Evidence map›Paper›PMID 27672048›Full record

ArticleProtein engineering, design & selection : PEDS2016

Engineering a minimal G protein to facilitate crystallisation of G protein-coupled receptors in their active conformation.

Byron Carpenter, Christopher G Tate

Open access · bronzeAbstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

96 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
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  9. Structure of the GNature communications · 2025
    Article
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  15. Review
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  17. Molecular mechanism of ligand recognition and activation of lysophosphatidic acid receptor LPAR6.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Review
  19. Review
  20. Agonist efficacy at the βFrontiers in pharmacology · 2025
    Article

36 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Byron CarpenterMRC Laboratory of Molecular Biology, Cambridge Biomedical Campus , Francis Crick Avenue, Cambridge CB2 0QH, UK byronc@mrc-lmb.cam.ac.uk cgt@mrc-lmb.cam.ac.uk.
Christopher G TateMRC Laboratory of Molecular Biology, Cambridge Biomedical Campus , Francis Crick Avenue, Cambridge CB2 0QH, UK byronc@mrc-lmb.cam.ac.uk cgt@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105197215
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) modulate cytoplasmic signalling in response to extracellular stimuli, and are important therapeutic targets in a wide range of diseases. Structure determination of GPCRs in all activation states is important to elucidate the precise mechanism of signal transduction and to facilitate optimal drug design. However, due to their inherent instability, crystallisation of GPCRs in complex with cytoplasmic signalling proteins, such as heterotrimeric G proteins and β-arrestins, has proved challenging. Here, we describe the design of a minimal G protein, mini-G

Indexed as

Protein EngineeringBinding SitesCrystallizationGTP-Binding ProteinsModels, MolecularMutagenesisPeptide FragmentsProtein DomainsProtein StabilityReceptor, Adenosine A2ATemperatureGTP-Binding ProteinsPeptide FragmentsReceptor, Adenosine A2AcomplexGPCRG proteinG protein-coupled receptorGsmini G proteinmini-Gs

Identifiers

PMID27672048
PMCPMC5181381
OpenAlexW2524451022

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.