ArticleBiophysical journal2010
Acetylcholine receptor channels activated by a single agonist molecule.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 45 citations in OpenAlex.
- Dynamics of receptor activation by agonists.Biophysical journal · 2024Review
- Bibliometric analysis of nicotinic acetylcholine receptors channel research (2000-2020).Channels (Austin, Tex.) · 2021Review
- Agonist efficiency from concentration-response curves: Structural implications and applications.Biophysical journal · 2021Article
- A 3D culture model of innervated human skeletal muscle enables studies of the adult neuromuscular junction.eLife · 2019Article
- Efficiency measures the conversion of agonist binding energy into receptor conformational change.The Journal of general physiology · 2019Article
- Cyclic activation of endplate acetylcholine receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Molecular recognition at cholinergic synapses: acetylcholine versus choline.The Journal of physiology · 2017Article
- A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.The Journal of general physiology · 2017Article
- Dose-Response Analysis When There Is a Correlation between Affinity and Efficacy.Molecular pharmacology · 2016Article
- Activation of endplate nicotinic acetylcholine receptors by agonists.Biochemical pharmacology · 2015Review
- Agonist activation of a nicotinic acetylcholine receptor.Neuropharmacology · 2015Review
- Function of the M1 π-helix in endplate receptor activation and desensitization.The Journal of physiology · 2015Article
- Catch-and-hold activation of muscle acetylcholine receptors having transmitter binding site mutations.Biophysical journal · 2014Article
- The additional ACh binding site at the α4(+)/α4(-) interface of the (α4β2)2α4 nicotinic ACh receptor contributes to desensitization.British journal of pharmacology · 2013Article
- Asymmetric transmitter binding sites of fetal muscle acetylcholine receptors shape their synaptic response.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The energy and work of a ligand-gated ion channel.Journal of molecular biology · 2013Review
- Function of interfacial prolines at the transmitter-binding sites of the neuromuscular acetylcholine receptor.The Journal of biological chemistry · 2013Article
- Loop C and the mechanism of acetylcholine receptor-channel gating.The Journal of general physiology · 2013Article
- Energy for wild-type acetylcholine receptor channel gating from different choline derivatives.Biophysical journal · 2013Article
- Action of nicotine and analogs on acetylcholine receptors having mutations of transmitter-binding site residue αG153.The Journal of general physiology · 2013Article
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 at 1 institution in 1 country.
Funding
Abstract
The neuromuscular acetylcholine receptor (AChR) is an allosteric protein that alternatively adopts inactive versus active conformations (R<-->R). The R shape has a higher agonist affinity and ionic conductance than R. To understand how agonists trigger this gating isomerization, we examined single-channel currents from adult mouse muscle AChRs that isomerize normally without agonists but have only a single site able to use agonist binding energy to motivate gating. We estimated the monoliganded gating equilibrium constant E(1) and the energy change associated with the R versus R change in affinity for agonists. AChRs with only one operational binding site gave rise to a single population of currents, indicating that the two transmitter binding sites have approximately the same affinity for the transmitter ACh. The results indicated that E(1) approximately 4.3 x 10(-3) with ACh, and approximately 1.7 x 10(-4) with the partial-agonist choline. From these values and the diliganded gating equilibrium constants, we estimate that the unliganded AChR gating constant is E(0) approximately 6.5 x 10(-7). Gating changes the stability of the ligand-protein complex by approximately 5.2 kcal/mol for ACh and approximately 3.3 kcal/mol for choline.
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What OpenQuestion holds
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.