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

Contributions of conserved serine residues to the interactions of ligands with dopamine D2 receptors.

Journal of neurochemistry - 1 Aug 1992

Cox B A, Henningsen R A, Spanoyannis A, Neve R L, Neve K A

Abstract excerpt

Four dopamine D2 receptor mutants were constructed, in each of which an alanine residue was substituted for one of four conserved serine residues, i.e., Ser-193, Ser-194, Ser-197, and Ser-391. Wild-type and mutant receptors were expressed transiently in COS-7 cells and stably in C6 glioma cells for analysis of ligand-receptor interactions. In radioligand binding assays, the affinity of D2 receptors for dopamine...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Line
Share to Immunoblotting

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

Share to Ligands

Share to Molecular Sequence Data

Share to Mutation

Share to Nucleic Acid Hybridization

Share to RNA, Messenger

Source

Identifiers

PMID: 1321233
DOI: 10.1111/j.1471-4159.1992.tb09416.x

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

Contributions of conserved serine residues to the interactions of ligands with dopamine D2 receptors.PMID 1321233Read ↗

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

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

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

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 ↗

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

Comparison of the function of two novel human dopamine D2 receptor variants identifies a likely mechanism for their pathogenicity.Semantic proximity Read ↗

Importance of a N-terminal aspartate in the internalization of the neuropeptide Y Y2 receptor.Semantic proximity Read ↗

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

Identification of amino acid determinants of dopamine 2 receptor synthetic agonist function.Semantic proximity Read ↗

Computational design of constitutively active mutants of Dopamine D2 receptor inspired by ligand-independent activation mechanisms.Semantic proximity Read ↗

Mutation of three residues in the third intracellular loop of the dopamine D2 receptor creates an internalization-defective receptor.Semantic proximity Read ↗

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