ArticleThe Journal of physiology2002
Desensitization of diliganded mouse muscle nicotinic acetylcholine receptor channels.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Structural insights into the progressive recovery of α7 nicotinic acetylcholine receptor from nicotine-induced desensitization.Science advances · 2025Article
- Φ value analysis underscores strong functional and structural compactness of the GABAProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dynamics of receptor activation by agonists.Biophysical journal · 2024Review
- Fast desensitization of acetylcholine receptors induced by a spider toxin.Channels (Austin, Tex.) · 2021Article
- Article
- Agonist efficiency from concentration-response curves: Structural implications and applications.Biophysical journal · 2021Article
- Obtaining transition rates from single-channel data without initial parameter seeding.Channels (Austin, Tex.) · 2020Article
- Reduced Activation of the Synaptic-Type GABAMolecular pharmacology · 2020Article
- The desensitization pathway of GABANature communications · 2020Article
- Pathways for nicotinic receptor desensitization.The Journal of general physiology · 2020Article
- Measurements of the Timescale and Conformational Space of AMPA Receptor Desensitization.Biophysical journal · 2020Article
- Cryo-EM structures of a lipid-sensitive pentameric ligand-gated ion channel embedded in a phosphatidylcholine-only bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Efficiency measures the conversion of agonist binding energy into receptor conformational change.The Journal of general physiology · 2019Article
- The dual-gate model for pentameric ligand-gated ion channels activation and desensitization.The Journal of physiology · 2018Review
- Article
- Molecular recognition at cholinergic synapses: acetylcholine versus choline.The Journal of physiology · 2017Article
- Structural mechanisms of activation and desensitization in neurotransmitter-gated ion channels.Nature structural & molecular biology · 2016Review
- Modal affinities of endplate acetylcholine receptors caused by loop C mutations.The Journal of general physiology · 2015Article
- Activation of endplate nicotinic acetylcholine receptors by agonists.Biochemical pharmacology · 2015Review
- Agonist activation of a nicotinic acetylcholine receptor.Neuropharmacology · 2015Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Nicotinic ACh receptor channels (AChRs) exposed to high concentrations of ACh adopt 'desensitized' conformations that have a high affinity for the transmitter and no measurable ion conductance. Single-channel currents elicited by 0.1 or 1 mM ACh were recorded from human embryonic kidney (HEK) cells that had been transiently transfected with mouse alpha, beta, delta, and epsilon subunits. On the time scale of approximately 0.1 ms to approximately 1 h, apparent open intervals are described by a single exponential component, and shut intervals associated with desensitization are described by the sum of four or five exponential components. The kinetic behaviour appeared to be stationary and homogeneous. Desensitization rate constants were estimated by kinetic modelling of currents from cell-attached and outside-out patches (where the number of channels in the patch was measured). A single AChR recovered from the longest-lived desensitized state only after approximately 5 min. The occupancy of an AChR for each of the desensitized states was calculated as a function of time after the continuous application of a pulse of saturating ACh. The longest-lived desensitized state accounted for 90 % of the total only after several seconds. The fractional recovery from desensitization (during a 200 ms wash period) decreased as the duration of the desensitizing pulse increased, suggesting that recovery is slower from the longer-lived desensitized states. The free energy landscape for the AChR desensitization reaction in cell-attached patches exhibited an initial destabilization, followed by a plateau region of gradually increasing stability, followed by a deep well.
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