ReviewThe Journal of physiology2010
Novel structural determinants of single channel conductance and ion selectivity in 5-hydroxytryptamine type 3 and nicotinic acetylcholine receptors.
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 27 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
27 citing papers in PubMed.
- The muscarinic antagonists scopolamine and atropine are competitive antagonists at 5-HT3 receptors.Neuropharmacology · 2016Article
- Ethanol effects on glycinergic transmission: From molecular pharmacology to behavior responses.Pharmacological research · 2015Review
- High yield and efficient expression and purification of the human 5-HT3A receptor.Acta pharmacologica Sinica · 2015Article
- Article
- Evidence for α-helices in the large intracellular domain mediating modulation of the α1-glycine receptor by ethanol and Gβγ.The Journal of pharmacology and experimental therapeutics · 2015Article
- Tracking the molecular evolution of calcium permeability in a nicotinic acetylcholine receptor.Molecular biology and evolution · 2014Article
- International Union of Basic and Clinical Pharmacology. XC. multisite pharmacology: recommendations for the nomenclature of receptor allosterism and allosteric ligands.Pharmacological reviews · 2014Article
- Article
- Utrophin regulates modal gating of mechanosensitive ion channels in dystrophic skeletal muscle.The Journal of physiology · 2014Article
- Impact of intracellular domain flexibility upon properties of activated human 5-HT3 receptors.British journal of pharmacology · 2014Article
- Long distance effect on ligand-gated ion channels extracellular domain may affect interactions with the intracellular machinery.Communicative & integrative biology · 2014Article
- Seeking structural specificity: direct modulation of pentameric ligand-gated ion channels by alcohols and general anesthetics.Pharmacological reviews · 2014Review
- Elucidation of molecular impediments in the α6 subunit for in vitro expression of functional α6β4* nicotinic acetylcholine receptors.The Journal of biological chemistry · 2013Article
- Mutagenic analysis of the intracellular portals of the human 5-HT3A receptor.The Journal of biological chemistry · 2013Article
- Agonist-dependent endocytosis of γ-aminobutyric acid type A (GABAA) receptors revealed by a γ2(R43Q) epilepsy mutation.The Journal of biological chemistry · 2013Article
- The 5-HT3AB receptor shows an A3B2 stoichiometry at the plasma membrane.Biophysical journal · 2013Article
- The structural mechanism of the Cys-loop receptor desensitization.Molecular neurobiology · 2013Review
- Discriminating between 5-HT₃A and 5-HT₃AB receptors.British journal of pharmacology · 2013Review
- Approaching the 5-HT₃ receptor heterogeneity by computational studies of the transmembrane and intracellular domains.Journal of computer-aided molecular design · 2013Article
- The basic property of Lys385 is important for potentiation of the human α1 glycine receptor by ethanol.The Journal of pharmacology and experimental therapeutics · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Nicotinic acetylcholine (nACh) and 5-hydroxytryptamine type 3 (5-HT(3)) receptors are cation-selective ion channels of the pentameric ligand-gated ion channel (pLGIC) superfamily. Multiple lines of evidence adduced over the last 30 years indicate that the lining of the channel of such receptors is formed by the alpha-helical second transmembrane (TM2) domain and flanking sequences contributed by each of the five subunits present within the receptor complex. Specific amino acid residues within, and adjacent to, the TM2 domain influence single channel conductance, ion selectivity, and other aspects of receptor function that include gating and desensitization. However, more recent work has revealed important structural determinants of single channel conductance and ion selectivity that are not associated with the TM2 domain. Direct experimental evidence indicates that the intracellular domain of eukaryotic pLGICs, in particular a region of the loop linking TM3 and TM4 termed the membrane-associated (MA) stretch, exerts a strong influence upon ion channel biophysics. Moreover, recent computational approaches, complemented by experimentation, implicate the extracellular domain as an additional important determinant of ion conduction. This brief review describes how our knowledge of ion conduction and selectivity in cation-selective pLGICs has evolved beyond TM2.
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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.