Abstract
The transcription factor c-Myc is overexpressed in many tumors in human beings and has been identified as a highly promising target for cancer therapy. Most biological functions of c-Myc require heterodimerization with its activation partner Max. Inhibition of the protein–protein interactions between c-Myc and Max by small molecules has been shown to be a feasible and powerful approach toward the inhibition of c-Myc functions. More recently, stabilization of Max homodimers to reduce the amount of Max available for activating c-Myc has also been demonstrated to counteract Myc activity. This review summarizes our current knowledge on small organic molecules that inhibit c-Myc by modulating protein–protein interactions relevant for the biological function of this important oncoprotein.
Keywords
- Fluorescence Resonance Energy Transfer
- Leucine Zipper
- Oncogenic Transformation
- Chicken Embryo Fibroblast
- Fluorescence Polarization Assay
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Acknowledgments
Work in my research group is supported by the Deutsche Krebshilfe (German Cancer Aid). I would like to thank Wolfgang Reindl for generating Fig. 1b, and Angela Hollis for critical reading of the manuscript.
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Berg, T. (2010). Small-Molecule Modulators of c-Myc/Max and Max/Max Interactions. In: Vassilev, L., Fry, D. (eds) Small-Molecule Inhibitors of Protein-Protein Interactions. Current Topics in Microbiology and Immunology, vol 348. Springer, Berlin, Heidelberg. https://doi.org/10.1007/82_2010_90
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DOI: https://doi.org/10.1007/82_2010_90
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