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Sergey V. Novoselov

Researcher at University of Nebraska–Lincoln

Publications -  33
Citations -  7135

Sergey V. Novoselov is an academic researcher from University of Nebraska–Lincoln. The author has contributed to research in topics: Selenoprotein & Selenocysteine. The author has an hindex of 25, co-authored 28 publications receiving 6543 citations. Previous affiliations of Sergey V. Novoselov include Science Applications International Corporation & Pompeu Fabra University.

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The Chlamydomonas Genome Reveals the Evolution of Key Animal and Plant Functions

Sabeeha S. Merchant, +118 more
- 12 Oct 2007 - 
TL;DR: Analyses of the Chlamydomonas genome advance the understanding of the ancestral eukaryotic cell, reveal previously unknown genes associated with photosynthetic and flagellar functions, and establish links between ciliopathy and the composition and function of flagella.
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Characterization of Mammalian Selenoproteomes

TL;DR: This work identified selenoprotein genes in sequenced mammalian genomes by methods that rely on identification of selenocysteine insertion RNA structures, the coding potential of UGA codons, and the presence of cysteine-containing homologs.
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Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtii

TL;DR: Selenoproteins present in Chlamydomonas and animals evolved early, and were independently lost in land plants, yeast and some animals, indicating a common origin of plant and animal Sec insertion systems.
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Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2.

TL;DR: The Grx2 structural model suggested a common reaction mechanism for this class of proteins and provided the first example of a mitochondrial Grx and also indicate the occurrence of a second functional Grx in mammals.
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SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family.

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.