Evidence map›Paper›PMID 23473665›Full record

ArticleStructure (London, England : 1993)2013

A "new twist" on RGS protein selectivity.

Scott P Heximer

Abstract readComment
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. A bronchoprotective role forAllergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2018
    Article
  2. Article
  3. Digoxin-Mediated Upregulation of RGS2 Protein Protects against Cardiac Injury.The Journal of pharmacology and experimental therapeutics · 2016
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Scott P HeximerDepartment of Physiology, Heart and Stroke/Richard Lewar Centre of Excellence in Cardiovascular Research, University of Toronto, 1 King's College Circle, Toronto, Ontario, Canada. scott.heximer@utoronto.ca

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G protein-coupled receptors mediate a wide array of physiologic stimuli and, together with their regulators such as RGS2, are essential components of cellular signaling and function. RGS2 is a selective inhibitor of the Gαq class of α subunits. In this issue of Structure, Nance and colleagues provide structural insight into the features of RGS2 that mediate its potent and selective regulation of Gαq function.

Identifiers

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.