Evidence map›Paper›PMID 30479582›Full record

ArticleJournal of biomolecular techniques : JBT2018

Predicting the HILIC Retention Behavior of the N-Linked Glycopeptides Produced by Trypsin Digestion of Immunoglobulin Gs (IgGs).

Majors J Badgett, Emily Mize, Tyler Fletcher, Barry Boyes, Ron Orlando

Open access · diamondAbstract read
In one paragraph

Article in Journal of biomolecular techniques : JBT, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 8 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

5 authors at 2 institutions in 1 country.

Majors J BadgettComplex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA; and.
Emily MizeComplex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA; and.
Tyler FletcherComplex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA; and.
Barry BoyesAdvanced Materials Technology, Wilmington, Delaware 19810, USA.
Ron OrlandoComplex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA; and.
University of Georgia · USAdvanced Materials Technology (United States) · US

Funding

Novel Materials and Methods for Separations of Glycopeptides and GlycansR44GM093747 · NIGMS · ADVANCED MATERIALS TECHNOLOGY, INC. · PI BOYES, BARRY E · 2013 to 2015
$1.2M
Development of Isotopically Labeled Glycoproteins for use as Internal StandardsR42GM113666 · NIGMS · GLYCOSCIENTIFIC, LLC · PI ORLANDO, RON · 2020 to 2021
$697k
Development of Isotopically Labeled Glycoproteins for use as Internal StandardsR41GM113666 · NIGMS · GLYCOSCIENTIFIC, LLC · PI ORLANDO, RON · 2015 to 2015
$270k
Generation of antibodies to monitor Notch O-fucosylation in vivoR41GM119879 · NIGMS · GLYCOSCIENTIFIC, LLC · PI ORLANDO, RON · 2016 to 2016
$242k
NIGMS NIH HHS R41 GM113666NIGMS NIH HHS R41 GM119879NIGMS NIH HHS R42 GM113666NIGMS NIH HHS R44 GM093747
6 · The paper itself

Abstract

The prediction of the retention behavior/time would facilitate the identification and characterization of glycoproteins, particularly the analytical challenges, such as the characterization of low-abundance glycoforms. This task is essential in the biotherapeutics industry, where the type and amount of glycosylation on recombinant IgG alter the efficacy, function, and immunogenicity. Models exist for the prediction of the hydrophilic interaction liquid chromatography retention of peptides and glycans. Here, we have devised a unified model to predict the retention behavior of glycopeptides from human IgGs and applied this to the analysis of glycopeptides from rabbit IgGs. The combined model is capable of accurately predicting the retention of native IgG glycopeptides on 2 completely different liquid chromatography-mass spectrometry systems.

Indexed as

AcetylglucosamineAnimalsChromatography, LiquidGlycopeptidesHumansHydrophobic and Hydrophilic InteractionsImmunoglobulin GMass SpectrometryRabbitsTime FactorsTrypsinAcetylglucosamineGlycopeptidesImmunoglobulin GTrypsin

Identifiers

PMID30479582
PMCPMC6237148
OpenAlexW2907307248

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.