Evidence map›Paper›PMID 32091889›Full record

ArticleAnalytical chemistry2020

Simultaneous Immunoglobulin A and G Glycopeptide Profiling for High-Throughput Applications.

Ana Momčilović, Noortje de Haan, Agnes L Hipgrave Ederveen, Albert Bondt, Carolien A M Koeleman, David Falck, Louise A de Neef, Wilma E Mesker, Rob Tollenaar, Arnoud de Ru and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

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  19. High-Throughput Glycomic Methods.Chemical reviews · 2022
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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

13 authors at 1 institution in 1 country.

Ana MomčilovićCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Noortje de HaanCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.ORCID 0000-0001-7026-6750
Agnes L Hipgrave EderveenCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Albert BondtCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Carolien A M KoelemanCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
David FalckCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.ORCID 0000-0003-3908-2376
Louise A de NeefCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Wilma E MeskerDepartment of Surgery, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Rob TollenaarDepartment of Surgery, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Arnoud de RuCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Peter van VeelenCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.
Manfred WuhrerCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.ORCID 0000-0002-0814-4995
Viktoria DotzCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2300RC Leiden, The Netherlands.ORCID 0000-0002-9888-7409
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunoglobulin (Ig) glycosylation is recognized for its influence on Ig turnover and effector functions. However, the large-scale profiling of Ig glycosylation in a biomedical setting is challenged by the existence of different Ig isotypes and subclasses, their varying serum concentrations, and the presence of multiple glycosylation sites per Ig. Here, a high-throughput nanoliquid chromatography (LC)- mass spectrometry (MS)-based method for simultaneous analysis of IgG and IgA glycopeptides was developed and applied on a serum sample set from 185 healthy donors. Sample preparation from minute amounts of serum was performed in 96-well plate format. Prior to trypsin digestion, IgG and IgA were enriched simultaneously, followed by a one-step denaturation, reduction, and alkylation. The obtained nanoLC-MS data were subjected to semiautomated, targeted feature integration and quality control. The combined and simplified protocol displayed high overall method repeatability, as assessed using pooled plasma and serum standards. Taking all samples together, 143 individual

Indexed as

High-Throughput Screening AssaysFemaleGlycopeptidesHealthy VolunteersHumansImmunoglobulin AImmunoglobulin GMaleGlycopeptidesImmunoglobulin AImmunoglobulin G

Identifiers

PMID32091889
PMCPMC7252899
OpenAlexW3006972050

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.