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To determine whether the evolutionary constraints acting upon hormone and G protein interacting sites has changed within mammals, I examined the variability of amino acid residues at sites implicated in interacting with hormone ligands and G proteins in the Gcgr, Glp1r, and Glp2r protein sequences based on the alignments of the receptor protein sequences ( Supplementary Figures 6 8 )

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In the vasculature, cuproptosis directly induces EC death and drives VSMCs toward a pro-inflammatory synthetic phenotype