Evidence map›Paper›PMID 29680984›Full record

ReviewGlycoconjugate journal2018

Serum sialylation changes in cancer.

Zejian Zhang, Manfred Wuhrer, Stephanie Holst

Open access · hybridAbstract readReview
In one paragraph

Review in Glycoconjugate journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

88 citing papers in PubMed, 182 citations in OpenAlex.

  1. Article
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  5. Expression of 9-Life (Basel, Switzerland) · 2025
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  11. The Human BloodJACS Au · 2024
    Review
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28 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Zejian ZhangCenter for Proteomics and Metabolomics, Leiden University Medical Center, Postzone S3, Postbus 9600, 2300 RC, Leiden, NL, The Netherlands.
Manfred WuhrerCenter for Proteomics and Metabolomics, Leiden University Medical Center, Postzone S3, Postbus 9600, 2300 RC, Leiden, NL, The Netherlands.
Stephanie HolstCenter for Proteomics and Metabolomics, Leiden University Medical Center, Postzone S3, Postbus 9600, 2300 RC, Leiden, NL, The Netherlands. s.holst@lumc.nl.ORCID http://orcid.org/0000-0002-5303-0428
Leiden University Medical Center · NLFudan University · CN

Funding

China Scholarship Council 201606100187H2020 Marie Skłodowska-Curie Actions 676421H2020 Marie Skłodowska-Curie Actions 722095National Key Research and Development Program of China 2016YFA0501303
6 · The paper itself

Abstract

Cancer is a major cause of death in both developing and developed countries. Early detection and efficient therapy can greatly enhance survival. Aberrant glycosylation has been recognized to be one of the hallmarks of cancer as glycans participate in many cancer-associated events. Cancer-associated glycosylation changes often involve sialic acids which play important roles in cell-cell interaction, recognition and immunological response. This review aims at giving a comprehensive overview of the literature on changes of sialylation in serum of cancer patients. Furthermore, the methods available to measure serum and plasma sialic acids as well as possible underlying biochemical mechanisms involved in the serum sialylation changes are surveyed. In general, total serum sialylation levels appear to be increased with various malignancies and show a potential for clinical applications, especially for disease monitoring and prognosis. In addition to overall sialic acid levels and the amount of sialic acid per total protein, glycoprofiling of specific cancer-associated glycoproteins, acute phase proteins and immunoglobulins in serum as well as the measurements of sialylation-related enzymes such as sialidases and sialyltransferases have been reported for early detection of cancer, assessing cancer progression and improving prognosis of cancer patients. Moreover, sialic-acid containing glycan antigens such as CA19-9, sialyl Lewis X and sialyl Tn on serum proteins have also displayed their value in cancer diagnosis and management whereby increased levels of these factors positively correlated with metastasis or poor prognosis.

Indexed as

Protein Processing, Post-TranslationalBiomarkers, TumorHumansNeoplasmsSialic AcidsBiomarkers, TumorSialic AcidsCancer biomarkerGlycosylationSerumSialylation

Identifiers

PMID29680984
PMCPMC5916985
OpenAlexW2799688212

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.