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Cuadrado and colleagues first showed that GSK-3 inhibits NRF2 activity, but the identification of sites in NRF2 that are phosphorylated by GSK-3 was achieved several years later using two-dimensional electrophoresis and mass spectrometry: GSK-3 phosphorylates a group of Ser residues at the level of DSGIS motif in the Neh6 domain of NRF2, and this event represents the signal for the recognition by the adapter protein -TrCP, that targets NRF2 for ubiquitination and proteasomal degradation in a KEAP1-independent manner [150, 151]
We next assessed X(PC) activity in caspase-1 + cell lines, as determined by CASP1 transcript levels
2022 Mar 7;20(1):111
The Future of Incretin-Based Therapy Understanding GLP-1 versus GIP provides context for where this field is heading
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