Evidence map›Paper›PMID 24254578›Full record

ArticleJournal of the American Society for Mass Spectrometry2014

High-field asymmetric-waveform ion mobility spectrometry and electron detachment dissociation of isobaric mixtures of glycosaminoglycans.

Muchena J Kailemia, Melvin Park, Desmond A Kaplan, Andre Venot, Geert-Jan Boons, Lingyun Li, Robert J Linhardt, I Jonathan Amster

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Review
  2. Primary open-angle glaucoma: a perspective from plasma metabolomics.Expert review of molecular diagnostics · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Analysis of the Glycosaminoglycan Chains of Proteoglycans.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021
    Review
  12. Volatile Metabolic Markers for MonitoringJournal of microbiology and biotechnology · 2021
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. A Scoring Algorithm for the Automated Analysis of Glycosaminoglycan MS/MS Data.Journal of the American Society for Mass Spectrometry · 2019
    Article
  18. Article
  19. Article
  20. Article
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.

Muchena J KailemiaDepartment of Chemistry, University of Georgia, Athens, GA, 30602, USA.
Melvin Park
Desmond A Kaplan
Andre Venot
Geert-Jan Boons
Lingyun Li
Robert J Linhardt
I Jonathan Amster

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
SEQUENCING THE POLYSACCHARIDE COMPONENT OF PROTEOGLYCANSR01GM038060 · NIGMS · UNIVERSITY OF IOWA · PI LINHARDT, ROBERT J · 1988 to 2012
$2.8M
NIGMS NIH HHS P41 GM103390NIGMS NIH HHS P41-GM103390NIGMS NIH HHS R01 GM038060NIGMS NIH HHS R01-GM038060
6 · The paper itself

Abstract

High-field asymmetric waveform ion mobility spectrometry (FAIMS) is shown to be capable of resolving isomeric and isobaric glycosaminoglycan negative ions and to have great utility for the analysis of this class of molecules when combined with Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) and tandem mass spectrometry. Electron detachment dissociation (EDD) and other ion activation methods for tandem mass spectrometry can be used to determine the sites of labile sulfate modifications and for assigning the stereochemistry of hexuronic acid residues of glycosaminoglycans (GAGs). However, mixtures with overlapping mass-to-charge values present a challenge, as their precursor species cannot be resolved by a mass analyzer prior to ion activation. FAIMS is shown to resolve two types of mass-to-charge overlaps. A mixture of chondroitin sulfate A (CSA) oligomers with 4-10 saccharides units produces ions of a single mass-to-charge by electrospray ionization, as the charge state increases in direct proportion to the degree of polymerization for these sulfated carbohydrates. FAIMS is shown to resolve the overlapping charge. A more challenging type of mass-to-charge overlap occurs for mixtures of diastereomers. FAIMS is shown to separate two sets of epimeric GAG tetramers. For the epimer pairs, the complexity of the separation is reduced when the reducing end is alkylated, suggesting that anomers are also resolved by FAIMS. The resolved components were activated by EDD and the fragment ions were analyzed by FTICR-MS. The resulting tandem mass spectra were able to distinguish the two epimers from each other.

Indexed as

GlycosaminoglycansIsomerismModels, MolecularPrincipal Component AnalysisSpectrometry, Mass, Electrospray IonizationSpectroscopy, Fourier Transform InfraredGlycosaminoglycans

Identifiers

PMID24254578
PMCPMC3946938

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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.