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Using reporter genes whose activity is driven by ARE half sites or by canonical AREs consisting of two such hexamers, the authors found that cooperativity between the LBDs enables transactivation from weaker, imperfect AREs and noted that direct AREs repeats do reinforce but are not required for AR dimerization

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The name reflects the three amino acids that form the peptide structure: Glycine Histidine Lysine Although GHK itself is biologically active, its most studied and therapeutically relevant form is GHK-Cu, which is formed when the peptide binds with a copper ion