RBCK1 inhibitors, also known as RBR E3 ligase inhibitors, belong to a specialized class of chemical compounds that target a specific protein interaction network involved in cellular processes such as protein degradation and regulation. These inhibitors are designed to disrupt the activity of RBCK1, a critical component of the E3 ubiquitin ligase complex, which plays a pivotal role in the ubiquitin-proteasome system. This system is responsible for the controlled degradation of proteins within cells, a fundamental process in maintaining cellular homeostasis and regulating various cellular functions.
RBCK1, short for ring finger and CCCH-type domains-containing protein 1, is an E3 ubiquitin ligase that acts as a bridge between the ubiquitin-conjugating enzyme (E2) and the target protein, facilitating the transfer of ubiquitin molecules to the protein substrate. This ubiquitination process tags the target protein for degradation by the proteasome or modulates its activity and localization within the cell. RBCK1 inhibitors are designed to interfere with this specific protein-protein interaction, preventing the ubiquitination of target proteins and thereby disrupting their regulated degradation or modification. By modulating the activity of RBCK1, these inhibitors have the ability to impact various cellular pathways and processes, making them valuable tools for research and development efforts. RBCK1 inhibitors represent a chemical class of compounds that selectively target RBCK1, an E3 ubiquitin ligase involved in protein degradation and regulation within cells. By disrupting the protein-protein interaction essential for ubiquitination, these inhibitors have the ability to influence diverse cellular pathways and processes, offering a valuable tool for scientific investigations into cellular biology.
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