Evidence map›Paper›PMID 23351749›Full record

ArticleMethods in enzymology2013

Expression, purification, and analysis of G-protein-coupled receptor kinases.

Rachel Sterne-Marr, Alison I Baillargeon, Kevin R Michalski, John J G Tesmer

Abstract read
In one paragraph

Article in Methods in enzymology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Rachel Sterne-MarrBiology Department, Siena College, Morrell Science Center, Loudonville, New York, USA.
Alison I Baillargeon
Kevin R Michalski
John J G Tesmer
Siena College · USUniversity of Michigan–Ann Arbor · US

Funding

TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
Structure, function, and inhibition of G protein-coupled receptor kinasesR01HL071818 · NHLBI · UNIVERSITY OF TEXAS AUSTIN · PI TESMER, JOHN · 2004 to 2023
$7.1M
Structural Studies of Galphaq and Its Complexes at the Cell MembraneR01HL086865 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESMER, JOHN · 2007 to 2015
$3.0M
SFG Investigation of Peptide and Protein Orientations in MembranesR01GM081655 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHEN, ZHAN · 2008 to 2012
$1.5M
NHLBI NIH HHS HL071818NHLBI NIH HHS HL086865NHLBI NIH HHS R01 HL071818NHLBI NIH HHS R01 HL086865NIGMS NIH HHS GM081655NIGMS NIH HHS R01 GM081655NIGMS NIH HHS T32 GM008267
6 · The paper itself

Abstract

G-protein-coupled receptor (GPCR) kinases (GRKs) were first identified based on their ability to specifically phosphorylate activated GPCRs. Although many soluble substrates have since been identified, the chief physiological role of GRKs still remains the uncoupling of GPCRs from heterotrimeric G-proteins by promoting β-arrestin binding through the phosphorylation of the receptor. It is expected that GRKs recognize activated GPCRs through a docking site that not only recognizes the active conformation of the transmembrane domain of the receptor but also stabilizes a more catalytically competent state of the kinase domain. Many of the recent gains in understanding GRK-receptor interactions have been gleaned through biochemical and structural analysis of recombinantly expressed GRKs. Described herein are current techniques and procedures being used to express, purify, and assay GRKs in both in vitro and living cells.

Indexed as

AnimalsBaculoviridaeBase SequenceChromatography, AgaroseChromatography, Ion ExchangeCloning, MolecularCrystallizationGenetic VectorsG-Protein-Coupled Receptor KinasesHumansMolecular Sequence DataPhosphorylationRecombinant ProteinsTransfectionG-Protein-Coupled Receptor KinasesRecombinant Proteins

Identifiers

PMID23351749
PMCPMC4297658
OpenAlexW1436642584

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.