Evidence map›Paper›PMID 31859488›Full record

ArticleAnalytical chemistry2020

An Integrated Workflow for Global, Glyco-, and Phospho-proteomic Analysis of Tumor Tissues.

Yangying Zhou, Tung-Shing Mamie Lih, Ganglong Yang, Shao-Yung Chen, Lijun Chen, Daniel W Chan, Hui Zhang, Qing Kay Li

Abstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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  14. Putting the pieces together: mapping the O-glycoproteome.Current opinion in biotechnology · 2021
    Review
  15. Article
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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

8 authors.

Yangying ZhouDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.ORCID 0000-0002-2181-0841
Tung-Shing Mamie LihDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.ORCID 0000-0002-5431-3948
Ganglong YangDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.ORCID 0000-0001-5361-7344
Shao-Yung ChenDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.
Lijun ChenDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.
Daniel W ChanDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.
Hui ZhangDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.ORCID 0000-0001-8726-7098
Qing Kay LiDepartment of Pathology , Johns Hopkins University School of Medicine , Baltimore , Maryland 21231 , United States.

Funding

Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
The Comprehensive Proteome Characterization Center at Johns Hopkins: High Precision Discovery and Confirmation of Genoproteomic TargetsU24CA210985 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2016 to 2020
$5.3M
NCI NIH HHS U01 CA152813NCI NIH HHS U24 CA210985
6 · The paper itself

Abstract

Recently, the rapid development and application of mass spectrometry (MS)-based technologies have markedly improved the comprehensive proteomic characterization of global proteome and protein post-translational modifications (PTMs). However, the current conventional approach for global proteomic analysis is often carried out separately from PTM analysis. In our study, we developed an integrated workflow for multiplex analysis of global, glyco-, and phospho-proteomics using breast cancer patient-derived xenograft (PDX) tumor samples. Our approach included the following steps: trypsin-digested tumor samples were enriched for phosphopeptides through immobilized metal ion affinity chromatography (IMAC), followed by enrichment of glycopeptides through mixed anion exchange (MAX) method, and then the flow-through peptides were analyzed for global proteomics. Our workflow demonstrated an increased identification of peptides and associated proteins in global proteome, as compared to those using the peptides without PTM depletion. In addition to global proteome, the workflow identified phosphopeptides and glycopeptides from the PTM enrichment. We also found a subset of glycans with unique distribution profiles in the IMAC flow-through, as compared to those enriched directly using the MAX method. Our integrated workflow provided an effective platform for simultaneous global proteomic and PTM analysis of biospecimens.

Indexed as

WorkflowAnimalsBreast NeoplasmsChromatography, LiquidGlycopeptidesHeterograftsHumansMicePhosphopeptidesProteolysisProteomeProteomicsTandem Mass SpectrometryTrypsinGlycopeptidesPhosphopeptidesProteomeTrypsin

Identifiers

PMID31859488
PMCPMC7725359

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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.