PHF11C inhibitors are a class of chemicals that can modulate the interaction of the protein with chromatin or affect its expression levels and stability within the nucleus. Trichostatin A and sodium butyrate are inhibitors of histone deacetylases, which can lead to more open and transcriptionally active chromatin, thereby affecting the ability of PHF11C to bind to its chromatin targets. Similarly, vorinostat, another HDAC inhibitor, can also lead to chromatin relaxation and thus potentially disrupt PHF11C function. BIX-01294 and JQ1 target the methylation and acetylation readers of the chromatin, which can indirectly influence the genomic interaction points for PHF11C. These compounds can modify the epigenetic context in which PHF11C operates.
5-Azacytidine can be incorporated into DNA or RNA, which can affect the methylation status of DNA, a key epigenetic modification that could influence PHF11C's binding to methylated DNA. Mithramycin A, by binding to G-C rich DNA sequences, can block the genomic binding sites of PHF11C directly or its partner transcription factors indirectly. Chloroquine, through its DNA intercalating properties, can disrupt DNA-protein interactions, potentially affecting the binding dynamics of PHF11C. Genistein, by inhibiting tyrosine kinases, can alter the phosphorylation states of proteins and thereby modify PHF11C's interaction with other proteins. MG132, a proteasome inhibitor, can lead to an increase in the protein levels of nuclear proteins like PHF11C by inhibiting their degradation. Disulfiram, known for its primary action on acetaldehyde dehydrogenase, can also affect acetylation processes within the nucleus, thereby potentially modulating PHF11C's activity. Finally, I-CBP112 is a selective inhibitor of the BET family of proteins, which can have an indirect influence on the function of PHF11C by altering the recruitment of transcriptional machinery to specific loci where PHF11C may be active.
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