Boyington, Jeffrey C., Gladyshev, Vadim, Khangulov, Sergei V., Stadtman, Thressa C., Sun, Peter D.
Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and...
Nosovelov, Sergey V., Lobanov, Alexey V., Hua, Deame, Kasaikina, Marina V., Hatfield, Dolph L., Gladyshev, Vadim
Selenoproteins are an elite group of proteins containing a rare amino acid, selenocysteine (Sec), encoded by the codon, UGA. In eukaryotes, incorporation of Sec requires a Sec insertion sequence...
Novoselov, Sergey V., Lobanov, Alexey V., Hua, Deame, Kasaikina, Marina V., Hatfield, Dolph L., Gladyshev, Vadim
Selenoproteins are an elite group of proteins containing a rare amino acid, selenocysteine (Sec), encoded by the codon, UGA. In eukaryotes, incorporation of Sec requires a Sec insertion sequence...
Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis (2007)
Xu, Xue-Ming, Carlson, Bradley A., Irons, Robert, Mix, Heiko, Zhong, Nianxin, Gladyshev, Vadim, ...
Selenophosphate synthetase (SelD) generates the selenium donor for selenocysteine biosynthesis in eubacteria. One homologue of SelD in eukaryotes is SPS1 (selenophosphate synthetase 1) and a second...
High-Throughput Identification of Catalytic Redox-Active Cysteine Residues (2007)
Fomenko, Dmitri E., Xing, Weibing, Adair, Blakely M., Thomas, David J., Gladyshev, Vadim
Cysteine (Cys) residues often play critical roles in proteins; however, identification of their specific functions has been limited to case-by-case experimental approaches. We developed a procedure...
Fomenko, Dmitri E., Xing, Weibing, Adair, Blakely M., Thomas, David J., Gladyshev, Vadim
Identification of redox-active Cys by homology to selenoproteins Identification of Cys/Sec pairsStatistical analysis of redox-active Cys neighborhoodsAdoMet-dependent methyltransferaseActivity of...
Biosynthesis of Selenocysteine on Its tRNA in Eukaryotes (2007)
Xu, Xue-Ming, Carlson, Bradley A., Mix, Heiko, Zhang, Yan, Saira, Kazima, Glass, Richard S., ...
Selenocysteine (Sec) is cotranslationally inserted into protein in response to UGA codons and is the 21st amino acid in the genetic code. However, the means by which Sec is synthesized in eukaryotes...
Mix, Heiko, Lobanov, Alexey V., Gladyshev, Vadim
Expression of selenocysteine (Sec)-containing proteins requires the presence of a cis-acting mRNA structure, called selenocysteine insertion sequence (SECIS) element. In bacteria, this structure is...
Zhang, Yan, Romero, Hector, Salinas, Gustavo, Gladyshev, Vadim
Background: Selenocysteine (Sec) is co-translationally inserted into protein in response to UGA codons. It occurs in oxidoreductase active sites and often is catalytically superior to cysteine (Cys)....
Lobanov, Alexey V., Gromer, Stephan, Salinas, Gustavo, Gladyshev, Vadim
Proteins containing the 21st amino acid selenocysteine (Sec) are present in the three domains of life. However, within lower eukaryotes, particularly parasitic protists, the dependence on the trace...
Mix, Heiko, Lobanov, Alexey V., Gladyshev, Vadim
Figure S1. Nucleotide sequence alignment of GPx4 sequences. For: M. musculus, H. sapiens, G. gallus, A. thaliana, Fowlpox virus, and Canarypox virus Figure S2. Alignment of GPx4 SECIS elements. For:...
Is there a twenty third amino acid in the genetic code? (2006)
Lobanov, Alexey V., Kryukov, Gregory V., Hatfield, Dolph L., Gladyshev, Vadim
The universal genetic code includes 20 common amino acids. In addition, selenocysteine (Sec) and pyrrolysine (Pyl), known as the twenty first and twenty second amino acids, are encoded by UGA and...
Kim, Hwa-Young, Gladyshev, Vadim
Background: Methionine sulfoxide reduction is an important protein repair pathway that protects against oxidative stress, controls protein function and has a role in regulation of aging. There are...
The Plasmodium selenoproteome (2006)
Lobanov, Alexey V., Delgado, Cesar, Rahlfs, Stefan, Novoselov, Sergey V., Kryukov, Gregory V., Gromer, Stephan, ...
The use of selenocysteine (Sec) as the 21st amino acid in the genetic code has been described in all three major domains of life. However, within eukaryotes, selenoproteins are only known in animals...
Kim, Hwa-Young, Gladyshev, Vadim
Selenocysteine (Sec) is found in active sites of several oxidoreductases in which this residue is essential for catalytic activity. However, many selenoproteins have fully functional orthologs,...
Evolution of selenium utilization traits (2005)
Romero, Hector, Zhang, Yan, Gladyshev, Vadim, Salinas, Gustavo
Background: The essential trace element selenium is used in a wide variety of biological processes. Selenocysteine (Sec), the 21st amino acid, is co-translationally incorporated into a restricted set...
Selenocysteine insertion directed by the 3'-UTR SECIS element in Escherichia coli (2005)
Su, Dan, Li, Yehua, Gladyshev, Vadim
Co-translational insertion of selenocysteine (Sec) into proteins in response to UGA codons is directed by selenocysteine insertion sequence (SECIS) elements. In known bacterial selenoprotein genes,...
Taskov, Kalin, Chapple, Charles, Kryukov, Gregory V., Castenello, Sergi, Lobanov, Alexei V., Korotkov, Konstantin V., ...
Selenocysteine (Sec) is co-translationally inserted into selenoproteins in response to codon UGA with the help of the selenocysteine insertion sequence (SECIS) element.The number of...
The microbial selenoproteome of the Sargasso Sea (2005)
Zhang, Yan, Fomenko, Dmitri E., Gladyshev, Vadim
Background: Selenocysteine (Sec) is a rare amino acid which occurs in proteins in major domains of life. It is encoded by TGA, which also serves as the signal for termination of translation,...
Kim, Hwa-Young, Gladyshev, Vadim
Methionine residues in proteins are susceptible to oxidation by reactive oxygen species, but can be repaired via reduction of the resulting methionine sulfoxides by methionine-S-sulfoxide reductase...
Kwon, So Yeon, Badenhorst, Paul, Martin-Romero, F. Javier, Carlson, Bradley A., Paterson, Bruce M., Gladyshev, Vadim, ...
Selenium is implicated in many diseases, including cancer, but its function at the molecular level is poorly understood. BthD is one of three selenoproteins recently identified in Drosophila. To...
Chlamydomonas reinhardtii selenocysteine tRNA [Ser]Sec (2003)
Rao, Mahadev, Carlson, Bradley A., Novoselov, Sergey V., Weeks, Donald P., Gladyshev, Vadim, Hatfield, Dolph L.
Eukaryotic selenocysteine (Sec) protein insertion machinery was thought to be restricted to animals, but the occurrence of both Sec-containing proteins and the Sec insertion system was recently found...
Selective Removal of the Selenocysteine tRNA [Ser]Sec Gene (Trsp) in Mouse Mammary Epithelium (2003)
Kumaraswamy, Easwari, Carlson, Bradley A., Morgan, Fanta, Miyoshi, Keiko, Robinson, Gertraud W., Su, Dan, ...
Mice homozygous for an allele encoding the selenocysteine (Sec) tRNA [Ser]Sec gene (Trsp) flanked by loxP sites were generated. Cre recombinase-dependent removal of Trsp in these mice was lethal to...
Novoselov, Sergey V., Rao, Mahadev, Onoshko, Natalia V., Zhi, Huijun, Kryukov, Gregory V., Xiang, Youbin, ...
Known eukaryotic selenocysteine (Sec)-containing proteins are animal proteins, whereas selenoproteins have not been found in yeast and plants. Surprisingly, we detected selenoproteins in a member of...
Minireview: How Selenium Has Altered Our Understanding of the Genetic Code (2002)
Hatfield, Dolph L., Gladyshev, Vadim
Selenium is an essential micronutrient in the diet of many life forms, including humans and other mammals. Significant health benefits have been attributed to this element. It is rapidly becoming...
Korotkov, Konstantin V., Novoselov, Sergey V., Hatfield, Dolph L., Gladyshev, Vadim
Selenocysteine (Sec), the 21st amino acid in protein, is encoded by UGA. The Sec insertion sequence (SECIS) element, which is the stem-loop structure present in 3' untranslated regions (UTRs) of...
Moustafa, Mohamed E., Carlson, Bradley A., El-Saadani, Muhammed A., Kryukov, Gregory V., Sun, Qi-An, Harney, John W., ...
Selenocysteine (Sec) tRNA (tRNA [Ser]Sec) serves as both the site of Sec biosynthesis and the adapter molecule for donation of this amino acid to protein. The consequences on selenoprotein...
Gladyshev, Vadim, Diamond, Alan M., Hatfield, Dolph L.
The 15 kDa selenoprotein (Sepl5) is one of several recently identified selenoproteins. It contains a single selenocysteine residue in the middle of a 162-amino acid open reading frame and has no...
Chapter 25. Selenium in biology and human health: Controversies and perspectives (2001)
Important unresolved questions raised by the contributors of this book and addressing roles of selenium in biology and human health are discussed. Resolving major scientific controversies in the...
Gladyshev, Vadim, Stadtman, Thressa C., Hatfield, Dolph L., Jeang, Kuan-Teh
It has been observed previously that plasma selenium and glutathione levels are subnormal in HIV-infected individuals, and plasma glutathione peroxidase activity is decreased. Under these conditions...
Gladyshev, Vadim, Jeang, Kuan-Teh, Stadtman, Thressa C.
The possible relationship of selenium to immunological function which has been suggested for decades was investigated in studies on selenuim metabolism in human T cells. One of the major 75Se-labeled...
Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli (1994)
Gladyshev, Vadim, Khangulov, Sergei V., Axley, Milton J., Stadtman, Thressa A.
Formate dehydrogenase H from Escherichia col contains multiple redox centers, which include a molybdopterin cofactor, an iron-sulfur center, and a selenocysteine residue (SeCys-140 in the polypeptide...
Gladyshev, Vadim, Khangulov, Sergei V., Stadtman, Thressa C.
Nicotinic acid hydroxylase from Clostidum barkeri contains selenium in an unidentified form that is dissociated as a low molecular weight compound upon denaturation of the enzyme. Other cofactors of...