thioredoxin glutathione reductase Structure and mechanism of mammalian reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Non-covalent inhibitors of thioredoxin glutathione

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This dual mechanism allows both expansion of the stem cell pool and directed tissue repair depending on copper availability

Epub 2020/02/23

In studies simultaneously investigating concentrations in different specimen, a preferential distribution of individual compounds has been observed, e.g., of ferulic acid and 5-(3,4-dihydroxyphenyl)--valerolactone into synovial fluid compared to serum

Insulin-mediated activation of PI3K and PKB/AKT is necessary for the translocation of GLUT4 from an intracellular pool to the plasma membrane to allow for uptake of plasma glucose