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

Transmembrane segment five serines of the D4 dopamine receptor uniquely influence the interactions of dopamine, norepinephrine, and Ro10-4548.

The Journal of pharmacology and experimental therapeutics - 1 Jun 2010

Cummings David F, Ericksen Spencer S, Goetz Angela, Schetz John A

Abstract excerpt

Conserved serines of transmembrane segment (TM) five (TM5) are critical for the interactions of endogenous catecholamines with alpha(1)- and alpha(2)-adrenergic, beta(2)-adrenergic, and D1, D2, and D3 dopamine receptors. The unique high-affinity interaction of the D4 dopamine receptor subtype with both norepinephrine and dopamine, and the fact that TM5 serine interactions have never been studied for this receptor...

Read the complete abstract on PubMed

Topics

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

Share to Dopamine
Share to Dopamine Agonists

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dopamine Antagonists

Share to Molecular Conformation

Share to Norepinephrine

Share to Piperazines

Share to Radioligand Assay

Share to Receptors, Dopamine D4

Source

Open in PubMed Open full text

Identifiers

PMID: 20215412
DOI: 10.1124/jpet.109.164962
PMCID: PMC2879936

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Transmembrane segment five serines of the D4 dopamine receptor uniquely influence the interactions of dopamine, norepinephrine, and Ro10-4548.PMID 20215412Read ↗

Functional analysis of human D1 and D5 dopaminergic G protein-coupled receptors: lessons from mutagenesis of a conserved serine residue in the cytosolic end of transmembrane region 6.Semantic proximity Read ↗

Effect of multiple serine/alanine mutations in the transmembrane spanning region V of the D2 dopamine receptor on ligand binding.Semantic proximity Read ↗

Receptor conformations involved in dopamine D(2L) receptor functional selectivity induced by selected transmembrane-5 serine mutations.Semantic proximity Read ↗

Dopamine D5 receptor agonist high affinity and constitutive activity profile conferred by carboxyl-terminal tail sequence.Semantic proximity Read ↗

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

Contributions of conserved serine residues to the interactions of ligands with dopamine D2 receptors.Semantic proximity Read ↗

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

Dopamine D2 Receptor Agonist Binding Kinetics-Role of a Conserved Serine Residue.Semantic proximity Read ↗

Site-directed mutagenesis of the human dopamine D2 receptor.Semantic proximity Read ↗

Functional activation by central monoamines of human dopamine D(4) receptor polymorphic variants coupled to GIRK channels in Xenopus oocytes.Semantic proximity Read ↗

Three amino acids in the D2 dopamine receptor regulate selective ligand function and affinity.Semantic proximity Read ↗

Key amino acids located within the transmembrane domains 5 and 7 account for the pharmacological specificity of the human V1b vasopressin receptor.Semantic proximity Read ↗

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