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This study suggests that residues Val-889 and Arg-752 in the androgen receptor's steroid binding domain are crucial for NH2-/carboxyl-terminal interaction, affecting receptor stability and function.

This study suggests that the residues Val-889 and Arg-752 in the androgen receptor steroid binding domain are crucial for the intermolecular interaction necessary for receptor dimerization and function.

This study comprehensively compared different crystalline forms of finasteride, including the new finasteride DMF solvate hemihydrate, to better understand their structural characteristics and intermolecular interactions.

This study investigated the molecular mechanisms behind the formation of drug-polymer inclusion complexes and found that carbamazepine can self-assemble into stable channel structures without guest polymers, unlike griseofulvin, which requires guest molecules for structural stability.

This study provides insight into the specific disulfide bond interactions between keratins and keratin associated proteins, suggesting non-random cysteine interactions crucial for stabilizing hair fiber structure.