Nicotinic acetylcholine receptors at the single-channel level
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چکیده
منابع مشابه
Single-channel properties of α3β4, α3β4α5 and α3β4β2 nicotinic acetylcholine receptors in mice lacking specific nicotinic acetylcholine receptor subunits
Previous attempts to measure the functional properties of recombinant nicotinic acetylcholine receptors (nAChRs) composed of known receptor subunits have yielded conflicting results. The use of knockout mice that lack α5, β2, α5β2 or α5β2α7 nAChR subunits enabled us to measure the single-channel properties of distinct α3β4, α3β4α5 and α3β4β2 receptors in superior cervical ganglion (SCG) neurons...
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The nicotinic acetylcholine receptor (nAChR) is a ligand-gated ion channel composed of 5 protein subunits arranged around a central cation selective pore. Several classes of natural and synthetic insecticides mediate their effect through interacting at nAChRs. This review examines the basic pharmacology of the neonicotinoids and related chemistry, with an emphasis on sapfeeding insects from the...
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....................................................................................................... 2 List of Figures .............................................................................................. 7 List of Tables ................................................................................................ 8 List of Abbreviations .............................................
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Qian, Hai, "Nematode nicotinic acetylcholine receptors: a single-channel study in Ascaris suum and Caenorhabditis elegans" (2007). Retrospective Theses and Dissertations. Paper 15930.
متن کاملNovel structural determinants of single-channel conductance in nicotinic acetylcholine and 5-hydroxytryptamine type-3 receptors.
Nicotinic ACh (acetylcholine) and 5-HT3 (5-hydroxytryptamine type-3) receptors are cation-selective ion channels of the Cys-loop transmitter-gated ion channel superfamily. Numerous lines of evidence indicate that the channel lining domain of such receptors is formed by the alpha-helical M2 domain (second transmembrane domain) contributed by each of five subunits present within the receptor comp...
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ژورنال
عنوان ژورنال: British Journal of Pharmacology
سال: 2017
ISSN: 0007-1188
DOI: 10.1111/bph.13770