Evidence map›Paper›PMID 28484426›Full record

ReviewFrontiers in endocrinology2017

Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at Work.

Gunnar Kleinau, Catherine L Worth, Annika Kreuchwig, Heike Biebermann, Patrick Marcinkowski, Patrick Scheerer, Gerd Krause

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in endocrinology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 94 citations in OpenAlex.

  1. Pooled it
  2. Review
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  7. Article
  8. Review
  9. Thyroid dysfunction in women with a menopausal syndrome.Przeglad menopauzalny = Menopause review · 2024
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Gunnar KleinauInstitute of Experimental Pediatric Endocrinology, Charité-Universitätsmedizin, Berlin, Germany.
Catherine L WorthLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Annika KreuchwigLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Heike BiebermannInstitute of Experimental Pediatric Endocrinology, Charité-Universitätsmedizin, Berlin, Germany.
Patrick MarcinkowskiLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Patrick ScheererGroup Protein X-Ray Crystallography and Signal Transduction, Institute of Medical Physics and Biophysics, Charité-Universitätsmedizin, Berlin, Germany.
Gerd KrauseLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DECharité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The thyroid-stimulating hormone receptor (TSHR) is a member of the glycoprotein hormone receptors, a sub-group of class A G-protein-coupled receptors (GPCRs). TSHR and its endogenous ligand thyrotropin (TSH) are of essential importance for growth and function of the thyroid gland and proper function of the TSH/TSHR system is pivotal for production and release of thyroid hormones. This receptor is also important with respect to pathophysiology, such as autoimmune (including ophthalmopathy) or non-autoimmune thyroid dysfunctions and cancer development. Pharmacological interventions directly targeting the TSHR should provide benefits to disease treatment compared to currently available therapies of dysfunctions associated with the TSHR or the thyroid gland. Upon TSHR activation, the molecular events conveying conformational changes from the extra- to the intracellular side of the cell across the membrane comprise reception, conversion, and amplification of the signal. These steps are highly dependent on structural features of this receptor and its intermolecular interaction partners, e.g., TSH, antibodies, small molecules, G-proteins, or arrestin. For better understanding of signal transduction, pathogenic mechanisms such as autoantibody action and mutational modifications or for developing new pharmacological strategies, it is essential to combine available structural data with functional information to generate homology models of the entire receptor. Although so far these insights are fragmental, in the past few decades essential contributions have been made to investigate in-depth the involved determinants, such as by structure determination

Indexed as

arrestin interactionglycoprotein hormone receptorsG-protein interactionhomology modelsoligomerssignal transductionstructure–function relationshipsthyroid-stimulating hormone receptor structure

Identifiers

PMID28484426
PMCPMC5401882
OpenAlexW2608333701

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.