Chemical inhibitors of TTC28 include a variety of compounds that interfere with microtubule dynamics, an essential component of cell division and cytoskeletal organization, processes with which TTC28 is associated. Palbociclib, for example, can impede TTC28's role in cell division by inhibiting cyclin-dependent kinases 4 and 6, which are crucial for cell cycle progression. Similarly, Vincristine can inhibit TTC28's function by preventing microtubule formation, which is critical for mitotic spindle assembly and thus could disrupt TTC28's role in cell division. Paclitaxel, by stabilizing microtubules, can interfere with the proper disassembly required for cell cycle progression, thereby indirectly inhibiting TTC28. Nocodazole and Colchicine both inhibit microtubule polymerization, which could hamper TTC28's potential role in stabilizing these cellular structures.
Further, Podophyllotoxin can inhibit TTC28's function by targeting tubulin polymerization, which is necessary for microtubule assembly and cell division. Eribulin, by inhibiting the growth phase of microtubule dynamics, can disrupt cellular processes that TTC28 may influence. Vinblastine, through its binding to tubulin, can inhibit microtubule formation, potentially affecting TTC28's role in cellular architecture and division processes. Monastrol, an inhibitor of kinesin Eg5, can indirectly inhibit TTC28's function in mitosis by disrupting spindle fiber mechanics essential for chromosome segregation. Griseofulvin, Thiabendazole, and Albendazole are all microtubule-interfering agents that can inhibit TTC28 by binding to tubulin or inhibiting microtubule polymerization, thus disrupting the microtubule movements and assembly. These actions can indirectly inhibit TTC28's function if it is involved in processes that require intact microtubules, such as vesicle transport, intracellular organization, and cell division. The disruption of these microtubule-dependent processes by these chemicals can thereby inhibit the proper functioning of TTC28 within the cell.
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