ArticleBiochemistry2010
Lessons from free energy simulations of delta-opioid receptor homodimers involving the fourth transmembrane helix.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Single-molecule methods for characterizing receptor dimers reveal metastable opioid receptor homodimers that induce functional modulation.Nature communications · 2025Article
- Computational Modeling of Claudin Structure and Function.International journal of molecular sciences · 2020Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Single Proteoliposome High-Content Analysis Reveals Differences in the Homo-Oligomerization of GPCRs.Biophysical journal · 2018Article
- Molecular details of dimerization kinetics reveal negligible populations of transient µ-opioid receptor homodimers at physiological concentrations.Scientific reports · 2018Article
- Closely related, yet unique: Distinct homo- and heterodimerization patterns of G protein coupled chemokine receptors and their fine-tuning by cholesterol.PLoS computational biology · 2018Article
- An Ensemble-Based Protocol for the Computational Prediction of Helix-Helix Interactions in G Protein-Coupled Receptors using Coarse-Grained Molecular Dynamics.Journal of chemical theory and computation · 2017Article
- Methods used to study the oligomeric structure of G-protein-coupled receptors.Bioscience reports · 2017Review
- Article
- Impact of Lipid Composition and Receptor Conformation on the Spatio-temporal Organization of μ-Opioid Receptors in a Multi-component Plasma Membrane Model.PLoS computational biology · 2016Article
- The dopamine D2 receptor dimer and its interaction with homobivalent antagonists: homology modeling, docking and molecular dynamics.Journal of molecular modeling · 2016Article
- Molecular Pharmacology of δ-Opioid Receptors.Pharmacological reviews · 2016Review
- Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association.PLoS computational biology · 2015Article
- Computational approaches for modeling GPCR dimerization.Current pharmaceutical biotechnology · 2014Review
- Differential stability of the crystallographic interfaces of mu- and kappa-opioid receptors.PloS one · 2014Article
- Beyond standard molecular dynamics: investigating the molecular mechanisms of G protein-coupled receptors with enhanced molecular dynamics methods.Advances in experimental medicine and biology · 2014Review
- Novel structural and functional insights into M3 muscarinic receptor dimer/oligomer formation.The Journal of biological chemistry · 2013Article
- Membrane driven spatial organization of GPCRs.Scientific reports · 2013Article
- The prevalence, maintenance, and relevance of G protein-coupled receptor oligomerization.Molecular pharmacology · 2013Review
- Functional relevance of μ-δ opioid receptor heteromerization: a role in novel signaling and implications for the treatment of addiction disorders: from a symposium on new concepts in mu-opioid pharmacology.Drug and alcohol dependence · 2012Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Several G protein-coupled receptors (GPCRs), including opioid receptors deltaOR, muOR, and kappaOR, have been reported to form stable dimers or oligomers in lipid bilayers and cell membranes. This notion has been recently challenged by imaging data supporting a transient nature of GPCR association. Here we use umbrella sampling reconstructed free energies of deltaOR homodimers involving the fourth transmembrane helix to predict their association constant. The results of these simulations, combined with estimates of diffusion-limited association rates, suggest a short lifetime for deltaOR homodimers in the membrane, in agreement with recent trends.
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Registered trials
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