Evidence map›Paper›PMID 28630934›Full record

ArticleScience advances2017

Ligand binding to a G protein-coupled receptor captured in a mass spectrometer.

Hsin-Yung Yen, Jonathan T S Hopper, Idlir Liko, Timothy M Allison, Ya Zhu, Dejian Wang, Monika Stegmann, Shabaz Mohammed, Beili Wu, Carol V Robinson

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 65 citations in OpenAlex.

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  18. Molecular insights into mechanisms of GPCR hijacking byProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. 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

10 authors at 3 institutions in 2 countries.

Hsin-Yung YenChemistry Research Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
Jonathan T S HopperOMass Technologies Ltd., Centre for Innovation and Enterprise, Begbroke Science Park, Woodstock Road, Oxford OX5 1PF, UK.
Idlir LikoChemistry Research Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
Timothy M AllisonChemistry Research Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
Ya ZhuCAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Pudong, Shanghai 201203, China.
Dejian WangCAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Pudong, Shanghai 201203, China.
Monika StegmannDepartments of Chemistry and Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
Shabaz MohammedDepartments of Chemistry and Biochemistry, University of Oxford, Oxford OX1 3QU, UK.ORCID 0000-0003-2640-9560
Beili WuCAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Pudong, Shanghai 201203, China.
Carol V RobinsonChemistry Research Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
University of Oxford · GBChinese Academy of Sciences · CNOxford Medical Diagnostics (United Kingdom) · GB

Funding

European Research Council 695511Medical Research Council G1000819Medical Research Council MR/N020413/1Wellcome Trust
6 · The paper itself

Abstract

G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors belong to the largest family of membrane-embedded cell surface proteins and are involved in a diverse array of physiological processes. Despite progress in the mass spectrometry of membrane protein complexes, G protein-coupled receptors have remained intractable because of their low yield and instability after extraction from cell membranes. We established conditions in the mass spectrometer that preserve noncovalent ligand binding to the human purinergic receptor P2Y

Indexed as

LigandsMass SpectrometryAdenosine DiphosphateModels, MolecularMolecular ConformationPhosphorylationProtein BindingReceptors, G-Protein-CoupledReceptors, Purinergic P2Y1Structure-Activity RelationshipAdenosine DiphosphateLigandsReceptors, G-Protein-CoupledReceptors, Purinergic P2Y1G-protein coupled receptorsligand bindingmass spectrometry

Identifiers

PMID28630934
PMCPMC5473672
OpenAlexW2625178910

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.