Evidence map›Paper›PMID 24828102›Full record

ArticleAnalytical chemistry2014

In-depth method for the characterization of glycosylation in manufactured recombinant monoclonal antibody drugs.

Ting Song, Sureyya Ozcan, Alicia Becker, Carlito B Lebrilla

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 48 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Ting SongDepartment of Chemistry, University of California , One Shields Avenue, Davis, California 95616, United States.
Sureyya Ozcan
Alicia Becker
Carlito B Lebrilla
University of California, Davis · US

Funding

The incorporation of human milk oligosaccharides in brain glycoconjugatesR01GM049077 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI LEBRILLA, CARLITO B · 1999 to 2024
$6.3M
NIGMS NIH HHS R01 GM049077NIGMS NIH HHS R01GM049077
6 · The paper itself

Abstract

The glycosylation in recombinant monoclonal antibody (rMab) drugs is a major concern in the biopharmaceutical industry as it impacts the drugs' many attributes. Characterization is important but complicated by the intricate structures, microheterogeneity, and the limitations of current tools for structural analysis. In this study, we developed a liquid chromatography-mass spectrometry (LC-MS) N-glycan library based on eight commercial rMab drugs. A library of over 70 structures was developed for the rapid characterization of rMab. N-Glycans were separated on a porous graphitized carbon (PGC) column incorporated on a chip and then analyzed by an electrospray ionization hybrid quadrupole time-of-flight (ESI-Q-TOF) MS. The retention time and accurate mass for each N-glycan were recorded in the library. The complete structures were obtained through exoglycosidase sequencing. The results showed that most of the N-glycans between different antibodies are nearly the same with different abundances. The utility of this library enables one to identify structures in a rapid manner by matching LC retention times and accurate masses.

Indexed as

Antibodies, MonoclonalBlood ProteinsGlycoproteinsGlycosylationHumansRecombinant ProteinsAntibodies, MonoclonalBlood ProteinsGlycoproteinsRecombinant Proteins

Identifiers

PMID24828102
PMCPMC4066919
OpenAlexW2065595227

What OpenQuestion holds

Textmetadata
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.