

Sorgenfrei, O., Linder, D., Karas, M., & Klein, A. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17888.x · Cited by 79

Allium Chemistry: Synthesis, Natural Occurrence, Biological Activity, and Chemistry of Se-Alk(en)ylselenocysteines and Their γ-Glutamyl Derivatives and Oxidation Products

Block, E., Birringer, M., Jiang, W., et al. (2000) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf001097b · Cited by 77

Thioredoxins: universal, yet specific thiol-disulfide redox cofactors.

Follmann, H., & Häberlein, I. (1997) · PubMed · Cited by 75

Substrate‐specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum: Biochemical and molecular analysis

Wagner, M., Sonntag, D., Grimm, R., Pich, A., Eckerskorn, C., Söhling, B., & Andreesen, J. R. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00107.x · Cited by 74

A selenium‐dependent and a selenium‐independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri

Vorholt, J. A., Vaupel, M., & Thauer, R. K. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.2931653.x · Cited by 74

The Role of Se, Mo and Fe in the Structure and Function of Carbon Monoxide Dehydrogenase

Meyer, O. O., Gremer, L., Ferner, R., Ferner, M., Dobbek, H., Gnida, M., Meyer‐Klaucke, W., & Huber, R. (2000) · Biological Chemistry · doi:10.1515/bc.2000.108 · Cited by 73

The Caenorhabditis elegans Homologue of Thioredoxin Reductase Contains a Selenocysteine Insertion Sequence (SECIS) Element That Differs from Mammalian SECIS Elements but Directs Selenocysteine Incorporation

Buettner, C., Harney, J. W., & Berry, M. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21598 · Cited by 73

Identification of d-Proline Reductase fromClostridium sticklandiias a Selenoenzyme and Indications for a Catalytically Active Pyruvoyl Group Derived from a Cysteine Residue by Cleavage of a Proprotein

Kabisch, U., Graentzdoerffer, A., Schierhorn, A., Rücknagel, K. P., Andreesen, J. R., & Pich, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8445 · Cited by 73

Selenocysteine incorporation directed from the 3′UTR: Characterization of eukaryotic EFsec and mechanistic implications

Berry, M. J., Tujebajeva, R. M., Copeland, P. R., Xu, X., Carlson, B. A., Martin, G. W., Low, S. C., Mansell, J. B., Grundner‐Culemann, E., Harney, J. W., et al. (2001) · BioFactors · doi:10.1002/biof.5520140104 · Cited by 72

Selenium Metabolism in Neptunia amplexicaulis

Burnell, J. N. (1981) · PLANT PHYSIOLOGY · doi:10.1104/pp.67.2.316 · Cited by 69

ISOLATION FROM ASTRAGALUS PECTINATUS OF A CRYSTALLINE AMINO ACID COMPLEX CONTAINING SELENIUM AND SULFUR

Horn, M. J., & Jones, D. B. (1941) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)72938-4 · Cited by 68

Significance of Selenocystathionine in an Australian Selenium-accumulating Plant, Neptunia amplexicaulis

Peterson, P. J., & Butler, G. (1967) · Nature · doi:10.1038/213599a0 · Cited by 67

Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria

Godeas, C., Sandri, G., & Panfili, E. (1994) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(94)90242-9 · Cited by 67

Purification and Characterization of a Glutathione Peroxidase from the Aloe vera Plant

Sabeh, F., Wright, T. A., & Norton, S. J. (2017) · Enzyme and Protein · doi:10.1159/000468662 · Cited by 66

Bioavailability of selenium accumulated by selenite-reducing bacteria

Combs, G. F., Garbisu, C., Yee, B. C., et al. (1996) · Biological Trace Element Research · doi:10.1007/bf02789163 · Cited by 65

Selenocysteyl-tRNAs recognize UGA in Betavulgaris, a higher plant, and in Gliocladium virens, a filamentous fungus

Hatfield, D. L., Choi, I. S., Mischke, S., & Owens, L. D. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91186-t · Cited by 65

Biosynthesis of 5-methylaminomethyl-2-selenouridine, a naturally occurring nucleoside in Escherichia coli tRNA

Wittwer, A. J., & Stadtman, T. C. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90507-2 · Cited by 64

Physiological mechanisms regulating the conversion of selenite to elemental selenium by Bacillus subtilis.

Garbisu, C., Gonzalez, S. A., Wh, Y., Yee, B. C., Dl, C., Yee, A., Nr, S., Otero, R., Bb, B., & Leighton, T. G. (1995) · PubMed · Cited by 63

Selenium‐containing xanthine dehydrogenase from Eubacterium barkeri

Schrader, T. H., Rienhöfer, A., & Andreesen, J. R. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00678.x · Cited by 62

A Selenium‐Containing Phospholipid‐Hydroperoxide Glutathione Peroxidase in Schistosoma mansoni

Maiorino, M., Roche‐Lestienne, C., Kieß, M., Koenig, K., Gawlik, D., Matthes, M., Naldini, E., Pierce, R. J., & Flohé, L. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0838w.x · Cited by 62

Antioxidant Defenses Influence HIV-1 Replication and Associated Cytopathic Effects

Sandstrom, P. A., Murray, J. L., Folks, T. M., & Diamond, A. M. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00023-9 · Cited by 61

Bioenergetics of Methanogenesis

Müller, V., Blaut, M., & Gottschalk, G. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2391-8_9 · Cited by 60

Functions of GI‐GPx: Lessons from selenium‐dependent expression and intracellular localization

Brigelius‐Flohé, R., Müller, C., Menard, J., Florian, S., Schmehl, K., & Wingler, K. (2001) · BioFactors · doi:10.1002/biof.5520140114 · Cited by 60

Functional expression of rat thioredoxin reductase: selenocysteine insertion sequence element is essential for the active enzyme

Fujiwara, N., Fujii, T., Fujii, J., & Taniguchi, N. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3400439 · Cited by 60

The Role of Selenocysteine 133 in Catalysis by the Human Type 2 Iodothyronine Deiodinase

Buettner, C., Harney, J. W., & Larsen, P. R. (2000) · Endocrinology · doi:10.1210/endo.141.12.7831 · Cited by 60

Properties of the Selenium- and Molybdenum-Containing Nicotinic Acid Hydroxylase from Clostridium barkeri

Gladyshev, V. N., Khangulov, S. V., & Stadtman, T. C. (1996) · Biochemistry · doi:10.1021/bi951793i · Cited by 60

The [NiFe] hydrogenases of Methanococcus voltae: genes, enzymes and regulation

Sorgenfrei, O., Müller, S., Pfeiffer, M. M., Sniezko, I., & Klein, A. R. (1997) · Archives of Microbiology · doi:10.1007/s002030050434 · Cited by 59

The effect of a selenium supplementation on the outcome of patients with severe systemic inflammation, burn and trauma

Gärtner, R., Albrich, W. C., & Angstwurm, M. (2001) · BioFactors · doi:10.1002/biof.5520140125 · Cited by 58

PHGPx and spermatogenesis

Roveri, A., Ursini, F., Flohé, L., & Maiorino, M. (2001) · BioFactors · doi:10.1002/biof.5520140127 · Cited by 57

Kinetics of the Interaction of Translation Factor SelB fromEscherichia coli with Guanosine Nucleotides and Selenocysteine Insertion Sequence RNA

Thanbichler, M. R., Böck, A., & Goody, R. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002496200 · Cited by 56

Effects of dietary selenium on the tissue concentrations of type I iodothyronine 5′-deiodinase and other selenoproteins

BEHNE, D., & Kyriakopoulos, A. M. (1993) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/57.2.310s · Cited by 56

Role of stoichiometry between mRNA, translation factor SeIB and selenocysteyl‐tRNA in selenoprotein synthesis

Tormay, P., Sawers, A., & Böck, A. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.881450.x · Cited by 52

Various functions of selenols and thiols in anaerobic Gram‐positive, amino acids‐utilizing bacteria

Andreesen, J. R., Wagner, M., Sonntag, D., Kohlstock, M., Harms, C., Gursinsky, T., Jäge, J., Parther, T., Kabisch, U., Gräntzdöffer, A., et al. (1999) · BioFactors · doi:10.1002/biof.5520100226 · Cited by 52

Formation of dimethyl selenide and trimethylselenonium from selenobetaine in the rat

Foster, S. J., Kraus, R. J., & Ganther, H. E. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90527-8 · Cited by 52

Cytokines suppress apoptosis independent of increases in reactive oxygen levels

Packham, G., Ashmun, R. A., & Cleveland, J. L. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.8.2792 · Cited by 51

Seleno amino compounds from Astragalus bisulcatus isolation and identification of γ-L-glutamyl-Se-methyl-seleno-L-cysteine and Se-methylseleno-L-cysteine

Nigam, S. N., & McConnell, W. B. (1969) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(69)90354-7 · Cited by 51

Bacterial selenocysteine synthase

Tormay, P., Wilting, R., Lottspeich, F., Mehta, P. K., Christen, P., & Böck, A. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2540655.x · Cited by 51

Evidence for a functional relevance of the selenocysteine residue in mammalian thioredoxin reductase

Marcocci, L., Flohé, L., & Packer, L. (1997) · BioFactors · doi:10.1002/biof.5520060305 · Cited by 50

Eukaryotic Selenocysteine Incorporation Follows a Nonprocessive Mechanism That Competes with Translational Termination

Nasim, T., Jaenecke, S., Beldüz, A. O., Kollmus, H., Flohé, L., & McCarthy, J. E. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.14846 · Cited by 49

Distribution of Free Seleno-amino Acids in Plant Tissue ofMelilotus indicaL. Grown in Selenium-Laden Soils

Guo, X., & Wu, L. (1998) · Ecotoxicology and Environmental Safety · doi:10.1006/eesa.1997.1628 · Cited by 49

Tissue specificity of selenoprotein gene expression in rats

Christensen, M. J., Cammack, P. M., & Wray, C. D. (1995) · The Journal of Nutritional Biochemistry · doi:10.1016/0955-2863(95)80004-v · Cited by 49

Protection against Peroxynitrite by Selenoproteins

Sies, H., Klotz, L., Sharov, V. S., Assmann, A., & Briviba, K. (1998) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1998-3-412 · Cited by 49

Catalytic properties of selenophosphate synthetases: Comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli

Lacourciere, G. M., & Stadtman, T. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.44 · Cited by 48

Selenium deficiency and human disease

Coppinger, R. J., & Diamond, A. M. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_18 · Cited by 47

Analysis of the Mouse Selenoprotein P Gene

Steinert, P., Bächner, D., & Flohé, L. (1998) · Biological Chemistry · doi:10.1515/bchm.1998.379.6.683 · Cited by 47

Knockout of cellular glutathione peroxidase affects selenium‐dependent parameters similarly in mice fed adequate and excessive dietary selenium

Cheng, W., Combs, G. F., & Lei, X. G. (1998) · BioFactors · doi:10.1002/biof.5520070403 · Cited by 46

Seleno-Cystathionine, a Pharmacologically Active Factor in the Seeds of Lecythis ollaria: Cytotoxic and Depilatory Effects of Extracts of Lecythis ollaria

Aronow, L., & Kerdel-Vegas, F. (1965) · Nature · doi:10.1038/2051185a0 · Cited by 46

Identification of Selenocysteine in the Proteins of Selenate-grown Vigna radiata

Brown, T. A., & Shrift, A. (1980) · PLANT PHYSIOLOGY · doi:10.1104/pp.66.4.758 · Cited by 45

Purification and properties of S-alkyl-L-cysteine lyase from seedlings of Acacia farnesiana Willd.

Mazelis, M., & Creveling, R. K. (1975) · Biochemical Journal · doi:10.1042/bj1470485 · Cited by 44

Mechanism of action of clostridial glycine reductase: isolation and characterization of a covalent acetyl enzyme intermediate

Arkowitz, R. A., & Abeles, R. H. (1991) · Biochemistry · doi:10.1021/bi00230a039 · Cited by 44

Selenium as a cancer preventive agent

Combs, G. F., & Lü, J. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_17 · Cited by 44

SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity

Persson, B. C., Böck, A., Jäckle, H., & Vorbrüggen, G. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1371 · Cited by 43

Acquisition of selenium tolerance by a selenium non‐accumulating Astragalus species via selection

Wang, Y., Böck, A., & Neuhierl, B. (1999) · BioFactors · doi:10.1002/biof.5520090102 · Cited by 43

Biosynthesis of selenocystathionine from selenate in Stanleya pinnata

Virupaksha, T. K., & Shrift, A. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)91436-7 · Cited by 42

Glutathione peroxidase activity and selenoprotein W levels in different brain regions of selenium-depleted rats

Sun, Y., Butler, J. A., & Whanger, P. D. (2001) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(00)00130-3 · Cited by 42

A New Toxicant Occurring Naturally in Certain Samples of Plant Foodstuffs

Franke, K. W. (1934) · Journal of Nutrition · doi:10.1093/jn/8.5.609 · Cited by 40

Expression and characterization of nonmammalian selenoprotein P in the zebrafish,Danio rerio

Tujebajeva, R. M., Ransom, D. G., Harney, J. W., & Berry, M. J. (2000) · Genes to Cells · doi:10.1046/j.1365-2443.2000.00375.x · Cited by 40

The presence of 4-selenouridine in Escherichia coli tRNA

Hoffman, J. L., & McConnell, K. P. (1974) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(74)90323-2 · Cited by 40

Selenocysteylation in Eukaryotes Necessitates the Uniquely Long Aminoacyl Acceptor Stem of Selenocysteine tRNASec

Sturchler, C., Hubert, N., Totsuka, T., Mizutani, T., Carbon, P., & Krol, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.31.18570 · Cited by 39

Isolation and characterization of a covalent selenocysteine intermediate in the glycine reductase system

Arkowitz, R. A., & Abeles, R. H. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00158a059 · Cited by 39

Barriers to heterologous expression of a selenoprotein gene in bacteria

Tormay, P., & Böck, A. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.3.576-582.1997 · Cited by 39

Regulation of Glutathione Peroxidases

Flohé, L., Wingender, E., & Brigelius‐Flohé, R. (1997) · Springer eBooks · doi:10.1007/978-1-4615-5981-8_17 · Cited by 38

Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri

Dilworth, G. L. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90176-5 · Cited by 38

Selenoprotein P: recent studies in rats and in humans.

Kristinae·Hill, & Raymondf·Burk (1997) · PubMed · Cited by 38

Study of mammalian selenocysteyl‐tRNA synthesis with [75Se]HSe−

Mizutani, T., Kurata, H., & Yamada, K. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80908-l · Cited by 36

Effect of Dietary Selenium on Plasma Selenoprotein P, Selenoprotein P1 and Glutathione Peroxidase in the Rat

Motsenbocker, M. A., & Tappel, A. L. (1984) · Journal of Nutrition · doi:10.1093/jn/114.2.279 · Cited by 34

Biosynthesis of Se-methylselenocysteine from selenite in selenium-accumulating plants

Shrift, A., & Virupaksha, T. K. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)91113-2 · Cited by 34

Chemical examination of seleniferous cabbage Brassica oleracea capitata

Hamilton, J. (1975) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60202a046 · Cited by 33

A Selenocysteine-Containing Peroxiredoxin from the Strictly Anaerobic Organism Eubacterium acidaminophilum

Söhling, B., Parther, T., Rücknagel, K. P., Wagner, M., & Andreesen, J. R. (2001) · Biological Chemistry · doi:10.1515/bc.2001.123 · Cited by 32

Comparative impacts of glutathione peroxidase-1 gene knockout on oxidative stress induced by reactive oxygen and nitrogen species in mouse hepatocytes

Yangxin, F. U., Porres, J. M., & Lei, X. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590687 · Cited by 32

Recognition of UGA as a selenocysteine codon in eukaryotes: a review of recent progress

Berry, M. J., & Larsen, P. R. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210827 · Cited by 31

Selenoproteins of the glutathione system

Flohé, L., & Brigelius‐Flohé, R. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_14 · Cited by 31

The Effect of Aging on Glutathione Peroxidase-I Knockout Mice—Resistance of the Lens to Oxidative Stress

Spector, A., Kuszak, J. R., Ma, W., & Wang, R.-R. (2001) · Experimental Eye Research · doi:10.1006/exer.2001.0980 · Cited by 30

Glutathione peroxidase and viral replication: Implications for viral evolution and chemoprevention

Diamond, A. M., Hu, Y. J., & Mansur, D. B. (2001) · BioFactors · doi:10.1002/biof.5520140126 · Cited by 30

Functional Analysis of Prokaryotic SELB proteins

Thanbichler, M. R., & Böck, A. (2001) · BioFactors · doi:10.1002/biof.5520140108 · Cited by 30

Interplay between termination and translation machinery in eukaryotic selenoprotein synthesis

Grundner‐Culemann, E., Martin, G. W., Tujebajeva, R. M., Harney, J. W., & Berry, M. J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4809 · Cited by 29

Enzyme catalysed α,β-elimination of selenocystathionine and selenocystine and their sulphur isologues by plant extracts

MCCLUSKEY, T. J., SCARF, A. R., & Anderson, J. W. (1986) · Phytochemistry · doi:10.1016/0031-9422(86)80067-x · Cited by 29

Selenocysteyl‐tRNA occurs in the diatom Thalassiosira and in the ciliate Tetrahymena

Hatfield, D. L., Lee, B. J., Price, N. M., et al. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb01891.x · Cited by 28

The Mammalian Homolog of the Frog Type II Selenodeiodinase Does Not Encode a Functional Enzyme in the Rat

Leonard, J. L., Leonard, D. M., Safran, M., Wu, R. J., Zapp, M. L., & Farwell, A. P. (1999) · Endocrinology · doi:10.1210/endo.140.5.6727 · Cited by 27

Incorporation of cysteine and selenocysteine into cystathionine and selenocystathionine by crude extracts of spinach

Dawson, J. C., & Anderson, J. W. (1988) · Phytochemistry · doi:10.1016/0031-9422(88)80747-7 · Cited by 27

The green technology of selenium phytoremediation

Bañuelos, G. S. (2001) · BioFactors · doi:10.1002/biof.5520140131 · Cited by 27

Selenium as an antiviral agent

Beck, M. A. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_19 · Cited by 25

The Occurrence of Selenocystathionine in Morinda Reticulata Benth A Toxic Seleniferous Plant

Peterson, P. J., & Butler, G. (1971) · Australian Journal of Biological Sciences · doi:10.1071/bi9710175 · Cited by 24

Biosynthesis of Se-methylselenocysteine and S-methylcysteine in Astragalus bisulcatus

Chen, D. M., Nigam, S. N., & McConnell, W. B. (1970) · Canadian Journal of Biochemistry · doi:10.1139/o70-197 · Cited by 23

Cloning, Expression, and Chromosomal Localization of the Rat Mitochondrial Capsule Selenoprotein Gene (MCS): The Reading Frame Does Not Contain Potential UGA Selenocysteine Codons

Adham, I. M., Tessmann, D., SOLIMAN, K. A., Murphy, D. B., Kremling, H., Szpirer, C., & Engel, W. (1996) · DNA and Cell Biology · doi:10.1089/dna.1996.15.159 · Cited by 21

Identity, evolution and function of selenoproteins and selenoprotein genes

Gladyshev, V. N. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_9 · Cited by 17

Biosynthesis of Se-Methylselenocysteine in lima beans

Nigam, S. N., & McConnell, W. B. (1973) · Phytochemistry · doi:10.1016/0031-9422(73)80018-4 · Cited by 16

An extended Escherichia coli “Selenocysteine Insertion Sequence” (SECIS) as a multifunctional RNA structure

Engelberg–Kulka, H., Liu, Z., Li, C., & Reches, M. (2001) · BioFactors · doi:10.1002/biof.5520140109 · Cited by 15

Comparative enzymology of cystathionine and selenocystathionine synthesis of selenium-accumulator and non-accumulator plants

Dawson, J. C., & Anderson, J. W. (1989) · Phytochemistry · doi:10.1016/0031-9422(89)85006-x · Cited by 15

Isolation and identification of two isomeric glutamylselenocystathionines from the seeds of Astragalus pectinatus

Nigam, S., & McConnell, W. B. (1976) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(76)90352-4 · Cited by 14

Selenoproteins of the thioredoxin system

Holmgren, A. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_15 · Cited by 14

Expression of Phospholipid Hydroperoxide Glutathione Peroxidase(PHGPx) mRNA in Rat Testes.

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