ReviewJournal of medicinal chemistry2026
Selective Inhibition of CK2: Emerging Strategies and Future Directions.
Review in Journal of medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
9 authors.
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Abstract
CK2 is a constitutively active serine/threonine kinase implicated in cancer, viral infection, and neurodegeneration, but its conserved ATP-binding site and complex holoenzyme assembly have long made selective inhibition challenging. This Perspective discusses three complementary strategies for selective CK2 inhibition: targeting the CK2α/β interface with small molecules, disrupting the same interface with conformationally constrained peptides, and exploiting the cryptic αD pocket for dual-site inhibitor design. CK2α/β-interface inhibitors, including CAM187, CAM7117 and P8C9, established structurally validated routes to modulate holoenzyme assembly and β-dependent substrate phosphorylation. Validation of the αD pocket as a ligandable cryptosteric site enabled dual-site ligands such as CAM4066 and αD-directed inhibitors such as CAM4712, followed by related advances including AB668, KDX1381 and Biv5. These efforts culminated in APL-5125, a highly selective, subnanomolar dual-site inhibitor now in Phase 1/2 clinical evaluation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.