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GLUT1 is palmitoylated at Cys207 and S-palmitoylation is required for maintaining GLUT1 PM localization To determine the site of GLUT1 palmitoylation, we mutated every cysteine to serine in the GLUT1 protein, and their S-palmitoylation levels were characterized by using the alkynyl palmitic acid incorporation assay

PPAR alpha mediates transcriptional upregulation of novel organic cation transporters-2 and 3 and enzymes involved in hepatic carnitine synthesis

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Activation of the Nrf2/HO-1 pathway restores N-acetylcysteine-induced impairment of the hypothalamus-pituitary-adrenal axis negative feedback by up-regulating GR expression and down-regulating GR expression into pituitary glands

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not FDA-approved