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

Bulk is a determinant of oxymetazoline affinity for the alpha1A-adrenergic receptor.

Receptors & channels - 1 Jan 2004

McCune Dan, Gaivin Robert, Rorabaugh Boyd, Perez Dianne

Abstract excerpt

The alpha1A-adrenergic receptor (AR) has a higher affinity for several agonists and antagonists compared to alpha1B or alpha1D ARs. Mutagenesis studies were used to determine residues potentially responsible for this subtype selectivity. Oxymetazoline has a 50-fold lower affinity for alpha1D ARs...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Chlorocebus aethiops
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Receptors, Adrenergic, alpha-1

Share to Sequence Alignment

Source

Identifiers

PMID: 15512845
DOI: 10.1080/10606820490514923

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15512845-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Bulk is a determinant of oxymetazoline affinity for the alpha1A-adrenergic receptor.PMID 15512845Read ↗

Mechanism of alpha-subunit selectivity of benzodiazepine pharmacology at gamma-aminobutyric acid type A receptors.Semantic proximity Read ↗

Identification of critical extracellular loop residues involved in alpha 1-adrenergic receptor subtype-selective antagonist binding.Semantic proximity Read ↗

Extracellular surface residues of the α1B-adrenoceptor critical for G protein-coupled receptor function.Semantic proximity Read ↗

Structural insight into the mechanism of 4-aminoquinolines selectivity for the alpha2A-adrenoceptorSemantic proximity Read ↗

Structural Basis for Ligand Recognition and Functional Selectivity at Angiotensin Receptor.Semantic proximity Read ↗

A point mutation in the seventh hydrophobic domain of the alpha 2 adrenergic receptor increases its affinity for a family of beta receptor antagonists.Semantic proximity Read ↗

Distinct ETA receptor binding mode of macitentan as determined by site directed mutagenesis.Semantic proximity Read ↗

Single amino acid residue determinants of non-peptide antagonist binding to the corticotropin-releasing factor1 (CRF1) receptor.Semantic proximity Read ↗

The binding of propranolol at 5-hydroxytryptamine1D beta T355N mutant receptors may involve formation of two hydrogen bonds to asparagine.Semantic proximity Read ↗

The second extracellular loop of alpha2A-adrenoceptors contributes to the binding of yohimbine analogues.Semantic proximity Read ↗

Amino acids of the human alpha1d-adrenergic receptor involved in antagonist binding.Semantic proximity Read ↗

Ring substituents on substituted benzamide ligands indirectly mediate interactions with position 7.39 of transmembrane helix 7 of the D4 dopamine receptor.Semantic proximity Read ↗

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