Conformational variability of the glycine receptor M2 domain in response to activation by different agonists. - Wikidata - wikimedia - TriplyDB

Conformational variability of the glycine receptor M2 domain in response to activation by different agonists.

Conformational variability of the glycine receptor M2 domain in response to activation by different agonists.

http://www.wikidata.org/entity/Q46970552

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Structural studies of the actions of anesthetic drugs on the γ-aminobutyric acid type A receptor Open-channel structures of the human glycine receptor α1 full-length transmembrane domain.Ethanol effects on glycinergic transmission: From molecular pharmacology to behavior responses Glycine receptor mouse mutants: model systems for human hyperekplexia Site-specific fluorescence reveals distinct structural changes induced in the human rho 1 GABA receptor by inhibitory neurosteroids.Bacterial Sphingomyelinase is a State-Dependent Inhibitor of the Cystic Fibrosis Transmembrane conductance Regulator (CFTR)β Subunit M2-M3 loop conformational changes are uncoupled from α1 β glycine receptor channel gating: implications for human hereditary hyperekplexia.Molecular characterization of agonists that bind to an insect GABA receptor.Atomistic insights into human Cys-loop receptors by solution NMR.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 A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists.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.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 Two amino acid residues contribute to a cation-π binding interaction in the binding site of an insect GABA receptor.Incompatibility between a pair of residues from the pre-M1 linker and Cys-loop blocks surface expression of the glycine receptor Molecular mechanisms of Cys-loop ion channel receptor modulation by ivermectin.Distinct properties of glycine receptor β+/α- interface: unambiguously characterizing heteromeric interface reconstituted in homomeric protein Xenopus borealis as an alternative source of oocytes for biophysical and pharmacological studies of neuronal ion channels.Function of hyperekplexia-causing α1R271Q/L glycine receptors is restored by shifting the affected residue out of the allosteric signalling pathway The relative orientation of the TM3 and TM4 domains varies between α1 and α3 glycine receptors Identification of an Inhibitory Alcohol Binding Site in GABAA ρ1 Receptors A cation-pi interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue.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.Ligand-specific conformational changes in the alpha1 glycine receptor ligand-binding domain Structural rearrangements in loop F of the GABA receptor signal ligand binding, not channel activation.Distinct structural changes in the GABAA receptor elicited by pentobarbital and GABA.New hyperekplexia mutations provide insight into glycine receptor assembly, trafficking, and activation mechanisms.Analysis of hyperekplexia mutations identifies transmembrane domain rearrangements that mediate glycine receptor activation.Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activation High Throughput Techniques for Discovering New Glycine Receptor Modulators and their Binding Sites.Magnitude of a conformational change in the glycine receptor beta1-beta2 loop is correlated with agonist efficacy.The structural basis of function in Cys-loop receptors.Agonist-dependent single channel current and gating in alpha4beta2delta and alpha1beta2gamma2S GABAA receptors Structure-activity analysis of ginkgolide binding in the glycine receptor pore.Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.Agonist- and antagonist-induced conformational changes of loop F and their contributions to the rho1 GABA receptor function.

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P2860

Conformational variability of the glycine receptor M2 domain in response to activation by different agonists.

http://www.wikidata.org/entity/Q46970552

description

2007 nî lūn-bûn

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Conformational variability of ...... ivation by different agonists.

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Henry A Lester

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Joseph W Lynch

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Mohammed I Dibas

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P2860

Kinetic determinants of agonist action at the recombinant human glycine receptor

Refined structure of the nicotinic acetylcholine receptor at 4A resolution

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

Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers, and transbilayer bundles.

Pore conformations and gating mechanism of a Cys-loop receptor.

A fluorophore attached to nicotinic acetylcholine receptor beta M2 detects productive binding of agonist to the alpha delta site.

Molecular structure and function of the glycine receptor chloride channel.

Probing ion-channel pores one proton at a time.

Shedding light on membrane proteins.

Emerging molecular mechanisms of general anesthetic action.

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10.1074/JBC.M706468200

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282

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Stephan A. Pless

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2007-10-02T00:00:00Z

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5934160

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