A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists.
about
Principles of agonist recognition in Cys-loop receptorsFunctional probes of drug-receptor interactions implicated by structural studies: Cys-loop receptors provide a fertile testing groundDisturbed neuronal ER-Golgi sorting of unassembled glycine receptors suggests altered subcellular processing is a cause of human hyperekplexia.Contributions of conserved residues at the gating interface of glycine receptors.Two amino acid residues contribute to a cation-π binding interaction in the binding site of an insect GABA receptor.A molecular characterization of the agonist binding site of a nematode cys-loop GABA receptor.Variations in binding among several agonists at two stoichiometries of the neuronal, α4β2 nicotinic receptor.Cation-π interactions: computational analyses of the aromatic box motif and the fluorination strategy for experimental evaluationIntermediate state trapping of a voltage sensorGenetic and functional analyses demonstrate a role for abnormal glycinergic signaling in autism.Fluorinated amino acids: compatibility with native protein structures and effects on protein-protein interactions.Incorporation of Non-Canonical Amino Acids.Structure and Pharmacologic Modulation of Inhibitory Glycine Receptors.Disturbances of Ligand Potency and Enhanced Degradation of the Human Glycine Receptor at Affected Positions G160 and T162 Originally Identified in Patients Suffering from Hyperekplexia.The GlyR Extracellular β8-β9 Loop - A Functional Determinant of Agonist Potency.Molecular basis for class Ib anti-arrhythmic inhibition of cardiac sodium channels.A systematic analysis of atomic protein-ligand interactions in the PDB.Probing the molecular basis of hERG drug block with unnatural amino acids.Functional Consequences of the Postnatal Switch From Neonatal to Mutant Adult Glycine Receptor α1 Subunits in the Shaky Mouse Model of Startle Disease.The roles of aromatic residues in the glycine receptor transmembrane domain
P2860
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P2860
A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A cation-π interaction at a ph ...... served for different agonists.
@ast
A cation-π interaction at a ph ...... served for different agonists.
@en
A cation-π interaction at a ph ...... served for different agonists.
@nl
type
label
A cation-π interaction at a ph ...... served for different agonists.
@ast
A cation-π interaction at a ph ...... served for different agonists.
@en
A cation-π interaction at a ph ...... served for different agonists.
@nl
prefLabel
A cation-π interaction at a ph ...... served for different agonists.
@ast
A cation-π interaction at a ph ...... served for different agonists.
@en
A cation-π interaction at a ph ...... served for different agonists.
@nl
P2093
P2860
P356
P1476
A cation-π interaction at a ph ...... served for different agonists.
@en
P2093
Ariele P Hanek
Dennis A Dougherty
Henry A Lester
Joseph W Lynch
Kerry L Price
Sarah C R Lummis
Stephan A Pless
P2860
P304
P356
10.1124/MOL.110.069583
P577
2011-01-25T00:00:00Z