Evidence map›Paper›PMID 18246094›Full record

ReviewBritish journal of pharmacology2008

The A(2A)-adenosine receptor: a GPCR with unique features?

J Zezula, M Freissmuth

Abstract readReview
In one paragraph

Review in British journal of pharmacology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

41 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Purinergic system dysfunction in mood disorders: a key target for developing improved therapeutics.Progress in neuro-psychopharmacology & biological psychiatry · 2015
    Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Enhancement of adenosine AFrontiers in neuroscience · 2022
    Article
  10. Novel positive allosteric modulators of AJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  11. Article
  12. Illuminating insights into opsin 3 function in the skin.Advances in biological regulation · 2020
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

2 authors.

J ZezulaCenter of Biomolecular Medicine and Pharmacology, Institute of Pharmacology, Medical University of Vienna, Austria.
M Freissmuth

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The A(2A)-adenosine receptor is a prototypical G(s)-coupled receptor. However, the A(2A)-receptor has several structural and functional characteristics that make it unique. In contrast to the classical model of collision coupling described for the beta-adrenergic receptors, the A(2A)-receptor couples to adenylyl cyclase by restricted collision coupling and forms a tight complex with G(s). The mechanistic basis for this is not clear; restricted collision coupling may arise from the interaction of the receptor with additional proteins or due to the fact that G protein-coupling is confined to specialized membrane microdomains. The A(2A)-receptor has a long C-terminus (of >120 residues), which is for the most part dispensable for coupling to G(s). It was originally viewed as the docking site for kinases and the beta-arrestin family to initiate receptor desensitization and endocytosis. The A(2A)-receptor is, however, fairly resistant to agonist-induced internalization. Recently, the C-terminus has also been appreciated as a binding site for several additional 'accessory' proteins. Established interaction partners include alpha-actinin, ARNO, USP4 and translin-associated protein-X. In addition, the A(2A)-receptor has also been reported to form a heteromeric complex with the D(2)-dopamine receptor and the metabotropic glutamate receptor-5. It is clear that (i) this list cannot be exhaustive and (ii) that all these proteins cannot bind simultaneously to the receptor. There must be rules of engagement, which allow the receptor to elicit different biological responses, which depend on the cellular context and the nature of the concomitant signal(s). Thus, the receptor may function as a coincidence detector and a signal integrator.

Indexed as

ADP-Ribosylation FactorsAnimalsGTPase-Activating ProteinsHumansReceptor, Adenosine A2AReceptors, G-Protein-CoupledSignal TransductionADP-Ribosylation Factorscytohesin-2GTPase-Activating ProteinsReceptor, Adenosine A2AReceptors, G-Protein-Coupled

Identifiers

PMID18246094
PMCPMC2268059

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.