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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Methionine sulfoxide reductase B2

MsrB, MsrB2, CBS1
Top mentioned proteins: MsrA, CAN, ACID, Thioredoxin, MsrB1
Papers on MsrB
Identification of activators of methionine sulfoxide reductases A and B.
New
Weissbach et al., Port Saint Lucie, United States. In Biochem Biophys Res Commun, Jan 2016
The two major Msr enzymes, MsrA and MsrB, can repair oxidative damage to proteins due to reactive oxygen species, by reducing the methionine sulfoxide in proteins back to methionine.
Methionine sulfoxide reductase A deficiency exacerbates progression of kidney fibrosis induced by unilateral ureteral obstruction.
New
Park et al., Taegu, South Korea. In Free Radic Biol Med, Dec 2015
UUO reduced the kidney expression of MsrA, MsrB1, and MsrB2, thereby decreasing MsrA and MsrB activity.
Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1.
Review
New
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 discovery of methionine sulfoxide reductase enzymes: An historical account and future perspectives.
Review
New
Minetti et al., Pavia, Italy. In Biofactors, Jun 2015
A fundamental discovery revealed the existence of two unrelated families of enzymes, MsrA and MsrB, whose members display opposite stereospecificity of reduction for the two sulfoxides.
Corynebacterium glutamicum methionine sulfoxide reductase A uses both mycoredoxin and thioredoxin for regeneration and oxidative stress resistance.
New
Liu et al., China. In Appl Environ Microbiol, Apr 2015
Oxidation of methionine leads to the formation of the S and R diastereomers of methionine sulfoxide (MetO), which can be reversed by the actions of two structurally unrelated classes of methionine sulfoxide reductase (Msr), MsrA and MsrB, respectively.
Prevalence and characterization of methicillin susceptible Staphylococcus aureus ST398 isolates from retail foods.
New
Meng et al., China. In Int J Food Microbiol, Apr 2015
No isolate carried mecA, tet(M), tet(O), fexA, aac(6')/aph(2″), cfr, ermT, msrB, cat::pC194, cat::pC223, catpIp-501, dfrD, dfrG and dfrS1 genes.
Direct interactions between ENaC gamma subunit and ClCN2 in cystic fibrosis epithelial cells.
Zeitlin et al., Baltimore, United States. In Physiol Rep, 2015
These regulatory effects of ClCN2 on ENaCγ appear to be dependent on the CBS-1 domain located within the c-terminus of ClCN2, which is necessary for the targeting of ClCN2 to the apical surface.
[Investigation of macrolide, lincosamide and streptogramin B resistance in Staphylococcus aureus strains isolated from clinical samples by phenotypical and genotypical methods].
Kaleli et al., Denizli, Turkey. In Mikrobiyol Bul, 2015
The resistance genes of 136 isolates with MLS(B) resistance phenotype were determined genotypically and among 111 isolates showing iMLS(B) phenotype ermA gene was found in 81.9% (83 MRSA, 8 MSSA), ermC gene in 10.8% (7 MRSA, 5 MSSA), msrA gene in 10.8% (11 MRSA, 1 MSSA), msrB gene in 1.8% (2 MRSA) and ermB gene in 0.9% (1 MRSA).
Regulation of Expression of Oxacillin-Inducible Methionine Sulfoxide Reductases in Staphylococcus aureus.
Singh et al., Kirksville, United States. In Int J Microbiol, 2014
Cell wall-active antibiotics cause induction of a locus that leads to elevated synthesis of two methionine sulfoxide reductases (MsrA1 and MsrB) in Staphylococcus aureus.
Methionine sulfoxide reductase: chemistry, substrate binding, recycling process and oxidase activity.
Review
Branlant et al., Vandœuvre-lès-Nancy, France. In Bioorg Chem, 2014
Three classes of methionine sulfoxide reductases are known: MsrA and MsrB which are implicated stereo-selectively in the repair of protein oxidized on their methionine residues; and fRMsr, discovered more recently, which binds and reduces selectively free L-Met-R-O.
Significance of four methionine sulfoxide reductases in Staphylococcus aureus.
Moskovitz et al., Lawrence, United States. In Plos One, 2014
Cell wall-active antibiotics cause elevated synthesis of methionine sulfoxide reductases (Msrs: MsrA1 and MsrB) in S. aureus.
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.
SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics.
Impact
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.
The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions.
Review
Kim, Taegu, South Korea. In Antioxid Redox Signal, 2013
Methionine sulfoxide reductases (Msrs), MsrA and MsrB, are the enzymes responsible for this system.
Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine.
GeneRIF
Kim, Taegu, South Korea. In Acta Biochim Biophys Sin (shanghai), 2012
Data show that glutaredoxin acts as a reductant for methionine sulfoxide reductases A and B (MsrA and MsrB) with or without resolving cysteine.
Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2.
GeneRIF
Dikiy et al., Trondheim, Norway. In Proteins, 2011
overall structure is composed of two beta-sheets consisting of eight antiparallel beta-strands and three N-terminal alpha-helices and is more similar to those of bacterial MsrBs than to that of mammalian MsrB1
The biological significance of methionine sulfoxide stereochemistry.
Review
Gladyshev et al., Boston, United States. In Free Radic Biol Med, 2011
Both free amino acid and protein-based forms of methionine-S-sulfoxide are stereospecifically reduced by MsrA, whereas the reduction of methionine-R-sulfoxide requires two enzymes, MsrB and fRMsr, which act on its protein-based and free amino acid forms, respectively.
Arabidopsis thaliana plastidial methionine sulfoxide reductases B, MSRBs, account for most leaf peptide MSR activity and are essential for growth under environmental constraints through a role in the preservation of photosystem antennae.
GeneRIF
Rey et al., France. In Plant J, 2010
Data suggest that plastidial MSRBs fulfil an essential function in maintaining vegetative growth of plants during environmental constraints, through a role in the preservation of photosynthetic antennae.
Overexpression of methionine-R-sulfoxide reductases has no influence on fruit fly aging.
GeneRIF
Gladyshev et al., Lincoln, United States. In Mech Ageing Dev, 2009
MsrA and MsrB2, the two proteins with similar function in antioxidant protein repair, have different effects on aging in fruit flies.
Differential expression of the antioxidant repair enzyme methionine sulfoxide reductase (MSRA and MSRB) in human skin.
GeneRIF
Thiele et al., Boston, United States. In Am J Dermatopathol, 2009
MSR enzymes are differentially expressed in human skin.
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