Synthesis and Biochemical Characterization of a Series of 17α-Perfluoroalkylated Estradiols as Selective Ligands for Estrogen Receptor α

2010 ◽  
Vol 53 (19) ◽  
pp. 6947-6953 ◽  
Author(s):  
Barbara Eignerová ◽  
David Sedlák ◽  
Martin Dračínský ◽  
Petr Bartůněk ◽  
Martin Kotora
Keyword(s):  
Estrogen Receptor ◽  
Biochemical Characterization ◽  
Estrogen Receptor Α ◽  
Selective Ligands

scholarly journals Functional characterization of somatic point mutations of the human estrogen receptor α (hERα) in adenomyosis uteri

2004 ◽  
Vol 10 (12) ◽  
pp. 853-860 ◽  
Author(s):  
Martin K. Oehler ◽  
Holger Greschik ◽  
Dagmar-C. Fischer ◽  
Xiaowen Tong ◽  
Roland Schuele ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Functional Characterization ◽  
Point Mutations ◽  
Estrogen Receptor Α ◽  
Human Estrogen Receptor

scholarly journals A Computational-Based Approach to Identify Estrogen Receptor α/β Heterodimer Selective Ligands

2018 ◽  
Vol 93 (3) ◽  
pp. 197-207 ◽  
Author(s):  
Carlos G. Coriano ◽  
Fabao Liu ◽  
Chelsie K. Sievers ◽  
Muxuan Liang ◽  
Yidan Wang ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Selective Ligands

Characterization of rodent constitutively active estrogen receptor α variants and their constitutive transactivation mechanisms

2017 ◽  
Vol 248 ◽  
pp. 16-26 ◽  
Author(s):  
Hirotaka Ishii ◽  
Yujiro Hattori ◽  
Arisa Munetomo ◽  
Hiroshi Watanabe ◽  
Yasuo Sakuma ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Constitutively Active

scholarly journals Generation and characterization of a complete null estrogen receptor α mouse using Cre/LoxP technology

2008 ◽  
Vol 321 (1-2) ◽  
pp. 145-153 ◽  
Author(s):  
Ming Chen ◽  
Andrew Wolfe ◽  
Xi Wang ◽  
Chawnshang Chang ◽  
Shuyuan Yeh ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α

Characterization of the fundamental properties of the N-terminal truncation (Δ exon 1) variant of estrogen receptor α in the rat

Gene ◽  
2015 ◽  
Vol 571 (1) ◽  
pp. 117-125 ◽  
Author(s):  
Yujiro Hattori ◽  
Hirotaka Ishii ◽  
Akio Morita ◽  
Yasuo Sakuma ◽  
Hitoshi Ozawa
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Fundamental Properties ◽  
Exon 1

scholarly journals Ligand-Selective Interdomain Conformations of Estrogen Receptor-α

2007 ◽  
Vol 21 (1) ◽  
pp. 49-61 ◽  
Author(s):  
Adrian Padron ◽  
Li Li ◽  
Eric M. Kofoed ◽  
Fred Schaufele
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Energy Transfer ◽  
Hormone Replacement ◽  
Estrogen Receptor Α ◽  
Full Length ◽  
Estrogen Receptor Modulators ◽  
Interaction Kinetics ◽  
Receptor Modulators

Abstract Selective estrogen receptor modulators (SERMs) inhibit estrogen activation of the estrogen receptor (ER) in some tissues but activate ER in other tissues. These tissue-selective actions suggest that SERMs may be identified with tissue specificities that would improve the safety of breast cancer and hormone replacement therapies. The identification of an improved SERM would be aided by understanding the effects of each SERM on the structure and interactions of ER. To date, the inability to obtain structures of the full-length ER has limited our structural characterization of SERM action to their antiestrogenic effects on the isolated ER ligand binding domain. We studied the effects of estradiol and the clinically useful SERMs 4-hydroxytamoxifen and fulvestrant on the conformation of the full-length ERα dimer complex by comparing, in living human breast cancer cells, the amounts of energy transfer between fluorophores attached to different domains of ERα. Estradiol, 4-hydroxytamoxifen, and fulvestrant all promoted the rapid formation of ERα dimers with equivalent interaction kinetics. The amino- and carboxyl-terminal ERα domains both contain activation functions differentially affected by these ligands, but the positions of only the carboxyl termini differed upon binding with estradiol, 4-hydroxytamoxifen, or fulvestrant. The association of a specific ERα dimer conformation with the binding of ligands of different clinical effect will assist the identification of a SERM with optimal tissue-selective estrogenic and antiestrogenic activities. These studies also provide a roadmap for dissecting important structural and kinetic details for any protein complex from the quantitative analysis of energy transfer.

Cloning and In Vitro Expression and Characterization of the Androgen Receptor and Isolation of Estrogen Receptor α from the Fathead Minnow (Pimephales promelas)

2004 ◽  
Vol 38 (23) ◽  
pp. 6314-6321 ◽  
Author(s):  
Vickie S. Wilson ◽  
Mary C. Cardon ◽  
Joseph Thornton ◽  
Joseph J. Korte ◽  
Gerald T. Ankley ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Fathead Minnow ◽  
Pimephales Promelas ◽  
Estrogen Receptor Α ◽  
In Vitro Expression
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