Evidence map›Paper›PMID 32364434›Full record

ArticleSLAS technology2020

Simplifying Glycan Profiling through a High-Throughput Micropermethylation Strategy.

Asif Shajahan, Nitin T Supekar, Digantkumar Chapla, Christian Heiss, Kelley W Moremen, Parastoo Azadi

Abstract read
In one paragraph

Article in SLAS technology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Toward Automatic Inference of Glycan Linkages Using MSJournal of the American Society for Mass Spectrometry · 2023
    Article
  7. Article
  8. Article
  9. 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

6 authors.

Asif ShajahanComplex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA.
Nitin T SupekarComplex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA.
Digantkumar ChaplaComplex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA.
Christian HeissComplex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA.ORCID 0000-0003-1118-8953
Kelley W MoremenComplex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA.
Parastoo AzadiComplex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA.

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
Orbitrap Fusion Tribrid Mass SpectrometerS10OD018530 · OD · UNIVERSITY OF GEORGIA · PI AZADI, PARASTOO · 2014 to 2014
$750k
NIGMS NIH HHS P41 GM103390NIH HHS S10 OD018530
6 · The paper itself

Abstract

Glycoproteins play key roles in various molecular and cellular functions and are among the most difficult to analyze biomolecules on account of their microheterogeneity, non-template-driven synthesis, and low abundances. The stability, serum half-life, immunogenicity, and biological activity of therapeutic glycoproteins, including antibodies, vaccines, and biomarkers, are regulated by their glycosylation profile. Thus, there is increasing demand for the qualitative and quantitative characterization and validation of glycosylation on glycoproteins. One of the most important derivatization processes for the structural characterization of released glycans by mass spectrometry (MS) is permethylation. We have recently developed a permethylation strategy in microscale that allows facile permethylation of glycans and permits the processing of large sample sets in nanogram amounts through high-throughput sample handling. Here, we are reporting the wide potential of micropermethylation-based high-throughput structural analysis of glycans from various sources, including human plasma, mammalian cells, and purified glycoproteins, through an automated tandem electrospray ionization-mass spectrometry (ESI-MSn) platform. The glycans released from the plasma, cells, and glycoproteins are permethylated in microscale in a 96-well plate or microcentrifuge tube and isolated by a C18 tip-based cleanup through a shorter and simple process. We have developed a workflow to accomplish an in-depth automated structural characterization MS program for permethylated N/O-glycans through an automated high-throughput multistage tandem MS acquisition. We have demonstrated the utility of this workflow using the examples of sialic acid linkages and bisecting GlcNAc (

Indexed as

MicrotechnologyAcetylglucosamineAutomationBuffersGlycomicsHEK293 CellsHigh-Throughput Screening AssaysHumansIonsIsomerismMethylationN-Acetylneuraminic AcidPolysaccharidesSolid Phase ExtractionSolutionsSpectrometry, Mass, Electrospray IonizationAcetylglucosamineBuffersIonsN-Acetylneuraminic AcidPolysaccharidesSolutionsautomated ESI-MSglycan branchingglycomicshigh-throughput glycan analysispermethylation

Identifiers

PMID32364434
PMCPMC7931992

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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.