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The structures solved in LCP are consistent with the large number of mutagenesis studies of the receptor function in membranes, leaving little doubt about the absence of a second TM domain
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MOTS-c, whose research intersects this pathway through Nrf2 — Nrf2/Keap1–ARE stabilisation coordinately induces the GCL catalytic and modifier subunits that build glutathione (Wild, Moinova & Mulcahy, 2000, PMID 10741850), and an engineered LAT1-targeted MOTS-c analogue activated Nrf2 and preserved GSH and SOD levels in irradiated mouse lung (Zhang et al., 2026, PMID 42142418) — note carefully: that study used the engineered R13A-MOTS-c analogue rather than wild-type MOTS-c, and glutathione peroxidase was not among the enzymes measured
