thioredoxin glutathione reductase

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 Glutathione and Thioredoxin Antioxidant Pathways

Name: 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 Glutathione and Thioredoxin Antioxidant Pathways
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Description

Mass spectrometry of protein complexes: from origins to applications

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

Additionally, P53, a tumor suppressor protein, has also been implicated in ferroptosis

[24] [25] The labile iron pool [edit] In the cytoplasm, ferrous iron is found in a soluble, chelatable state which constitutes the labile iron pool (~0.001 mM)