Evidence map›Paper›PMID 27432553›Full record

ArticleJournal of proteome research2016

Mass Spectrometric Quantification of N-Linked Glycans by Reference to Exogenous Standards.

Nickita Mehta, Mindy Porterfield, Weston B Struwe, Christian Heiss, Parastoo Azadi, Pauline M Rudd, Michael Tiemeyer, Kazuhiro Aoki

Abstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
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  5. Article
  6. Article
  7. ReliableMolecules (Basel, Switzerland) · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Platelet and myeloid cell phenotypes in a rat model of Fabry disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  12. Article
  13. Review
  14. Serum N-Glycome Diversity in Teleost and Chondrostrean Fishes.Frontiers in molecular biosciences · 2021
    Article
  15. Article
  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

8 authors.

Nickita Mehta
Mindy Porterfield
Weston B StruweNational Institute for Bioprocessing Research and Training (NIBRT) , Dublin, Ireland.
Christian Heiss
Parastoo Azadi
Pauline M RuddNational Institute for Bioprocessing Research and Training (NIBRT) , Dublin, Ireland.
Michael Tiemeyer
Kazuhiro Aoki

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BLIXT, OLA KLAS · 2001 to 2010
$80.3M
Treating lung inflammation by targeting SiglecsP01HL107151 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI SCHNAAR, RONALD L · 2011 to 2017
$15.4M
TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
NHLBI NIH HHS P01 HL107151NIGMS NIH HHS P41 GM103490NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Environmental and metabolic processes shape the profile of glycoprotein glycans expressed by cells, whether in culture, developing tissues, or mature organisms. Quantitative characterization of glycomic changes associated with these conditions has been achieved historically by reductive coupling of oligosaccharides to various fluorophores following release from glycoprotein and subsequent HPLC or capillary electrophoretic separation. Such labeling-based approaches provide a robust means of quantifying glycan amount based on fluorescence yield. Mass spectrometry, on the other hand, has generally been limited to relative quantification in which the contribution of the signal intensity for an individual glycan is expressed as a percent of the signal intensity summed over the total profile. Relative quantification has been valuable for highlighting changes in glycan expression between samples; sensitivity is high, and structural information can be derived by fragmentation. We have investigated whether MS-based glycomics is amenable to absolute quantification by referencing signal intensities to well-characterized oligosaccharide standards. We report the qualification of a set of N-linked oligosaccharide standards by NMR, HPLC, and MS. We also demonstrate the dynamic range, sensitivity, and recovery from complex biological matrices for these standards in their permethylated form. Our results indicate that absolute quantification for MS-based glycomic analysis is reproducible and robust utilizing currently available glycan standards.

Indexed as

AnimalsHumansOligosaccharidesPolysaccharidesProteomicsReference StandardsReproducibility of ResultsSensitivity and SpecificitySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationStaining and LabelingOligosaccharidesPolysaccharidesmass spectrometryN-glycanpermethylationquantificationstandard

Identifiers

PMID27432553
PMCPMC5501980

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.