ReviewBritish journal of pharmacology2018
Insights into the function of opioid receptors from molecular dynamics simulations of available crystal structures.
Review in British journal of pharmacology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 38 citations in OpenAlex.
- Identification of Subtype-Selective Binding Sites in the Opioid Receptor Family.Journal of chemical information and modeling · 2026Article
- Structure-Guided Repurposing of Approved Drugs Identifies Aprepitant and Mavorixafor as Putative δ-Opioid Receptor Agonist Candidates.International journal of molecular sciences · 2026Article
- Mechanistic insights into the therapeutic properties of delta opioid receptor.Science advances · 2026Article
- Evidencing the role of a conserved polar signaling channel in the activation mechanism of the μ-opioid receptor.Computational and structural biotechnology journal · 2025Article
- MDFit: automated molecular simulations workflow enables high throughput assessment of ligands-protein dynamics.Journal of computer-aided molecular design · 2024Article
- Three-Dimensional Structural Insights Have Revealed the Distinct Binding Interactions of Agonists, Partial Agonists, and Antagonists with the µ Opioid Receptor.International journal of molecular sciences · 2023Review
- Computational Methods for Understanding the Selectivity and Signal Transduction Mechanism of Aminomethyl Tetrahydronaphthalene to Opioid Receptors.Molecules (Basel, Switzerland) · 2022Article
- Recent Molecular Insights into Agonist-specific Binding to the Mu-Opioid Receptor.Frontiers in molecular biosciences · 2022Review
- Fundamentals of the Dynorphins/Kappa Opioid Receptor System: From Distribution to Signaling and Function.Handbook of experimental pharmacology · 2022Article
- Universal Properties and Specificities of the βInternational journal of molecular sciences · 2021Article
- Correlated Motions of Conserved Polar Motifs Lay out a Plausible Mechanism of G Protein-Coupled Receptor Activation.Biomolecules · 2021Article
- Exploring the putative mechanism of allosteric modulations by mixed-action kappa/mu opioid receptor bitopic modulators.Future medicinal chemistry · 2021Article
- Mechanistic Understanding of Peptide Analogues, DALDA, [DmtMolecules (Basel, Switzerland) · 2020Article
- Computer simulations of protein-membrane systems.Progress in molecular biology and translational science · 2020Article
- Recent Insights from Molecular Dynamics Simulations for G Protein-Coupled Receptor Drug Discovery.International journal of molecular sciences · 2019Review
- Molecular dynamics of fentanyl bound to μ-opioid receptor.Journal of molecular modeling · 2019Article
- Repurposing of a Nucleoside Scaffold from Adenosine Receptor Agonists to Opioid Receptor Antagonists.ACS omega · 2018Article
- Insights into the function of opioid receptors from molecular dynamics simulations of available crystal structures.British journal of pharmacology · 2018Review
- Emerging areas of opioid pharmacology.British journal of pharmacology · 2018Article
- Highly Potent and Selective New Diphenethylamines Interacting with the κ-Opioid Receptor: Synthesis, Pharmacology, and Structure-Activity Relationships.Journal of medicinal chemistry · 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
3 authors at 1 institution in 1 country.
Funding
Abstract
The opioid receptors are key targets in the treatment of acute and chronic pain, and the development of novel analgesics with reduced side effects is crucial in the search for more effective medications. The crystal structures of opioid receptors have provided a wealth of knowledge on many aspects of opioid receptor pharmacology and function, including ligand binding poses, location of the sodium allosteric binding site, conformational changes associated with activation and putative dimeric interfaces. These crystal structures also offer a starting point for molecular dynamics (MD) simulations to capture one aspect of drug design that static structures cannot resolve, namely protein dynamics. With the increase in computing power, MD simulations of crystal structures have become an influential tool in understanding the function of GPCRs in general. Here, we discuss lessons learned from MD simulations of opioid receptor crystal structures with reference to (i) the binding pathway of sodium to its crystallographic allosteric site, (ii) the dynamics of ligand-receptor and receptor-receptor interactions, both at the ligand- and G protein-binding sites, (iii) the binding pathway and binding pose of novel ligands, and (iv) opioid receptor oligomerization. LINKED ARTICLES: This article is part of a themed section on Emerging Areas of Opioid Pharmacology. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v175.14/issuetoc.
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.