ZNF83 Inhibitors

Chemical inhibitors of ZNF83 can interfere with its function through various molecular mechanisms. Chelerythrine and Gö6976 act as inhibitors of protein kinase C (PKC), a family of kinases that phosphorylate a wide array of proteins, potentially including ZNF83. By inhibiting PKC, these chemicals can prevent the phosphorylation of ZNF83, which is a post-translational modification that can affect the protein's function. Similarly, genistein, a tyrosine kinase inhibitor, can impede the phosphorylation of ZNF83 by tyrosine kinases, which may be necessary for ZNF83's activity. Ibrutinib, which targets Bruton's tyrosine kinase (BTK), may disrupt signaling pathways that regulate ZNF83, leading to its functional inhibition. Moreover, C646 can inhibit the histone acetyltransferase p300, and if ZNF83 requires acetylation by p300 for its activity, then inhibition by C646 can lead to a decrease in ZNF83 function.

In addition to these mechanisms, other chemicals may affect ZNF83 through different pathways. Triptolide, an inhibitor of the transcription factor NF-κB, can inhibit the function of ZNF83 by preventing its regulation by NF-κB. PD173074, an inhibitor of fibroblast growth factor receptors (FGFRs), can inhibit ZNF83 function if ZNF83 is regulated by FGFR signaling pathways. Apigenin's inhibition of casein kinase 2 (CK2) can prevent the phosphorylation of ZNF83 by CK2, which may be necessary for ZNF83's function. GW5074, an inhibitor of Raf kinase, may lead to ZNF83 functional inhibition if ZNF83 relies on Raf-mediated signaling. Emodin, with its broad kinase inhibition profile, can interfere with ZNF83 function if ZNF83 is regulated by any of the kinases targeted by emodin. Lastly, alsterpaullone and AT7519, inhibitors of cyclin-dependent kinases, can inhibit ZNF83 if its function is modulated by cell cycle-dependent phosphorylation.