Evidence map›Paper›PMID 26330015›Full record

ReviewBiomarkers in medicine2015

Defining glycoprotein cancer biomarkers by MS in conjunction with glycoprotein enrichment.

Ehwang Song, Yehia Mechref

Abstract readReview
In one paragraph

Review in Biomarkers in medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
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  5. Review
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  9. Review
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  13. Glycosylation and its implications in breast cancer.Expert review of proteomics · 2019
    Review
  14. Review
  15. Article
  16. 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

2 authors.

Ehwang SongDepartment of Chemistry & Biochemistry, Texas Tech University, Lubbock, TX 79409, USA.
Yehia MechrefDepartment of Chemistry & Biochemistry, Texas Tech University, Lubbock, TX 79409, USA.

Funding

Sensitive and Quantitative MS-bases Glycomic Mapping PlatformR01GM112490 · NIGMS · TEXAS TECH UNIVERSITY · PI MECHREF, YEHIA · 2014 to 2024
$3.2M
NIGMS NIH HHS 1R01GM112490-01NIGMS NIH HHS R01 GM112490
6 · The paper itself

Abstract

Protein glycosylation is an important and common post-translational modification. More than 50% of human proteins are believed to be glycosylated to modulate the functionality of proteins. Aberrant glycosylation has been correlated to several diseases, such as inflammatory skin diseases, diabetes mellitus, cardiovascular disorders, rheumatoid arthritis, Alzheimer's and prion diseases, and cancer. Many approved cancer biomarkers are glycoproteins which are not highly abundant proteins. Therefore, effective qualitative and quantitative assessment of glycoproteins entails enrichment methods. This chapter summarizes glycoprotein enrichment methods, including lectin affinity, immunoaffinity, hydrazide chemistry, hydrophilic interaction liquid chromatography, and click chemistry. The use of these enrichment approaches in assessing the qualitative and quantitative changes of glycoproteins in different types of cancers are presented and discussed. This chapter highlights the importance of glycoprotein enrichment techniques for the identification and characterization of new reliable cancer biomarkers.

Indexed as

Biomarkers, TumorGlycoproteinsHumansMass SpectrometryNeoplasmsBiomarkers, TumorGlycoproteinscancer biomarkersclick-chemistry enrichmentglycoprotein enrichmentglycoproteomicsHILIC enrichmenthydrazide chemistryimmunoaffinity-based enrichmentLC-MS/MSlectin chromatography

Identifiers

PMID26330015
PMCPMC4889013

What OpenQuestion holds

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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.