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Peptide inhibitors (such as VY-9) occupy hydrophobic pockets (His85, Phe264, etc.) near the cavity entrance, which prevent the substrate L-tyrosine from entering the active cavity and interfere with the coordination between Cu and His residues (such as the chelation of imidazole ring of His85 with Cu), resulting in the loss of enzyme activity (Baskaran et al., 2021

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RoB 2: a revised tool for assessing risk of bias in randomised trials

C., Buszinski, A