Evidence map›Paper›PMID 19212142›Full record

ReviewNeuro-Signals2009

Structural determinants involved in the formation and activation of G protein betagamma dimers.

William E McIntire

Open access · bronzeAbstract readReview
In one paragraph

Review in Neuro-Signals, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Development and validation of a sensitive LC-MS/MS assay of GT-14, a novel GαJournal of pharmaceutical and biomedical analysis · 2024
    Article
  3. Review
  4. An atypical heterotrimeric Gα and its interactome suggest an extra-large role in overcoming abiotic and biotic stress.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  5. Article
  6. Review
  7. G-Protein Subunit GαFrontiers in microbiology · 2020
    Article
  8. GPCR regulation of secretion.Pharmacology & therapeutics · 2018
    Review
  9. Review
  10. Article
  11. Article
  12. Comprehensive analysis of heterotrimeric G-protein complex diversity and their interactions with GPCRs in solution.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. The inhibitory effect of Gβγ and Gβ isoform specificity on ENaC activity.American journal of physiology. Renal physiology · 2013
    Article
  17. Article
  18. Review
  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

1 author at 1 institution in 1 country.

William E McIntireDepartment of Pharmacology, University of Virginia Health System, Charlottesville, VA 22908, USA. wem2p@virginia.edu
University of Virginia Health System · US

Funding

UVA Digestive Health Research CenterP30DK067629 · NIDDK · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PIZARRO, THERESA TORRES · 2004 to 2008
$5.6M
REGULATION OF CELL SIGNALING BY G-PROTEIN SUBUNITSR01DK019952 · NIDDK · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI GARRISON, JAMES CARLTON · 1986 to 2008
$2.2M
NIDDK NIH HHS P30 DK067629NIDDK NIH HHS R01 DK019952NIDDK NIH HHS R01-DK-19952
6 · The paper itself

Abstract

Heterotrimeric G proteins, composed of an alpha, beta and gamma subunit, represent one of the most important and dynamic families of signaling proteins. As a testament to the significance of G protein signaling, the hundreds of seven-transmembrane-spanning receptors that interact with G proteins are estimated to occupy 1-2% of the human genome. This broad diversity of receptors is echoed in the number of potential heterotrimer combinations that can arise from the 23 alpha subunit, 7 beta subunit and 12 gamma subunit isoforms that have been identified. The potential for such vast complexity implies that the receptor G protein interface is the site of much regulation. The historical model for the activation of a G protein holds that activated receptor catalyzes the exchange of GDP for GTP on the alpha subunit, inducing a conformational change that substantially lowers the affinity of alpha for betagamma. This decreased affinity enables dissociation of betagamma from alpha and receptor. The free form of betagamma is thought to activate effectors, until the hydrolysis of GTP by G alpha (aided by RGS proteins) allows the subunits to re-associate, effectively deactivating the G protein until another interaction with activated receptor.

Indexed as

Protein MultimerizationAnimalsGenetic HeterogeneityGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHumansModels, MolecularProtein BindingProtein IsoformsProtein Processing, Post-TranslationalProtein StabilityProtein Structure, QuaternaryReceptors, Adenosine A2Receptors, Adrenergic, betaSignal TransductionGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsProtein IsoformsReceptors, Adenosine A2Receptors, Adrenergic, beta

Identifiers

PMID19212142
PMCPMC2836951
OpenAlexW2089086780

What OpenQuestion holds

Textmetadata
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.