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[DOI] [PubMed] [Google Scholar] 11.Doessing S., Heinemeier K.M., Holm L., Mackey A.L., Schjerling P., Rennie M., Smith K., Reitelseder S., Kappelgaard A.M., Rasmussen M.H., et al

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Since its discovery, the compound has been studied extensively in laboratory settings examining peptide communication pathways and molecular regulatory processes

At the molecular level, the mechanism has been structurally resolved by NMR spectroscopy (Nature Communications, 2025): FOXO4-DRI binds to the disordered p53 TAD2 domain and forms a transiently folded complex through both the FOXO4-derived peptide region and its cationic cell permeability element