Evidence map›Paper›PMID 23251911›Full record

ReviewActa biochimica Polonica2012

G protein-coupled receptors--recent advances.

Dorota Latek, Anna Modzelewska, Bartosz Trzaskowski, Krzysztof Palczewski, Sławomir Filipek

Abstract readReview
In one paragraph

Review in Acta biochimica Polonica, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Pooled it
  2. Review
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  12. Article
  13. Article
  14. Phosphorylation at Serine 21 in G protein-coupled receptor kinase 1 (GRK1) is required for normal kinetics of dark adaption in rod but not cone photoreceptors.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  15. Cannabinoids, Endocannabinoids and Sleep.Frontiers in molecular neuroscience · 2020
    Article
  16. G proteins: binary switches in health and disease.Central-European journal of immunology · 2020
    Article
  17. Article
  18. Review
  19. SeQuery: an interactive graph database for visualizing the GPCR superfamily.Database : the journal of biological databases and curation · 2019
    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

5 authors at 3 institutions in 2 countries.

Dorota LatekBiomodeling Laboratory, International Institute of Molecular and Cell Biology, Warsaw, Poland.
Anna Modzelewska
Bartosz Trzaskowski
Krzysztof Palczewski
Sławomir Filipek
University of Warsaw · PLCase Western Reserve University · USInternational Institute of Molecular and Cell Biology · PL

Funding

REGULATION OF RHODOPSIN KINASE AND GUANYLATE CYCLASER01EY008061 · NEI · UNIVERSITY OF WASHINGTON · PI PALCZEWSKI, KRZYSZTOF · 1994 to 2014
$9.5M
RHODOPSIN KINASE: REGULATION, FUNCTION AND STRUCTURER29EY008061 · NEI · UNIVERSITY OF WASHINGTON · PI PALCZEWSKI, KRZYSZTOF NMI · 1989 to 1993
–
NEI NIH HHS EY008061NEI NIH HHS R01 EY008061
6 · The paper itself

Abstract

The years 2000 and 2007 witnessed milestones in current understanding of G protein-coupled receptor (GPCR) structural biology. In 2000 the first GPCR, bovine rhodopsin, was crystallized and the structure was solved, while in 2007 the structure of β(2)-adrenergic receptor, the first GPCR with diffusible ligands, was determined owing to advances in microcrystallization and an insertion of the fast-folding lysozyme into the receptor. In parallel with those crystallographic studies, the biological and biochemical characterization of GPCRs has advanced considerably because those receptors are molecular targets for many of currently used drugs. Therefore, the mechanisms of activation and signal transduction to the cell interior deduced from known GPCRs structures are of the highest importance for drug discovery. These proteins are the most diversified membrane receptors encoded by hundreds of genes in our genome. They participate in processes responsible for vision, smell, taste and neuronal transmission in response to photons or binding of ions, hormones, peptides, chemokines and other factors. Although the GPCRs share a common seven-transmembrane α-helical bundle structure their binding sites can accommodate thousands of different ligands. The ligands, including agonists, antagonists or inverse agonists change the structure of the receptor. With bound agonists they can form a complex with a suitable G protein, be phosphorylated by kinases or bind arrestin. The discovered signaling cascades invoked by arrestin independently of G proteins makes the GPCR activating scheme more complex such that a ligand acting as an antagonist for G protein signaling can also act as an agonist in arrestin-dependent signaling. Additionally, the existence of multiple ligand-dependent partial activation states as well as dimerization of GPCRs result in a 'microprocessor-like' action of these receptors rather than an 'on-off' switch as was commonly believed only a decade ago.

Indexed as

GTP-Binding ProteinsProtein ConformationReceptors, G-Protein-CoupledAnimalsCattleCrystallography, X-RayDrug DiscoveryHumansLigandsPhosphorylationReceptors, Adrenergic, beta-2RhodopsinSignal TransductionGTP-Binding ProteinsLigandsReceptors, Adrenergic, beta-2Receptors, G-Protein-CoupledRhodopsin

Identifiers

PMID23251911
PMCPMC4322417
OpenAlexW2101445177

What OpenQuestion holds

Textmetadata
LicenceTDM
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.