NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists.
about
Emerging models of glutamate receptor ion channel structure and functionComputational study of synthetic agonist ligands of ionotropic glutamate receptorsMechanisms of Antagonism of the GluR2 AMPA Receptor: Structure and Dynamics of the Complex of Two Willardiine Antagonists with the Glutamate Binding DomainDynamics connect substrate recognition to catalysis in protein kinase AMechanisms of Modal Activation of GluA3 ReceptorsMechanism of AMPA Receptor Activation by Partial Agonists: DISULFIDE TRAPPING OF CLOSED LOBE CONFORMATIONSThermodynamics and Mechanism of the Interaction of Willardiine Partial Agonists with a Glutamate Receptor: Implications for Drug DevelopmentHydrophobic side chain dynamics of a glutamate receptor ligand binding domainOn the mechanisms of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor binding to glutamate and kainate.Characterizing single-channel behavior of GluA3 receptorsDynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor.Structural dynamics of the glycine-binding domain of the N-methyl-D-aspartate receptor.Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation.Role of conformational dynamics in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor partial agonism.Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange.Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution.Retour aux sources: defining the structural basis of glutamate receptor activation.Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.Luminescence resonance energy transfer investigation of conformational changes in the ligand binding domain of a kainate receptorA quantum biochemistry investigation of willardiine partial agonism in AMPA receptors.Mechanism of partial agonism in AMPA-type glutamate receptors.
P2860
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P2860
NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
NMR spectroscopy of the ligand ...... willardiine partial agonists.
@en
type
label
NMR spectroscopy of the ligand ...... willardiine partial agonists.
@en
prefLabel
NMR spectroscopy of the ligand ...... willardiine partial agonists.
@en
P2860
P1476
NMR spectroscopy of the ligand ...... willardiine partial agonists.
@en
P2093
Michael K Fenwick
Robert E Oswald
P2860
P304
P356
10.1016/J.JMB.2008.03.012
P407
P577
2008-03-14T00:00:00Z