Evidence map›Paper›PMID 28895795›Full record

ArticlemAbs

Glycan characterization of the NIST RM monoclonal antibody using a total analytical solution: From sample preparation to data analysis.

Mark Hilliard, William R Alley, Ciara A McManus, Ying Qing Yu, Sinead Hallinan, John Gebler, Pauline M Rudd

Open access · goldAbstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

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  13. Glycosylation of Therapeutic Proteins: A Critical Quality Attribute.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
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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

7 authors at 2 institutions in 2 countries.

Mark Hilliarda GlycoScience Group, NIBRT-The National Institute for Bioprocessing Research and Training, Foster Avenue, Mount Merrion, Blackrock, Co. Dublin , Ireland.
William R Alleyb Waters Corporation , Milford , MA , USA.
Ciara A McManusa GlycoScience Group, NIBRT-The National Institute for Bioprocessing Research and Training, Foster Avenue, Mount Merrion, Blackrock, Co. Dublin , Ireland.
Ying Qing Yub Waters Corporation , Milford , MA , USA.
Sinead Hallinana GlycoScience Group, NIBRT-The National Institute for Bioprocessing Research and Training, Foster Avenue, Mount Merrion, Blackrock, Co. Dublin , Ireland.
John Geblerb Waters Corporation , Milford , MA , USA.
Pauline M Rudda GlycoScience Group, NIBRT-The National Institute for Bioprocessing Research and Training, Foster Avenue, Mount Merrion, Blackrock, Co. Dublin , Ireland.
National Institute for Bioprocessing Research and Training · IEWaters (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is an important attribute of biopharmaceutical products to monitor from development through production. However, glycosylation analysis has traditionally been a time-consuming process with long sample preparation protocols and manual interpretation of the data. To address the challenges associated with glycan analysis, we developed a streamlined analytical solution that covers the entire process from sample preparation to data analysis. In this communication, we describe the complete analytical solution that begins with a simplified and fast N-linked glycan sample preparation protocol that can be completed in less than 1 hr. The sample preparation includes labelling with RapiFluor-MS tag to improve both fluorescence (FLR) and mass spectral (MS) sensitivities. Following HILIC-UPLC/FLR/MS analyses, the data are processed and a library search based on glucose units has been included to expedite the task of structural assignment. We then applied this total analytical solution to characterize the glycosylation of the NIST Reference Material mAb 8761. For this glycoprotein, we confidently identified 35 N-linked glycans and all three major classes, high mannose, complex, and hybrid, were present. The majority of the glycans were neutral and fucosylated; glycans featuring N-glycolylneuraminic acid and those with two galactoses connected via an α1,3-linkage were also identified.

Indexed as

Analytic Sample Preparation MethodsAntibodies, MonoclonalChromatography, High Pressure LiquidFluorescent DyesGlycoproteinsGlycosylationHumansMass SpectrometryPolysaccharidesReproducibility of ResultsTime FactorsAntibodies, MonoclonalFluorescent DyesGlycoproteinsPolysaccharidesglycan analysisGU libraryHILIC-UPLC/FLR/MSmonoclonal antibodyRapiFluor-MS

Identifiers

PMID28895795
PMCPMC5680791
OpenAlexW2756296675

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.