Date published: 2025-10-10

021-6093-6350

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Cdc23 抑制因子

Common Cdc23 Inhibitors include, but are not limited to Purvalanol A CAS 212844-53-6, Roscovitine CAS 186692-46-6, Flavopiridol CAS 146426-40-6, Indirubin-3'-monoxime CAS 160807-49-8 and RO-3306 CAS 872573-93-8.

Cdc23 inhibitors are a class of chemical compounds that specifically target and inhibit the activity of the Cdc23 protein, a crucial component of the anaphase-promoting complex/cyclosome (APC/C). The APC/C is a multi-subunit E3 ubiquitin ligase that plays a pivotal role in regulating the cell cycle by targeting specific proteins for degradation via the ubiquitin-proteasome pathway. Cdc23, along with other core subunits, is essential for the proper functioning of the APC/C, which in turn ensures the accurate progression of cells through mitosis and the maintenance of genomic stability. Inhibition of Cdc23 disrupts the activity of the APC/C, leading to the accumulation of key mitotic regulators and interference with the cell cycle progression, particularly in the metaphase-anaphase transition.

Chemically, Cdc23 inhibitors can vary widely in their structures but typically share a common feature of being able to bind to the Cdc23 protein or its interacting partners within the APC/C complex. This binding can occur through various mechanisms, such as direct interaction with the Cdc23 protein or by targeting the interfaces between Cdc23 and other APC/C components, thereby blocking the assembly or function of the complex. The specificity and potency of these inhibitors depend on their molecular configuration, which is often optimized through chemical modifications to enhance their binding affinity and stability. Understanding the structural basis of Cdc23 inhibition is crucial for designing more effective compounds that can selectively target this protein without affecting other cellular processes. Consequently, research into Cdc23 inhibitors focuses heavily on elucidating their binding mechanisms, structure-activity relationships, and the molecular dynamics involved in their interaction with the APC/C complex.

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