Associated Papers
Targeted therapy guided by circulating tumor DNA analysis in advanced gastrointestinal tumors.
Nakamura Y et al.
Nature Medicine, 2025
39284955 (PubMed )
Supplement: 41591_2024_3244_MOESM2_ESM.xlsx › Suppementary_Table_1
Disease characterization in liquid biopsy from HER2-mutated, non-amplified metastatic breast cancer patients treated with neratinib.
Shishido SN et al.
Npj Breast Cancer, 2022
35181666 (PubMed )
Supplement: 41523_2022_390_MOESM1_ESM.pdf
Decoding the Therapeutic Implications of the ERα Stability and Subcellular Distribution in Breast Cancer.
Tecalco-Cruz AC et al.
Frontiers in Endocrinology, 2022
Endocrine Resistance in Breast Cancer: The Role of Estrogen Receptor Stability.
Jeffreys SA et al.
Cells, 2020
Structural underpinnings of oestrogen receptor mutations in endocrine therapy resistance.
Katzenellenbogen JA et al.
Nature Reviews. Cancer, 2018
Highly sensitive detection of ESR1 mutations in cell-free DNA from patients with metastatic breast cancer using molecular barcode sequencing.
Masunaga N et al.
Breast Cancer Research and Treatment, 2018
Tyrosine dephosphorylation enhances the therapeutic target activity of epidermal growth factor receptor (EGFR) by disrupting its interaction with estrogen receptor (ER).
Ma S et al.
Oncotarget, 2015
Mutations of tyrosine 537 in the human estrogen receptor-alpha selectively alter the receptor's affinity for estradiol and the kinetics of the interaction.
Zhong L et al.
Biochemistry, 2002
Formation of a powerful capping motif corresponding to start of "helix 12" in agonist-bound estrogen receptor-alpha contributes to increased constitutive activity of the protein.
Skafar DF
Cell Biochemistry and Biophysics, 2000
Function of estrogen receptor tyrosine 537 in hormone binding, DNA binding, and transactivation.
Yudt MR et al.
Biochemistry, 1999
Constitutively active human estrogen receptors containing amino acid substitutions for tyrosine 537 in the receptor protein.
Weis KE et al.
Molecular Endocrinology (baltimore, Md.), 1996
Steroid receptor phosphorylation: Assigning function to site-specific phosphorylation.
Ward RD et al.
Biofactors (oxford, England), 0
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