Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel - sprookjes - yvandenbroek - TriplyDB

Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel

Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel

http://www.wikidata.org/entity/Q28379427

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A novel recessive hyperekplexia allele GLRA1 (S231R): genotyping by MALDI-TOF mass spectrometry and functional characterisation as a determinant of cellular glycine receptor trafficking Kinetic determinants of agonist action at the recombinant human glycine receptor The impact of human hyperekplexia mutations on glycine receptor structure and function A Recombinant Human Pluripotent Stem Cell Line Stably Expressing Halide-Sensitive YFP-I152L for GABAAR and GlyR-Targeted High-Throughput Drug Screening and Toxicity Testing.Recessive hyperekplexia mutations of the glycine receptor alpha1 subunit affect cell surface integration and stability Activation of human alpha1 and alpha2 homomeric glycine receptors by taurine and GABA Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels Slow phases of GABA(A) receptor desensitization: structural determinants and possible relevance for synaptic function Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor.Mechanisms of channel gating of the ligand-gated ion channel superfamily inferred from protein structure.Glycine receptor mouse mutants: model systems for human hyperekplexia 4-Chloropropofol enhances chloride currents in human hyperekplexic and artificial mutated glycine receptors.Glycine receptor mutants of the mouse: what are possible routes of inhibitory compensation?The role of intracellular linkers in gating and desensitization of human pentameric ligand-gated ion channels Structure and functions of inhibitory and excitatory glycine receptors.Building new function into glycine receptors: a structural model for the activation of the glycine-gated chloride channel.β Subunit M2-M3 loop conformational changes are uncoupled from α1 β glycine receptor channel gating: implications for human hereditary hyperekplexia.Genetics, an alternative way to discover, characterize and understand ion channels.M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective.NMR structures of the second transmembrane domain of the human glycine receptor alpha(1) subunit: model of pore architecture and channel gating.Zinc-mediated inhibition of GABA(A) receptors: discrete binding sites underlie subtype specificity.Structure and function of the glycine receptor and related nicotinicoid receptors.Theoretical studies of the M2 transmembrane segment of the glycine receptor: models of the open pore structure and current-voltage characteristics.Ligand- and subunit-specific conformational changes in the ligand-binding domain and the TM2-TM3 linker of {alpha}1 {beta}2 {gamma}2 GABAA receptors The neuronal channelopathies.Correlating structural and energetic changes in glycine receptor activation.Allosteric and hyperekplexic mutant phenotypes investigated on an α1 glycine receptor transmembrane structure Contributions of conserved residues at the gating interface of glycine receptors.Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor Function of hyperekplexia-causing α1R271Q/L glycine receptors is restored by shifting the affected residue out of the allosteric signalling pathway Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker.Fixation of allosteric states of the nicotinic acetylcholine receptor by chemical cross-linking.Mutation of a single residue in the S2-S3 loop of CNG channels alters the gating properties and sensitivity to inhibitors The extracellular linker of muscle acetylcholine receptor channels is a gating control element.Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels Characterization of 5-HT3 receptor mutations identified in schizophrenic patients.Probing protein packing surrounding the residues in and flanking the nicotinic acetylcholine receptor M2M3 loop.Phosphorylation of α3 glycine receptors induces a conformational change in the glycine-binding site.Intermediate closed state for glycine receptor function revealed by cysteine cross-linking.New hyperekplexia mutations provide insight into glycine receptor assembly, trafficking, and activation mechanisms.

P2860

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P2860

Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel

http://www.wikidata.org/entity/Q28379427

description

1997 nî lūn-bûn

@nan

1997 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի հունվարին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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name

Identification of intracellula ...... cine receptor chloride channel

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Identification of intracellula ...... cine receptor chloride channel

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Identification of intracellula ...... cine receptor chloride channel

@nl

type

label

Identification of intracellula ...... cine receptor chloride channel

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Identification of intracellula ...... cine receptor chloride channel

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Identification of intracellula ...... cine receptor chloride channel

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prefLabel

Identification of intracellula ...... cine receptor chloride channel

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Identification of intracellula ...... cine receptor chloride channel

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Identification of intracellula ...... cine receptor chloride channel

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The EMBO Journal

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Identification of intracellula ...... cine receptor chloride channel

@en

P2093

Barry PH

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Handford CA

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Lynch JW

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Rajendra S

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P2860

Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches

Importance of Arg-219 for correct biogenesis of alpha 1 homooligomeric glycine receptors

Mutations in the alpha 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia

Analysis of GLRA1 in hereditary and sporadic hyperekplexia: a novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis

Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia

A novel mutation (Gln266-->His) in the alpha 1 subunit of the inhibitory glycine-receptor gene (GLRA1) in hereditary hyperekplexia

High-efficiency transformation of mammalian cells by plasmid DNA

Evidence for recessive as well as dominant forms of startle disease (hyperekplexia) caused by mutations in the alpha 1 subunit of the inhibitory glycine receptor

Mutational analysis of familial and sporadic hyperekplexia

The atypical M2 segment of the beta subunit confers picrotoxinin resistance to inhibitory glycine receptor channels

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110-120

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4729864

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10.1093/EMBOJ/16.1.110

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1

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16

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Peter R Schofield

Kerrie D Pierce

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1997-01-01T00:00:00Z

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14199931

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9009272

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1169618

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