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A structural explanation for these findings was provided from our previous cryo-EM structures of CT(Pro32) and rAmy(Tyr37)-bound AMYRs structures where the bulky phenolic side chain of Y37 rAmy forms perpendicular stacking interactions with W79 ECD 15 , and additional interactions with the respective RAMP protomer that are likely important for selectivity of rAmy for AMYRs over CTR

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The peptide occurs naturally as part of thymosin beta-4, present in virtually all human and animal cells

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4e, IVDs from patients who had undergone PELD were found to express both KRT19 and FSP1, further indicating fibrotic changes in the NP

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