Evidence map›Paper›PMID 27311011›Full record

ArticleAnalytical chemistry2016

Quantitation of Site-Specific Glycosylation in Manufactured Recombinant Monoclonal Antibody Drugs.

Nan Yang, Elisha Goonatilleke, Dayoung Park, Ting Song, Guorong Fan, Carlito B Lebrilla

Registry-linked trialOpen access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03394092 (Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis), which is not on this map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.4field-weighted citation impact, top 4% 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.

NCT03394092 completednot on this mapstarted 2018, after this paper: background citation

Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis

TypeobservationalSponsorThe First Affiliated Hospital of Dalian Medical UniversityRan2018 to 2019Enrolled100ConditionsAcute Coronary SyndromeArmsQuantitative measurements the changes of IgG glycosylation
3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 31 citations in OpenAlex.

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  7. CE-MS for Proteomics and Intact Protein Analysis.Advances in experimental medicine and biology · 2021
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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

6 authors at 2 institutions in 2 countries.

Nan YangSchool of Pharmacy, Second Military Medical University , Guohe Road, Shanghai, 200433, China.
Elisha GoonatillekeDepartment of Chemistry, University of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Dayoung ParkDepartment of Chemistry, University of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Ting SongDepartment of Chemistry, University of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Guorong FanSchool of Pharmacy, Second Military Medical University , Guohe Road, Shanghai, 200433, China.
Carlito B LebrillaDepartment of Chemistry, University of California, Davis , One Shields Avenue, Davis, California 95616, United States.
University of California, Davis · USSecond Military Medical University · CN

Funding

The incorporation of human milk oligosaccharides in brain glycoconjugatesR01GM049077 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI LEBRILLA, CARLITO B · 1999 to 2024
$6.3M
Activation of probiotic bifidobacteria by milk glyansR01AT008759 · NCCIH · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERMAN, BRUCE, LEBRILLA, CARLITO B · 2014 to 2018
$4.2M
Mechanism of Activation of Probiotic Bifidobacteria by Prebiotic Milk GlycansR01AT007079 · NCCIH · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERMAN, BRUCE, LEBRILLA, CARLITO B · 2012 to 2016
$2.2M
NCCIH NIH HHS R01 AT007079NCCIH NIH HHS R01 AT008759NIGMS NIH HHS R01 GM049077
6 · The paper itself

Abstract

During the development of recombinant monoclonal antibody (rMAb) drugs, glycosylation receives particular focus because changes in the attached glycans can have a significant impact on the antibody effector functions. The vast heterogeneity of structures that exist across glycosylation sites hinders the in-depth analysis of glycan changes specific to an individual protein within a complex mixture. In this study, we established a sensitive and specific method for monitoring site-specific glycosylation in rMAbs using multiple reaction monitoring (MRM) on an ultrahigh-performance liquid chromatography-triple quadrupole MS (UHPLC-QqQ-MS). Our results showed that irrespective of the IgG subclass expressed in the drugs, the N-glycopeptide profiles are nearly the same but differ in abundances. In all rMAb drugs, a single subclass of IgG comprised over 97% of the total IgG content and showed over 97% N-glycan site occupancy. This study demonstrates the utility of an MRM-based method to rapidly characterize over 130 distinct glycopeptides and determine the extent of site occupancy within minutes. Such multilevel structural characterization is important for the successful development of therapeutic antibodies.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalChromatography, High Pressure LiquidGlycopeptidesGlycosylationImmunoglobulin GMass SpectrometryPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseRecombinant ProteinsAntibodies, MonoclonalGlycopeptidesImmunoglobulin GPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseRecombinant Proteins

Identifiers

PMID27311011
PMCPMC4955800
OpenAlexW2433026617

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

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.