Varaico: Literature-Extracted Genetic Variants

Gene:ESR1
Variant:p.L540Q
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ESR1

NM_000125.4:p.L540Q

Associated Papers

Concurrent genomic assessment of circulating tumour cells and ctDNA to guide therapy in metastatic breast cancer.

Allsopp RC et al.

Bmc Cancer, 2025

41351070 (PubMed )
Supplement: 12885_2025_15187_MOESM1_ESM.zip › Supp_Table_1.xlsx › Sheet1

Somatic estrogen receptor α mutations that induce dimerization promote receptor activity and breast cancer proliferation.

Irani S et al.

The Journal of Clinical Investigation, 2024

37883178 (PubMed )
Supplement: jci-134-163242-s231.xlsx › TableS5

ESR1 Gene Mutations and Liquid Biopsy in ER-Positive Breast Cancers: A Small Step Forward, a Giant Leap for Personalization of Endocrine Therapy?

Betz M et al.

Cancers, 2023

ESR1 activating mutations: From structure to clinical application.

Grinshpun A et al.

Biochimica Et Biophysica Acta. Reviews on Cancer, 2023

Estrogen Receptor Alpha and ESR1 Mutations in Breast Cancer.

Patel JM et al.

Advances in Experimental Medicine and Biology, 2022

Structural underpinnings of oestrogen receptor mutations in endocrine therapy resistance.

Katzenellenbogen JA et al.

Nature Reviews. Cancer, 2018

Estrogen receptor coregulator binding modulators (ERXs) effectively target estrogen receptor positive human breast cancers.

Raj GV et al.

Elife, 2017

Dynamic assembly and activation of estrogen receptor α enhancers through coregulator switching.

Murakami S et al.

Genes & Development, 2017

Estrogen receptor α L543A,L544A mutation changes antagonists to agonists, correlating with the ligand binding domain dimerization associated with DNA binding activity.

Arao Y et al.

The Journal of Biological Chemistry, 2013

A human estrogen receptor (ER)alpha mutation with differential responsiveness to nonsteroidal ligands: novel approaches for studying mechanism of ER action.

Paulmurugan R et al.

Molecular Endocrinology (baltimore, Md.), 2008

Agonist-like SERM effects on ERalpha-mediated repression of MMP1 promoter activity predict in vivo effects on bone and uterus.

Scafonas A et al.

The Journal of Steroid Biochemistry and Molecular Biology, 2008

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

Evolutionary identification of a subtype specific functional site in the ligand binding domain of steroid receptors.

Raviscioni M et al.

Proteins, 2006

Estrogen-occupied estrogen receptor represses cyclin G2 gene expression and recruits a repressor complex at the cyclin G2 promoter.

Stossi F et al.

The Journal of Biological Chemistry, 2006

Selective recognition of distinct classes of coactivators by a ligand-inducible activation domain.

Acevedo ML et al.

Molecular Cell, 2004

Mutual repression of transcriptional activation between the ETS-related factor ERG and estrogen receptor.

Vlaeminck-Guillem V et al.

Oncogene, 2003

Mutation of Leu-536 in human estrogen receptor-alpha alters the coupling between ligand binding, transcription activation, and receptor conformation.

Zhao C et al.

The Journal of Biological Chemistry, 2003

Modulation of estrogen receptor alpha function and stability by tamoxifen and a critical amino acid (Asp-538) in helix 12.

Pearce ST et al.

The Journal of Biological Chemistry, 2003

A role for coactivators and histone acetylation in estrogen receptor alpha-mediated transcription initiation.

Kim MY et al.

The Embo Journal, 2001

Estrogen receptor binding to DNA is not required for its activity through the nonclassical AP1 pathway.

Jakacka M et al.

The Journal of Biological Chemistry, 2001

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

A fusion protein of the estrogen receptor (ER) and nuclear receptor corepressor (NCoR) strongly inhibits estrogen-dependent responses in breast cancer cells.

Chien PY et al.

Molecular Endocrinology (baltimore, Md.), 1999

Function of estrogen receptor tyrosine 537 in hormone binding, DNA binding, and transactivation.

Yudt MR et al.

Biochemistry, 1999

Different positioning of the ligand-binding domain helix 12 and the F domain of the estrogen receptor accounts for functional differences between agonists and antagonists.

Nichols M et al.

The Embo Journal, 1998

The role of estrogen receptor mutations in tamoxifen-stimulated breast cancer.

Tonetti DA et al.

The Journal of Steroid Biochemistry and Molecular Biology, 1997

Neutral mutations to three acidic AF2 residues in the mouse estrogen receptor confer agonist activity to A-ring isomers of estradiol.

Schwartz JA et al.

The Journal of Steroid Biochemistry and Molecular Biology, 1997

A transcriptionally active estrogen receptor mutant is a novel type of dominant negative inhibitor of estrogen action.

McInerney EM et al.

Molecular Endocrinology (baltimore, Md.), 1996

Human estrogen receptor ligand activity inversion mutants: receptors that interpret antiestrogens as estrogens and estrogens as antiestrogens and discriminate among different antiestrogens.

Montano MM et al.

Molecular Endocrinology (baltimore, Md.), 1996

Analysis of mechanisms that determine dominant negative estrogen receptor effectiveness.

Schodin DJ et al.

The Journal of Biological Chemistry, 1995

Hormone binding and transcription activation by estrogen receptors: analyses using mammalian and yeast systems.

Katzenellenbogen BS et al.

The Journal of Steroid Biochemistry and Molecular Biology, 1993

Structure-function analysis of the hormone binding domain of the human estrogen receptor by region-specific mutagenesis and phenotypic screening in yeast.

Wrenn CK et al.

The Journal of Biological Chemistry, 1993

Powerful dominant negative mutants of the human estrogen receptor.

Ince BA et al.

The Journal of Biological Chemistry, 1993

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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."