Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.
about
The molecular pharmacology of volatile anestheticsZinc-dependent modulation of α2- and α3-glycine receptor subunits by ethanol.Crosslinking constraints and computational models as complementary tools in modeling the extracellular domain of the glycine receptorEthanol effects on glycinergic transmission: From molecular pharmacology to behavior responsesMutation of a zinc-binding residue in the glycine receptor α1 subunit changes ethanol sensitivity in vitro and alcohol consumption in vivoThe Molecular Mechanisms of Anesthetic Action: Updates and Cutting Edge Developments from the Field of Molecular Modeling.A transmembrane amino acid in the GABAA receptor β2 subunit critical for the actions of alcohols and anesthetics.Modeling anesthetic binding sites within the glycine alpha one receptor based on prokaryotic ion channel templates: the problem with TM4.Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases.Characterization of two mutations, M287L and Q266I, in the α1 glycine receptor subunit that modify sensitivity to alcohols.The relative orientation of the TM3 and TM4 domains varies between α1 and α3 glycine receptorsInter- and Intra-Subunit Butanol/Isoflurane Sites of Action in the Human Glycine Receptor.A novel alcohol-sensitive position in the N-methyl-D-aspartate receptor GluN2A subunit M3 domain regulates agonist affinity and ion channel gating.Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activationReversal of ion-charge selectivity renders the pentameric ligand-gated ion channel GLIC insensitive to anaestheticsAlcohol-binding sites in distinct brain proteins: the quest for atomic level resolution.Titrating Tipsy Targets: The Neurobiology of Low-Dose Alcohol.Structure and Pharmacologic Modulation of Inhibitory Glycine Receptors.
P2860
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P2860
Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@ast
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@en
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@nl
type
label
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@ast
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@en
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@nl
prefLabel
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@ast
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@en
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@nl
P2093
P2860
P356
P1476
Linking of Glycine Receptor Tr ...... Intrasubunit-Facing Residues.
@en
P2093
J R Trudell
L M McCracken
M L McCracken
R A Harris
P2860
P356
10.1021/CN100019G
P577
2010-07-01T00:00:00Z