Evidence map›Paper›PMID 19751189›Full record

ReviewCurrent protein & peptide science2009

Theoretical considerations on the topological organization of receptor mosaics.

Agnati Luigi Francesco, Fuxe Kjell, Woods Amina, Genedani Susanna, Guidolin Diego

Open access · greenAbstract readReview
In one paragraph

Review in Current protein & peptide science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Histidine, the less interactive cousin of arginine.European journal of mass spectrometry (Chichester, England) · 2019
    Article
  5. Review
  6. Imaging of noncovalent complexes by MALDI-MS.Journal of the American Society for Mass Spectrometry · 2013
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. The dopamine D(4) receptor, the ultimate disordered protein.Journal of receptor and signal transduction research · 2010
    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

5 authors at 4 institutions in 3 countries.

Agnati Luigi FrancescoDepartment BioMedical Sciences, University of Modena and Reggio Emilia and IRCCS Lido, Venezia, Italy. luigiagnati@tin.it
Fuxe Kjell
Woods Amina
Genedani Susanna
Guidolin Diego
University of Modena and Reggio Emilia · ITKarolinska Institutet · SENational Institutes of Health · USUniversity of Padua · IT

Funding

Intramural NIH HHS Z99 DA999999
6 · The paper itself

Abstract

The concept of Receptor Mosaic (RM) is discussed; hence the integrative functions of the assemblage of G-protein coupled receptors physically interacting in the plane of the plasma membrane. The main focus is on a hetero-trimer of G-protein coupled receptors, namely the A2A-D2-CB1 receptor trimer. A bioinformatics analysis was carried out on the amino acid sequence of these receptors to indicate domains possibly involved in the receptor-receptor interactions. Such a bioinformatic analysis was also carried out on the RM formed by mGLU R5, D2 and A2A. The importance of topology, i.e., of the reciprocal localisation of the three interacting receptors in the plan of the membrane for the RM integrative functions is underlined. However, it is also pointed out that this fundamental aspect still waits techniques capable of an appropriate investigation. Finally, it is discussed how RM topology can give hints for a structural definition of the concept of hub receptor. Thus, just as in any network, the receptor operating as a hub is the one that in the molecular network formed by the receptors has the highest number of inputs.

Indexed as

Allosteric RegulationAnimalsCell MembraneHumansMembrane ProteinsModels, BiologicalProtein BindingProtein MultimerizationProtein SubunitsReceptors, G-Protein-CoupledMembrane ProteinsProtein SubunitsReceptors, G-Protein-Coupled

Identifiers

PMID19751189
PMCPMC2949285
OpenAlexW2095847773

What OpenQuestion holds

Textmetadata
LicenceTDM
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.