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10058-F4 is a cell-permeable small molecule thiazolidinone that functions as a selective inhibitor of the **c-Myc-Max protein-protein interaction**. It binds specifically to the basic helix-loop-helix leucine zipper (bHLH-Zip) domain of c-Myc, preventing its dimerization with its partner protein Max. This disruption inhibits the binding of the c-Myc-Max heterodimer to E-box DNA sequences, thereby blocking the transcriptional activation of target genes involved in cell cycle progression, growth, and oncogenesis. Preclinically, 10058-F4 has demonstrated the ability to induce G0/G1 cell cycle arrest, promote caspase-3-dependent apoptosis, and induce myeloid differentiation in various malignant models, including acute myeloid leukemia (AML), hepatocellular carcinoma, and ovarian cancer. It is primarily utilized as a chemical research tool to study Myc-dependent pathways and is not currently in clinical development as a therapeutic agent.
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