Associated Papers
A close-up shot of protein-protein docking, from experiment to theory and reverse with the PROTAC performers.
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Journal of Biomolecular Structure & Dynamics, 2025
Detection of ESR1 Mutations in Tissue and Liquid Biopsy with Novel Next-Generation Sequencing and Digital Droplet PCR Assays: Insights from Multi-Center Real Life Data of Almost 6000 Patients.
Borkar S et al.
Cancers, 2025
40282442 (PubMed )
Supplement: cancers-17-01266-s001.zip › cancers-3540268-supplementary.pdf
Targeting unique ligand binding domain structural features downregulates DKK1 in Y537S ESR1 mutant breast cancer cells.
Young KS et al.
Breast Cancer Research : Bcr, 2025
Targeting Unique Ligand Binding Domain Structural Features Downregulates DKK1 in Y537S ESR1 Mutant Breast Cancer Cells.
Young KS et al.
Research Square, 2024
Targeting Unique Ligand Binding Domain Structural Features Downregulates DKK1 in Y537S ESR1 Mutant Breast Cancer Cells.
Young KS et al.
Biorxiv : the Preprint Server for Biology, 2024
Discovery of novel covalent selective estrogen receptor degraders against endocrine-resistant breast cancer.
Wang Y et al.
Acta Pharmaceutica Sinica. B, 2023
Unconventional isoquinoline-based SERMs elicit fulvestrant-like transcriptional programs in ER+ breast cancer cells.
Hancock GR et al.
Npj Breast Cancer, 2022
Covalent ERα Antagonist H3B-6545 Demonstrates Encouraging Preclinical Activity in Therapy-Resistant Breast Cancer.
Furman C et al.
Molecular Cancer Therapeutics, 2022
A PROSS-designed extensively mutated estrogen receptor α variant displays enhanced thermal stability while retaining native allosteric regulation and structure.
Kriegel M et al.
Scientific Reports, 2021
Different ligands-different receptor conformations: modeling of the hER alpha LBD in complex with agonists and antagonists.
Egner U et al.
Medicinal Research Reviews, 2001
Crystal structure of a mutant hERalpha ligand-binding domain reveals key structural features for the mechanism of partial agonism.
Gangloff M et al.
The Journal of Biological Chemistry, 2001
Mutational analysis of cysteine residues within the hormone-binding domain of the human estrogen receptor identifies mutants that are defective in both DNA-binding and subcellular distribution.
Neff S et al.
Molecular Endocrinology (baltimore, Md.), 1994
Mutagenesis of cysteines in the hormone binding domain of the human estrogen receptor. Alterations in binding and transcriptional activation by covalently and reversibly attaching ligands.
Reese JC et al.
The Journal of Biological Chemistry, 1991
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