Evidence map›Paper›PMID 28982002›Full record

ReviewACS chemical neuroscience2018

Glycosylation Changes in Brain Cancer.

Lucas Veillon, Christina Fakih, Hadi Abou-El-Hassan, Firas Kobeissy, Yehia Mechref

Abstract readReview
In one paragraph

Review in ACS chemical neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing 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

80 citing papers in PubMed.

  1. Article
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  5. Review
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  10. Review
  11. Article
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  14. Article
  15. Cancers · 2024
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

20 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

5 authors.

Lucas VeillonDepartment of Chemistry and Biochemistry, Texas Tech University , Lubbock Texas 79409, United States.
Christina FakihDepartment of Biochemistry and Molecular Genetics, Faculty of Medicine, American University of Beirut , Beirut, Lebanon.
Hadi Abou-El-HassanDepartment of Biochemistry and Molecular Genetics, Faculty of Medicine, American University of Beirut , Beirut, Lebanon.
Firas KobeissyDepartment of Biochemistry and Molecular Genetics, Faculty of Medicine, American University of Beirut , Beirut, Lebanon.ORCID 0000-0002-5008-6944
Yehia MechrefDepartment of Chemistry and Biochemistry, Texas Tech University , Lubbock Texas 79409, United States.ORCID 0000-0002-6661-6073

Funding

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

Abstract

Protein glycosylation is a posttranslational modification that affects more than half of all known proteins. Glycans covalently bound to biomolecules modulate their functions by both direct interactions, such as the recognition of glycan structures by binding partners, and indirect mechanisms that contribute to the control of protein conformation, stability, and turnover. The focus of this Review is the discussion of aberrant glycosylation related to brain cancer. Altered sialylation and fucosylation of N- and O-glycans play a role in the development and progression of brain cancer. Additionally, aberrant O-glycan expression has been implicated in brain cancer. This Review also addresses the clinical potential and applications of aberrant glycosylation for the detection and treatment of brain cancer. The viable roles glycans may play in the development of brain cancer therapeutics are addressed as well as cancer-glycoproteomics and personalized medicine. Glycoprotein alterations are considered as a hallmark of cancer while high expression in body fluids represents an opportunity for cancer assessment.

Indexed as

AnimalsBrain NeoplasmsGlycosylationHumansPolysaccharidesPolysaccharidesaberrant glycosylationbone marrow-derived human mesenchymal stem cellsBrain cancercancer stem cellscarcinoembryonic antigencentral nervous systemglioblastomaglioma stem cellsglycosylationhuman mucin familyposttranslational modification of proteinssmall cell lung carcinomas

Identifiers

PMID28982002
PMCPMC5771830

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.