RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells.
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Muscle-like nicotinic receptor accessory molecules in sensory hair cells of the inner earMammalian nicotinic acetylcholine receptors: from structure to functionDrug-dependent behaviors and nicotinic acetylcholine receptor expressions in Caenorhabditis elegans following chronic nicotine exposure.Novel and conserved protein macoilin is required for diverse neuronal functions in Caenorhabditis elegansChemical chaperones exceed the chaperone effects of RIC-3 in promoting assembly of functional α7 AChRsUBXD4, a UBX-containing protein, regulates the cell surface number and stability of alpha3-containing nicotinic acetylcholine receptorsα7 and β2 Nicotinic Acetylcholine Receptor Subunits Form Heteromeric Receptor Complexes that Are Expressed in the Human Cortex and Display Distinct Pharmacological PropertiesMouse RIC-3, an endoplasmic reticulum chaperone, promotes assembly of the alpha7 acetylcholine receptor through a cytoplasmic coiled-coil domainLooking below the surface of nicotinic acetylcholine receptorsFunctional expression of human α9* nicotinic acetylcholine receptors in X. laevis oocytes is dependent on the α9 subunit 5' UTR.Length and amino acid sequence of peptides substituted for the 5-HT3A receptor M3M4 loop may affect channel expression and desensitizationA mutation in the extracellular domain of the α7 nAChR reduces calcium permeability.The role of intracellular linkers in gating and desensitization of human pentameric ligand-gated ion channelsFunctional characterisation of a nicotinic acetylcholine receptor α subunit from the brown dog tick, Rhipicephalus sanguineus.Proteomic analysis of an alpha7 nicotinic acetylcholine receptor interactome.α7β2 nicotinic acetylcholine receptors assemble, function, and are activated primarily via their α7-α7 interfaces.RIC-3 exclusively enhances the surface expression of human homomeric 5-hydroxytryptamine type 3A (5-HT3A) receptors despite direct interactions with 5-HT3A, -C, -D, and -E subunitsRic-3 promotes alpha7 nicotinic receptor assembly and trafficking through the ER subcompartment of dendrites.Nicotine-induced up regulation of α4β2 neuronal nicotinic receptors is mediated by the protein kinase C-dependent phosphorylation of α4 subunits.The duplicated α7 subunits assemble and form functional nicotinic receptors with the full-length α7.Xenopus laevis RIC-3 enhances the functional expression of the C. elegans homomeric nicotinic receptor, ACR-16, in Xenopus oocytes.Cell-specific effects on surface α7 nicotinic receptor expression revealed by over-expression and knockdown of rat RIC3 protein.The Drosophila nicotinic acetylcholine receptor subunits Dα5 and Dα7 form functional homomeric and heteromeric ion channelsDifferential subcellular localization of RIC-3 isoforms and their role in determining 5-HT3 receptor composition.RIC-3 differentially modulates α4β2 and α7 nicotinic receptor assembly, expression, and nicotine-induced receptor upregulationStructural answers and persistent questions about how nicotinic receptors work.An allosteric modulator of alpha7 nicotinic receptors, N-(5-Chloro-2,4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea (PNU-120596), causes conformational changes in the extracellular ligand binding domain similar to those caused by acetylcholine.Structurally similar allosteric modulators of α7 nicotinic acetylcholine receptors exhibit five distinct pharmacological effects.Neural systems governed by nicotinic acetylcholine receptors: emerging hypotheses.Use of concatemers of ligand-gated ion channel subunits to study mechanisms of steroid potentiation.Resistance to Inhibitors of Cholinesterase 3 (Ric-3) Expression Promotes Selective Protein Associations with the Human α7-Nicotinic Acetylcholine Receptor Interactome.PICK1 interacts with alpha7 neuronal nicotinic acetylcholine receptors and controls their clustering.Identification and Characterization of a G Protein-binding Cluster in α7 Nicotinic Acetylcholine ReceptorsStoichiometry for α-bungarotoxin block of α7 acetylcholine receptors.The influence of allosteric modulators and transmembrane mutations on desensitisation and activation of α7 nicotinic acetylcholine receptorsTranscriptional Changes in nAChRs, Interactive Proteins and P450s in Locusta migratoria manilensis (Orthoptera: Acrididae) CNS in Response to High and Low Oral Doses of Imidacloprid.A three amino acid deletion in the transmembrane domain of the nicotinic acetylcholine receptor α6 subunit confers high-level resistance to spinosad in Plutella xylostella.RIC-3: a nicotinic acetylcholine receptor chaperoneAn overview of trafficking and assembly of neurotransmitter receptors and ion channels (Review).Trafficking of 5-HT(3) and GABA(A) receptors (Review).
P2860
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P2860
RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@ast
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@en
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@nl
type
label
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@ast
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@en
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@nl
prefLabel
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@ast
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@en
RIC-3 enhances functional expr ...... r subtypes in mammalian cells.
@nl
P2093
P356
P1476
RIC-3 enhances functional expr ...... or subtypes in mammalian cells
@en
P2093
Anne I Doward
Elizabeth R Baker
Neil S Millar
Patricia C Harkness
Stuart J Lansdell
Veronica J Gee
P304
P356
10.1124/MOL.105.017459
P577
2005-08-24T00:00:00Z