Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Agonist-induced cell surface trafficking of an intracellularly sequestered D1 dopamine receptor homo-oligomer.

Molecular pharmacology - 1 Jul 2006

Kong Michael M C, Fan Theresa, Varghese George, O'dowd Brian F, George Susan R

Abstract excerpt

The role of oligomerization in D1 dopamine receptor trafficking to the cell surface was examined using conformationally distinct variants of this receptor. Substitution of the highly conserved aspartic acid (Asp103) in transmembrane domain 3 resulted in a constitutively active receptor, D103A, that did not bind agonists or antagonists but trafficked to the cell surface as oligomers. Coexpression of D103A with the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Benzazepines
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Membrane Permeability

Share to Cyclic AMP

Share to Dopamine

Share to Dopamine Agonists

Share to Radioligand Assay

Share to Receptors, Dopamine D1

Source

Identifiers

PMID: 16597839
DOI: 10.1124/mol.105.021246

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Agonist-induced cell surface trafficking of an intracellularly sequestered D1 dopamine receptor homo-oligomer.PMID 16597839Read ↗

Oligomerization of dopamine transporters visualized in living cells by fluorescence resonance energy transfer microscopy.Semantic proximity Read ↗

Constitutive activities and inverse agonism in dopamine receptors.Semantic proximity Read ↗

Development of tolerance in D3 dopamine receptor signaling is accompanied by distinct changes in receptor conformation.Semantic proximity Read ↗

The tolerance property of human D3 dopamine receptor is determined by specific amino acid residues in the second cytoplasmic loop.Semantic proximity Read ↗

Probing the constitutive activity among dopamine D1 and D5 receptors and their mutants.Semantic proximity Read ↗

Interrelation of dopamine transporter oligomerization and surface presence as studied with mutant transporter proteins and amphetamine.Semantic proximity Read ↗

Studies on the role of the receptor protein motifs possibly involved in electrostatic interactions on the dopamine D1 and D2 receptor oligomerization.Semantic proximity Read ↗

The D1 dopamine receptor is constitutively phosphorylated by G protein-coupled receptor kinase 4.Semantic proximity Read ↗

Efficient G protein coupling is not required for agonist-mediated internalization and membrane reorganization of the adenosine A3 receptor.Semantic proximity Read ↗

Impact of T161, Y318 and S363 alanine mutations on regulation of the human delta-opioid receptor (hDOPr) induced by peptidic and alkaloid agonists.Semantic proximity Read ↗

Oligomerization and trafficking of the human dopamine transporter. Mutational analysis identifies critical domains important for the functional expression of the transporter.Semantic proximity Read ↗

Identification of transmembrane regions critical for ligand binding to the human D3 dopamine receptor using various D3/D1 transmembrane chimeras.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.