ArticleScientific reports2017
Binding of N-methylscopolamine to the extracellular domain of muscarinic acetylcholine receptors.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Xanomeline displays concomitant orthosteric and allosteric binding modes at the MNature communications · 2023Article
- Recessive CHRM5 variant as a potential cause of neurogenic bladder.American journal of medical genetics. Part A · 2023Article
- The Third Extracellular Loop of Mammalian Odorant Receptors Is Involved in Ligand Binding.International journal of molecular sciences · 2022Article
- Live-cell microscopy or fluorescence anisotropy with budded baculoviruses-which way to go with measuring ligand binding to MOpen biology · 2022Article
- Predicting Residence Time of GPCR Ligands with Machine Learning.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Allostery of atypical modulators at oligomeric G protein-coupled receptors.Scientific reports · 2021Article
- Current Advances in Allosteric Modulation of Muscarinic Receptors.Biomolecules · 2020Review
- Novel long-acting antagonists of muscarinic ACh receptors.British journal of pharmacology · 2018Article
- Acetylcholine Neurotransmitter Receptor Densities in the Striatum of Hemiparkinsonian Rats Following Botulinum Neurotoxin-A Injection.Frontiers in neuroanatomy · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interaction of orthosteric ligands with extracellular domain was described at several aminergic G protein-coupled receptors, including muscarinic acetylcholine receptors. The orthosteric antagonists quinuclidinyl benzilate (QNB) and N-methylscopolamine (NMS) bind to the binding pocket of the muscarinic acetylcholine receptor formed by transmembrane α-helices. We show that high concentrations of either QNB or NMS slow down dissociation of their radiolabeled species from all five subtypes of muscarinic acetylcholine receptors, suggesting allosteric binding. The affinity of NMS at the allosteric site is in the micromolar range for all receptor subtypes. Using molecular modelling of the M
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