D
Dmitri E. Fomenko
Researcher at University of Nebraska–Lincoln
Publications - 44
Citations - 2969
Dmitri E. Fomenko is an academic researcher from University of Nebraska–Lincoln. The author has contributed to research in topics: Selenoprotein & Methionine sulfoxide reductase. The author has an hindex of 28, co-authored 44 publications receiving 2718 citations. Previous affiliations of Dmitri E. Fomenko include Karolinska Institutet & National Institutes of Health.
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Journal ArticleDOI
MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation
Byung Cheon Lee,Zalán Péterfi,Fu Kun W. Hoffmann,Richard Moore,Alaattin Kaya,Andrei Avanesov,Lionel Tarrago,Yani Zhou,Eranthie Weerapana,Dmitri E. Fomenko,Peter R. Hoffmann,Vadim N. Gladyshev +11 more
TL;DR: The study shows that proteins can be regulated by reversible site-specific methionine-R-sulfoxidation, and identified the regulatory role of MsrB1 as a Mical antagonist in orchestrating actin dynamics and macrophage function.
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SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family.
Alexander Dikiy,Sergey V. Novoselov,Dmitri E. Fomenko,Aniruddha Sengupta,Bradley A. Carlson,Ronald L. Cerny,Krzysztof Ginalski,Krzysztof Ginalski,Nick V. Grishin,Dolph L. Hatfield,Vadim N. Gladyshev +10 more
TL;DR: A new protein family is defined that includes mammalian selenoproteins SelW, SelV, SelT and SelH, bacterial SelW-like proteins and cysteine-containing proteins of unknown function in all three domains of life, and a mechanism for redox regulation of the 14-3-3 family of proteins is suggested.
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Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life
Alexey V. Lobanov,Dmitri E. Fomenko,Yan Zhang,Aniruddha Sengupta,Dolph L. Hatfield,Vadim N. Gladyshev +5 more
TL;DR: It is suggested that, with the exception of vertebrates, aquatic life supports selenium utilization, whereas terrestrial habitats lead to reduced use of this trace element due to an unknown environmental factor.
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NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.
Andrew D. Ferguson,Vyacheslav M. Labunskyy,Dmitri E. Fomenko,Demet Araç,Yogarany Chelliah,Carlos A. Amezcua,Josep Rizo,Vadim N. Gladyshev,Johann Deisenhofer,Johann Deisenhofer,Johann Deisenhofer +10 more
TL;DR: These data reveal that Sep15 and SelM are structural homologs that establish a new thioredoxin-like protein family and their contribution to the quality control pathways of the endoplasmic reticulum are discussed.
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High-throughput identification of catalytic redox-active cysteine residues.
TL;DR: In this paper, a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases was developed.