Evidence map›Paper›PMID 20448545›Full record

ArticleNature protocols2010

High-performance liquid chromatography-mass spectrometry for mapping and sequencing glycosaminoglycan-derived oligosaccharides.

Nicola Volpi, Robert J Linhardt

Open access · greenAbstract read
In one paragraph

Article in Nature protocols, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 58 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. A high molecular weight hyaluronic acid biphasic dispersion as potential therapeutics for interstitial cystitis.Journal of biomedical materials research. Part B, Applied biomaterials · 2021
    Article
  8. Analysis of the Glycosaminoglycan Chains of Proteoglycans.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Glycosaminoglycanomics: where we are.Glycoconjugate journal · 2017
    Review
  16. Article
  17. 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

2 authors at 2 institutions in 2 countries.

Nicola VolpiDepartment of Biology, University of Modena and Reggio Emilia, Modena, Italy. volpi@unimo.it
Robert J Linhardt
Rensselaer Polytechnic Institute · USUniversity of Modena and Reggio Emilia · IT

Funding

Development of a Bioengineered Heparin from a Non-Animal SourceR01HL096972 · NHLBI · RENSSELAER POLYTECHNIC INSTITUTE · PI DORDICK, JONATHAN S., LINHARDT, ROBERT J · 2009 to 2013
$3.9M
SEQUENCING THE POLYSACCHARIDE COMPONENT OF PROTEOGLYCANSR01GM038060 · NIGMS · UNIVERSITY OF IOWA · PI LINHARDT, ROBERT J · 1988 to 2012
$2.8M
Characterization of Anticoagulant Heparin and Related PolysaccharidesRC2HL101721 · NHLBI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LINHARDT, ROBERT J, SASISEKHARAN, RAM · 2009 to 2010
$1.3M
Metabolic Engineering of Chinese Hamster Ovary Cells for Production of HeparinR01GM090127 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI SHARFSTEIN, SUSAN T · 2009 to 2011
$1.0M
NHLBI NIH HHS HL096972NHLBI NIH HHS HL101721NHLBI NIH HHS R01 HL096972NHLBI NIH HHS RC2 HL101721NIGMS NIH HHS GM090127NIGMS NIH HHS GM38060NIGMS NIH HHS R01 GM038060NIGMS NIH HHS R01 GM090127
6 · The paper itself

Abstract

Glycosaminoglycans (GAGs) have proven to be very difficult to analyze and characterize because of their high negative charge density, polydispersity and sequence heterogeneity. As the specificity of the interactions between GAGs and proteins results from the structure of these polysaccharides, an understanding of GAG structure is essential for developing a structure-activity relationship. Electrospray ionization (ESI) mass spectrometry (MS) is particularly promising for the analysis of oligosaccharides chemically or enzymatically generated by GAGs because of its relatively soft ionization capacity. Furthermore, on-line high-performance liquid chromatography (HPLC)-MS greatly enhances the characterization of complex mixtures of GAG-derived oligosaccharides, providing important structural information and affording their disaccharide composition. A detailed protocol for producing oligosaccharides from various GAGs, using controlled, specific enzymatic or chemical depolymerization, is presented, together with their HPLC separation, using volatile reversed-phase ion-pairing reagents and on-line ESI-MS structural identification. This analysis provides an oligosaccharide map together with sequence information from a reading frame beginning at the nonreducing end of the GAG chains. The preparation of oligosaccharides can be carried out in 10 h, with subsequent HPLC analysis in 1-2 h and HPLC-MS analysis taking another 2 h.

Indexed as

AnimalsBacterial CapsulesCarbohydrate SequenceChromatography, High Pressure LiquidEscherichia coliGlycosaminoglycansMolecular Sequence DataOligosaccharidesSequence AnalysisSpectrometry, Mass, Electrospray Ionizationcapsular polysaccharide K4GlycosaminoglycansOligosaccharides

Identifiers

PMID20448545
PMCPMC3359136
OpenAlexW2018553041

What OpenQuestion holds

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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.