Evidence map›Paper›PMID 26229520›Full record

ArticleJournal of biomolecular techniques : JBT2015

Protein Mobility Shifts Contribute to Gel Electrophoresis Liquid Chromatography Analysis.

Nicholas J Carruthers, Graham C Parker, Theresa Gratsch, Joseph A Caruso, Paul M Stemmer

Open access · bronzeAbstract read
In one paragraph

Article in Journal of biomolecular techniques : JBT, 2015. 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
0.3field-weighted citation impact, top 38% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 1 institution in 1 country.

Nicholas J Carruthers1 Institute of Environmental Health Sciences and 2 Carman and Ann Adam Department of Pediatrics, Wayne State University, Detroit, Michigan 48201, USA.
Graham C Parker1 Institute of Environmental Health Sciences and 2 Carman and Ann Adam Department of Pediatrics, Wayne State University, Detroit, Michigan 48201, USA.
Theresa Gratsch1 Institute of Environmental Health Sciences and 2 Carman and Ann Adam Department of Pediatrics, Wayne State University, Detroit, Michigan 48201, USA.
Joseph A Caruso1 Institute of Environmental Health Sciences and 2 Carman and Ann Adam Department of Pediatrics, Wayne State University, Detroit, Michigan 48201, USA.
Paul M Stemmer1 Institute of Environmental Health Sciences and 2 Carman and Ann Adam Department of Pediatrics, Wayne State University, Detroit, Michigan 48201, USA.
Wayne State University · US

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI PAUL M STEMMER · 1985 to 2026
$68.4M
Pilot Project ProgramP30ES020957 · NIEHS · WAYNE STATE UNIVERSITY · PI RUNGE-MORRIS, MELISSA A · 2014 to 2021
$10.1M
Enhancing neoadjuvant chemotherpay responses with targeted T cellsR01CA140314 · NCI · WAYNE STATE UNIVERSITY · PI BEPLER, GEROLD · 2010 to 2015
$2.5M
Orbitrap Velos with ETD for Wayne State ProteomicsS10OD010700 · OD · WAYNE STATE UNIVERSITY · PI STEMMER, PAUL M · 2012 to 2012
$575k
Alpha-synuclein downregulation in Spinal Muscular AtrophyR21NS071339 · NINDS · WAYNE STATE UNIVERSITY · PI PARKER, GRAHAM C · 2011 to 2012
$418k
NCI NIH HHS P30 CA022453NCI NIH HHS R01 CA140314NIEHS NIH HHS P30 ES020957NIH HHS S10 OD010700NINDS NIH HHS 1R21NS071339NINDS NIH HHS R21 NS071339
6 · The paper itself

Abstract

Profiling of cellular and subcellular proteomes by liquid chromatography with tandem mass spectrometry (MS) after fractionation by SDS-PAGE is referred to as GeLC (gel electrophoresis liquid chromatography)-MS. The GeLC approach decreases complexity within individual MS analyses by size fractionation with SDS-PAGE. SDS-PAGE is considered an excellent fractionation technique for intact proteins because of good resolution for proteins of all sizes, isoelectric points, and hydrophobicities. Additional information derived from the mobility of the intact proteins is available after an SDS-PAGE fractionation, but that information is usually not incorporated into the proteomic analysis. Any chemical or proteolytic modification of a protein that changes the mobility of that protein in the gel can be detected. The ability of SDS-PAGE to resolve proteins with chemical modifications has not been widely utilized within profiling experiments. In this work, we examined the ability of the GeLC-MS approach to help identify proteins that were modified after a small hairpin RNA-dependent knockdown in an experiment using stable isotope labeling by amino acids in cell culture-based quantitation.

Indexed as

AnimalsCells, CulturedChromatography, LiquidElectrophoresis, Polyacrylamide GelElectrophoretic Mobility Shift AssayGene Knockdown TechniquesMiceMouse Embryonic Stem CellsPhosphoproteinsProtein Processing, Post-TranslationalProteomeRNA, Small InterferingSurvival of Motor Neuron 1 ProteinTandem Mass SpectrometryPhosphoproteinsProteomeRNA, Small InterferingSmn1 protein, mouseSurvival of Motor Neuron 1 ProteinGeLC-MSmass spectrometryphosphoproteomicsSDS-PAGESILAC

Identifiers

PMID26229520
PMCPMC4512738
OpenAlexW2444315669

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.