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The role of complex I in ferroptosis under such reverse ETC conditions remains unexplored but may diverge markedly from its function in forward ETC

Compromised detoxification processes, leading to toxin accumulation

In this study, we used cryogenic electron microscopy (cryo-EM) to determine structures of Cagri bound to Gs-coupled, active, AMY 1 R, AMY 2 R, AMY 3 R and CTR and compared the mode of interaction of Cagri and the associated dynamics of the Cagri-bound receptor complexes with previously reported cryo-EM structures and dynamics of receptors bound to rat amylin (rAmy, all receptor subtypes), sCT (CTR, AMY 1 R, AMY 2 R) 15 or recently developed amylin-based peptides (CTR and/or AMY 3 R) 16

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