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161 results on '"Fomenko, Dmitri E."'

4. Roles of the 15-kDa Selenoprotein (Sep15) in Redox Homeostasis and Cataract Development Revealed by the Analysis of Sep 15 Knockout Mice

Author

Kasaikina, Marina V., Fomenko, Dmitri E., Labunskyy, Vyacheslav M., Lachke, Salil A., Qiu, Wenya, Moncaster, Juliet A., Zhang, Jie, Wojnarowicz, Mark W., Jr., Natarajan, Sathish Kumar, Malinouski, Mikalai, Schweizer, Ulrich, Tsuji, Petra A., Carlson, Bradley A., Maas, Richard L., Lou, Marjorie F., Goldstein, Lee E., Hatfield, Dolph L., and Gladyshev, Vadim N.

Published
2011
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12. A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins

Author

Dan Su, Berndt, Carsten, Fomenko, Dmitri E., Holmgren, Arne, and Gladyshev, Vadim N.

Subjects
Proline -- Structure, Proline -- Chemical properties, Binding sites (Biochemistry) -- Structure, Thiols -- Chemical properties, Thiols -- Structure, Thioredoxin -- Structure, Thioredoxin -- Chemical properties, Biological sciences, Chemistry
Abstract

The cis-proline in human thioredoxin is a guardian residue that protects the active site cysteines from binding iron in the form of iron-sulfur clusters and other metals. This cis-proline in combination with the active site motif can be used to distinguish between oxidoreductases and metal binding proteins.

Published
2007

13. SelT, SelW, SelH, and Rdx 12: Genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family

Author

Dikiy, Alexander, Novoselov, Sergey V., Fomenko, Dmitri E., Sengupta, Aniruddha, Carlson, Bradley A., Cerny, Ronald L., Ginalski, Krzysztof, Grishin, Nick V., Hatfield, Dolph L., and Gladyshev, Vadim N.

Subjects
Selenium compounds -- Structure, Selenium compounds -- Chemical properties, Oxidation-reduction reaction -- Research, Thioredoxin -- Chemical properties, Thioredoxin -- Structure, Biological sciences, Chemistry
Abstract

Extensive sequence similarity searches are performed to define a new protein family, designated Rdx, which includes mammalian selenoproteins SelW, SelV, SelT and SelH. Rdx12 is found to interact with glutathione peroxidase 1, whereas 14-3-3 protein is identified as one of the targets of mammalian SelW.

Published
2007

15. Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases

Author

Hwa-Young Kim, Fomenko, Dmitri E., Yeo Eun Yoon, and Gladyshev, Vadim N.

Subjects
Cysteine -- Chemical properties, Methionine -- Chemical properties, Sulfur compounds -- Chemical properties, Biological sciences, Chemistry
Abstract

A study conducted identified the multiple selenoprotein MsrA(methionine-S-sulfoxide reductase) sequences in organisms from bacteria to animals. The study demonstrated that sporadically evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advantages provided by Sec in these and likely other thiol-dependent oxidoreductases.

Published
2006

19. Compartmentalization and regulation of mitochondrial function by methionine sulfoxide reductases in yeast

Author

Kaya, Alaattin, Koc, Ahmet, Byung Cheon Lee, Fomenko, Dmitri E., Rederstorff, Mathieu, Krol, Lescure, Alain, and Gladyshev, Vadim N.

Subjects
Methionine -- Chemical properties, Mitochondria -- Physiological aspects, Organosulfur compounds -- Structure, Organosulfur compounds -- Chemical properties, Oxidoreductases -- Chemical properties, Oxidoreductases -- Structure, Biological sciences, Chemistry
Abstract

Methionine sulfoxide reductases MsrA and MsrB are shown to be involved in the regulation of mitochondrial function. The results have shown that oxidative stress has contributed to mitochondrial dysfunction through oxidation of methionine residues in proteins located in different cellular compartments.

Published
2010

20. Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiae

Author

Marino, Stefano, Yehua Li, Fomenko, Dmitri E., Agisheva, Natalia, Cerny, Ronald L., and Gladyshev, Vadim N.

Subjects
Cysteine -- Chemical properties, Oxidoreductases -- Structure, Oxidoreductases -- Chemical properties, Proteomics -- Usage, Brewer's yeast -- Genetic aspects, Brewer's yeast -- Physiological aspects, Sulfides -- Chemical properties, Biological sciences, Chemistry
Abstract

Proteomic approaches are used to characterize proteins that reactive thiols and Saccharomyces cerevisiae is used as a eukaryotic model organism for identifying proteins with exposed reactive cysteine (Cys) and the identities of the residues. The studies have shown that approximately one-fourth of exposed Cys in the yeast proteome is regarded as functional sites, either subject to regulation by thiol oxidoreductases or involved in structural disulfides and metal binding.

Published
2010

21. Analysis of methionine/selenomethionine oxidation and methionine sulfoxide reductase function using methionine-rich proteins and antibodies against their oxidized forms

Author

Dung Tien Le, Xinwen Liang, Fomenko, Dmitri E., Raza, Ashraf S., Chom-Kyu Chong, Carlson, Bradley A., Hatfield, Dolph L., and Gladyshev, Vadim N.

Subjects
Aging -- Research, Methionine -- Chemical properties, Oxidation-reduction reaction -- Analysis, Oxidative stress -- Analysis, Biological sciences, Chemistry
Abstract

The identification and characterization of three natural methoinine (Met)-rich proteins (MRPs) containing 21-33 percent Met residues is described. The Met-rich proteins (MRPs) and antibodies specific for their oxidized forms could be used as application tools for examining MsrA- and MsrB-dependent processes such as Met sulfoxide reduction, oxidative stress, and aging.

Published
2008

23. Identity and functions of CxxC-derived motifs

Author

Fomenko, Dmitri E. and Gladyshev, Vadim N.

Subjects
Proteins -- Structure, Amino acids -- Structure-activity relationships, Substitution reactions -- Analysis, Molecular structure -- Models, Biological sciences, Chemistry
Abstract

Research discusses the functional aspects of some new CxxC-derived redox motifs, which contain serine and threonine, instead of cysteines, at the N- or C-terminals. Structural data suggest that threonines can stabilize thiolates, a departure from the known catalytic triads, as represented by glutathione peroxidases and peroxiredoxins.

Published
2003

25. Specialized Methods

Author

Raza, Ashraf, primary, Engen, John R., additional, Ragsdale, Stephen W., additional, Seravalli, Javier, additional, Becker, Donald F., additional, Fomenko, Dmitri E., additional, Gladyshev, Vadim N., additional, Thomas, Mark P., additional, Schultz, Harold D., additional, and Grisham, Matthew B., additional

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36. One codon – two amino acids.

Author

Turanov, Anton A, primary, Lobanov, Alexey V, additional, Fomenko, Dmitri E, additional, Morrison, Hilary G, additional, Sogin, Mitchell L, additional, Klobutcher, Lawrence A, additional, Hatfield, Dolph L, additional, and Gladyshev, Vadim N, additional

Published
2009
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40. SelT, SelW, SelH, and Rdx12: Genomics and Molecular Insights into the Functions of Selenoproteins of a Novel Thioredoxin-like Family

Author

Dikiy, Alexander, primary, Novoselov, Sergey V., additional, Fomenko, Dmitri E., additional, Sengupta, Aniruddha, additional, Carlson, Bradley A., additional, Cerny, Ronald L., additional, Ginalski, Krzysztof, additional, Grishin, Nick V., additional, Hatfield, Dolph L., additional, and Gladyshev, Vadim N., additional

Published
2007
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50. Diversity of Protein and mRNA Forms of Mammalian Methionine Sulfoxide Reductase B1 Due to Intronization and Protein Processing.

Author

Xinwen Liang, Fomenko, Dmitri E., Hua, Deame, Kaya1, Alaattin, and Gladyshev, Vadim N.

Subjects
*METHIONINE, *OXIDATIVE stress, *SULFOXIDES, *SELENOPROTEINS, *CYSTEINE proteinases, *GENE expression, *LIVER, *KIDNEYS, *PROTEINS
Abstract

Background: Methionine sulfoxide reductases (Msrs) are repair enzymes that protect proteins from oxidative stress by catalyzing stereospecific reduction of oxidized methionine residues. MsrB1 is a selenocysteine-containing cytosolic/nuclear Msr with high expression in liver and kidney. Principal Findings: Here, we identified differences in MsrB1 gene structure among mammals. Human MsrB1 gene consists of four, whereas the corresponding mouse gene of five exons, due to occurrence of an additional intron that flanks the stop signal and covers a large part of the 39-UTR. This intron evolved in a subset of rodents through intronization of exonic sequences, whereas the human gene structure represents the ancestral form. In mice, both splice forms were detected in liver, kidney, brain and heart with the five-exon form being the major form. We found that both mRNA forms were translated and supported efficient selenocysteine insertion into MsrB1. In addition, MsrB1 occurs in two protein forms that migrate as 14 and 5 kDa proteins. We found that each mRNA splice form generated both protein forms. The abundance of the 5 kDa form was not influenced by protease inhibitors, replacement of selenocysteine in the active site or mutation of amino acids in the cleavage site. However, mutation of cysteines that coordinate a structural zinc decreased the levels of 5 and 14 kDa forms, suggesting importance of protein structure for biosynthesis and/stability of these forms. Conclusions: This study characterized unexpected diversity of protein and mRNA forms of mammalian selenoprotein MsrB1. [ABSTRACT FROM AUTHOR]

Published
2010
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