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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

To say something causes a reaction in science, we need strong evidence across multiple well-designed studies