Dopamine D2 receptor dimer formation: evidence from ligand binding.
about
Metabotropic glutamate mGlu2 receptor is necessary for the pharmacological and behavioral effects induced by hallucinogenic 5-HT2A receptor agonistsAdenosine A(2A) receptors assemble into higher-order oligomers at the plasma membraneA critical role for the histidine residues in the catalytic function of acyl-CoA:cholesterol acyltransferase catalysis: evidence for catalytic difference between ACAT1 and ACAT2Functional crosstalk and heteromerization of serotonin 5-HT2A and dopamine D2 receptorsAllostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapesCocaine inhibits dopamine D2 receptor signaling via sigma-1-D2 receptor heteromersVisualization and ligand-induced modulation of dopamine receptor dimerization at the single molecule level.A new mechanism of allostery in a G protein-coupled receptor dimerCharacterisation of the interaction of the C-terminus of the dopamine D2 receptor with neuronal calcium sensor-1Schizophrenia, amphetamine-induced sensitized state and acute amphetamine exposure all show a common alteration: increased dopamine D2 receptor dimerizationTrans-activation between 7TM domains: implication in heterodimeric GABAB receptor activationOn the fitting of binding data when receptor dimerization is suspected.BRET and Time-resolved FRET strategy to study GPCR oligomerization: from cell lines toward native tissues.Fluorescent protein complementation assays: new tools to study G protein-coupled receptor oligomerization and GPCR-mediated signaling.Methods used to study the oligomeric structure of G-protein-coupled receptors.Relationship between homo-oligomerization of a mammalian olfactory receptor and its activation state demonstrated by bioluminescence resonance energy transfer.Allosteric interactions across native adenosine-A3 receptor homodimers: quantification using single-cell ligand-binding kinetics.Interaction between the D2 dopamine receptor and neuronal calcium sensor-1 analyzed by fluorescence anisotropyOligomerization of G protein-coupled receptors: past, present, and future.Functional homomers and heteromers of dopamine D2L and D3 receptors co-exist at the cell surfaceCoactivation of D1 and D2 dopamine receptors: in marriage, a case of his, hers, and theirs.Time-resolved FRET between GPCR ligands reveals oligomers in native tissues.Dopamine receptor homooligomers and heterooligomers in schizophreniaModelling the interdependence between the stoichiometry of receptor oligomerization and ligand binding for a coexisting dimer/tetramer receptor system.Molecular pathways in dystonia.Clozapine, atypical antipsychotics, and the benefits of fast-off D2 dopamine receptor antagonism.Agonist high- and low-affinity states of dopamine D₂ receptors: methods of detection and clinical implications.Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than betweenMultivalent approaches and beyond: novel tools for the investigation of dopamine D2 receptor pharmacology.Allosteric Modulators of the Class A G Protein Coupled Receptors.Orexin-1 receptor-cannabinoid CB1 receptor heterodimerization results in both ligand-dependent and -independent coordinated alterations of receptor localization and function.Effects of N-ethylmaleimide on conformational equilibria in purified cardiac muscarinic receptors.Assays for enhanced activity of low efficacy partial agonists at the D(2) dopamine receptor.Constitutive oligomerization of human D2 dopamine receptors expressed in Spodoptera frugiperda 9 (Sf9) and in HEK293 cells. Analysis using co-immunoprecipitation and time-resolved fluorescence resonance energy transfer.Design, synthesis, and preliminary in vitro and in vivo pharmacological evaluation of 2-{4-[4-(2,5-disubstituted thiazol-4-yl)phenylethyl]piperazin-1-yl}-1,8-naphthyridine-3-carbonitriles as atypical antipsychotic agents.The action of a negative allosteric modulator at the dopamine D2 receptor is dependent upon sodium ions.
P2860
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P2860
Dopamine D2 receptor dimer formation: evidence from ligand binding.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Dopamine D2 receptor dimer formation: evidence from ligand binding.
@en
Dopamine D2 receptor dimer formation: evidence from ligand binding.
@nl
type
label
Dopamine D2 receptor dimer formation: evidence from ligand binding.
@en
Dopamine D2 receptor dimer formation: evidence from ligand binding.
@nl
prefLabel
Dopamine D2 receptor dimer formation: evidence from ligand binding.
@en
Dopamine D2 receptor dimer formation: evidence from ligand binding.
@nl
P356
P1476
Dopamine D2 receptor dimer formation: evidence from ligand binding.
@en
P2093
Armstrong D
Strange PG
P304
22621-22629
P356
10.1074/JBC.M006936200
P407
P577
2001-02-23T00:00:00Z