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• W2891648995 abstract "As a ubiquitous, highly pleiotropic and constitutively active serine/threonine protein kinase, casein kinase 2 (CK2) is closely associated with tumorigenesis by its overexpression in cancer cells. Here we report several proteolysis targeting chimeras (PROTACs) via click reaction to connect a CK2 inhibitor (CX-4945) and pomalidomide for degradation of CK2 protein. Among them, compound 2 degraded CK2 in a dose and time-dependent manner, and kept CK2 at a low basal level by recruiting ubiquitin-proteasome system. The degradation of CK2 resulted in the reduced phosphorylation of Akt and the up-regulation of p53. As a CK2 protein degrader, 2 showed the analogous cytotoxicity to CX-4945 but with a quite different mechanism of action from the CK2 inhibitor, hinting that degradation of CK2 proteins by PROTACs is a potential way for cancer treatments." @default.
• W2891648995 created "2018-09-27" @default.
• W2891648995 creator A5002793870 @default.
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• W2891648995 date "2018-12-01" @default.
• W2891648995 modified "2023-10-15" @default.
• W2891648995 title "Chemically induced degradation of CK2 by proteolysis targeting chimeras based on a ubiquitin–proteasome pathway" @default.
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• W2891648995 doi "https://doi.org/10.1016/j.bioorg.2018.09.005" @default.
• W2891648995 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30245235" @default.
• W2891648995 hasPublicationYear "2018" @default.
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