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Upon attachment of androgen to the hormone-binding domain of the androgen receptor, conformational changes allow the complex to enter the nucleus, where it activates target-gene transcription through a DNA-binding domain interacting with the androgen-response element, producing protein products that effect androgen action

The study confirmed that FOXO4-DRI binds directly to the disordered p53 TAD2 domain and forms a transiently folded complex a disordered-to-ordered transition involving both the FOXO4-derived region of the DRI peptide and its cationic cell permeability element

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3D bioprinting of heterogeneous aortic valve conduits with alginate/gelatin hydrogels