Varaico: Literature-Extracted Genetic Variants

Gene:ESR1
Variant:p.C381S
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ESR1

NM_000125.4:p.C381S

Associated Papers

A close-up shot of protein-protein docking, from experiment to theory and reverse with the PROTAC performers.

Nguyen KQT et al.

Journal of Biomolecular Structure & Dynamics, 2025

Surveying helix 12 dynamics within constitutively active estrogen receptors using bipartite tetracysteine display.

Sendanayake LR et al.

The Journal of Biological Chemistry, 2025

39864623 (PubMed )
Supplement: mmc1.docx

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

Raloxifene and ICI182,780 increase estrogen receptor-alpha association with a nuclear compartment via overlapping sets of hydrophobic amino acids in activation function 2 helix 12.

Lupien M et al.

Molecular Endocrinology (baltimore, Md.), 2007

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

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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."