Prediction of 5-HT3 receptor agonist-binding residues using homology modeling.
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5-HT3 receptorsThe 5-HT3 receptor as a therapeutic targetPathways and Barriers for Ion Translocation through the 5-HT3A Receptor ChannelMarine Toxins Targeting Ion ChannelsExtracellular domain nicotinic acetylcholine receptors formed by alpha4 and beta2 subunits.Noninvasive imaging of 5-HT3 receptor trafficking in live cells: from biosynthesis to endocytosis.Agonists and antagonists bind to an A-A interface in the heteromeric 5-HT3AB receptor.Atomic force microscopy reveals the stoichiometry and subunit arrangement of 5-HT3 receptors.Binding interactions of antagonists with 5-hydroxytryptamine3A receptor models.Cell surface expression of 5-hydroxytryptamine type 3 receptors is promoted by RIC-3.Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel.A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists.Structural answers and persistent questions about how nicotinic receptors work.The antimalarial drugs quinine, chloroquine and mefloquine are antagonists at 5-HT3 receptors.5-HT(3) receptors.Bacterially expressed human serotonin receptor 3A is functionally reconstituted in proteoliposomesLoop B is a major structural component of the 5-HT3 receptor.A hydrogen bond in loop A is critical for the binding and function of the 5-HT3 receptor.A cation-pi interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue.5-Fluorotryptamine is a partial agonist at 5-HT3 receptors, and reveals that size and electronegativity at the 5 position of tryptamine are critical for efficient receptor function.The structural basis of function in Cys-loop receptors.An overview of recent developments in GPCR modelling: methods and validation.Cysteine modification reveals which subunits form the ligand binding site in human heteromeric 5-HT3AB receptors.Toward a multiscale modeling framework for understanding serotonergic function.Toward biophysical probes for the 5-HT3 receptor: structure-activity relationship study of granisetron derivatives.The F-loop of the GABA A receptor gamma2 subunit contributes to benzodiazepine modulation.Locating the carboxylate group of GABA in the homomeric rho GABA(A) receptor ligand-binding pocket.Mutagenesis and molecular modeling reveal the importance of the 5-HT3 receptor F-loop.Ligand binding transmits conformational changes across the membrane-spanning region to the intracellular side of the 5-HT3 serotonin receptor.Locating an antagonist in the 5-HT3 receptor binding site using modeling and radioligand binding.The role of tyrosine residues in the extracellular domain of the 5-hydroxytryptamine3 receptor.Defining the roles of Asn-128, Glu-129 and Phe-130 in loop A of the 5-HT3 receptorUnbinding pathways of an agonist and an antagonist from the 5-HT3 receptorExploring the binding of serotonin to the 5-HT3 receptor by density functional theory.Trans-cis switching mechanisms in proline analogues and their relevance for the gating of the 5-HT3 receptor.Loose protein packing around the extracellular half of the GABA(A) receptor beta1 subunit M2 channel-lining segment.The extracellular subunit interface of the 5-HT3 receptors: a computational alanine scanning mutagenesis study.Combining structure-based pharmacophore and in silico approaches to discover novel selective serotonin reuptake inhibitors.
P2860
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P2860
Prediction of 5-HT3 receptor agonist-binding residues using homology modeling.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Prediction of 5-HT3 receptor agonist-binding residues using homology modeling.
@en
type
label
Prediction of 5-HT3 receptor agonist-binding residues using homology modeling.
@en
prefLabel
Prediction of 5-HT3 receptor agonist-binding residues using homology modeling.
@en
P2093
P2860
P1433
P1476
Prediction of 5-HT3 receptor agonist-binding residues using homology modeling
@en
P2093
David C Reeves
Muhammed F R Sayed
Pak-Lee Chau
Sarah C R Lummis
P2860
P304
P356
10.1016/S0006-3495(03)75039-5
P407
P577
2003-04-01T00:00:00Z