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1 synthesize active formate dehydrogenase H, a selenoenzyme.
2 ated through the antioxidative properties of selenoenzymes.
3 tion into selenocysteine and its function in selenoenzymes.
4 metabolism is catalyzed by a small family of selenoenzymes.
5 ression of a wild-type thioredoxin reductase selenoenzyme, a cysteine mutant enzyme, and the UGA-term
6 ity is impaired by Hg and results in altered selenoenzyme activities and loss of optimal control of T
7 identify a new GSH peroxidase that is not a selenoenzyme and can reduce phospholipid hydroperoxides.
9 st characterized member of a small family of selenoenzymes catalyzing the bioactivation and disposal
11 oxide-destroying mimetics of the antioxidant selenoenzyme glutathione peroxidase (GPx), via oxidation
16 a unique dependency on the lipid antioxidant selenoenzyme, glutathione peroxidase 4 (GPx4), that acts
19 lic regulation and function of this abundant selenoenzyme has greatly advanced during the past decade
20 e suppressed by selenium through antioxidant selenoenzymes including glutathione peroxidase 1 (GPX1)
22 nhibitors of thioredoxin reductases (TrxRs), selenoenzymes involved in cellular redox regulation.
24 nt interest, and the antioxidant activity of selenoenzymes is now known to be dependent upon redox cy
25 primarily for the antioxidant properties of selenoenzymes, is obtained mainly from meat, seafood and
27 s encoding the protein components of two key selenoenzyme reductases, glycine reductase and d-proline
28 M) is required for synthesis of redox active selenoenzymes such as glutathione peroxidases and thiore
30 ase (D2) is an integral membrane ER-resident selenoenzyme that activates the pro-hormone thyroxine (T
31 peroxide glutathione peroxidase (PHGPX) is a selenoenzyme that can catalyze the direct reduction of v
32 methionine sulfoxide reductase B1 (MsrB1), a selenoenzyme that catalyzes the reduction of oxidized me
35 duction of a fully functional, semisynthetic selenoenzyme that is amenable to structure-function stud
37 odothyronine deiodinases (IDs) are mammalian selenoenzymes that catalyze the conversion of thyroxine
39 Type 2 iodothyronine deiodinase (D2) is a selenoenzyme, the product of the recently cloned cAMP-de
43 ase families, and functionally characterized selenoenzymes typically have a single Sec residue used d