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  • Title: Studies of C-terminal naphthoquinone dipeptides as 20S proteasome inhibitors.
    Author: Scotti A, Trapella C, Ferretti V, Gallerani E, Gavioli R, Marastoni M.
    Journal: J Enzyme Inhib Med Chem; 2016; 31(3):456-63. PubMed ID: 25942361.
    Abstract:
    The ubiquitin proteasome pathway is crucial in regulating many processes in the cell. Modulation of proteasome activities has emerged as a powerful strategy for potential therapies against much important pathologies. In particular, specific inhibitors may represent a useful tool for the treatment of tumors. Here, we report studies of a new series of peptide-based analogues bearing a naphthoquinone pharmacophoric unit at the C-terminal position. Some derivatives showed inhibition in the µM range of the post-acidic-like and chymotrypsin-like active sites of the proteasome.
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