Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: serine-262 of the delta subunit is labeled by [3H]chlorpromazine
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End-plate acetylcholine receptor: structure, mechanism, pharmacology, and diseaseThe concept of allosteric interaction and its consequences for the chemistry of the brainThe nicotinic acetylcholine receptor: the founding father of the pentameric ligand-gated ion channel superfamilyGalanthamine and Non-competitive Inhibitor Binding to ACh-binding Protein: Evidence for a Binding Site on Non-α-subunit Interfaces of Heteromeric Neuronal Nicotinic ReceptorsX-ray structure of a pentameric ligand-gated ion channel in an apparently open conformationStructural basis for ion permeation mechanism in pentameric ligand-gated ion channelsA locally closed conformation of a bacterial pentameric proton-gated ion channelNeuronal nicotinic receptors: from protein structure to functionThe atypical M2 segment of the beta subunit confers picrotoxinin resistance to inhibitory glycine receptor channelsRelationships of agonist properties to the single channel kinetics of nicotinic acetylcholine receptorsTryptophan substitutions at lipid-exposed positions of the gamma M3 transmembrane domain increase the macroscopic ionic current response of the Torpedo californica nicotinic acetylcholine receptorPhotoaffinity Labeling of Pentameric Ligand-Gated Ion Channels: A Proteomic Approach to Identify Allosteric Modulator Binding Sites.Physicochemical and immunological studies of the N-terminal domain of the Torpedo acetylcholine receptor alpha-subunit expressed in Escherichia coli.The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: implications for the alpha-helical organization of regions MII and for the structure of the ion channel.M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor.Synporins--synthetic proteins that emulate the pore structure of biological ionic channels.Homologous mutations on different subunits cause unequal but additive effects on n-alcohol block in the nicotinic receptor poreTransmembrane topography of the nicotinic acetylcholine receptor delta subunit.Channel blocking properties of a series of nicotinic cholinergic agonists.Photolabeling reveals the proximity of the alpha-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor.Sensitivity to voltage-independent inhibition determined by pore-lining region of the acetylcholine receptor.Homology model of the GABAA receptor examined using Brownian dynamicsNormal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanismNicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranesStructure and function of inhibitory glycine receptors.The functional architecture of the acetylcholine nicotinic receptor explored by affinity labelling and site-directed mutagenesis.Allosteric regulation of pentameric ligand-gated ion channels: an emerging mechanistic perspectiveAntagonist activities of mecamylamine and nicotine show reciprocal dependence on beta subunit sequence in the second transmembrane domain.Desformylflustrabromine (dFBr) and [3H]dFBr-Labeled Binding Sites in a Nicotinic Acetylcholine Receptor.Genes expressed in the brain define three distinct neuronal nicotinic acetylcholine receptorsConservation of neural nicotinic acetylcholine receptors from Drosophila to vertebrate central nervous systemsAgonist-induced closure of constitutively open gamma-aminobutyric acid channels with mutated M2 domains.Three-dimensional structure of the nicotinic acetylcholine receptor and location of the major associated 43-kD cytoskeletal protein, determined at 22 A by low dose electron microscopy and x-ray diffraction to 12.5 A.Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction.Block of muscle nicotinic receptors by choline suggests that the activation and desensitization gates act as distinct molecular entities.Fixation of allosteric states of the nicotinic acetylcholine receptor by chemical cross-linking.Charge scan reveals an extended region at the intracellular end of the GABA receptor pore that can influence ion selectivity.Heterogeneity of the inhibitory glycine receptor.Saturable binding of anesthetics to nicotinic acetylcholine receptors. A possible mechanism of anesthetic action.Tris+/Na+ permeability ratios of nicotinic acetylcholine receptors are reduced by mutations near the intracellular end of the M2 region
P2860
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P2860
Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: serine-262 of the delta subunit is labeled by [3H]chlorpromazine
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Structure of the high-affinity ...... labeled by [3H]chlorpromazine
@ast
Structure of the high-affinity ...... labeled by [3H]chlorpromazine
@en
type
label
Structure of the high-affinity ...... labeled by [3H]chlorpromazine
@ast
Structure of the high-affinity ...... labeled by [3H]chlorpromazine
@en
prefLabel
Structure of the high-affinity ...... labeled by [3H]chlorpromazine
@ast
Structure of the high-affinity ...... labeled by [3H]chlorpromazine
@en
P2093
P2860
P356
P1476
Structure of the high-affinity ...... labeled by [3H]chlorpromazine
@en
P2093
P2860
P304
P356
10.1073/PNAS.83.8.2719
P407
P577
1986-04-01T00:00:00Z