Evidence map›Paper›PMID 21586576›Full record

ArticleThe Journal of biological chemistry2011

From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs).

Gunnar Kleinau, Inna Hoyer, Annika Kreuchwig, Ann-Karin Haas, Claudia Rutz, Jens Furkert, Catherine L Worth, Gerd Krause, Ralf Schülein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. New small molecule agonists to the thyrotropin receptor.Thyroid : official journal of the American Thyroid Association · 2015
    Article
  12. Review
  13. Probing the interaction of SR141716A with the CB1 receptor.The Journal of biological chemistry · 2012
    Article
  14. Article
  15. Article
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

9 authors at 2 institutions in 1 country.

Gunnar KleinauLeibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany. GKrause@FMP-Berlin.de
Inna Hoyer
Annika Kreuchwig
Ann-Karin Haas
Claudia Rutz
Jens Furkert
Catherine L Worth
Gerd Krause
Ralf Schülein
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DECharité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmembrane helices (TMHs) 5 and 6 are known to be important for signal transduction by G-protein-coupled receptors (GPCRs). Our aim was to characterize the interface between TMH5 and TMH6 of the thyrotropin receptor (TSHR) to gain molecular insights into aspects of signal transduction and regulation. A proline at TMH5 position 5.50 is highly conserved in family A GPCRs and causes a twist in the helix structure. Mutation of the TSHR-specific alanine (Ala-593⁵·⁵⁰) at this position to proline resulted in a 20-fold reduction of cell surface expression. This indicates that TMH5 in the TSHR might have a conformation different from most other family A GPCRs by forming a regular α-helix. Furthermore, linking our own and previous data from directed mutagenesis with structural information led to suggestions of distinct pairs of interacting residues between TMH5 and TMH6 that are responsible for stabilizing either the basal or the active state. Our insights suggest that the inactive state conformation is constrained by a core set of polar interactions among TMHs 2, 3, 6, and 7 and in contrast that the active state conformation is stabilized mainly by non-polar interactions between TMHs 5 and 6. Our findings might be relevant for all family A GPCRs as supported by a statistical analysis of residue properties between the TMHs of a vast number of GPCR sequences.

Indexed as

Signal TransductionAnimalsCell MembraneConserved SequenceCyclic AMPHEK293 CellsHumansInositol PhosphatesModels, MolecularMutagenesis, Site-DirectedMutationProtein Structure, SecondaryReceptors, G-Protein-CoupledReceptors, ThyrotropinCyclic AMPInositol PhosphatesReceptors, G-Protein-CoupledReceptors, Thyrotropin

Identifiers

PMID21586576
PMCPMC3138303
OpenAlexW2051347366

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.