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

A high affinity gonadotropin-releasing hormone (GnRH) tracer, radioiodinated at position 6, facilitates analysis of mutant GnRH receptors.

Endocrinology - 1 Oct 1998

Flanagan C A, Fromme B J, Davidson J S, Millar R P

Abstract excerpt

Cloning of GnRH receptors from several animal species has made it possible to investigate receptor function using site-directed mutagenesis. However, many mutant GnRH receptors exhibit decreased ligand binding, which makes analysis of their ligand binding characteristics technically difficult. To increase the affinity of binding to the GnRH receptor, a novel tracer ligand, 125I-[His5,D-Tyr6]GnRH, was designed and...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to COS Cells
Share to Gonadotropin-Releasing Hormone

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

Share to Iodine Radioisotopes

Share to Mutation

Source

Identifiers

PMID: 9751490
DOI: 10.1210/endo.139.10.6260

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

A high affinity gonadotropin-releasing hormone (GnRH) tracer, radioiodinated at position 6, facilitates analysis of mutant GnRH receptors.PMID 9751490Read ↗

Conserved mammalian gonadotropin-releasing hormone receptor carboxyl terminal amino acids regulate ligand binding, effector coupling and internalization.Semantic proximity Read ↗

A Chicken Gonadotropin-releasing Hormone Receptor That Confers Agonist Activity to Mammalian AntagonistsSemantic proximity Read ↗

Residues within transmembrane helices 2 and 5 of the human gonadotropin-releasing hormone receptor contribute to agonist and antagonist binding.Semantic proximity Read ↗

Conformational constraint of mammalian, chicken, and salmon GnRHs, but not GnRH II, enhances binding at mammalian and nonmammalian receptors: evidence for preconfiguration of GnRH II.Semantic proximity Read ↗

Overlapping, nonidentical binding sites of different classes of nonpeptide antagonists for the human gonadotropin-releasing hormone receptor.Semantic proximity Read ↗

Role of aspartate7.32(302) of the human gonadotropin-releasing hormone receptor in stabilizing a high-affinity ligand conformation.Semantic proximity Read ↗

Unexpected Effects of Epitope and Chimeric Tags on Gonadotropin-Releasing Hormone Receptors: Implications for Understanding the Molecular Etiology of Hypogonadotropic HypogonadismSemantic proximity Read ↗

Influence of a species-specific extracellular amino acid on expression and function of the human gonadotropin-releasing hormone receptor.Semantic proximity Read ↗

A single amino acid substitution in somatostatin receptor subtype 5 increases affinity for somatostatin-14.Semantic proximity Read ↗

Desensitization and Internalization of Human andXenopusGonadotropin-Releasing Hormone Receptors Expressed in αT4 Pituitary Cells Using Recombinant Adenovirus1Semantic proximity Read ↗

Interaction of tryptamine and ergoline compounds with threonine 196 in the ligand binding site of the 5-hydroxytryptamine6 receptor.Semantic proximity Read ↗

Multiple interactions of the Asp(2.61(98)) side chain of the gonadotropin-releasing hormone receptor contribute differentially to ligand interaction.Semantic proximity Read ↗

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