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Article

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

Thyroid : official journal of the American Thyroid Association - 1 Feb 2001

Tanaka K, Chazenbalk G D, Rapoport B, McLachlan S M

Abstract excerpt

Cleavage of thyrotropin receptors (TSHR) on the cell surface into disulfide-linked A and B subunits involves deletion of an intervening region that corresponds approximately to a 50 amino acid "insertion" in the TSHR relative to the noncleaving luteinizing hormone/choriogonadotropin receptor (LH/CGR). The location of this insertion is imprecise because of the relatively low homology between the two receptors in...

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Identifiers

PMID: 11288979
DOI: 10.1089/105072501300042721

Genes

TSHR

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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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reassessment of the location of the thyrotropin receptor 50 amino acid "insertion" provides evidence in favor of a second downstream cleavage site.PMID 11288979Read ↗

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 ↗

Insight into thyrotropin receptor cleavage by engineering the single polypeptide chain luteinizing hormone receptor into a cleaving, two subunit receptor.Semantic proximity Read ↗

Thyrotropin receptor cleavage at site 1 involves two discontinuous segments at each end of the unique 50-amino acid insertion.Semantic proximity Read ↗

Cleavage of the thyrotropin receptor does not occur at a classical subtilisin-related proprotein convertase endoproteolytic site.Semantic proximity Read ↗

An insertion in the human thyrotropin receptor critical for high affinity hormone binding.Semantic proximity Read ↗

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

A tyrosine residue on the TSH receptor stabilizes multimer formation.Semantic proximity Read ↗

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

On the functional importance of thyrotropin receptor intramolecular cleavage.Semantic proximity Read ↗

Defining structural and functional dimensions of the extracellular thyrotropin receptor region.Semantic proximity Read ↗

Extended and Structurally Supported Insights into Extracellular Hormone Binding, Signal Transduction and Organization of the Thyrotropin ReceptorSemantic proximity Read ↗

Thyrotropin (TSH) receptor residue E251 in the extracellular leucine-rich repeat domain is critical for linking TSH binding to receptor activation.Semantic proximity Read ↗

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