ReviewThe Journal of physiology2010
What single-channel analysis tells us of the activation mechanism of ligand-gated channels: the case of the glycine receptor.
Review in The Journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 42 citations in OpenAlex.
- Ligand Binding Dynamics of Ion Channels and GPCRs Using Single-Molecule Fluorescence.Annual review of biophysics · 2026Review
- Hidden complexity of α7 nicotinic acetylcholine receptor desensitization revealed by MD simulations and Markov state modeling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring the Activation Process of the Glycine Receptor.Journal of the American Chemical Society · 2024Article
- Divergent mechanisms of steroid inhibition in the human ρ1 GABANature communications · 2024Article
- Electrophysiological Properties of Endogenous Single CaInternational journal of molecular sciences · 2021Article
- State-dependent protein-lipid interactions of a pentameric ligand-gated ion channel in a neuronal membrane.PLoS computational biology · 2021Article
- String method solution of the gating pathways for a pentameric ligand-gated ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Startle Disease Mutation E103K Impairs Activation of Human Homomeric α1 Glycine Receptors by Disrupting an Intersubunit Salt Bridge across the Agonist Binding Site.The Journal of biological chemistry · 2017Article
- Trapping of ivermectin by a pentameric ligand-gated ion channel upon open-to-closed isomerization.Scientific reports · 2017Article
- Mutational Analysis at Intersubunit Interfaces of an Anionic Glutamate Receptor Reveals a Key Interaction Important for Channel Gating by Ivermectin.Frontiers in molecular neuroscience · 2017Article
- Amino acid composition in eyes from zebrafish (Danio rerio) and sardine (Sardina pilchardus) at the larval stage.SpringerPlus · 2016Article
- Correlating structural and energetic changes in glycine receptor activation.The Journal of biological chemistry · 2015Article
- Mechanism of activation of the prokaryotic channel ELIC by propylamine: a single-channel study.The Journal of general physiology · 2015Article
- Unraveling mechanisms underlying partial agonism in 5-HT3A receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- The Concise Guide to PHARMACOLOGY 2013/14: ligand-gated ion channels.British journal of pharmacology · 2013Article
- Influence of GluN2 subunit identity on NMDA receptor function.Neuropharmacology · 2013Review
- P2X receptor intermediate activation states have altered nucleotide selectivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- The α1K276E startle disease mutation reveals multiple intermediate states in the gating of glycine receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Inhibition of the prokaryotic pentameric ligand-gated ion channel ELIC by divalent cations.PLoS biology · 2012Article
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Authors and funding
1 author at 1 institution in 1 country.
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Abstract
Glycine receptors are, in several ways, the member of the nicotinic superfamily that is best-suited for single-channel recording. That means that they are ideal for testing ideas about how activation proceeds in a ligand-gated ion channel from the binding of the agonist to the opening of the channel. This review describes the quantitative characterization by single-channel analysis of a novel activation mechanism for the glycine receptor. The favourable properties of the glycine receptor allowed the first detection of a conformation change that follows the binding of the agonist but precedes the opening of the channel. We used the term 'flipping' to describe this pre-opening conformational change. The 'flipped' state has a binding affinity higher than the resting state, but lower than the open state. This increased affinity presumably reflects a structural change near the agonist binding site, possibly the 'capping' of the C-loop. The significance of the 'flip' activation mechanism goes beyond understanding the behaviour and the structure-function relation of glycine channels, as this mechanism can be applied also to other members of the superfamily, such as the muscle nicotinic receptor. The 'flip' mechanism has thrown light on the question of why partial agonists are not efficacious at keeping the channel open, a question that is fundamental to rational drug design. In both muscle nicotinic and glycine receptors, partial agonists are as good as full agonists at opening the channel once flipping has occurred, but are not as effective as full agonists in eliciting this early conformational change.
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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.