ubiquitin ligase inhibitor activity

Definition

Target type: molecularfunction

Binds to and stops, prevents or reduces the activity of a ubiquitin ligase. [GOC:dph, GOC:vw, PMID:21389117]

Ubiquitin ligase inhibitors are molecules that block the activity of ubiquitin ligases, enzymes responsible for attaching ubiquitin proteins to target proteins. Ubiquitination is a crucial post-translational modification that regulates a wide range of cellular processes, including protein degradation, signal transduction, DNA repair, and immune responses. Ubiquitin ligases catalyze the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate protein, forming a polyubiquitin chain. This chain acts as a signal that can target the substrate protein for degradation by the proteasome or for other cellular processes. Ubiquitin ligase inhibitors can disrupt this process by binding to the ubiquitin ligase and blocking its activity, thereby preventing ubiquitination of the target protein. This inhibition can have a variety of effects, depending on the specific ubiquitin ligase and its target protein. For example, inhibiting a ubiquitin ligase that targets a tumor suppressor protein can lead to increased levels of the tumor suppressor protein and potentially inhibit cancer growth. Similarly, inhibiting a ubiquitin ligase that targets a protein involved in inflammation can potentially reduce inflammation. The development of ubiquitin ligase inhibitors is a promising area of research for the development of new therapeutic agents for a variety of diseases, including cancer, inflammatory diseases, and neurodegenerative diseases.'
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Proteins (7)

Compounds (2)