Evidence map›Paper›PMID 24143209›Full record

ArticlePloS one2013

Identification of N-glycosylation in hepatocellular carcinoma patients' serum with a comparative proteomic approach.

Yingnan Huang, Hao Wu, Ruyi Xue, Taotao Liu, Ling Dong, Jun Yao, Yang Zhang, Xizhong Shen

Abstract readComparative Study
In one paragraph

Article in PloS one, 2013. 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
–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

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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.

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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.

Yingnan HuangDepartment of Gastroenterology, Zhongshan Hospital of Fudan University, Shanghai, China.
Hao Wu
Ruyi Xue
Taotao Liu
Ling Dong
Jun Yao
Yang Zhang
Xizhong Shen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aimThis study is to explore the different expressions of serum N-glycoproteins and glycosylation sites between hepatocellular carcinoma (HCC) patients and healthy controls.

methodWe combined high abundant proteins depletion and hydrophilic affinity method to enrich the glycoproteins. Through liquid chromatography-tandem mass spectrometry (LC-MS/MS), we extensively surveyed different expressions of glycosylation sites and glycoproteins between the two groups.

resultThis approach identified 152 glycosylation sites and 54 glycoproteins expressed differently between HCC patients and healthy controls. With the absolute values of Pearson coefficients of at least 0.8, eight proteins were identified significantly up or down regulated in HCC serum. Those proteins are supposed to be involved in several biological processes, cellular components and molecular functions of hepatocarcinogenesis. Several of them had been reported abnormally regulated in several kinds of malignant tumors, and may be promising biomarkers of HCC.

conclusionOur work provides a systematic and quantitative method of glycoproteomics and demonstrates some key changes in clinical HCC serum. These proteomic signatures may help to unveil the underlying mechanisms of hepatocarcinogenesis and may be useful for the exploration of candidate biomarkers.

Indexed as

ProteomicsAgedCarcinoma, HepatocellularCase-Control StudiesGene OntologyGlycosylationHumansIn Vitro TechniquesLiver NeoplasmsMaleMiddle Aged

Identifiers

PMID24143209
PMCPMC3797089

What OpenQuestion holds

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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.