Evidence map›Paper›PMID 7633949›Full record

ReviewJournal of molecular medicine (Berlin, Germany)1995

Receptors and G proteins as primary components of transmembrane signal transduction. Part 2. G proteins: structure and function.

B Nürnberg, T Gudermann, G Schultz

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
14.6field-weighted citation impact, top 1% 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

17 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. GαOncotarget · 2018
    Article
  3. Article
  4. Article
  5. Article
  6. New vistas in GPCR 3D structure prediction.Journal of molecular modeling · 2010
    Article
  7. Modulation of alpha2-adrenoceptor functions by heterotrimeric Galphai protein isoforms.The Journal of pharmacology and experimental therapeutics · 2009
    Article
  8. G-protein signaling: back to the future.Cellular and molecular life sciences : CMLS · 2005
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. A heterotrimeric G protein complex couples the muscarinic m1 receptor to phospholipase C-beta.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  15. Review
  16. Review
  17. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

B NürnbergInstitut für Pharmakologie, Freie Universität Berlin, Germany.
T Gudermann
G Schultz
Freie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Seven-transmembrane receptors signal through nucleotide-binding proteins (G proteins) into the cell. G proteins are membrane-associated proteins composed of three subunits termed alpha, beta and gamma, of which the G alpha subunit classifies the heterotrimer. So far, 23 different mammalian G alpha subunits are known, which are grouped in four subfamilies (Gs, Gi, Gq, G12) on the basis of their amino acid similarity. They carry an endogenous GTPase activity allowing reversible functional coupling between ligand-bound receptors and effectors such as enzymes and ion channels. In addition, five G beta and seven G gamma subunits have been identified which form tightly associated beta gamma heterodimers. Upon activation by a ligand-bound receptor the G protein dissociates into G alpha and G beta gamma, which both transmit signal by interacting with effectors. On the G protein level, specificity and selectivity of the incoming signal is accomplished by G protein trimers composed of distinct subunits. On the other hand, many receptors have been shown to activate different G proteins, thereby regulating diverse signal transduction pathways.

Indexed as

Signal TransductionAmino Acid SequenceAnimalsGTP-Binding ProteinsMolecular Sequence DataProtein ConformationProtein Processing, Post-TranslationalProtein Structure, SecondaryGTP-Binding Proteins

Identifiers

PMID7633949
OpenAlexW1517658624

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.