Evidence map›Paper›PMID 30103608›Full record

ArticleAnalytical chemistry2018

High-Throughput Phosphorylation Screening and Validation through Ti(IV)-Nanopolymer Functionalized Reverse Phase Phosphoprotein Array.

Ying Zhang, Chunzhao Zhao, Li Li, Chuan-Chih Hsu, Jian-Kang Zhu, Anton Iliuk, W Andy Tao

Open access · greenAbstract readValidation Study
In one paragraph

Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
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

7 authors at 4 institutions in 2 countries.

Ying ZhangShanghai Minhang Hospital and Institutes of Biomedical Sciences , Fudan University , Shanghai 200032 , P. R. China.ORCID 0000-0003-0509-1098
Chunzhao ZhaoDepartment of Horticulture and Landscape Architecture , Purdue University , West Lafayette , Indiana 47907 , United States.
Li LiTymora Analytical Operations , West Lafayette , Indiana 47906 , United States.
Chuan-Chih HsuDepartment of Biochemistry , Purdue University , West Lafayette , Indiana 47907 , United States.
Jian-Kang ZhuDepartment of Horticulture and Landscape Architecture , Purdue University , West Lafayette , Indiana 47907 , United States.
Anton IliukTymora Analytical Operations , West Lafayette , Indiana 47906 , United States.
W Andy TaoDepartment of Biochemistry , Purdue University , West Lafayette , Indiana 47907 , United States.ORCID 0000-0002-5535-5517
Chinese Academy of Sciences · CNPurdue University West Lafayette · USTymora Analytical Operations (United States) · USFudan University · CN

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI Andrea L Kasinski · 1985 to 2026
$43.4M
New Proteomic Technologies for the Analysis of Tyrosine Kinase Signaling PathwaysR01GM088317 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2010 to 2014
$1.6M
Acquisition of a High Resolution Orbitrap Mass Spectrometer for Analysis of ProteS10RR025044 · NCRR · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2009 to 2009
$969k
A Proteomic Platform to identify and Validate Biomarkers in Metabolic Syndrome and Coronary Artery DiseaseR01GM111788 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2015 to 2017
$900k
Multiplexed detection and imaging of protein phosphorylation based on soluble nanopolymersR44CA200040 · NCI · TYMORA ANALYTICAL OPERATIONS, LLC · PI ILIUK, ANTON · 2015 to 2016
$897k
Developing novel RPPA for the detection of metastatic prostate cancerR41CA210772 · NCI · TYMORA ANALYTICAL OPERATIONS, LLC · PI TAO, W. ANDY · 2016 to 2018
$227k
NCI NIH HHS P30 CA023168NCI NIH HHS R41 CA210772NCI NIH HHS R44 CA200040NCRR NIH HHS S10 RR025044NIGMS NIH HHS R01 GM088317NIGMS NIH HHS R01 GM111788
6 · The paper itself

Abstract

Protein phosphorylation is one of the most important and widespread molecular regulatory mechanisms that controls almost all aspects of cellular functions in animals and plants. Here, we introduce a novel chemically functionalized reverse phase phosphoprotein array (RP3A) to capture and measure phosphoproteomes. RP3A uses polyamidoamine (PAMAM) dendrimer immobilized with Ti(IV) ions to functionalize nitrocellulose membrane, facilitating specific chelation of phosphoproteins from complex protein samples on the array. Globular, water-soluble Ti(IV)-dendrimer allows the RP3A surface to be highly accessible to phosphoproteins multidimensionally, and the captured phosphoproteins were subsequently detected using the same validated antibodies as in regular reverse-phase protein arrays. The novel chemical strategy demonstrated superior specificity (1:10 000), high sensitivity (fg level), and good quantitative nature ( R

Indexed as

ArabidopsisArabidopsis ProteinsChromatography, LiquidDatabases, ProteinNanostructuresPhosphoproteinsPhosphorylationPolymersProtein Array AnalysisTandem Mass SpectrometryArabidopsis ProteinsPhosphoproteinsPolymers

Identifiers

PMID30103608
PMCPMC6719555
OpenAlexW2886136466

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.