Evidence map›Paper›PMID 30130580›Full record

ArticleProtein expression and purification2019

A modified clear-native polyacrylamide gel electrophoresis technique to investigate the oligomeric state of MBP-5-HT

Akash Pandhare, Antonia G Stuebler, Elham Pirayesh, Michaela Jansen

Abstract read
In one paragraph

Article in Protein expression and purification, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Native DIGE for Quantitative and Functional Analysis of Protein Interactomes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  3. Review
  4. CaMolecules (Basel, Switzerland) · 2021
    Article
  5. 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.

Akash PandhareDepartment of Cell Physiology and Molecular Biophysics, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, USA; Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA. Electronic address: akash.pandhare@ttuhsc.edu.
Antonia G StueblerDepartment of Cell Physiology and Molecular Biophysics, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, USA; Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Elham PirayeshDepartment of Cell Physiology and Molecular Biophysics, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, USA; Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Michaela JansenDepartment of Cell Physiology and Molecular Biophysics, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, USA; Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA. Electronic address: michaela.jansen@ttuhsc.edu.

Funding

Probing the structure and function of the intracellular domain of cys-loop receptorsR01NS077114 · NINDS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI JANSEN, MICHAELA · 2014 to 2025
$3.1M
Probing the structure and function of the intracellular domain of cys-loop receptorsR56NS077114 · NINDS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI JANSEN, MICHAELA · 2020 to 2020
$382k
NINDS NIH HHS R01 NS077114NINDS NIH HHS R56 NS077114
6 · The paper itself

Abstract

The main principles of higher-order protein oligomerization are elucidated by many structural and biophysical studies. An astonishing number of proteins self-associate to form dimers or higher-order quaternary structures which further interact with other biomolecules to elicit complex cellular responses. In this study, we describe a simple and convenient approach to determine the oligomeric state of purified protein complexes that combines implementation of a novel form of clear-native gel electrophoresis and size exclusion chromatography in line with multi-angle light scattering. Here, we demonstrate the accuracy of this ensemble approach by characterizing the previously established pentameric state of the intracellular domain of serotonin type 3A (5-HT

Indexed as

Cloning, MolecularDensitometryElectrophoresis, Polyacrylamide GelEscherichia coliGene ExpressionGenetic VectorsHumansLightMaltose-Binding ProteinsProtein Interaction Domains and MotifsProtein MultimerizationReceptors, Serotonin, 5-HT3Recombinant Fusion ProteinsRecombinant ProteinsScattering, RadiationMaltose-Binding ProteinsReceptors, Serotonin, 5-HT3Recombinant Fusion ProteinsRecombinant ProteinsClear-native PAGEMulti-angle light scatteringNative gel electrophoresisProtein oligomerizationProtein quaternary structuresSize exclusion chromatography

Identifiers

PMID30130580
PMCPMC6261512

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Registered trials

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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.