Chemical inhibitors of zinc finger protein 945 can be characterized by their distinct mechanisms of action that directly impact the functionality of the protein. Chelerythrine operates by obstructing the DNA binding site of zinc finger protein 945, resulting in the inhibition of its interaction with target gene sequences. Similarly, NSC 624206 exerts its inhibitory effect by directly binding to the zinc finger motif, which is integral to the DNA-binding activity of the protein. Luteolin disrupts the function of zinc finger protein 945 by altering its phosphorylation state, thus impacting its ability to bind DNA. Another inhibitor, PDTC, compromises the structural integrity of zinc finger protein 945 by chelating zinc ions, which are crucial for maintaining the protein's zinc finger domains. Disulfiram targets the protein differently by modifying cysteine residues within the zinc finger domain, which is necessary for DNA binding, while ellagic acid competes with zinc finger protein 945 for specific DNA binding sites, thereby inhibiting its gene regulatory activity. Epigallocatechin gallate also impairs the DNA-binding domain of the protein, which is essential for its role in gene expression modulation.
Continuing with the theme of targeting the structural aspects of zinc finger protein 945, clotrimazole functions by binding to the zinc ion within the finger-like domain, which is vital for DNA interaction. Similarly, clioquinol acts by sequestering metal ions needed for the zinc finger motifs to fold properly and function effectively. Ebselen inhibits zinc finger protein 945 by disrupting the redox state required for the protein's activity, mimicking glutathione peroxidase activity. Pyrithione zinc disrupts zinc homeostasis, a key factor in maintaining the structure of zinc finger proteins, thereby inhibiting zinc finger protein 945. Lastly, stattic serves as an inhibitor by blocking STAT3 phosphorylation, which is presumed to be essential for the activity of zinc finger protein 945 in certain signaling pathways. Each chemical described here targets specific aspects of zinc finger protein 945, leading to its functional inhibition without affecting gene expression or protein translation pathways.
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