ArticleJournal of molecular biology2012
Gating movement of acetylcholine receptor caught by plunge-freezing.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 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.
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.
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Who cites it
98 citing papers in PubMed.
- Article
- Targeted Mutations Activate Allosteric Modulation of α5-Containing Nicotinic Acetylcholine Receptors.ACS chemical neuroscience · 2026Article
- Challenges of conventional iterative all-atom and coarse-grained multiscale molecular dynamics.Scientific reports · 2026Article
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- A Simple Modification of a Commercial Plunge-Freezer to Allow Time-Resolved Vitrification for Cryo-EM Analyses of Light-Activated Proteins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Advancing time-resolved structural biology: latest strategies in cryo-EM and X-ray crystallography.Nature methods · 2025Review
- Functions and pharmacology of α2β2 nicotinic acetylcholine receptors; in and out of the shadow of α4β2 nicotinic acetylcholine receptors.Biochemical pharmacology · 2024Article
- Influence of lipid bilayer on the structure of the muscle-type nicotinic acetylcholine receptor.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanism of hydrophobic gating in the acetylcholine receptor channel pore.The Journal of general physiology · 2024Article
- Real-time tilting and twisting motions of ligand-bound states of α7 nicotinic acetylcholine receptor.European biophysics journal : EBJ · 2024Article
- Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking.International journal of molecular sciences · 2023Article
- Article
- Frozen in time: analyzing molecular dynamics with time-resolved cryo-EM.Structure (London, England : 1993) · 2023Review
- Recent advances and current trends in cryo-electron microscopy.Current opinion in structural biology · 2022Review
- Article
- Electron microscopy of cardiac 3D nanodynamics: form, function, future.Nature reviews. Cardiology · 2022Review
- Structural dynamics: review of time-resolved cryo-EM.Acta crystallographica. Section D, Structural biology · 2022Review
- Microsecond melting and revitrification of cryo samples: protein structure and beam-induced motion.Acta crystallographica. Section D, Structural biology · 2022Article
- Recent Insight into Lipid Binding and Lipid Modulation of Pentameric Ligand-Gated Ion Channels.Biomolecules · 2022Review
- Structural mechanism of muscle nicotinic receptor desensitization and block by curare.Nature structural & molecular biology · 2022Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The nicotinic acetylcholine (ACh) receptor converts transiently to an open-channel form when activated by ACh released into the synaptic cleft. We describe here the conformational change underlying this event, determined by electron microscopy of ACh-sprayed and freeze-trapped postsynaptic membranes. ACh binding to the α subunits triggers a concerted rearrangement in the ligand-binding domain, involving an ~1-Å outward displacement of the extracellular portion of the β subunit where it interacts with the juxtaposed ends of α-helices shaping the narrow membrane-spanning pore. The β-subunit helices tilt outward to accommodate this displacement, destabilising the arrangement of pore-lining helices, which in the closed channel bend inward symmetrically to form a central hydrophobic gate. Straightening and tangential motion of the pore-lining helices effect channel opening by widening the pore asymmetrically and increasing its polarity in the region of the gate. The pore-lining helices of the α(γ) and δ subunits, by flexing between alternative bent and straight conformations, undergo the greatest movements. This coupled allosteric transition shifts the structure from a tense (closed) state toward a more relaxed (open) state.
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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.