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Beclin-1 is comprised of three specific structural regions: a BH3 domain at the N-terminal (amino acids 114-123), a coiled-coil domain (CCD) (amino acids 144-269), and an evolutionarily conserved domain (ECD) (amino acids 244-337)

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Experimental investigations have demonstrated that S-23 possesses a high-affinity interaction profile at the androgen receptor, making it useful for comparative studies involving receptor selectivity, ligand binding characteristics, and structure-activity relationships among non-steroidal androgen receptor modulators

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