Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen.
about
Ionotropic glutamate receptor AMPA 1 is associated with ovulation rateCharacterization of the hepatitis C virus NS2/3 processing reaction by using a purified precursor proteinGluR2 ligand-binding core complexes: importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonistsMolecular mechanism of ligand recognition by NR3 subtype glutamate receptorsCrystal Structure and Catalytic Mechanism of PglD from Campylobacter jejuniStructure of the S1S2 glutamate binding domain of GLuR3Mechanisms of Antagonism of the GluR2 AMPA Receptor: Structure and Dynamics of the Complex of Two Willardiine Antagonists with the Glutamate Binding DomainMechanism of AMPA Receptor Activation by Partial Agonists: DISULFIDE TRAPPING OF CLOSED LOBE CONFORMATIONSX-Ray Structure of Acid-Sensing Ion Channel 1–Snake Toxin Complex Reveals Open State of a Na+-Selective ChannelThermodynamics and Mechanism of the Interaction of Willardiine Partial Agonists with a Glutamate Receptor: Implications for Drug DevelopmentL-Asp is a useful tool in the purification of the ionotropic glutamate receptor A2 ligand-binding domainRecombinant pheromone binding protein 1 from Mamestra brassicae (MbraPBP1). Functional and structural characterization.Structural insights into phenylethanolamines high-affinity binding site in NR2B from binding and molecular modeling studies.Soluble expression, purification and characterization of the full length IS2 Transposase.Development and characterization of an automated high throughput screening method for optimization of protein refolding processes.Physicochemical and immunological studies of the N-terminal domain of the Torpedo acetylcholine receptor alpha-subunit expressed in Escherichia coli.Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactionsAntidepressant interactions with the NMDA NR1-1b subunitHydrophobic side chain dynamics of a glutamate receptor ligand binding domainEnergy transfer ligands of the GluR2 ligand binding coreOn the mechanisms of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor binding to glutamate and kainate.Structural determinants of agonist-specific kinetics at the ionotropic glutamate receptor 2.The relationship between agonist potency and AMPA receptor kinetics.Isoxazole analogues bind the system xc- transporter: structure-activity relationship and pharmacophore model.Rhodopsin kinase: two mAbs binding near the carboxyl terminus cause time-dependent inactivation.Differential regulation of ionotropic glutamate receptors.A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase.Chemical interplay in the mechanism of partial agonist activation in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors.Expression and characterization of soluble amino-terminal domain of NR2B subunit of N-methyl-D-aspartate receptor.High-throughput automated refolding screening of inclusion bodies.Preparation and Analysis of N-Terminal Chemokine Receptor Sulfopeptides Using Tyrosylprotein Sulfotransferase Enzymes.Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange.Binding of spermine and ifenprodil to a purified, soluble regulatory domain of the N-methyl-D-aspartate receptorMechanism 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.Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2.NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists.Is the isolated ligand binding domain a good model of the domain in the native receptor?Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors.Large-scale expression and thermodynamic characterization of a glutamate receptor agonist-binding domain.
P2860
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P2860
Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen.
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Overexpression of a glutamate ...... novel protein folding screen.
@ast
Overexpression of a glutamate ...... novel protein folding screen.
@en
type
label
Overexpression of a glutamate ...... novel protein folding screen.
@ast
Overexpression of a glutamate ...... novel protein folding screen.
@en
prefLabel
Overexpression of a glutamate ...... novel protein folding screen.
@ast
Overexpression of a glutamate ...... novel protein folding screen.
@en
P2860
P921
P356
P1476
Overexpression of a glutamate ...... novel protein folding screen.
@en
P2093
P2860
P304
13431-13436
P356
10.1073/PNAS.94.25.13431
P407
P577
1997-12-01T00:00:00Z