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Article

A tyrosine residue on the TSH receptor stabilizes multimer formation.

PloS one - 26 Feb 2010

Latif Rauf, Michalek Krzysztof, Morshed Syed Ahmed, Davies Terry F

Abstract excerpt

BACKGROUND: The thyrotropin stimulating hormone receptor (TSHR) is a G protein coupled receptor (GPCR) with a large ectodomain. The ligand, TSH, acting via this receptor regulates thyroid growth and thyroid hormone production and secretion. The TSH receptor (TSHR) undergoes complex post-translati...

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Source

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Identifiers

PMID: 20195479
DOI: 10.1371/journal.pone.0009449
PMCID: PMC2829087

Genes

TSHR
GPI

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20195479-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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A tyrosine residue on the TSH receptor stabilizes multimer formation.PMID 20195479Read ↗

Novel insights on thyroid-stimulating hormone receptor signal transduction.Semantic proximity Read ↗

Minireview: Structural and Functional Evolution of the Thyrotropin ReceptorSemantic proximity Read ↗

Transmembrane domains of attraction on the TSH receptor.Semantic proximity Read ↗

Rearrangement of the Extracellular Domain/Extracellular Loop 1 Interface Is Critical for Thyrotropin Receptor Activation.Semantic proximity Read ↗

Understanding the thyrotropin receptor function-structure relationship.Semantic proximity Read ↗

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The extracellular domain suppresses constitutive activity of the transmembrane domain of the human TSH receptor: implications for hormone-receptor interaction and antagonist design.Semantic proximity Read ↗

Reassessment of the location of the thyrotropin receptor 50 amino acid "insertion" provides evidence in favor of a second downstream cleavage site.Semantic proximity Read ↗

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Evidence that cleavage of the thyrotropin receptor involves a "molecular ruler" mechanism: deletion of amino acid residues 305-320 causes a spatial shift in cleavage site 1 independent of amino acid motif.Semantic proximity Read ↗

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