ArticleBiophysical journal2011
Temperature dependence of acetylcholine receptor channels activated by different agonists.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 41 citations in OpenAlex.
- The impact of diffusion on receptor binding during synaptic transmission.Biophysical journal · 2024Article
- Dynamics of receptor activation by agonists.Biophysical journal · 2024Review
- Article
- Pathways for nicotinic receptor desensitization.The Journal of general physiology · 2020Article
- Effects of hyperthermia on the effective concentration of rocuronium and sugammadex-mediated reversal in isolated phrenic nerve hemidiaphragm preparations of rats.BMC anesthesiology · 2020Article
- Efficiency measures the conversion of agonist binding energy into receptor conformational change.The Journal of general physiology · 2019Article
- A single molecular distance predicts agonist binding energy in nicotinic receptors.The Journal of general physiology · 2019Article
- Nicotinic acetylcholine receptors at the single-channel level.British journal of pharmacology · 2018Review
- Cyclic activation of endplate acetylcholine receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural correlates of affinity in fetal versus adult endplate nicotinic receptors.Nature communications · 2016Article
- Activation of endplate nicotinic acetylcholine receptors by agonists.Biochemical pharmacology · 2015Review
- Agonist activation of a nicotinic acetylcholine receptor.Neuropharmacology · 2015Review
- Quasithermodynamic contributions to the fluctuations of a protein nanopore.ACS chemical biology · 2015Article
- Functional differences between neurotransmitter binding sites of muscle acetylcholine receptors.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Catch-and-hold activation of muscle acetylcholine receptors having transmitter binding site mutations.Biophysical journal · 2014Article
- 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
- Loop C and the mechanism of acetylcholine receptor-channel gating.The Journal of general physiology · 2013Article
- Functional anatomy of an allosteric protein.Nature communications · 2013Article
- Entropy-enthalpy Compensation of Biomolecular Systems in Aqueous Phase: a Dry Perspective.Monatshefte fur chemie · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The temperature dependence of agonist binding and channel gating were measured for wild-type adult neuromuscular acetylcholine receptors activated by acetylcholine, carbamylcholine, or choline. With acetylcholine, temperature changed the gating rate constants (Q(10) ≈ 3.2) but had almost no effect on the equilibrium constant. The enthalpy change associated with gating was agonist-dependent, but for all three ligands it was approximately equal to the corresponding free-energy change. The equilibrium dissociation constant of the resting conformation (K(d)), the slope of the rate-equilibrium free-energy relationship (Φ), and the acetylcholine association and dissociation rate constants were approximately temperature-independent. In the mutant αG153S, the choline association and dissociation rate constants were temperature-dependent (Q(10) ≈ 7.4) but K(d) was not. By combining two independent mutations, we were able to compensate for the catalytic effect of temperature on the decay time constant of a synaptic current. At mouse body temperature, the channel-opening and -closing rate constants are ∼400 and 16 ms(-1). We hypothesize that the agonist dependence of the gating enthalpy change is associated with differences in ligand binding, specifically to the open-channel conformation of the protein.
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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.