The Complete Primary Structure of Human Estrogen Receptor β (hERβ) and Its Heterodimerization with ER αin Vivoandin Vitro

1998 ◽  
Vol 243 (1) ◽  
pp. 122-126 ◽  
Author(s):  
Sumito Ogawa ◽  
Satoshi Inoue ◽  
Toru Watanabe ◽  
Hisahiko Hiroi ◽  
Akira Orimo ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Primary Structure ◽  
Estrogen Receptor Β ◽  
Human Estrogen Receptor ◽  
Complete Primary Structure

scholarly journals Human Estrogen Receptor β Binds DNA in a Manner Similar to and Dimerizes with Estrogen Receptor α

1997 ◽  
Vol 272 (41) ◽  
pp. 25832-25838 ◽  
Author(s):  
Paul Pace ◽  
Jacqueline Taylor ◽  
Sumathy Suntharalingam ◽  
R. Charles Coombes ◽  
Simak Ali
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Estrogen Receptor Β ◽  
Human Estrogen Receptor

Cloning and Characterization of Human Estrogen Receptor β Promoter

2000 ◽  
Vol 275 (2) ◽  
pp. 682-689 ◽  
Author(s):  
Long-Cheng Li ◽  
Che-Chung Yeh ◽  
Dana Nojima ◽  
Rajvir Dahiya
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Β ◽  
Human Estrogen Receptor

scholarly journals Human Estrogen Receptor β 548 Is Not a Common Variant in Three Distinct Populations

Endocrinology ◽  
2003 ◽  
Vol 144 (8) ◽  
pp. 3541-3546 ◽  
Author(s):  
Li Xu ◽  
Qiang Pan-Hammarström ◽  
Asta Försti ◽  
Kari Hemminki ◽  
Lennart Hammarström ◽  
...  
Keyword(s):  
Amino Acids ◽  
Estrogen Receptor ◽  
Base Pair ◽  
Estrogen Receptor Β ◽  
Common Variant ◽  
Human Populations ◽  
Functional Characteristics ◽  
Human Estrogen Receptor

Abstract Several isoforms of estrogen receptor (ER) β (also known as NR3A2) have been reported, including variants with different N-terminal ends. In rodents, two in-frame initiation codons (ATGs) are used to produce proteins of 530 and 549 amino acids, respectively. In humans, the upstream ATG is out of frame in all clones reported, until recently, when human clones with an extra A-T base pair placing the upstream ATG in frame were reported. The authors suggested that this could represent a novel polymorphism in the ERβ gene. Because human ERβ548 (hERβ548) and hERβ530 display different functional characteristics in vitro, it is of interest to determine if this variant constitutes a polymorphism in human populations. We therefore determined the frequency of this novel isoform in several populations including African (n = 96), Caucasian (n = 100), and Asian (n = 128) subjects using denaturing HPLC. We did not detect any alleles that correspond to hERβ548 in these samples or in additional samples of heterogeneous origin. It is concluded that hERβ548 is not a common variant in Africans, Caucasians, or Asians.

Cloning and Characterization of Human Estrogen Receptor β Isoforms

1998 ◽  
Vol 247 (1) ◽  
pp. 75-78 ◽  
Author(s):  
John T. Moore ◽  
David D. McKee ◽  
Kimberly Slentz-Kesler ◽  
Linda B. Moore ◽  
Stacey A. Jones ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Β ◽  
Human Estrogen Receptor

scholarly journals Identification and Characterization of a Functionally Distinct Form of Human Estrogen Receptor β

Endocrinology ◽  
2002 ◽  
Vol 143 (4) ◽  
pp. 1558-1558 ◽  
Author(s):  
Hilary A. Wilkinson ◽  
Johanna Dahllund ◽  
Hao Liu ◽  
Joel Yudkovitz ◽  
Sheng-Jian Cai ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Β ◽  
Distinct Form ◽  
Human Estrogen Receptor ◽  
Identification And Characterization
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