Associated Papers
The Impact of ESR1 Mutations on the Treatment of Metastatic Breast Cancer.
Pejerrey SM et al.
Hormones & Cancer, 2018
Structural underpinnings of oestrogen receptor mutations in endocrine therapy resistance.
Katzenellenbogen JA et al.
Nature Reviews. Cancer, 2018
Noninvasive detection of activating estrogen receptor 1 (ESR1) mutations in estrogen receptor-positive metastatic breast cancer.
Guttery DS et al.
Clinical Chemistry, 2015
Estrogen receptor mutations found in breast cancer metastases integrated with the molecular pharmacology of selective ER modulators.
Jordan VC et al.
Journal of the National Cancer Institute, 2015
Emergence of constitutively active estrogen receptor-α mutations in pretreated advanced estrogen receptor-positive breast cancer.
Jeselsohn R et al.
Clinical Cancer Research : an Official Journal of the American Association for Cancer Research, 2014
D538G mutation in estrogen receptor-α: A novel mechanism for acquired endocrine resistance in breast cancer.
Merenbakh-Lamin K et al.
Cancer Research, 2013
The tamoxifen-responsive estrogen receptor α mutant D351Y shows reduced tamoxifen-dependent interaction with corepressor complexes.
Yamamoto Y et al.
The Journal of Biological Chemistry, 2013
Pharmacogenetics of anti-estrogen treatment of breast cancer.
Del Re M et al.
Cancer Treatment Reviews, 2012
Amino-terminal domain of TIF2 is involved in competing for corepressor binding to glucocorticoid and progesterone receptors.
Wang D et al.
Biochemistry, 2007
Glutamic acid 709 substitutions highlight the importance of the interaction between androgen receptor helices H3 and H12 for androgen and antiandrogen actions.
Georget V et al.
Molecular Endocrinology (baltimore, Md.), 2006
Targeted mutation of key residues at the start of helix 12 in the hERalpha ligand-binding domain identifies the role of hydrogen-bonding and hydrophobic interactions in the activity of the protein.
Zhao C et al.
The Journal of Steroid Biochemistry and Molecular Biology, 2006
Repressive domain of unliganded human estrogen receptor alpha associates with Hsc70.
Ogawa S et al.
Genes to Cells : Devoted to Molecular & Cellular Mechanisms, 2005
Role of aspartate 351 in transactivation and active conformation of estrogen receptor alpha.
Kim JH et al.
Journal of Molecular Endocrinology, 2005
The clinical relevance of steroid hormone receptor corepressors.
Kumar R et al.
Clinical Cancer Research : an Official Journal of the American Association for Cancer Research, 2005
Estrogen receptor alpha (ESR1) mutant A908G is not a common feature in benign and malignant proliferations of the breast.
Tebbit CL et al.
Genes, Chromosomes & Cancer, 2004
MICoA, a novel metastasis-associated protein 1 (MTA1) interacting protein coactivator, regulates estrogen receptor-alpha transactivation functions.
Mishra SK et al.
The Journal of Biological Chemistry, 2003
The tamoxifen-responsive estrogen receptor alpha mutant D351Y shows reduced tamoxifen-dependent interaction with corepressor complexes.
Yamamoto Y et al.
The Journal of Biological Chemistry, 2001
Silencing and reactivation of the selective estrogen receptor modulator-estrogen receptor alpha complex.
Liu H et al.
Cancer Research, 2001
An antiestrogen-responsive estrogen receptor-alpha mutant (D351Y) shows weak AF-2 activity in the presence of tamoxifen.
Webb P et al.
The Journal of Biological Chemistry, 2000
The interaction of raloxifene and the active metabolite of the antiestrogen EM-800 (SC 5705) with the human estrogen receptor.
Schafer JI et al.
Cancer Research, 1999
The key to the antiestrogenic mechanism of raloxifene is amino acid 351 (aspartate) in the estrogen receptor.
Levenson AS et al.
Cancer Research, 1998
Estrogen receptor mutations and changes in estrogen receptor and progesterone receptor protein expression in metastatic or recurrent breast cancer.
Umekita Y et al.
Japanese Journal of Cancer Research : Gann, 1998
Control of the estrogen-like actions of the tamoxifen-estrogen receptor complex by the surface amino acid at position 351.
Levenson AS et al.
The Journal of Steroid Biochemistry and Molecular Biology, 0