The following articles (labelled with PubMed ID or TBD) are for your review
PMID | Data | Article Title | Organization |
24900588 |
25 |
Design and Synthesis of 4-(4-Benzoylaminophenoxy)phenol Derivatives As Androgen Receptor Antagonists. |
Tokyo Medical and Dental University |
23527816 |
7 |
SAR based design of nicotinamides as a novel class of androgen receptor antagonists for prostate cancer. |
Chonnam National University |
23462715 |
25 |
Development of silicon-containing bis-phenol derivatives as androgen receptor antagonists: selectivity switching by C/Si exchange. |
The University of Tokyo |
19856921 |
21 |
Synthesis, structure-activity relationships, and characterization of novel nonsteroidal and selective androgen receptor modulators. |
Acadia Pharmaceuticals |
20888766 |
50 |
Novel selective anti-androgens with a diphenylpentane skeleton. |
The University of Tokyo |
7707319 |
81 |
Synthesis and in vitro activity of 17 beta-(N-alkyl/arylformamido)- and 17 beta-[(N-alkyl/aryl)alkyl/arylamido]-4-methyl-4-aza-3-oxo-5 alpha-androstan-3-ones as inhibitors of human 5 alpha-reductases and antagonists of the androgen receptor. |
Chul Research Center |
12657271 |
71 |
Novel 6-aryl-1,4-dihydrobenzo[d]oxazine-2-thiones as potent, selective, and orally active nonsteroidal progesterone receptor agonists. |
Wyeth Research |
17574413 |
24 |
Synthesis and SAR of tetrahydropyrrolo[1,2-b][1,2,5]thiadiazol-2(3H)-one 1,1-dioxide analogues as highly potent selective androgen receptor modulators. |
Bristol-Myers Squibb Research and Development |
16019211 |
14 |
Ligands with dual vitamin D3-agonistic and androgen-antagonistic activities. |
The University of Tokyo |
12657272 |
47 |
Novel 5-aryl-1,3-dihydro-indole-2-thiones. potent, orally active progesterone receptor agonists. |
Wyeth Research |
30228001 |
26 |
Structure-activity relationship of novel (benzoylaminophenoxy)phenol derivatives as anti-prostate cancer agents. |
Ochanomizu University |
16935302 |
1 |
Thermodynamic penalty arising from burial of a ligand polar group within a hydrophobic pocket of a protein receptor. |
University of Leeds |