Research Topics
Genomes and Genes
| Vadim N GladyshevSummaryAffiliation: University of Nebraska Country: USA Publications
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Detail Information
Publications
Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residuesYan Zhang
Department of Biochemistry, University of Nebraska, 1901 Vine Street, Lincoln, NE 68588-0664, USA
Genome Biol 7:R94. 2006....- Comparative genomic analyses of nickel, cobalt and vitamin B12 utilizationYan Zhang
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, NE 68588 0664, USA
BMC Genomics 10:78. 2009..Although a number of Ni and Co-dependent enzymes have been characterized, systematic evolutionary analyses of utilization of these metals are limited... 
Evolution of selenocysteine-containing proteins: significance of identification and functional characterization of selenoproteinsV N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Biofactors 14:87-92. 2001..Further understanding of the evolution of selenoproteins as well as biological properties and biomedical applications of the trace element selenium requires identification and functional characterization of all mammalian selenoproteins...- Thioredoxin and peptide methionine sulfoxide reductase: convergence of similar structure and function in distinct structural foldsVadim N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
Proteins 46:149-52. 2002..The data suggest that similar structures and functions of Trx and PMSR were acquired independently during evolution and point to a general strategy of identifying new redox regulatory proteins... - Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2V N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 276:30374-80. 2001..The Grx2 structural model suggested a common reaction mechanism for this class of proteins. The data provide the first example of a mitochondrial Grx and also indicate the occurrence of a second functional Grx in mammals... - Identification of trace element-containing proteins in genomic databasesVadim N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
Annu Rev Nutr 24:579-96. 2004..It also should be possible to search for entire sets of other trace element-associated proteins, such as metal-containing proteins, although methods for their identification are still in development... - Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturationDan Su
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 280:26491-8. 2005..Together, TGR and GPx4 can serve as a novel disulfide bond formation system. Both enzymes contain a catalytic selenocysteine consistent with the role of selenium in male reproduction... - Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiaeDung Tien Le
Department of Biochemistry and Redox Biology Center, University of Nebraska Lincoln, Lincoln, Nebraska 68588, USA
J Biol Chem 284:4354-64. 2009..The data show that fRMsr is the main enzyme responsible for the reduction of free Met-R-SO in S. cerevisiae... - High-throughput identification of catalytic redox-active cysteine residuesDmitri E Fomenko
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Science 315:387-9. 2007..Rapid accumulation of sequence information from genomic and metagenomic projects should allow detection of many additional oxidoreductase families as well as identification of redox-active Cys in these proteins... - Mammalian thioredoxin reductase 1: roles in redox homoeostasis and characterization of cellular targetsAnton A Turanov
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, NE 68588, U S A
Biochem J 430:285-93. 2010..Diminished hepatic TR1 function was associated with elevated Trx1 levels, but this protein was mostly in the oxidized state. Overall, this study provides evidence for the key role of the TR1-Trx1 pair in redox homoeostasis... - SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like familyAlexander Dikiy
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Biochemistry 46:6871-82. 2007..Rdx12 was found to interact with glutathione peroxidase 1, whereas 14-3-3 protein was identified as one of the targets of mammalian SelW, suggesting a mechanism for redox regulation of the 14-3-3 family of proteins... - Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductaseQi An Sun
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
Biochemistry 44:14528-37. 2005.... - MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein formDmitri E Fomenko
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 284:5986-93. 2009..Overall, this study established an important contribution of MsrB1 to the redox control in mouse liver and kidney and identified a novel form of this protein... - Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductasesHwa Young Kim
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska, USA
PLoS Biol 3:e375. 2005..The data also suggested that Sec- and Cys-containing oxidoreductases require distinct sets of active-site features that maximize their catalytic efficiencies and provide strategies for protein design with improved catalytic properties... - The microbial selenoproteome of the Sargasso SeaYan Zhang
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Genome Biol 6:R37. 2005..Herein, we characterized the selenoproteome of the largest microbial sequence dataset, the Sargasso Sea environmental genome project... - Regulation of selenoproteins and methionine sulfoxide reductases A and B1 by age, calorie restriction, and dietary selenium in miceSergey V Novoselov
Department of Biochemistry, University of Nebraska, Lincoln, NE, USA
Antioxid Redox Signal 12:829-38. 2010..Taken together, these findings better define dietary regulation of methionine sulfoxide reduction and selenoprotein expression in mice with regard to age, calorie restriction, dietary Se, and a combination of these factors... - Analysis of methionine/selenomethionine oxidation and methionine sulfoxide reductase function using methionine-rich proteins and antibodies against their oxidized formsDung Tien Le
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, USA
Biochemistry 47:6685-94. 2008..These findings, reagents, assays, and approaches should facilitate research and applications in the area of Met sulfoxide reduction, oxidative stress, and aging... - Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distributionHwa Young Kim
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Biochemistry 44:8059-67. 2005.... - Identification and characterization of a selenoprotein family containing a diselenide bond in a redox motifValentina A Shchedrina
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Proc Natl Acad Sci U S A 104:13919-24. 2007..In a bacterial expression system, we directly demonstrated the formation of a diselenide bond between the two Sec, establishing it as the first diselenide bond found in a natural protein... - Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial lifeAlexey V Lobanov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Genome Biol 8:R198. 2007..Selenoproteins occur in both eukaryotes and prokaryotes, but the selenoprotein content of organisms (selenoproteome) is highly variable and some organisms do not utilize Sec at all... - Thiol peroxidases mediate specific genome-wide regulation of gene expression in response to hydrogen peroxideDmitri E Fomenko
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Proc Natl Acad Sci U S A 108:2729-34. 2011..The data suggest that thiol peroxidases sense and transfer oxidative signals to the signaling proteins and regulate transcription, whereas a direct interaction between H(2)O(2) and other cellular proteins plays a secondary role... - X-ray fluorescence microscopy reveals the role of selenium in spermatogenesisSebastian Kehr
Redox Biology Center and Department of Biochemistry, University of Nebraska, Lincoln, 68588, USA
J Mol Biol 389:808-18. 2009..Overall, the use of XFM allowed visualization of tissue and cellular Se and provided important insights in the role of this and other trace elements in spermatogenesis... - Selenoprotein H is a nucleolar thioredoxin-like protein with a unique expression patternSergey V Novoselov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 282:11960-8. 2007..Overall, these data establish SelH as a novel nucleolar oxidoreductase and suggest that some functions in this compartment are regulated by redox and dependent on the trace element selenium... - Identity and functions of CxxC-derived motifsDmitri E Fomenko
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664, USA
Biochemistry 42:11214-25. 2003..Each of the CxxC-derived motifs was also observed in natural selenium-containing proteins, in which selenocysteine was present in place of a catalytic cysteine... - Reduced reliance on the trace element selenium during evolution of mammalsAlexey V Lobanov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Genome Biol 9:R62. 2008.... - CUG start codon generates thioredoxin/glutathione reductase isoforms in mouse testesMaxim V Gerashchenko
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 285:4595-602. 2010..This study shows that CUG codon is used as an inefficient start codon to generate protein isoforms in mouse... - Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiaeStefano M Marino
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, USA
Biochemistry 49:7709-21. 2010.... - A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferaseVyacheslav M Labunskyy
Department of Biochemistry, University of Nebraska, Lincoln, 68588, USA
J Biol Chem 280:37839-45. 2005..These data indicate that the cysteine-rich domain of Sep15 exclusively mediates protein-protein interactions with GT... - Trends in selenium utilization in marine microbial world revealed through the analysis of the global ocean sampling (GOS) projectYan Zhang
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska, USA
PLoS Genet 4:e1000095. 2008..Overall, our study provides insights into global trends in microbial selenium utilization in marine environments... - Genetic code supports targeted insertion of two amino acids by one codonAnton A Turanov
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, NE 68588, USA
Science 323:259-61. 2009..Thus, the genetic code supports the use of one codon to code for multiple amino acids... - Nematode selenoproteome: the use of the selenocysteine insertion system to decode one codon in an animal genome?Kalin Taskov
Department of Biochemistry, University of Nebraska Lincoln, NE 68588, USA
Nucleic Acids Res 33:2227-38. 2005.... - Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductasesHwa Young Kim
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Mol Biol Cell 15:1055-64. 2004..The data suggested that different cellular compartments in mammals maintain a system for repair of oxidized methionine residues and that this function is tuned in enzyme- and stereo-specific manner... - Characterization of mammalian selenoproteomesGregory V Kryukov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Science 300:1439-43. 2003..The human selenoproteome consists of 25 selenoproteins... - Selenium metabolism in Trypanosoma: characterization of selenoproteomes and identification of a Kinetoplastida-specific selenoproteinAlexey V Lobanov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Nucleic Acids Res 34:4012-24. 2006..Overall, these data establish that Trypanosoma, Leishmania and likely other Kinetoplastida utilize and depend on the trace element selenium, and this dependence is due to occurrence of selenium in at least three selenoproteins... - In silico identification of genes involved in selenium metabolism: evidence for a third selenium utilization traitYan Zhang
Redox Biology Center and Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
BMC Genomics 9:251. 2008..Selenophosphate synthetase (SelD) is required for both utilization traits. However, previous research also revealed SelDs in two organisms lacking Sec and SeU, suggesting a possible additional use of Se that is dependent on SelD... - Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteinsValentina A Shchedrina
Redox Biology Center and Department of Biochemistry, University of Nebraska, Lincoln, NE, USA
Antioxid Redox Signal 12:839-49. 2010..This review discusses evolution and structure-function relations of the ER-resident selenoproteins and summarizes recent findings on these proteins, which reveal the emerging important role of selenium and selenoproteins in ER function... - Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductaseR Abhilash Kumar
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 277:37527-35. 2002..A Drosophila MsrA gene was also cloned, and the recombinant enzyme was found to be metal-free and specific for methionine S-sulfoxide and to employ a similar sulfenic acid/disulfide mechanism... - Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductasesHwa Young Kim
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
BMC Mol Biol 7:11. 2006..In mammals, a single MsrA gene is known, however, its product is present in cytosol, nucleus, and mitochondria. In contrast, three mammalian MsrB genes have been identified whose products are located in different cellular compartments... - Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processingXinwen Liang
Department of Biochemistry and Redox Biology Center, University of Nebraska Lincoln, Lincoln, Nebraska, United States of America
PLoS ONE 5:e11497. 2010..MsrB1 is a selenocysteine-containing cytosolic/nuclear Msr with high expression in liver and kidney... - Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide reductaseHwa Young Kim
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Biochem Biophys Res Commun 320:1277-83. 2004..The data suggest that, in mice, MsrB3 is largely or exclusively an ER-resident protein, and that the reduction of methionine-R-sulfoxides in different cellular compartments is provided by individual MsrB isozymes... - The Plasmodium selenoproteomeAlexey V Lobanov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Nucleic Acids Res 34:496-505. 2006..Dependence of the plasmodial parasites on selenium suggests possible strategies for antimalarial drug development... - Is there a twenty third amino acid in the genetic code?Alexey V Lobanov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Trends Genet 22:357-60. 2006..Our data suggest that the occurrence of additional amino acids that are widely distributed and genetically encoded is unlikely... - Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of agingAhmet Koc
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Proc Natl Acad Sci U S A 101:7999-8004. 2004..The data also suggest a model wherein factors implicated in aging (for example, ROS) may influence the lifespan yet not be the cause of aging... - Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein familySergey V Novoselov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Biochem J 394:575-9. 2006..Phylogenetic analyses of Sep15 family members suggest that Fep15 evolved by gene duplication... - Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductaseAnton A Turanov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
J Biol Chem 281:22953-63. 2006..Overall, these data establish that the function of TR3 is not limited to its role in Trx2 reduction... - Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1Dan Su
Department of Biochemistry, University of Nebraska--Lincoln, Lincoln, Nebraska 68588, USA
Biochemistry 43:12177-88. 2004..Our data also suggest that various N-terminal extensions in mammalian TRs are often expressed in testes... - A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteinsDan Su
Department of Biochemistry, Univeristy of Nebraska Lincoln, Lincoln, Nebraska 68588 0664, USA
Biochemistry 46:6903-10. 2007..Taken together, our data suggest that an important function of Pro75 in human thioredoxin, and likely other members of this superfamily, is to prevent metal binding by the reactive thiolate-based active site... - The prokaryotic selenoproteomeGregory V Kryukov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664, USA
EMBO Rep 5:538-43. 2004..Characterization of selenoproteomes allows interpretation of other UGA codons in completed genomes of prokaryotes as terminators, addressing the UGA dual-function problem... - An algorithm for identification of bacterial selenocysteine insertion sequence elements and selenoprotein genesYan Zhang
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Bioinformatics 21:2580-9. 2005..The availability of the bacterial SECIS consensus and the tool for identification of these structures should help in correct annotation of selenoprotein genes and characterization of bacterial selenoproteomes... - Pyrrolysine and selenocysteine use dissimilar decoding strategiesYan Zhang
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588-0664, USA
J Biol Chem 280:20740-51. 2005..Thus, Sec and Pyl follow dissimilar decoding and evolutionary strategies... - A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residuesStefano M Marino
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska, USA
PLoS Comput Biol 5:e1000383. 2009..This study provides insights into the structural properties of catalytic redox-active Cys and should further help to recognize thiol oxidoreductases in protein sequence and structure databases... - Mammals reduce methionine-S-sulfoxide with MsrA and are unable to reduce methionine-R-sulfoxide, and this function can be restored with a yeast reductaseByung Cheon Lee
Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
J Biol Chem 283:28361-9. 2008.... - Compartmentalization and regulation of mitochondrial function by methionine sulfoxide reductases in yeastAlaattin Kaya
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, USA
Biochemistry 49:8618-25. 2010..These results show that oxidative stress contributes to mitochondrial dysfunction through oxidation of methionine residues in proteins located in different cellular compartments... - New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elementsG V Kryukov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
J Biol Chem 274:33888-97. 1999..SelR homologs were present in every organism characterized by complete genome sequencing. The data suggest applicability of SECISearch for identification of new selenoprotein genes in nucleotide data bases... - Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductaseGregory V Kryukov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Proc Natl Acad Sci U S A 99:4245-50. 2002.... - CxxS: fold-independent redox motif revealed by genome-wide searches for thiol/disulfide oxidoreductase functionDmitri E Fomenko
Department of Biochemistry, University of Nebraska Lincoln, 68588 0664, USA
Protein Sci 11:2285-96. 2002..The data also indicate a general approach of genome-wide identification of redox proteins by searching for simple conserved motifs within secondary structure patterns... - Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtiiSergey V Novoselov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
EMBO J 21:3681-93. 2002.... - Functions and evolution of selenoprotein methionine sulfoxide reductasesByung Cheon Lee
Redox Biology Center and Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Biochim Biophys Acta 1790:1471-7. 2009..Msrs have roles in protecting cellular proteins from oxidative stress and through this function they may regulate lifespan in several model organisms... - SECIS elements in the coding regions of selenoprotein transcripts are functional in higher eukaryotesHeiko Mix
Department of Biochemistry, University of Nebraska Beadle Center, Lincoln, NE 68588, USA
Nucleic Acids Res 35:414-23. 2007..Our data provide evidence that the location of the SECIS element in the untranslated region is not a functional necessity but rather is an evolutionary adaptation to enable a more efficient synthesis of selenoproteins... - High content of proteins containing 21st and 22nd amino acids, selenocysteine and pyrrolysine, in a symbiotic deltaproteobacterium of gutless worm Olavius algarvensisYan Zhang
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Nucleic Acids Res 35:4952-63. 2007..Anaerobic conditions and consistent selenium supply might be the factors that support the use of amino acids that extend the genetic code... - Functional diversity of cysteine residues in proteins and unique features of catalytic redox-active cysteines in thiol oxidoreductasesDmitri E Fomenko
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, NE 68588 0664, USA
Mol Cells 26:228-35. 2008.... - Comparative analysis of selenocysteine machinery and selenoproteome gene expression in mouse brain identifies neurons as key functional sites of selenium in mammalsYan Zhang
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 283:2427-38. 2008..Overall, this study suggests that the main functions of selenium in mammals are confined to certain neurons in the brain... - Selenoprotein deficiency and high levels of selenium compounds can effectively inhibit hepatocarcinogenesis in transgenic miceSergey V Novoselov
Department of Biochemistry, University of Nebraska, N 151 Beadle Center, 1901 Vine Street, Lincoln, NE 68588, USA
Oncogene 24:8003-11. 2005..Since dietary Se may have opposing effects on cancer, it is important to identify the subjects who will benefit from Se supplementation as well as those who will not... - A highly efficient form of the selenocysteine insertion sequence element in protozoan parasites and its use in mammalian cellsSergey V Novoselov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Proc Natl Acad Sci U S A 104:7857-62. 2007..It contains an SBP2 gene and the most efficient tested SECIS element: an AUGA mutant of the GGGA-type Toxoplasma SelT structure... - Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylationStefano M Marino
Department of Biochemistry and Redox Biology Center, University of Nebraska Lincoln, Lincoln, NE 68588, USA
J Mol Biol 395:844-59. 2010..For proteins lacking the revised motif, we discuss alternative mechanisms including a potential role of nitrosoglutathione as a trans-acting agent... - Overexpression of methionine-R-sulfoxide reductases has no influence on fruit fly agingValentina A Shchedrina
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, NE 68588, USA
Mech Ageing Dev 130:429-43. 2009..Thus, MsrA and MsrB, the two proteins with similar function in antioxidant protein repair, have different effects on aging in fruit flies... - Mammalian selenoprotein gene signature: identification and functional analysis of selenoprotein genes using bioinformatics methodsGregory V Kryukov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Methods Enzymol 347:84-100. 2002 - Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductasesQ A Sun
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 274:24522-30. 1999..These observations identify the carboxyl-terminal selenocysteine of TR1 as a cellular redox sensor and support an essential role for mammalian TR isozymes in redox-regulated cell signaling... - Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residuesG V Kryukov
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Genes Cells 5:1049-60. 2000..Selenium is present in vertebrate proteins in the form of selenocysteine (Sec), the 21st natural amino acid in protein which is encoded by UGA... - Non-animal origin of animal thioredoxin reductases: implications for selenocysteine evolution and evolution of protein function through carboxy-terminal extensionsSergey V Novoselov
Department of Biochemistry, University of Nebraska, Lincoln 68588-0664, USA
Protein Sci 12:372-8. 2003..Our data implicate carboxy-terminal extension of proteins as a general mechanism of evolution of new protein function... - Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicingQ A Sun
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
J Biol Chem 276:3106-14. 2001..Multiple transcription start sites within TR genes may be relevant to complex regulation of expression and/or organelle- and cell type-specific location of animal thioredoxin reductases... - Levels of major selenoproteins in T cells decrease during HIV infection and low molecular mass selenium compounds increaseV N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Proc Natl Acad Sci U S A 96:835-9. 1999..In contrast to selenoproteins, low molecular mass [75Se]compounds accumulated during HIV infection and migrated as a diffuse band near the front of SDS/PAGE gels... - Selenocysteine-containing proteins in mammalsV N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
J Biomed Sci 6:151-60. 1999..This review describes known mammalian selenoproteins and discusses recent developments and future directions in the selenium field... - Contrasting patterns of regulation of the antioxidant selenoproteins, thioredoxin reductase, and glutathione peroxidase, in cancer cellsV N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska, 68588, USA
Biochem Biophys Res Commun 251:488-93. 1998..The data suggest that additional studies on selenoprotein regulation in different cancers are required to evaluate future implementation of selenium as a dietary supplement in individuals at risk for developing certain cancers... - Selenocysteine-containing thioredoxin reductase in C. elegansV N Gladyshev
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Biochem Biophys Res Commun 259:244-9. 1999..The data show that TR-Se is the major naturally occurring selenoprotein in C. elegans, and suggest an important role for selenium and the thioredoxin system in this organism... - A new human selenium-containing protein. Purification, characterization, and cDNA sequenceV N Gladyshev
Section on the Molecular Biology of Selenium, Basic Research Laboratory, NCI, National Institutes of Health, Bethesda, Maryland 20892
J Biol Chem 273:8910-5. 1998..The discovery of a new human selenoprotein provides an additional example of the role of selenium in mammalian systems... - Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cellsK V Korotkov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
J Biol Chem 276:15330-6. 2001..This report provides the first example of the ER-resident selenoprotein and suggests a possible role of the trace element selenium in the quality control of protein folding... - Genomics perspective on disulfide bond formationDmitri E Fomenko
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA
Antioxid Redox Signal 5:397-402. 2003..Emerging evidence suggests that these ER functions might be assisted by mammalian selenocysteine-containing oxidoreductases Sep15 and SelM... - Molybdoproteomes and evolution of molybdenum utilizationYan Zhang
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
J Mol Biol 379:881-99. 2008..Overall, our data provide new insights into Mo utilization and show its wide occurrence, yet limited use of this metal in individual organisms in all three domains of life... - Eukaryotic selenoproteins and selenoproteomesAlexey V Lobanov
Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, NE 68588, USA
Biochim Biophys Acta 1790:1424-8. 2009..We also discuss selenoprotein functions and evolutionary trends in the use of these proteins in eukaryotes. Functional analysis of selenoproteins is critical for better understanding of the role of selenium in human health and disease... - Mammalian selenoprotein in which selenocysteine (Sec) incorporation is supported by a new form of Sec insertion sequence elementKonstantin V Korotkov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Mol Cell Biol 22:1402-11. 2002..SelM is expressed in a variety of tissues, with increased levels in the brain. It is localized to the perinuclear structures, and its N-terminal signal peptide is necessary for protein translocation... - Comparative genomic analyses of copper transporters and cuproproteomes reveal evolutionary dynamics of copper utilization and its link to oxygenPerry G Ridge
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska, USA
PLoS ONE 3:e1378. 2008..Prokaryotic cuproproteomes were small and dominated by a single protein, cytochrome c oxidase. The data are consistent with the idea that proteins evolved to utilize copper following the oxygenation of the Earth... - Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systemsQ A Sun
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588 0664, USA
Proc Natl Acad Sci U S A 98:3673-8. 2001.... - Redox regulation of cell signaling by thioredoxin reductasesQi-An Sun
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Methods Enzymol 347:451-61. 2002 - Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductasesHwa-Young Kim
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Biochemistry 45:13697-704. 2006..Overall, this study demonstrates that sporadically evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advantages provided by Sec in these and likely other thiol-dependent oxidoreductases... - Semisynthesis and characterization of mammalian thioredoxin reductaseBrian Eckenroth
Department of Biochemistry, University of Vermont, 89 Beaumont Avenue, Given Laboratory, Room B413, Burlington, Vermont 05405, USA
Biochemistry 45:5158-70. 2006..This noncovalent peptide-enzyme complex has 350-500-fold lower activity than the semisynthetic enzyme produced by peptide ligation... - Selenoproteinless animals: selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesisAlexey V Lobanov
Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA
Protein Sci 17:176-82. 2008..Since SPS1 evolved from a protein that utilizes selenium for Sec biosynthesis, an attractive possibility is that SPS1 may define a new pathway of selenium utilization in animals... - Analysis of selenocysteine-containing proteinsV N Gladyshev
University of Nebraska, Lincoln, Nebraska, USA
Curr Protoc Protein Sci . 2001..This unit provides an overview of known selenocysteine-containing proteins, examples of targeted incorporation of selenium into proteins, and methods specific for selenoprotein identification and characterization... - Reconsidering the evolution of eukaryotic selenoproteins: a novel nonmammalian family with scattered phylogenetic distributionSergi Castellano
Grup de Recerca en Informàtica Biomèdica, Institut Municipal d Investigacio Medica, Universitat Pompeu Fabra, Dr Aiguader 80, 08003 Barcelona, Catalonia, Spain
EMBO Rep 5:71-7. 2004..Our data indicate a scattered evolutionary distribution of selenoproteins in eukaryotes, and suggest that, contrary to the picture emerging from data available so far, other taxa-specific selenoproteins probably exist... - NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like familyAndrew D Ferguson
Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA
J Biol Chem 281:3536-43. 2006..A physiological role for Sep15 and SelM as thiol-disulfide oxidoreductases and their contribution to the quality control pathways of the endoplasmic reticulum are discussed... - Evidence for direct roles of two additional factors, SECp43 and soluble liver antigen, in the selenoprotein synthesis machineryXue Ming Xu
Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 280:41568-75. 2005..The data also reveal a role of SECp43 in regulation of selenoprotein expression by affecting the synthesis of Um34 on tRNA([Ser]Sec) and the intracellular location of SLA... - Evolution of selenium utilization traitsHector Romero
Laboratorio de Organización y Evolución del Genoma, Dpto de Biología Celular y Molecular, Instituto de Biologia, Facultad de Ciencias, Igua 4225, Montevideo, CP 11400, Uruguay
Genome Biol 6:R66. 2005..Selenium is also found in the form of 2-selenouridine, a modified base present in the wobble position of certain tRNAs, whose synthesis is catalyzed by YbbB using selenophosphate as a precursor... - Selenocysteine tRNA identification in the model organisms Dictyostelium discoideum and Tetrahymena thermophilaRajeev K Shrimali
Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
Biochem Biophys Res Commun 329:147-51. 2005..discoideum is 91 nucleotides long making it the longest eukaryotic sequenced to date. Evolutionary analyses of known Sec tRNAs reveal the two forms identified herein are the most divergent eukaryotic Sec tRNAs thus far sequenced... - Specific excision of the selenocysteine tRNA[Ser]Sec (Trsp) gene in mouse liver demonstrates an essential role of selenoproteins in liver functionBradley A Carlson
Section on the Molecular Biology of Selenium, Basic Research Laboratory, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland, 20892, USA
J Biol Chem 279:8011-7. 2004..Death appeared to be due to severe hepatocellular degeneration and necrosis with concomitant necrosis of peritoneal and retroperitoneal fat. These studies revealed an essential role of selenoproteins in liver function... - How selenium has altered our understanding of the genetic codeDolph L Hatfield
Molecular Biology of Selenium Section, Basic Research Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Mol Cell Biol 22:3565-76. 2002 - Platyhelminth mitochondrial and cytosolic redox homeostasis is controlled by a single thioredoxin glutathione reductase and dependent on selenium and glutathioneMariana Bonilla
Catedra de Inmunologia, Facultad de Quimica Facultad de Ciencias, Instituto de Higiene, Universidad de la Republica, Piso 2, Montevideo, Uruguay
J Biol Chem 283:17898-907. 2008..These studies establish the selenium- and glutathione-dependent regulation of cytosolic and mitochondrial redox homeostasis through a single TGR enzyme in platyhelminths... - Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cellsM Rohan Fernando
Department of Veterinary and Biomedical Sciences, University of Nebraska Lincoln, Lincoln, NE 68583 0905, USA
FASEB J 20:2645-7. 2006..These results suggest that Grx2 has a novel function as a peroxidase, accepting electrons both from GSH and TR. This unique property may play a role in protecting the mitochondria from oxidative damage... - Biosynthesis of selenocysteine on its tRNA in eukaryotesXue Ming Xu
Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, United States of America
PLoS Biol 5:e4. 2007..Conservation of the overall pathway of Sec biosynthesis suggests that this pathway is also active in other eukaryotes and archaea that synthesize selenoproteins... - The Chlamydomonas genome reveals the evolution of key animal and plant functionsSabeeha S Merchant
Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095, USA
Science 318:245-50. 2007.... - New developments in selenium biochemistry: selenocysteine biosynthesis in eukaryotes and archaeaXue Ming Xu
Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, Center for Cancer Research, National Institutes of Health, Bethesda, MD 20892, USA
Biol Trace Elem Res 119:234-41. 2007..Conservation of the overall pathway of Sec biosynthesis suggests that this pathway is also active in other eukaryotes and archaea that contain selenoproteins... - Structure and catalytic mechanism of eukaryotic selenocysteine synthaseOleg M Ganichkin
Max Planck Institut fur biophysikalische Chemie, Zelluläre Biochemie Makromolekulare Röntgenkristallographie, Am Fassberg 11, D 37077 Gottingen, Germany
J Biol Chem 283:5849-65. 2008..Based on these results and on the activity profiles of mechanism-based inhibitors, we offer a detailed reaction mechanism for the enzyme...
Research Grants
- Redox mechanism of cancer prevention by seleniumVADIM GLADYSHEV; Fiscal Year: 2002..These approaches should yield insight into the mechanism of the anticancer effect of selenium and may lead to the identification of human cancers most susceptible to selenium chemoprevention. ..
- 2006 Thiol-based Redox Regulation and Signaling Gordon Research ConferenceVADIM GLADYSHEV; Fiscal Year: 2006..A diverse mix of established and emerging leaders in the field, and of junior and senior investigators will be included in the program. ..
- Redox Biology CenterVADIM GLADYSHEV; Fiscal Year: 2007..Elucidation of redox-linked mechanisms in diseases ranging from cataracts to cancers and neurodegeneration by RBC members hold promise for developing therapeutic strategies for intervention. ..