Evidence map›Paper›PMID 29535353›Full record

ArticleScientific reports2018

Structural insights into positive and negative allosteric regulation of a G protein-coupled receptor through protein-lipid interactions.

Agustín Bruzzese, Carles Gil, James A R Dalton, Jesús Giraldo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024
    Review
  5. Article
  6. The Role of Lipids in Allosteric Modulation of Dopamine DMolecules (Basel, Switzerland) · 2022
    Article
  7. Article
  8. Review
  9. Review
  10. Lipids and Phosphorylation Conjointly Modulate Complex Formation of βFrontiers in cell and developmental biology · 2021
    Article
  11. Article
  12. Review
  13. How Do Molecular Dynamics Data Complement Static Structural Data of GPCRs.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  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

4 authors at 1 institution in 2 countries.

Agustín BruzzeseLaboratory of Molecular Neuropharmacology and Bioinformatics, Institut de Neurociències and Unitat de Bioestadística, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain.
Carles GilDepartment of Biochemistry and Molecular Biology, Institut de Neurociències, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain.
James A R DaltonLaboratory of Molecular Neuropharmacology and Bioinformatics, Institut de Neurociències and Unitat de Bioestadística, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain. james.dalton@uab.es.ORCID 0000-0002-5279-4581
Jesús GiraldoLaboratory of Molecular Neuropharmacology and Bioinformatics, Institut de Neurociències and Unitat de Bioestadística, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain. jesus.giraldo@uab.es.
Universitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipids are becoming known as essential allosteric modulators of G protein-coupled receptor (GPCRs). However, how they exert their effects on GPCR conformation at the atomic level is still unclear. In light of recent experimental data, we have performed several long-timescale molecular dynamics (MD) simulations, totalling 24 μs, to rigorously map allosteric modulation and conformational changes in the β

Indexed as

Allosteric RegulationBinding SitesHumansHydrophobic and Hydrophilic InteractionsMembrane LipidsModels, MolecularMolecular Docking SimulationMolecular Dynamics SimulationPhospholipidsProtein BindingProtein ConformationReceptors, Adrenergic, beta-2ADRB2 protein, humanMembrane LipidsPhospholipidsReceptors, Adrenergic, beta-2

Identifiers

PMID29535353
PMCPMC5849739
OpenAlexW2793277387

What OpenQuestion 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 OpenQuestion graph.