CENP-C inhibitors belong to a distinctive chemical class that has garnered considerable attention in the realm of cellular and molecular research due to their significant impact on fundamental cellular processes. These inhibitors are specifically designed to target and modulate the activity of the Centromere Protein C (CENP-C), a crucial protein involved in various essential cellular functions. CENP-C is recognized for its pivotal role in centromere organization, kinetochore assembly, and chromosomal segregation during cell division. It acts as a linker between centromeric chromatin and kinetochore proteins, aiding in the establishment of a functional connection that ensures proper chromosomal alignment and segregation. The development of CENP-C inhibitors stems from a meticulous understanding of the protein's structural and functional attributes. These inhibitors are carefully crafted molecules that can selectively bind to CENP-C, interfering with its interactions with other macromolecules and disrupting its normal cellular functions. By modulating the activity of CENP-C, these inhibitors can influence critical processes such as kinetochore assembly, microtubule attachment, and mitotic checkpoint signaling. This intricate level of control over cellular events provides researchers with a powerful tool to dissect the molecular mechanisms underlying cell division and chromosome segregation.
Researchers have employed various strategies to design CENP-C inhibitors, often utilizing computational modeling, high-throughput screening, and structure-based drug design. These approaches enable the identification of small molecules with a high affinity for CENP-C, allowing for precise manipulation of its activity. Through experimental studies, scientists aim to unravel the intricate interplay between CENP-C and its binding partners, deciphering the complex regulatory network that orchestrates accurate chromosome segregation. In conclusion, CENP-C inhibitors constitute a significant chemical class that holds immense promise for advancing our understanding of essential cellular processes. By targeting the pivotal protein CENP-C, these inhibitors provide a valuable means to unravel the intricacies of cell division, kinetochore assembly, and chromosome segregation. Through rigorous research and experimentation, scientists strive to illuminate the molecular mechanisms underpinning these fundamental processes, paving the way for potential insights into various cellular dysfunctions and aberrations.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Monastrol | 254753-54-3 | sc-202710 sc-202710A | 1 mg 5 mg | $120.00 $233.00 | 10 | |
While primarily known as an inhibitor of the mitotic kinesin Eg5, monastrol can also impact CENP-C dynamics and centromere organization. | ||||||
Hesperadin | 422513-13-1 | sc-490384 | 10 mg | $304.00 | ||
An inhibitor that targets the mitotic checkpoint kinase Aurora B, affecting its interactions with CENP-C and impacting chromosome alignment and segregation. | ||||||
S-Trityl-L-cysteine | 2799-07-7 | sc-202799 sc-202799A | 1 g 5 g | $32.00 $66.00 | 6 | |
An inhibitor of the mitotic kinesin Eg5, which can indirectly influence CENP-C functions by disrupting mitotic spindle dynamics. | ||||||
GSK 923295 | 1088965-37-0 | sc-490136 | 5 mg | $290.00 | ||
An inhibitor of centromere-associated protein E (CENP-E), which indirectly affects CENP-C functions by disrupting the spindle assembly checkpoint. | ||||||
Reversine | 656820-32-5 | sc-203236 | 5 mg | $221.00 | 13 | |
While primarily targeting Aurora kinases and the microtubule-associated protein Hec1/Ndc80, reversine can also influence CENP-C localization and centromere function. | ||||||
AZD1152-HQPA | 722544-51-6 | sc-265334 | 10 mg | $375.00 | ||
An Aurora B kinase inhibitor that can impact its interaction with CENP-C and influence mitotic processes. | ||||||
AZ 3146 | 1124329-14-1 | sc-361114 sc-361114A | 10 mg 50 mg | $218.00 $905.00 | 7 | |
An inhibitor of Aurora B kinase, which regulates CENP-C interactions with other centromeric proteins. | ||||||