Evidence map›Paper›PMID 21449916›Full record

ArticleBritish journal of pharmacology2011

The subtleties of µ-opioid receptor phosphorylation.

Eamonn Kelly

Open access · bronzeAbstract readComment
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 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Eamonn KellySchool of Physiology and Pharmacology, University of Bristol, Bristol, UK. e.kelly@bristol.ac.uk
University of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelledThe link between µ-opioid receptor phosphorylation and function is of critical importance to our understanding of the mechanisms underlying tolerance to opioid drugs. Increasingly sophisticated techniques are needed to assess the phosphorylation status of GPCRs, such as the use of phosphosite-specific antibodies that can monitor the kinetics of phosphorylation and dephosphorylation of individual residues in a receptor. Here the use of phosphosite-specific antibodies, raised against phosphorylated residues in the COOH-terminus of the µ-opioid receptor is discussed, along with some of the important findings that this approach has so far revealed. These include the finding that the µ-opioid receptor is constitutively phosphorylated, and that upon agonist removal it undergoes dephosphorylation equally well whether it is at the cell surface or internalized in endosomes. Thus already these phosphosite-specific antibodies are providing important new information about µ-opioid receptor function and the actions of opioid drugs. LINKED ARTICLE: This article is a commentary on Doll et al., pp. 298-307 of this issue. To view this paper visit http://dx.doi.org/10.1111/j.1476-5381.2011.01382.x.

Indexed as

Analgesics, OpioidAnimalsAntibodies, Phospho-SpecificHumansReceptors, Opioid, muAnalgesics, OpioidAntibodies, Phospho-SpecificReceptors, Opioid, mu

Identifiers

PMID21449916
PMCPMC3174410
OpenAlexW1568113052

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.