ReviewThe Journal of physiology2010
Gating of nicotinic ACh receptors: latest insights into ligand binding and function.
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.
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.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- Arthropod repellent interactions with olfactory receptors and ionotropic receptors analyzed by molecular modeling.Current research in insect science · 2024Article
- Ion channels gated by acetylcholine and serotonin: structures, biology, and drug discovery.Acta pharmacologica Sinica · 2015Review
- Crystallization scale purification of α7 nicotinic acetylcholine receptor from mammalian cells using a BacMam expression system.Acta pharmacologica Sinica · 2015Article
- Nicotinic ACh receptors as therapeutic targets in CNS disorders.Trends in pharmacological sciences · 2015Review
- Nicotinic ACh receptors in the hippocampal circuit; functional expression and role in synaptic plasticity.The Journal of physiology · 2014Review
- Marine natural products acting on the acetylcholine-binding protein and nicotinic receptors: from computer modeling to binding studies and electrophysiology.Marine drugs · 2014Article
- Optogenetic studies of nicotinic contributions to cholinergic signaling in the central nervous system.Reviews in the neurosciences · 2014Review
- Two types of muscarinic acetylcholine receptors in Drosophila and other arthropods.Cellular and molecular life sciences : CMLS · 2013Article
- The structural mechanism of the Cys-loop receptor desensitization.Molecular neurobiology · 2013Review
- Article
- Functional α7 nicotinic ACh receptors on astrocytes in rat hippocampal CA1 slices.Journal of molecular neuroscience : MN · 2012Article
- Structure of the pentameric ligand-gated ion channel ELIC cocrystallized with its competitive antagonist acetylcholine.Nature communications · 2012Article
- Intersubunit bridge formation governs agonist efficacy at nicotinic acetylcholine α4β2 receptors: unique role of halogen bonding revealed.The Journal of biological chemistry · 2012Article
- Inhibition of the prokaryotic pentameric ligand-gated ion channel ELIC by divalent cations.PLoS biology · 2012Article
- Acetylcholine-binding protein in the hemolymph of the planorbid snail Biomphalaria glabrata is a pentagonal dodecahedron (60 subunits).PloS one · 2012Article
- Synaptic and intrinsic activation of GABAergic neurons in the cardiorespiratory brainstem network.PloS one · 2012Article
- Nicotinic acetylcholine receptor ligands, a patent review (2006-2011).Expert opinion on therapeutic patents · 2011Review
- Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor.The Journal of biological chemistry · 2011Article
- Allosteric modulators of the α4β2 subtype of neuronal nicotinic acetylcholine receptors.Biochemical pharmacology · 2011Review
- Blockade of neuronal α7-nAChR by α-conotoxin ImI explained by computational scanning and energy calculations.PLoS computational biology · 2011Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Nicotinic acetylcholine receptors (nAChRs) are in the superfamily of cys-loop receptors, and are widely expressed in the nervous system where they participate in a variety of physiological functions, including regulating excitability and neurotransmitter release, as well as neuromuscular contraction. Members of the cys-loop family of receptors, which also includes the molluscan ACh-binding protein (AChBP), a soluble protein that is analogous to the extracellular ligand-binding domain of the cys-loop receptors, are pentameric assemblies of five subunits, with each subunit arranged around a central pore. The binding of ACh to the extracellular interface between two subunits induces channel opening. With the recent 4 A resolution of the Torpedo nAChR, and the crystal structure of the AChBP, much has been learned about the structure of the ligand-binding domain and the channel pore, as well as major structural rearrangements that may confer channel opening, including a major rearrangement of the C-loop within the ligand binding pocket, and perhaps other regions including the F-loop (the beta8-beta9 linker), the beta1-beta2 linker and the cys-loop. Here I will review the latest findings from my lab aimed at a further understanding of the function of the neuronal nAChR channels (and in particular the role of desensitization), and our search for novel AChBP species that may lead to a further understanding of the function of the cys-loop receptor family.
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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.