Evidence map›Paper›PMID 19137549›Full record

ArticleProteomics2009

A chip-based amide-HILIC LC/MS platform for glycosaminoglycan glycomics profiling.

Gregory O Staples, Michael J Bowman, Catherine E Costello, Alicia M Hitchcock, James M Lau, Nancy Leymarie, Christine Miller, Hicham Naimy, Xiaofeng Shi, Joseph Zaia

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
7.1field-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

39 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. [Applications of chromatography in glycomics].Se pu = Chinese journal of chromatography · 2024
    Review
  3. Article
  4. Article
  5. Analysis of the Glycosaminoglycan Chains of Proteoglycans.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Glycosaminoglycan glycomics using mass spectrometry.Molecular & cellular proteomics : MCP · 2013
    Review
  20. Quantitative glycomics strategies.Molecular & cellular proteomics : MCP · 2013
    Review
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

10 authors at 2 institutions in 1 country.

Gregory O StaplesDepartment of Biochemistry, Boston University School of Medicine, Mass Spectrometry Resource, Boston, MA 02118, USA.
Michael J Bowman
Catherine E Costello
Alicia M Hitchcock
James M Lau
Nancy Leymarie
Christine Miller
Hicham Naimy
Xiaofeng Shi
Joseph Zaia
Boston University · USAgilent Technologies (United States) · US

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 1996 to 2011
$18.6M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Glycosaminoglycan-Protein BindingR01HL074197 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2003 to 2006
$1.3M
NCRR NIH HHS P41 RR010888NCRR NIH HHS P41RR10888NHLBI NIH HHS R01 HL074197NHLBI NIH HHS R01HL74197NIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

A key challenge to investigations into the functional roles of glycosaminoglycans (GAGs) in biological systems is the difficulty in achieving sensitive, stable, and reproducible mass spectrometric analysis. GAGs are linear carbohydrates with domains that vary in the extent of sulfation, acetylation, and uronic acid epimerization. It is of particular importance to determine spatial and temporal variations of GAG domain structures in biological tissues. In order to analyze GAGs from tissue, it is useful to couple MS with an on-line separation system. The purposes of the separation system are both to remove components that inhibit GAG ionization and to enable the analysis of very complex mixtures. This contribution presents amide-silica hydrophilic interaction chromatography (HILIC) in a chip-based format for LC/MS of heparin, heparan sulfate (HS) GAGs. The chip interface yields robust performance in the negative ion mode that is essential for GAGs and other acidic glycan classes while the built-in trapping cartridge reduces background from the biological tissue matrix. The HILIC chromatographic separation is based on a combination of the glycan chain lengths and the numbers of hydrophobic acetate (Ac) groups and acidic sulfate groups. In summary, chip based amide-HILIC LC/MS is an enabling technology for GAG glycomics profiling.

Indexed as

AnimalsCattleChromatography, LiquidGlycomicsGlycosaminoglycansHeparan SulfateHydrophobic and Hydrophilic InteractionsSpectrometry, Mass, Electrospray IonizationSwineGlycosaminoglycansHeparan Sulfate

Identifiers

PMID19137549
PMCPMC2771417
OpenAlexW1970128330

What OpenQuestion holds

Textmetadata
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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.