Sergey V Novoselov
Overview
Explore the profile of Sergey V Novoselov including associated specialties, affiliations and a list of published articles.
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25
Citations
2766
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Recent Articles
1.
Novoselova E, Novikov V, Lunin S, Glushkova O, Novoselova T, Parfenyuk S, et al.
Electromagn Biol Med
. 2018 Nov;
38(1):74-83.
PMID: 30472894
We investigated the effects of weak combined magnetic fields (MFs) produced by superimposing a constant MF (in the range 30 - 150 µT) and an alternating MF (100 or 200...
2.
Novoselov S, Kim H, Hua D, Lee B, Astle C, Harrison D, et al.
Antioxid Redox Signal
. 2009 Sep;
12(7):829-38.
PMID: 19769460
Methionine residues are susceptible to oxidation, but this damage may be reversed by methionine sulfoxide reductases MsrA and MsrB. Mammals contain one MsrA and three MsrBs, including a selenoprotein MsrB1....
3.
Fomenko D, Novoselov S, Natarajan S, Lee B, Koc A, Carlson B, et al.
J Biol Chem
. 2008 Nov;
284(9):5986-93.
PMID: 18990697
Protein oxidation has been linked to accelerated aging and is a contributing factor to many diseases. Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide...
4.
Hirosawa-Takamori M, Ossipov D, Novoselov S, Turanov A, Zhang Y, Gladyshev V, et al.
FASEB J
. 2008 Sep;
23(1):107-13.
PMID: 18772345
Translational read-through of the UGA stop codon is an evolutionarily conserved feature that most prominently represents the basis of selenoprotein biosynthesis. It requires a specific cis-acting stem loop control element,...
5.
Bonilla M, Denicola A, Novoselov S, Turanov A, Protasio A, Izmendi D, et al.
J Biol Chem
. 2008 Apr;
283(26):17898-907.
PMID: 18408002
Platyhelminth parasites are a major health problem in developing countries. In contrast to their mammalian hosts, platyhelminth thiol-disulfide redox homeostasis relies on linked thioredoxin-glutathione systems, which are fully dependent on...
6.
Sengupta A, Carlson B, Weaver J, Novoselov S, Fomenko D, Gladyshev V, et al.
Biochem J
. 2008 Apr;
413(1):151-61.
PMID: 18373496
Sec (selenocysteine) is biosynthesized on its tRNA and incorporated into selenium-containing proteins (selenoproteins) as the 21st amino acid residue. Selenoprotein synthesis is dependent on Sec tRNA and the expression of...
7.
Merchant S, Prochnik S, Vallon O, Harris E, Karpowicz S, Witman G, et al.
Science
. 2007 Oct;
318(5848):245-50.
PMID: 17932292
Chlamydomonas reinhardtii is a unicellular green alga whose lineage diverged from land plants over 1 billion years ago. It is a model system for studying chloroplast-based photosynthesis, as well as...
8.
Shchedrina V, Novoselov S, Malinouski M, Gladyshev V
Proc Natl Acad Sci U S A
. 2007 Aug;
104(35):13919-24.
PMID: 17715293
Selenocysteine (Sec, U) insertion into proteins is directed by translational recoding of specific UGA codons located upstream of a stem-loop structure known as Sec insertion sequence (SECIS) element. Selenoproteins with...
9.
Dikiy A, Novoselov S, Fomenko D, Sengupta A, Carlson B, Cerny R, et al.
Biochemistry
. 2007 May;
46(23):6871-82.
PMID: 17503775
Selenium is an essential trace element in many life forms due to its occurrence as a selenocysteine (Sec) residue in selenoproteins. The majority of mammalian selenoproteins, however, have no known...
10.
Novoselov S, Lobanov A, Hua D, Kasaikina M, Hatfield D, Gladyshev V
Proc Natl Acad Sci U S A
. 2007 May;
104(19):7857-62.
PMID: 17470795
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 (SECIS)...