Date published: 2025-11-8

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CCDC61 Inhibitors

The chemical class of CCDC61 inhibitors presents a range of compounds that directly or indirectly impact its functions in identical protein binding, microtubule binding, centriole assembly, and mitotic spindle assembly. Colchicine acts as a direct inhibitor by disrupting microtubule binding, impacting CCDC61's role in centriole assembly and mitotic spindle assembly. Paclitaxel, though indirect, stabilizes microtubules, affecting CCDC61's microtubule binding and influencing centriole assembly. Nocodazole, a direct inhibitor, depolymerizes microtubules, disrupting CCDC61's microtubule binding activity and impacting centriole assembly. Vinblastine indirectly inhibits CCDC61 by disrupting microtubule dynamics, influencing centriole assembly and mitotic spindle assembly. Griseofulvin acts as a direct inhibitor by inhibiting microtubule formation, affecting CCDC61's role in centriole assembly and mitotic spindle assembly. Colcemid indirectly inhibits CCDC61 by preventing microtubule polymerization, impacting its microtubule binding activity and influencing centriole assembly. Epothilone B directly promotes microtubule stabilization, disrupting CCDC61's microtubule binding and affecting centriole assembly. Podophyllotoxin, though indirect, disrupts microtubule dynamics, influencing CCDC61's microtubule binding and impacting centriole assembly.

Vinorelbine, a direct inhibitor, interferes with microtubule dynamics, disrupting CCDC61's role in centriole assembly and mitotic spindle assembly. Docetaxel acts indirectly by promoting microtubule stabilization, impacting CCDC61's microtubule binding and influencing centriole assembly. Vinflunine directly disrupts microtubule dynamics, affecting CCDC61's microtubule binding and influencing centriole assembly. Thiabendazole indirectly inhibits CCDC61 by interfering with microtubule polymerization, impacting its microtubule binding activity and influencing centriole assembly. These inhibitors collectively contribute to our understanding of CCDC61's intricate role in cellular processes and offer potential avenues for further research into its functions and implications in cellular organization and division. The chemical class of CCDC61 inhibitors provides a valuable framework for investigating the regulatory mechanisms associated with identical protein binding, microtubule binding, centriole assembly, and mitotic spindle assembly.

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