227 citations
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January 1998 in “Journal of biological chemistry/The Journal of biological chemistry” 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.
25 citations
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June 2019 in “Endocrine Related Cancer” This review discusses the structure and function of steroid nuclear receptors, particularly focusing on androgen receptor dysregulation in prostate cancer and androgen insensitivity syndromes, without reporting new experimental results.
2 citations
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July 2021 in “UNC Libraries” 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.
1 citations
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February 2022 in “bioRxiv (Cold Spring Harbor Laboratory)” This study uses cryo-electron microscopy to reveal how androgen receptor forms a non-obligate dimer to bind DNA, with implications for prostate cancer development.
October 2025 in “Proceedings of the National Academy of Sciences” This study identifies the PI4P-RHD4 module as a key regulator of GET pathway receptor dynamics in Arabidopsis, affecting TA protein insertion and root hair growth.