PLK1 and neoplasm: With the identification of several key binding sites of the PBD domain of PLK1, such as the broad pyrrolidine-binding pocket, the deep tyrosine-rich channel, and the phosphate-binding pocket, as well as the PLK1-specific residues (L478, L491, R516, and F535), non-ATP competitive PLK1 inhibitors developed against the unique PBD domain of PLK have shown great potential for reducing nonspecific cross-reactivity and inhibiting tumor growth in preclinical models (Zhang et al., 2022; Stafford et al., 2023).