Evidence map›Paper›PMID 28115169›Full record

ArticleAnalytical biochemistry2017

Development of a bimolecular luminescence complementation assay for RGS: G protein interactions in cells.

Christopher R Bodle, Michael P Hayes, Joseph B O'Brien, David L Roman

Open access · greenAbstract read
In one paragraph

Article in Analytical biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Probing RAS Function Using Monobody and NanoBiT Technologies.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
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  7. Article
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  9. Article
  10. Article
  11. Article
  12. Review
  13. NanoBRET: The Bright Future of Proximity-Based Assays.Frontiers in bioengineering and biotechnology · 2019
    Review
  14. 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

4 authors at 1 institution in 1 country.

Christopher R BodleDepartment of Pharmaceutical Sciences and Experimental Therapeutics University of Iowa, 115 S. Grand Avenue S338 PHAR, Iowa City, IA, 52242, USA. Electronic address: christopher-bodle@uiowa.edu.
Michael P HayesDepartment of Pharmaceutical Sciences and Experimental Therapeutics University of Iowa, 115 S. Grand Avenue S338 PHAR, Iowa City, IA, 52242, USA. Electronic address: michael-p-hayes@uiowa.edu.
Joseph B O'BrienDepartment of Pharmaceutical Sciences and Experimental Therapeutics University of Iowa, 115 S. Grand Avenue S338 PHAR, Iowa City, IA, 52242, USA. Electronic address: Joseph-obrien-1@uiowa.edu.
David L RomanDepartment of Pharmaceutical Sciences and Experimental Therapeutics University of Iowa, 115 S. Grand Avenue S327 PHAR, Iowa City, IA, 52242, USA; Cancer Signaling and Experimental Therapeutics Program, Holden Comprehensive Cancer Center, University of Iowa Hospitals and Clinics, Iowa City, IA, USA. Electronic address: david-roman@uiowa.edu.
University of Iowa · US

Funding

Predoctoral Training in the Pharmacological SciencesT32GM067795 · NIGMS · UNIVERSITY OF IOWA · PI STRACK, STEFAN · 2004 to 2021
$3.4M
Biochemical and Cell-Based HTS Assays for RGS17 InhibitorsR01CA160470 · NCI · UNIVERSITY OF IOWA · PI ROMAN, DAVID L. · 2012 to 2014
$888k
NCI NIH HHS R01 CA160470NIGMS NIH HHS T32 GM067795
6 · The paper itself

Abstract

Cell based assessment tools and screening platforms are the preferred paradigm for small molecule identification and validation due to selectively identifying molecules with cellular activity and validation of compound activity against target proteins in their native environment. With respect to Regulator of G Protein Signaling (RGS) proteins, current cell based methodologies are either low throughput or monitor downstream signaling consequences. The increasing number of reports indicating RGS function in various disease pathogeneses highlights the need for a robust RGS inhibitor discovery and characterization paradigm. Promega's NanoBit Protein Complementation Assay utilizes NanoLuc, an engineered luciferase with enhanced luminescence characteristics which allow for both robust and kinetic assessment of protein interaction formation and disruption. Here we characterized 15 separate RGS: G protein interactions using this system. The binding profile of RGS: Gα interactions correlates to prior published biochemical binding profiles of these proteins. Additionally, we demonstrated this system is suitable for high throughput screening efforts via calculation of Z-factors for three of the interactions and demonstrated that a known small molecule inhibitor of RGS4 disrupts the RGS4: Gα

Indexed as

AnimalsBiological AssayCell LineGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11HumansLuminescent MeasurementsRatsRGS ProteinsGNAI1 protein, humanGNAQ protein, humanGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11RGS ProteinsGα(i1)Gα(q)High throughput screeningNanoBitRGS

Identifiers

PMID28115169
PMCPMC5330260
OpenAlexW2578835417

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.