Evidence map›Paper›PMID 30919350›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2019

Using In Vitro Pull-Down and In-Cell Overexpression Assays to Study Protein Interactions with Arrestin.

Nicole A Perry, Xuanzhi Zhan, Eugenia V Gurevich, T M Iverson, Vsevolod V Gurevich

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

5 authors at 2 institutions in 1 country.

Nicole A PerryDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA.
Xuanzhi ZhanDepartment of Chemistry, Tennessee Technological University, Cookeville, TN, USA.
Eugenia V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA.
T M IversonDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA.
Vsevolod V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA. vsevolod.gurevich@vanderbilt.edu.
Vanderbilt University · USTennessee Technological University · US

Funding

STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
Targeted Engineering of Designer Arrestins to Regulate Cell SignalingR35GM122491 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2017 to 2021
$2.6M
Arrestin interactions with non-receptor binding partnersR01GM077561 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2007 to 2015
$2.3M
Molecular basis for arrestin-mediated signalingR01GM120569 · NIGMS · VANDERBILT UNIVERSITY · PI T M Iverson · 2016 to 2026
$1.9M
Signaling regulation in the striatum in Parkinson's diseaseR01NS065868 · NINDS · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2009 to 2013
$1.7M
Regulation of GPCR signaling with receptor-specific arrestinsR01GM109955 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2015 to 2017
$1.1M
Mechanisms of signal bias in arrestinsR21DA043680 · NIDA · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V., IVERSON, T M · 2017 to 2018
$432k
The role of receptor desensitization machinery in psychostimulant addictionR21DA030103 · NIDA · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2011 to 2012
$390k
NanoTemper Monolith NT.115 Microscale Thermophoresis (MST) instrumentS10OD021483 · OD · VANDERBILT UNIVERSITY · PI SPILLER, BENJAMIN W · 2016 to 2016
$136k
NEI NIH HHS R01 EY011500NIDA NIH HHS R21 DA030103NIDA NIH HHS R21 DA043680NIGMS NIH HHS R01 GM077561NIGMS NIH HHS R01 GM109955NIGMS NIH HHS R01 GM120569NIGMS NIH HHS R35 GM122491NINDS NIH HHS R01 NS065868
6 · The paper itself

Abstract

Nonvisual arrestins (arrestin-2/arrestin-3) interact with hundreds of G protein-coupled receptor (GPCR) subtypes and dozens of non-receptor signaling proteins. Here we describe the methods used to identify the interaction sites of arrestin-binding partners on arrestin-3 and the use of monofunctional individual arrestin-3 elements in cells. Our in vitro pull-down assay with purified proteins demonstrates that relatively few elements in arrestin engage each partner, whereas cell-based functional assays indicate that certain arrestin elements devoid of other functionalities can perform individual functions in living cells.

Indexed as

AnimalsArrestinBiological AssayChlorocebus aethiopsCOS CellsHEK293 CellsHumansImmobilized ProteinsMiceProtein BindingProtein Interaction MappingRecombinant Fusion ProteinsArrestinImmobilized ProteinsRecombinant Fusion ProteinsArrestinJNK3 activationMAPKProtein-protein interactions

Identifiers

PMID30919350
PMCPMC7039183
OpenAlexW2933723284

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.