Evidence map›Paper›PMID 32071147›Full record

ArticleMolecular & cellular proteomics : MCP2020

Tandem Mass Tag Approach Utilizing Pervanadate BOOST Channels Delivers Deeper Quantitative Characterization of the Tyrosine Phosphoproteome.

Xien Yu Chua, Theresa Mensah, Timothy Aballo, Samuel G Mackintosh, Ricky D Edmondson, Arthur R Salomon

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.2field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 54 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

6 authors at 2 institutions in 1 country.

Xien Yu ChuaDepartment of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, Rhode Island.
Theresa MensahDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island.
Timothy AballoDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island.
Samuel G MackintoshDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas.
Ricky D EdmondsonDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas.
Arthur R SalomonDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island. Electronic address: art@drsalomon.com.
Brown University · USUniversity of Arkansas for Medical Sciences · US

Funding

Understand the metabolic fitness of naïve T cellsP01AI091580 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JEROEN ROOSE · 2011 to 2026
$31.1M
Translational Regulation in Normal Erythropoiesis and Diamond Blackfan AnemiaP20GM121293 · NIGMS · ARKANSAS CHILDREN'S HOSPITAL RES INST · PI Alan Tackett · 2017 to 2026
$27.6M
Phosphoproteomic Analysis of T Cell Activation PathwaysR01AI083636 · NIAID · BROWN UNIVERSITY · PI SALOMON, ARTHUR ROBERT · 2010 to 2021
$4.0M
NIAID NIH HHS P01 AI091580NIAID NIH HHS R01 AI083636NIGMS NIH HHS P20 GM121293
6 · The paper itself

Abstract

Dynamic tyrosine phosphorylation is fundamental to a myriad of cellular processes. However, the inherently low abundance of tyrosine phosphorylation in the proteome and the inefficient enrichment of phosphotyrosine(pTyr)-containing peptides has led to poor pTyr peptide identification and quantitation, critically hindering researchers' ability to elucidate signaling pathways regulated by tyrosine phosphorylation in systems where cellular material is limited. The most popular approaches to wide-scale characterization of the tyrosine phosphoproteome use pTyr enrichment with pan-specific, anti-pTyr antibodies from a large amount of starting material. Methods that decrease the amount of starting material and increase the characterization depth of the tyrosine phosphoproteome while maintaining quantitative accuracy and precision would enable the discovery of tyrosine phosphorylation networks in rarer cell populations. To achieve these goals, the BOOST (

Indexed as

ProteomicsTandem Mass SpectrometryHumansIonsJurkat CellsPhosphopeptidesPhosphoproteinsPhosphotyrosineProteomeVanadatesIonspervanadatePhosphopeptidesPhosphoproteinsPhosphotyrosineProteomeVanadatesBOOST channellabel-free quantificationomicspervanadatephosphoproteomephosphorylationphosphotyrosine proteomicssuperbinderTandem mass spectrometrytandem mass tag

Identifiers

PMID32071147
PMCPMC7124467
OpenAlexW3007129594

What Socratic 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 Socratic graph.