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Selenoprotein X, 1

MsrB1, methionine-R-sulfoxide reductase, Selenoprotein R, SelR
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This protein belongs to the methionine sulfoxide reductase (Msr) protein family which includes repair enzymes that reduce oxidized methionine residues in proteins. The protein encoded by this gene is expressed in a variety of adult and fetal tissues and localizes to the cell nucleus and cytosol. [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: MsrB, Ethanolaminephosphotransferase, MsrA, CAN, Thioredoxin
Papers using MsrB1 antibodies
The CCP4 Suite: Programs for protein crystallography
Matthews Rowena, In PLoS Biology, 2001
... Wild-type and mutant forms of MsrB1 were further purified using Talon metal-affinity resin according to the manufacturer's protocol (Clontech, Palo Alto, California, United ...
Papers on MsrB1
Nuclear selenoproteins and genome maintenance.
Cheng et al., Wenzhou, China. In Iubmb Life, Jan 2016
To date, only five selenoproteins are experimentally demonstrated to reside in nucleus, exclusively or partially, including selenoprotein H, methionine-R-sulfoxide reductase 1, glutathione peroxidase-4, thioredoxin reductase-1, and thioredoxin glutathione reductase.
Effect of Inorganic Dietary Selenium Supplementation on Selenoprotein and Lipid Metabolism Gene Expression Patterns in Liver and Loin Muscle of Growing Lambs.
Pierzchała et al., Poland. In Biol Trace Elem Res, Jan 2016
Significant differences were found in the expression of GPX1, GPX2, SEPM, SEPW1, SEP15, SEPGS2, and TXNRD1 in the liver, and GPX1, SEPP1, SEPN1, SEPW1, SEP15, and MSRB1 in the LD muscle between S and C lambs.
Methionine sulfoxide reductase A deficiency exacerbates progression of kidney fibrosis induced by unilateral ureteral obstruction.
Park et al., Taegu, South Korea. In Free Radic Biol Med, Dec 2015
Methionine sulfoxide reductase A (MsrA), which stereospecifically catalyzes the reduction of methionine-S-sulfoxide, is an important reactive oxygen species (ROS) scavenger.
Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1.
Gladyshev et al., Seoul, South Korea. In Antioxid Redox Signal, Nov 2015
RECENT ADVANCES: Reversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies.
The evolving versatility of selenium in biology.
Brigelius-Flohé, Potsdam, Germany. In Antioxid Redox Signal, Nov 2015
Methionine sulfoxide reductase B1 (MsrB1) catalyzes a novel posttranslational protein modification.
A protective role of methionine-R-sulfoxide reductase against cadmium in Schizosaccharomyces pombe.
Kim et al., Ch'unch'ŏn, South Korea. In J Microbiol, 2014
The Schizosaccharomyces pombe cells harboring the methionine- R-sulfoxide reductase (MsrB)-overexpressing recombinant plasmid pFMetSO exhibited better growth than vector control cells, when shifted into fresh medium containing cadmium chloride (abbreviated as Cd).
Identification of the mitochondrial MSRB2 as a binding partner of LG72.
Zimmer et al., Bonn, Germany. In Cell Mol Neurobiol, 2014
In the present study, we now performed extensive interaction analyses and identified the mitochondrial methionine-R-sulfoxide reductase B2 (MSRB2) as a specific interaction partner of LG72.
Structural and biochemical analysis of a type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum.
Kim et al., Seoul, South Korea. In Arch Biochem Biophys, 2014
Free methionine-R-sulfoxide reductase (fRMsr) enzymes only reduce the free form of methionine-R-sulfoxide and can be grouped into two types with respect to the number of conserved Cys residues in the active sites.
Selenium and Methionine Sulfoxide Reduction.
Gladyshev, Boston, United States. In Free Radic Biol Med, 2014
Selenoprotein methionine-R-sulfoxide reductase B1 (MsrB1) is a repair enzyme that reduces ROS-oxidized methionine residues in proteins.
Unraveling the specificities of the different human methionine sulfoxide reductases.
Martens et al., Gent, Belgium. In Proteomics, 2014
We found that MSRB1 is the least specific MSRB enzyme, which is in agreement with the observation that MSRB1 is the only MSRB enzyme found in the cytosol and the nucleus, and therefore requires a broad specificity to reduce all possible substrates.
SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics.
Terman et al., Dallas, United States. In Nat Cell Biol, 2013
Employing a genetic approach, we identified a specific methionine sulfoxide reductase (MsrB) enzyme SelR that opposes Mical redox activity and Semaphorin-Plexin repulsion to direct multiple actin-dependent cellular behaviours in vivo.
Selenium and diabetes--evidence from animal studies.
Lei et al., Wuhan, China. In Free Radic Biol Med, 2013
Although its diabetogenic mechanism remains unclear, high Se intake elevated activity or production of selenoproteins including GPx1, MsrB1, SelS, and SelP.
Methionine sulfoxide reductase A, B1 and B2 are likely to be involved in the protection against oxidative stress in the inner ear.
Lee et al., Taegu, South Korea. In Cells Tissues Organs, 2013
The methionine sulfoxide reductase (Msr) family of proteins is a class of repair enzymes that reduce methionine-S (MsrA) or methionine-R (MsrB) sulfoxide to methionine.
The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions.
Kim, Taegu, South Korea. In Antioxid Redox Signal, 2013
RECENT ADVANCES: A selenoprotein MsrB1 knockout mouse has been developed.
Involvement of MsrB1 in the regulation of redox balance and inhibition of peroxynitrite-induced apoptosis in human lens epithelial cells.
Huang et al., Wuhan, China. In Exp Eye Res, 2012
The results demonstrate that in human lens epithelial cells MsrB1 may play important roles in regulating redox balance and mitigating endoplasmic reticulum stress.
Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin.
Dikiy et al., Trondheim, Norway. In J Biomed Biotechnol, 2011
MsrB1/Trx complex was studied in attempt to understand MsrB1 reduction mechanism. Using NMR data, molecular mechanics, protein docking & molecular dynamics simulations, found that intermediate MsrB1/Trx complex is stabilized by interprotein beta-layer.
Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase B1, reveal a role of selenoproteins in stress resistance.
Gladyshev et al., Boston, United States. In J Biol Chem, 2011
Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase B1, reveal a role of selenoproteins in stress resistance.
Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis.
Dikiy et al., Trondheim, Norway. In J Biol Chem, 2010
Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis.
Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processing.
Gladyshev et al., Lincoln, United States. In Plos One, 2009
Study characterized unexpected diversity of protein and mRNA forms of mammalian selenoprotein MsrB1.
Selenium and the methionine sulfoxide reductase system.
Moskovitz et al., Lawrence, United States. In Molecules, 2008
The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, respectively.
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