Evidence map›Paper›PMID 34270937›Full record

ArticleStructure (London, England : 1993)2021

Modulation of adenosine A2a receptor oligomerization by receptor activation and PIP

Wanling Song, Anna L Duncan, Mark S P Sansom

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–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

9 citing papers in PubMed.

  1. Dynamic mechanism for subtype selectivity of endocannabinoids.The Journal of biological chemistry · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. PI(4,5)P2: signaling the plasma membrane.The Biochemical journal · 2022
    Article
  9. Review
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

3 authors.

Wanling SongDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
Anna L DuncanDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
Mark S P SansomDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, UK. Electronic address: mark.sansom@bioch.ox.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/R00126X/1Wellcome TrustWellcome Trust 208361/Z/17/Z
6 · The paper itself

Abstract

GPCRs have been shown to form oligomers, which generate distinctive signaling outcomes. However, the structural nature of the oligomerization process remains uncertain. We have characterized oligomeric configurations of the adenosine A2a receptor (A2aR) by combining large-scale molecular dynamics simulations with Markov state models. These oligomeric structures may also serve as templates for studying oligomerization of other class A GPCRs. Our simulation data revealed that receptor activation results in enhanced oligomerization, more diverse oligomer populations, and a more connected oligomerization network. The active state conformation of the A2aR shifts protein-protein association interfaces to those involving intracellular loop ICL3 and transmembrane helix TM6. Binding of PIP

Indexed as

Molecular ConformationAdenosineBinding SitesHumansMolecular Dynamics SimulationReceptor, Adenosine A2AAdenosineReceptor, Adenosine A2AA2a receptorGPCRlipidsMarkov state modelsmolecular dynamicsoligomerization

Identifiers

PMID34270937
PMCPMC8581623

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.