Evidence map›Paper›PMID 28110657›Full record

ReviewAdvances in cancer research2017

MALDI Mass Spectrometry Imaging of N-Linked Glycans in Cancer Tissues.

R R Drake, T W Powers, E E Jones, E Bruner, A S Mehta, P M Angel

Open access · greenAbstract readReview
In one paragraph

Review in Advances in cancer research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
18.8field-weighted citation impact, top 1% 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

83 citing papers in PubMed, 150 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Journal of the American Society for Mass Spectrometry · 2025
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Glycosylation in Cancer.Handbook of experimental pharmacology · 2025
    Review
  15. Article
  16. Review
  17. Protein N -Glycans in Healthy and Sclerotic Glomeruli in Diabetic Kidney Disease.Journal of the American Society of Nephrology : JASN · 2024
    Article
  18. Review
  19. Article
  20. Article

23 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

6 authors at 1 institution in 1 country.

R R DrakeMedical University of South Carolina, Charleston, SC, United States. Electronic address: draker@musc.edu.
T W PowersMedical University of South Carolina, Charleston, SC, United States.
E E JonesMedical University of South Carolina, Charleston, SC, United States.
E BrunerMedical University of South Carolina, Charleston, SC, United States.
A S MehtaMedical University of South Carolina, Charleston, SC, United States.
P M AngelMedical University of South Carolina, Charleston, SC, United States.
Medical University of South Carolina · US

Funding

Direct Tumor Glycan Profiling on Tissue MicroarraysR21CA186799 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI DRAKE, RICHARD R. · 2015 to 2016
$496k
NCI NIH HHS R21 CA186799
6 · The paper itself

Abstract

Glycosylated proteins account for a majority of the posttranslation modifications of cell surface, secreted, and circulating proteins. Within the tumor microenvironment, the presence of immune cells, extracellular matrix proteins, cell surface receptors, and interactions between stroma and tumor cells are all processes mediated by glycan binding and recognition reactions. Changes in glycosylation during tumorigenesis are well documented to occur and affect all of these associated adhesion and regulatory functions. A MALDI imaging mass spectrometry (MALDI-IMS) workflow for profiling N-linked glycan distributions in fresh/frozen tissues and formalin-fixed paraffin-embedded tissues has recently been developed. The key to the approach is the application of a molecular coating of peptide-N-glycosidase to tissues, an enzyme that cleaves asparagine-linked glycans from their protein carrier. The released N-linked glycans can then be analyzed by MALDI-IMS directly on tissue. Generally 40 or more individual glycan structures are routinely detected, and when combined with histopathology localizations, tumor-specific glycans are readily grouped relative to nontumor regions and other structural features. This technique is a recent development and new approach in glycobiology and mass spectrometry imaging research methodology; thus, potential uses such as tumor-specific glycan biomarker panels and other applications are discussed.

Indexed as

AnimalsBiomarkers, TumorGlycosylationHumansImage Processing, Computer-AssistedMolecular ImagingNeoplasmsPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationBiomarkers, TumorPolysaccharidesBiomarkersFormalin-fixed paraffin-embedded tissueFucosylationGlycobiologyGlycomicsGlycoproteinsMALDI imaging mass spectrometryN-linked glycosylationTumor antigens glycoprotein

Identifiers

PMID28110657
PMCPMC6020705
OpenAlexW2560973744

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.