ArticleComputational toxicology (Amsterdam, Netherlands)2019
Homology models of mouse and rat estrogen receptor-
Article in Computational toxicology (Amsterdam, Netherlands), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
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- Molecular docking analysis of imeglimin and its derivatives with estrogen receptor-alpha.Bioinformation · 2024Article
- Chronic Exposure to Low Levels of Parabens Increases Mammary Cancer Growth and Metastasis in Mice.Endocrinology · 2023Article
- Immunohistochemical Detection of Estrogen Receptor-Beta (ERβ) with PPZ0506 Antibody in Murine Tissue: From Pitfalls to Optimization.Biomedicines · 2022Article
- Molecular docking analysis of phytochemicals with estrogen receptor alpha.Bioinformation · 2022Article
- A small-molecule activator of the unfolded protein response eradicates human breast tumors in mice.Science translational medicine · 2021Article
- Estrogen receptor alpha (ERα)-mediated coregulator binding and gene expression discriminates the toxic ERα agonist diethylstilbestrol (DES) from the endogenous ERα agonist 17β-estradiol (E2).Cell biology and toxicology · 2020Article
- Application of Various Molecular Modelling Methods in the Study of Estrogens and Xenoestrogens.International journal of molecular sciences · 2020Review
- The SeComputational toxicology (Amsterdam, Netherlands) · 2020Article
- A comprehensive analysis of racial disparities in chemical biomarker concentrations in United States women, 1999-2014.Environment international · 2020Article
- EO771, the first luminal B mammary cancer cell line from C57BL/6 mice.Cancer cell international · 2020Article
- Endocrine Disruptors Induced Distinct Expression of Thyroid and Estrogen Receptors in Rat versus Mouse Primary Cerebellar Cell Cultures.Brain sciences · 2019Article
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4 authors.
Funding
Abstract
Crystal structures exist for human, but not rodent, estrogen receptor-α ligand-binding domain (ERα-LBD). Consequently, rodent studies involving binding of compounds to ERα-LBD are limited in their molecular-level interpretation and extrapolation to humans. Because the sequences of rodent and human ERα-LBDs are > 95% identical, we expected their 3D structures and ligand binding to be highly similar. To test this hypothesis, we used the human ERα-LBD structure (PDB 3UUD) as a template to produce rat and mouse homology models. Employing the rodent models and human structure, we generated docking poses of 23 Group A ligands (17ß-estradiol, diethylstilbestrol, and 21 paraben analogs) in AutoDock Vina for interspecies comparisons. Ligand RMSDs (Å) (median, 95% CI) were 0.49 (0.21-1.82) (human-mouse) and 1.19 (0.22-1.82) (human-rat), well below the 2.0-2.5 Å range for equivalent docking poses. Numbers of interspecies ligand-receptor residue contacts were highly similar, with Sorensen Sc (%) = 96.8 (90.0-100) (human-mouse) and 97.7 (89.5-100) (human-rat). Likewise, numbers of interspecies ligand-receptor residue contacts were highly correlated: Pearson
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