Evidence map›Paper›PMID 21175569›Full record

ArticleBritish journal of pharmacology2011

Ligand-induced internalization of the orexin OX(1) and cannabinoid CB(1) receptors assessed via N-terminal SNAP and CLIP-tagging.

Richard J Ward, John D Pediani, Graeme Milligan

Open access · bronzeAbstract read
In one paragraph

Article in British journal of pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 11% 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, 38 citations in OpenAlex.

  1. Review
  2. How Carvedilol activates βNature communications · 2022
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  3. Article
  4. Single-molecule labeling for studying trafficking of renal transporters.American journal of physiology. Renal physiology · 2018
    Review
  5. Muscarinic receptor oligomerization.Neuropharmacology · 2018
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Orexin/hypocretin receptor signalling cascades.British journal of pharmacology · 2014
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

3 authors at 1 institution in 1 country.

Richard J WardMolecular Pharmacology Group, Neuroscience and Molecular Pharmacology, Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, UK.
John D Pediani
Graeme Milligan
University of Glasgow · GB

Funding

Medical Research Council G0900050
6 · The paper itself

Abstract

background and purposeMany G protein-coupled receptors internalize following agonist binding. The studies were designed to identify novel means to effectively quantify this process using the orexin OX(1) receptor and the cannabinoid CB(1) receptor as exemplars. EXPERIMENTAL APPROACH: The human OX(1) and CB(1) receptors were modified to incorporate both epitope tags and variants (SNAP and CLIP) of the enzyme O(6)-alkylguanine-DNA-alkyltransferase within their extracellular, N-terminal domain. Cells able to regulate expression of differing amounts of these constructs upon addition of an antibiotic were developed and analysed. KEY

resultsCell surface forms of each receptor construct were detected by both antibody recognition of the epitope tags and covalent binding of fluorophores to the O(6)-alkylguanine-DNA-alkyltransferase variants. Receptor internalization in response to agonists but not antagonists could be monitored by each approach but sensitivity was up to six- to 10-fold greater than other approaches when employing a novel, time-resolved fluorescence probe for the SNAP tag. Sensitivity was not enhanced, however, for the CLIP tag, possibly due to higher levels of nonspecific binding. CONCLUSIONS AND IMPLICATIONS: These studies demonstrate that highly sensitive and quantitative assays that monitor cell surface CB(1) and OX(1) receptors and their internalization by agonists can be developed based on introduction of variants of O(6)-alkylguanine-DNA-alkyltransferase into the N-terminal domain of the receptor. This should be equally suitable for other G protein-coupled receptors.

Indexed as

Alkyl and Aryl TransferasesBenzoxazolesCell LineCell MembraneCloning, MolecularCyclohexanolsExtracellular Signal-Regulated MAP KinasesHumansIntracellular Signaling Peptides and ProteinsLigandsNaphthyridinesNeuropeptidesOrexin ReceptorsOrexinsPhenylurea CompoundsPhosphorylation1-(2-methylbenzoxazol-6-yl)-3-(1,5)naphthyridin-4-yl urea3-(2-hydroxy-4-(1,1-dimethylheptyl)phenyl)-4-(3-hydroxypropyl)cyclohexanolAlkyl and Aryl TransferasesBenzoxazolesCyclohexanolsExtracellular Signal-Regulated MAP KinasesIntracellular Signaling Peptides and ProteinsLigandsNaphthyridinesNeuropeptidesOrexin ReceptorsOrexinsPhenylurea CompoundsPiperidinesPyrazolesPyrrolidinesReceptor, Cannabinoid, CB1Receptors, G-Protein-CoupledReceptors, NeuropeptideRimonabantSB 408124SB674042ThiazolesUrea

Identifiers

PMID21175569
PMCPMC3058174
OpenAlexW1938652716

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.