Evidence map›Paper›PMID 20512139›Full record

ArticleNature chemical biology2010

Structural basis of G protein-coupled receptor-G protein interactions.

Jianxin Hu, Yan Wang, Xiaohong Zhang, John R Lloyd, Jian Hua Li, Joel Karpiak, Stefano Costanzi, Jürgen Wess

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Review
  3. Development of Mutant MBiochemistry · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The binding of activated GαThe Journal of biological chemistry · 2017
    Article
  13. Priming GPCR signaling through the synergistic effect of two G proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

8 authors at 2 institutions in 1 country.

Jianxin HuMolecular Signaling Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA. jianxinh@niddk.nih.gov
Yan Wang
Xiaohong Zhang
John R Lloyd
Jian Hua Li
Joel Karpiak
Stefano Costanzi
Jürgen Wess
National Institutes of Health · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Molecular basis of G protein-coupled receptor functionZIADK031129 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WESS, JURGEN · 2009 to 2025
$6.7M
Molecular modeling of G protein-coupled receptorsZIADK013025 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI SHERMAN, ARTHUR · 2009 to 2012
$1.2M
Molecular basis of G protein-coupled receptor functionZ01DK031129 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WESS, JURGEN · 2007 to 2008
$832k
Intramural NIH HHS Z01 DK031129
6 · The paper itself

Abstract

The interaction of G protein-coupled receptors (GPCRs) with heterotrimeric G proteins represents one of the most fundamental biological processes. However, the molecular architecture of the GPCR-G protein complex remains poorly defined. In the present study, we applied a comprehensive GPCR-G protein alpha subunit (Galpha) chemical cross-linking strategy to map a receptor-Galpha interface, both before and after agonist-induced receptor activation. Using the M(3) muscarinic acetylcholine receptor (M3R)-Galpha(q) system as a model system, we examined the ability of approximately 250 combinations of cysteine-substituted M3R and Galpha(q) proteins to undergo cross-link formation. We identified many specific M3R-Galpha(q) contact sites, in both the inactive and active receptor conformations, allowing us to draw conclusions regarding the basic architecture of the M3R-Galpha(q) interface and the nature of the conformational changes following receptor activation. As heterotrimeric G proteins as well as most GPCRs share a high degree of structural homology, our findings should be of broad general relevance.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionGTP-Binding Protein alpha SubunitsImmunoprecipitationMass SpectrometryModels, MolecularMutationProtein BindingProtein ConformationReceptors, MuscarinicGTP-Binding Protein alpha SubunitsReceptors, Muscarinic

Identifiers

PMID20512139
PMCPMC3104732
OpenAlexW2010544588

What OpenQuestion holds

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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.