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DUBs (Deubiquitinating Enzymes) and related Inhibitors

Ubiquitination, the covalent attachment of ubiquitin to a target protein, is a posttranslational modification that regulates the stability, function, and/or localization of the modified substrate protein. Deubiquitinating enzymes (DUBs) are proteases that cleave ubiquitin or ubiquitin-like proteins from target proteins. They play several roles in the ubiquitin pathway.

DUBs

    • activate the ubiquitin pro-proteins to yield mature ubiquitin monomer,
    • recycle ubiquitin,
    • reverse the thioester bond formed during ubiquitination of target proteins,
    • regenerate monoubiquitin from unanchored polyubiquitin

Similar to ubiquitination, deubiquitination is a highly regulated process that has been implicated in various cellular functions, including cell cycle regulation, proteasome-and lysosome-dependent protein degradation, gene expression, DNA repair, kinase activation, microbial pathogenesis etc.

Because of their involvement on overall ubiquitin biology modulation of DUB enzyme activity offers an additional layer of control over various key cellular processes. Hence, DUB inhibitors have tremendous therapeutic potential for treatment of neurodegenerative diseases, lysosomal/autophagy-related disorders and certain forms of cancer. No wonder that advances in small molecule-based inhibitors specifically targeting DUBs are quickly becoming the forerunners in new approaches towards achieving cures for many human diseases. Biovision's catalog offers several DUB inhibitors including Spautin-1 which is a potent autophagy inhibitor in mammalian cells being extensively studied in the preclinical setting.

DUBs (Deubiquitinating Enzymes) and related Inhibitors Products

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