ReviewBritish journal of pharmacology2009
Role of protein kinase C in functional selectivity for desensitization at the mu-opioid receptor: from pharmacological curiosity to therapeutic potential.
Review in British journal of pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 17 citations in OpenAlex.
- Biasing G protein βγ subunit downstream signaling enhances the analgesic effects of endogenous opioid receptor agonists during nitroglycerin-induced thermal hypersensitivity.Molecular pharmacology · 2025Article
- Coincident Regulation of PLCMolecular pharmacology · 2022Article
- High-throughput screening and validation of antibodies against synaptic proteins to explore opioid signaling dynamics.Communications biology · 2021Article
- Post-translational Modifications of Opioid Receptors.Trends in neurosciences · 2020Review
- Opioid receptor interacting proteins and the control of opioid signaling.Current pharmaceutical design · 2013Review
- Chronic methadone treatment shows a better cost/benefit ratio than chronic morphine in mice.The Journal of pharmacology and experimental therapeutics · 2012Article
- Opioid receptor internalization contributes to dermorphin-mediated antinociception.Neuroscience · 2010Article
- GPCR theme editorial.British journal of pharmacology · 2009Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Opioid agonists are the best therapy for moderate to severe pain, but clinical use is limited due to the development of tolerance and dependence. For the first time, Bailey and co-workers have demonstrated functional selectivity for agonist-induced desensitization of mu-opioid receptors (MOR) in mature rat locus coeruleus neurons. Native MORs are differentially desensitized through separate, agonist-dependent signalling pathways; desensitization of the morphine-occupied receptor occurs via a protein kinase C alpha-dependent pathway while [D-Ala(2), N-MePhe(4), Gly-ol]enkephalin-mediated desensitization is via a G protein receptor kinase subtype 2-dependent mechanism. These results suggest that MORs adopt separate conformational states that either result in different efficiencies of G protein activation or access to phosphorylation by desensitization machinery (e.g. protein kinase C alpha or G protein receptor kinase subtype 2). Further study of the interaction of protein kinase C with MORs in native neurons will enhance our understanding of agonist-induced functional selectivity for desensitization at MORs and provide important insights into how to selectively modulate agonist efficacy to enhance therapeutic capabilities of opioid drugs.
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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.