ArticlePloS one2017
Structure-Based Understanding of Binding Affinity and Mode of Estrogen Receptor α Agonists and Antagonists.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Integrative Network Pharmacology and Molecular Docking Analysis Reveals the Multitarget Mechanisms of Pterostilbene in Neurodegenerative Diseases.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Dauricine Mitigates Hypoxia Through Targeting ESR1, PIK3CA, and MTOR: A Network Pharmacology and Molecular Dynamics Simulation Investigation.Current issues in molecular biology · 2026Article
- XAI-ACSM: An Ensemble-Based Explainable Artificial Intelligence Framework for the Accurate Prediction of Anticancer Small Molecules.ACS omega · 2025Article
- Estrogen-like Activity ofBiomedicines · 2025Article
- Benzestrol Isomer Stereochemistry Determines the Distinct Estrogenic Activities and Conformations of the Eight Isomers When Bound to Estrogen Receptor α.ACS pharmacology & translational science · 2025Article
- Machine Learning and Large Language Models for Modeling Complex Toxicity Pathways and Predicting Steroidogenesis.Environmental science & technology · 2025Article
- Adopting Mechanistic Molecular Biology Approaches in Exposome Research for Causal Understanding.Environmental science & technology · 2024Review
- Article
- 7,7″-Dimethoxyagastisflavone Inhibits Proinflammatory Cytokine Release and Inflammatory Cell Recruitment through Modulating ERα Signaling.Biomedicines · 2021Article
- ERpred: a web server for the prediction of subtype-specific estrogen receptor antagonists.PeerJ · 2021Article
- Computer-Aided Ligand Discovery for Estrogen Receptor Alpha.International journal of molecular sciences · 2020Review
- Homology models of mouse and rat estrogen receptor-Computational toxicology (Amsterdam, Netherlands) · 2019Article
- Comparing Multiple Machine Learning Algorithms and Metrics for Estrogen Receptor Binding Prediction.Molecular pharmaceutics · 2018Article
- A Workflow for Identifying Metabolically Active Chemicals to ComplementComputational toxicology (Amsterdam, Netherlands) · 2018Article
- 3D-QSAR study of steroidal and azaheterocyclic human aromatase inhibitors using quantitative profile of protein-ligand interactions.Journal of cheminformatics · 2018Article
- High-Affinity Nucleic-Acid-Based Receptors for Steroids.ACS chemical biology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The flexible hydrophobic ligand binding pocket (LBP) of estrogen receptor α (ERα) allows the binding of a wide variety of endocrine disruptors. Upon ligand binding, the LBP reshapes around the contours of the ligand and stabilizes the complex by complementary hydrophobic interactions and specific hydrogen bonds with the ligand. Here we present a framework for quantitative analysis of the steric and electronic features of the human ERα-ligand complex using three dimensional (3D) protein-ligand interaction description combined with 3D-QSAR approach. An empirical hydrophobicity density field is applied to account for hydrophobic contacts of ligand within the LBP. The obtained 3D-QSAR model revealed that hydrophobic contacts primarily determine binding affinity and govern binding mode with hydrogen bonds. Several residues of the LBP appear to be quite flexible and adopt a spectrum of conformations in various ERα-ligand complexes, in particular His524. The 3D-QSAR was combined with molecular docking based on three receptor conformations to accommodate receptor flexibility. The model indicates that the dynamic character of the LBP allows accommodation and stable binding of structurally diverse ligands, and proper representation of the protein flexibility is critical for reasonable description of binding of the ligands. Our results provide a quantitative and mechanistic understanding of binding affinity and mode of ERα agonists and antagonists that may be applicable to other nuclear receptors.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.