E2 conjugating inhibitors
E2 conjugating inhibitors are compounds that target the ubiquitin-proteasome system by inhibiting the activity of ubiquitin-conjugating enzymes (E2 enzymes). E2 enzymes play a crucial role in the ubiquitination process by facilitating the transfer of ubiquitin from ubiquitin-activating enzymes (E1 enzymes) to target proteins. This transfer is the second step in the ubiquitination cascade and determines the specificity of ubiquitin attachment to proteins. Inhibition of E2 enzymes disrupts ubiquitin conjugation, leading to impaired protein degradation by the proteasome and altering cellular processes regulated by ubiquitination, such as protein turnover, DNA repair, and signaling pathways. E2 conjugating inhibitors are explored for their therapeutic potential in various diseases, including cancer and neurodegenerative disorders, where dysregulation of the ubiquitin-proteasome system contributes to pathogenesis.
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