Associated Papers
Cadmium activation of wild-type and constitutively active estrogen receptor alpha.
Psaltis JB et al.
Frontiers in Endocrinology, 2024
Comparison of TCGA and GENIE genomic datasets for the detection of clinically actionable alterations in breast cancer.
Kaur P et al.
Scientific Reports, 2019
30728399 (PubMed )
Supplement: 41598_2018_37574_MOESM1_ESM.pdf
Agonist-like SERM effects on ERalpha-mediated repression of MMP1 promoter activity predict in vivo effects on bone and uterus.
Scafonas A et al.
The Journal of Steroid Biochemistry and Molecular Biology, 2008
Estrogenic effects of resveratrol in breast cancer cells expressing mutant and wild-type estrogen receptors: role of AF-1 and AF-2.
Gehm BD et al.
The Journal of Steroid Biochemistry and Molecular Biology, 2004
T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha.
Chen D et al.
The Journal of Biological Chemistry, 2003
Modulation of estrogen receptor alpha function and stability by tamoxifen and a critical amino acid (Asp-538) in helix 12.
Pearce ST et al.
The Journal of Biological Chemistry, 2003
Structural regions of ERalpha critical for synergistic transcriptional responses contain co-factor interacting surfaces.
Sathya G et al.
Molecular and Cellular Endocrinology, 2002
Fusion estrogen receptor proteins: toward the development of receptor-based agonists and antagonists.
Muyan M et al.
Molecular and Cellular Endocrinology, 2001
Silencing and reactivation of the selective estrogen receptor modulator-estrogen receptor alpha complex.
Liu H et al.
Cancer Research, 2001
Allosteric silencing of activating function 1 in the 4-hydroxytamoxifen estrogen receptor complex is induced by substituting glycine for aspartate at amino acid 351.
MacGregor Schafer J et al.
Cancer Research, 2000
The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation.
Lonard DM et al.
Molecular Cell, 2000
Human estrogen receptor ligand activity inversion mutants: receptors that interpret antiestrogens as estrogens and estrogens as antiestrogens and discriminate among different antiestrogens.
Montano MM et al.
Molecular Endocrinology (baltimore, Md.), 1996
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