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Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine (By similarity). Additionally we are shipping Methionine Sulfoxide Reductase B2 Antibodies (54) and Methionine Sulfoxide Reductase B2 Kits (9) and many more products for this protein.
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this study we have identified, for the first time, compounds structurally related to the natural products fusaricidins that markedly activate recombinant bovine and human MsrA (show MSRA Proteins) and human MsrB.
Silencing the expression of the main Msr elements-MsrA, MsrB1, or MsrB2 exacerbates sensitivity toward oxidative stress.
the mitochondrial methionine-R-sulfoxide reductase B2 (MSRB2) is a specific interaction partner of LG72 (show DAOA Proteins).
Data show that glutaredoxin (show GRX1 Proteins) acts as a reductant for methionine sulfoxide reductases A and B (MsrA (show MSRA Proteins) and MsrB) with or without resolving cysteine.
CBS1, a methionine sulfoxide reductase of type B, is most abundant in muscle tissues, especially in the heart and thereby shows an expression pattern different to the human methionine sulfoxide reductase A (show MSRA Proteins)
MSRB is down-regulated during cell aging.
showed the expression and function of both sulfoxide reductases together with thioredoxin reductase in the cytosol as well as in the nucleus of epidermal melanocytes which are especially sensitive to reactive oxygen
Methionine sulfoxide reductases A and B are seriously affected by hydrogen peroxide accumulation in acute vitiligo (show MITF Proteins).
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role
almost absent catalase (show CAT Proteins) and methionine sulfoxide reductase A (show MSRA Proteins) and B protein (show LEPREL2 Proteins) expression in human gray/white scalp hair shafts in association with a functional loss of methionine sulfoxide repair in the entire gray hair follicle
Data show that glutaredoxin (show GRX1 Proteins) acts as a reductant for methionine sulfoxide reductases A and B (MsrA (show MSR1 Proteins) and MsrB) with or without resolving cysteine.
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 (show SEPX1 Proteins)
Studies show all Met sulfoxide residues in an MRP (show ABCC1 Proteins) can be reduced by MsrA (show MSR1 Proteins) and MsrB.
Results show that mammalian MsrB and MsrA (show MSR1 Proteins) proteins perform crucial functions in protection against oxidative stress in lower eukaryotic yeast cells.
MsrA (show MSR1 Proteins) and MsrB2, the two proteins with similar function in antioxidant protein (show PRDX3 Proteins) repair, have different effects on aging in fruit flies.
Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine (By similarity). Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance (By similarity).
methionine-R-sulfoxide reductase B2, mitochondrial
, pilin-like transcription factor
, methionine sulfoxide reductase B2