Both N- and C-terminal transactivation functions of DNA-bound ERalpha are blocked by a novel synthetic estrogen ligand.

@article{Yamamoto2003BothNA,
  title={Both N- and C-terminal transactivation functions of DNA-bound ERalpha are blocked by a novel synthetic estrogen ligand.},
  author={Yasuji Yamamoto and Osamu Wada and Ichiro Takada and Yoshiko Yogiashi and Jiro Shibata and Junn Yanagisawa and Kenji Kitazato and Shunsuke Kato},
  journal={Biochemical and biophysical research communications},
  year={2003},
  volume={312 3},
  pages={
          656-62
        }
}
Estrogen receptors (ERs) play a central role in the diverse actions of estrogen. A number of synthetic ER ligands have been generated that can modulate various ER functions. Here we show that TAS-108, representing a novel class of synthetic ER ligands, blocked both ER transactivation functions without inhibiting DNA-binding activity. A transient expression assay showed that similar to ICI182,780, TAS-108 exhibited pure antagonistic activity as it blocked both the N-terminal AF-1 and C-terminal… CONTINUE READING
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A phase I and pharmacokinetic study of TAS-108 in postmenopausal female patients with locally advanced, locally recurrent inoperable, or progressive metastatic breast cancer.

  • Clinical cancer research : an official journal of the American Association for Cancer Research
  • 2004
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Evaluation of the safety and tolerability of oral TAS-108 in postmenopausal patients with metastatic breast cancer.

  • Annals of oncology : official journal of the European Society for Medical Oncology
  • 2009
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