Evidence map›Paper›PMID 41614148›Full record

ArticleJACS Au2026

Fc Profiling of Polyclonal IgG, IgA and IgM by Light Chain Capturing Coupled with NanoRP-LC-MS.

Yue Li, Sabrina Reusch, Bianca D M van Tol, Fiammetta Di Marco, Anna M Wasynczuk, Steinar Gijze, David Falck, Manfred Wuhrer, Constantin Blöchl, Christoph Gstöttner and 1 more

Abstract read
In one paragraph

Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Yue LiCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.ORCID https://orcid.org/0000-0002-8399-4113
Sabrina ReuschCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.
Bianca D M van TolCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.ORCID https://orcid.org/0000-0001-7486-8652
Fiammetta Di MarcoCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.
Anna M WasynczukCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.
Steinar GijzeCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.
David FalckCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.ORCID https://orcid.org/0000-0003-3908-2376
Manfred WuhrerCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.ORCID https://orcid.org/0000-0002-0814-4995
Constantin BlöchlCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.ORCID https://orcid.org/0000-0003-3406-4232
Christoph GstöttnerCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.
Elena Domínguez-VegaCentre for Proteomics and Metabolomics, Leiden University Medical Centre, PO Box 9600, Leiden, 2300 RC, The Netherlands.ORCID https://orcid.org/0000-0002-6394-0783

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteoform profile of antibody Fc domains determines antibody effector functions, not only for biopharmaceuticals but also for endogenous antibodies. Endogenous immunoglobulin G (IgG) Fc-proteoforms have been well characterized by using different MS-based approaches, comprising bottom-up and intact Fc domain workflows. However, assessment of IgA1 and IgM Fc domains is still challenging, due to the more complex structure, and analyses have been limited to the peptide level only. In this work, a light-chain affinity capturing workflow combined with isotype-specific hinge-region digestion and subsequent intact Fc domain nanoRP-LC-MS analysis has been developed. The novel approach shows very good sensitivity and precision, enabling simultaneous capturing of antibody isotypes with sequential release and analysis of IgG, IgA1 and IgM Fcs from 10 μL of plasma. Single donor human samples were successfully analyzed, providing a comprehensive overview on Fc proteoforms but also on associated Fc-components such as the joining (J) chain of IgA and IgM and CD5L.

Indexed as

antibody isotypesglycosylationmass spectrometrymiddle-up analysisPolyclonal immunoglobulinspost-translational modifications

Identifiers

PMID41614148
PMCPMC12848715

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.