ArticlePloS one2018
NOP receptor pharmacological profile - A dynamic mass redistribution study.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Structural basis of GPCR coupling to distinct signal transducers: implications for biased signaling.Trends in biochemical sciences · 2022Review
- Pharmacology of Kappa Opioid Receptors: Novel Assays and Ligands.Frontiers in pharmacology · 2022Article
- A Dynamic Mass Redistribution Assay for the Human Sweet Taste Receptor Uncovers G-Protein Dependent Biased Ligands.Frontiers in pharmacology · 2022Article
- Label-Free Investigations on the G Protein Dependent Signaling Pathways of Histamine Receptors.International journal of molecular sciences · 2021Article
- Novel Mixed NOP/Opioid Receptor Peptide Agonists.Journal of medicinal chemistry · 2021Article
- Functional Selectivity Does Not Predict Antinociceptive/Locomotor Impairing Potencies of NOP Receptor Agonists.Frontiers in neuroscience · 2021Article
- Phenotypic assessment and ligand screening of ETA/ETB receptors with label-free dynamic mass redistribution assay.Naunyn-Schmiedeberg's archives of pharmacology · 2020Article
- Pharmacological profile of the neuropeptide S receptor: Dynamic mass redistribution studies.Pharmacology research & perspectives · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Nociceptin/Orphanin FQ (N/OFQ) peptide NOP receptor is coupled to pertussis toxin (PTX)-sensitive G proteins (Gi/o) whose activation leads to the inhibition of both cAMP production and calcium channel activity, and to the stimulation of potassium currents. The label free dynamic mass redistribution (DMR) approach has been demonstrated useful for investigating the pharmacological profile of G protein-coupled receptors. Herein, we employ DMR technology to systematically characterize the pharmacology of a large panel of NOP receptor ligands. These are of peptide and non-peptide nature and display varying degrees of receptor efficacy, ranging from full agonism to pure antagonism. Using Chinese hamster ovary (CHO) cells expressing the human NOP receptor we provide rank orders of potency for full and partial agonists as well as apparent affinities for selective antagonists. We find the pharmacological profile of NOP receptor ligands to be similar but not identical to values reported in the literature using canonical assays for Gi/o-coupled receptors. Our data demonstrate that holistic label-free DMR detection can be successfully used to investigate the pharmacology of the NOP receptor and to characterize the cellular effects of novel NOP receptor ligands.
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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.