Evidence map›Paper›PMID 26378618›Full record

ArticleAnalytical chemistry2015

Integrated glycoprotein immobilization method for glycopeptide and glycan analysis of cardiac hypertrophy.

Shuang Yang, Sumita Mishra, Lijun Chen, Jian-Ying Zhou, Daniel W Chan, Subroto Chatterjee, Hui Zhang

Abstract read
In one paragraph

Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

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  11. βScientific reports · 2017
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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

7 authors at 1 institution in 1 country.

Shuang YangDepartment of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
Sumita MishraDepartment of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
Lijun ChenDepartment of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
Jian-Ying ZhouDepartment of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
Daniel W ChanDepartment of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
Subroto ChatterjeeDepartment of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
Hui ZhangDepartment of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
Johns Hopkins University · US

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Proteome Characterization Center: A Genoproteomics Pipeline for Cance ResearchU24CA160036 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2011 to 2016
$10.7M
Clinical and Analytical Validation of Cancer BiomarkersU24CA115102 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI · 2005 to 2021
$7.4M
Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
Probing the Connections between Monosaccharide Analogs, Sialic Acid Metabolism, aR01CA112314 · NCI · JOHNS HOPKINS UNIVERSITY · PI YAREMA, KEVIN J · 2005 to 2022
$4.5M
NCI NIH HHS R01 CA112314NCI NIH HHS R01CA112314NCI NIH HHS U01 CA152813NCI NIH HHS U01CA152813NCI NIH HHS U24 CA115102NCI NIH HHS U24CA115102NCI NIH HHS U24 CA160036NCI NIH HHS U24CA160036NHLBI NIH HHS N01-HV-00240NHLBI NIH HHS P01 HL107153NHLBI NIH HHS P01HL107153
6 · The paper itself

Abstract

Post-translational modifications of proteins can have a major role in disease initiation and progression. Incredible efforts have recently been made to study the regulation of glycoproteins for disease prognosis and diagnosis. It is essential to elucidate glycans and intact glycoproteins to understand the role of glycosylation in diseases. Sialylated N-glycans play crucial roles in physiological and pathological processes; however, it is laborious to study sialylated glycoproteins due to the labile nature of sialic acid residues. In this study, an integrated platform is developed for the analysis of intact glycoproteins and glycans using a chemoenzymatic approach for immobilization and derivatization of sialic acids. N-Glycans, deglycosylated proteins, and intact glycoproteins from heart tissues of wild type (WT) and transverse aortic constriction (TAC) mouse models were analyzed. We identified 291 unique glycopeptides from 195 glycoproteins; the comparative studies between WT and TAC mice indicate the overexpression of extracellular proteins for heart matrix remodeling and the down-regulation of proteins associated with energy metabolism in cardiac hypertrophy. The integrated platform is a powerful tool for the analysis of glycans and glycoproteins in the discovery of potential cardiac hypertrophy biomarkers.

Indexed as

AnimalsCardiomegalyEnergy MetabolismGlycopeptidesGlycoproteinsMaleMicePolysaccharidesGlycopeptidesGlycoproteinsPolysaccharides

Identifiers

PMID26378618
PMCPMC4592484
OpenAlexW2274749566

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.