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CiteWeb id: 20110000012

CiteWeb score: 5568

DOI: 10.1210/endo.138.3.4979

The rat estrogen receptor (ER) exists as two subtypes, ERα and ERβ, which differ in the C-terminal ligand binding domain and in the N-terminal transactivation domain. In this study we investigated the messenger RNA expression of both ER subtypes in rat tissues by RT-PCR and compared the ligand binding specificity of the ER subtypes. Saturation ligand binding analysis of in vitro synthesized human ERα and rat ERβ protein revealed a single binding component for 16α-iodo-17β-estradiol with high affinity[ dissociation constant (Kd) = 0.1 nm for ERα protein and 0.4 nm for ERβ protein]. Most estrogenic substances or estrogenic antagonists compete with 16α-[125I]iodo-17β-estradiol for binding to both ER subtypes in a very similar preference and degree; that is, diethylstilbestrol > hexestrol > dienestrol > 4-OH-tamoxifen > 17β-estradiol > coumestrol, ICI-164384 > estrone, 17α-estradiol > nafoxidine, moxestrol > clomifene > estriol, 4-OH-estradiol > tamoxifen, 2-OH-estradiol, 5-androstene-3β,17β-diol, genistein f...

The publication "Comparison of the Ligand Binding Specificity and Transcript Tissue Distribution of Estrogen Receptors α and β" is placed in the Top 10000 of the best publications in CiteWeb. Also in the category Biology it is included to the Top 1000. Additionally, the publicaiton "Comparison of the Ligand Binding Specificity and Transcript Tissue Distribution of Estrogen Receptors α and β" is placed in the Top 100 among other scientific works published in 2011.
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