Evidence map›Paper›PMID 32973813›Full record

ArticleFrontiers in immunology2020

MS-Based Allotype-Specific Analysis of Polyclonal IgG-Fc

Thomas Sénard, Andrea F G Gargano, David Falck, Steven W de Taeye, Theo Rispens, Gestur Vidarsson, Manfred Wuhrer, Govert W Somsen, Elena Domínguez-Vega

Abstract read
In one paragraph

Article in Frontiers in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. High sensitivity glycomics in biomedicine.Mass spectrometry reviews · 2022
    Review
  7. Poly(acrylamide-Analytical chemistry · 2021
    Article
  8. Review
  9. Article
  10. Review
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

9 authors.

Thomas SénardCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.
Andrea F G GarganoVan 't Hoff Institute for Molecular Sciences, University of Amsterdam Analytical Chemistry Group, Amsterdam, Netherlands.
David FalckCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.
Steven W de TaeyeDepartment of Experimental Immunohematology, Sanquin Research, Amsterdam, Netherlands.
Theo RispensDepartment of Immunopathology, Sanquin Research, Amsterdam, Netherlands.
Gestur VidarssonDepartment of Experimental Immunohematology, Sanquin Research, Amsterdam, Netherlands.
Manfred WuhrerCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.
Govert W SomsenAmsterdam Institute for Molecular and Life Sciences (AIMMS), Vrije Universiteit Amsterdam, Amsterdam, Netherlands.
Elena Domínguez-VegaCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Current approaches to study glycosylation of polyclonal human immunoglobulins G (IgG) usually imply protein digestion or glycan release. While these approaches allow in-depth characterization, they also result in a loss of valuable information regarding certain subclasses, allotypes and co-occuring post-translational modifications (PTMs). Unfortunately, the high variability of polyclonal IgGs makes their intact mass spectrometry (MS) analysis extremely challenging. We propose here a middle-up strategy for the analysis of the intact fragment crystallizable (Fc) region of human plasma IgGs, with the aim of acquiring integrated information of the

Indexed as

Mass SpectrometryChromatography, LiquidData AnalysisElectrophoresis, CapillaryGlycosylationHumansImmunoglobulin AllotypesImmunoglobulin Fc FragmentsImmunoglobulin GProtein Processing, Post-TranslationalWorkflowImmunoglobulin AllotypesImmunoglobulin Fc FragmentsImmunoglobulin Gallotypescapillary electrophoresisfragment crystallizablehydrophilic interaction liquid chromatographyimmunoglobulin Gmass spectrometryN-glycosylationpost-translational modifications

Identifiers

PMID32973813
PMCPMC7472933

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.