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Therefore, we anticipate that our subsequent screening might identify numerous cellular pathways, whose identification would be beneficial for elucidating the mechanism of targeted protein degradation

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Specifically, key residues Y108 3.32 , F109 3.33 , F112 3.36 , W248 6.48 and Y251 6.51 form a hydrophobic pocket that plays a crucial role in antagonist recognition and maintaining the receptor in an inactive conformation 106

two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states