Evidence map›Paper›PMID 31630606›Full record

ArticlemAbs

Monitoring glycation levels of a bispecific monoclonal antibody at subunit level by ultrahigh-resolution MALDI FT-ICR mass spectrometry.

Christoph Gstöttner, Dietmar Reusch, Markus Haberger, Irina Dragan, Peter Van Veelen, David P A Kilgour, Yury O Tsybin, Yuri E M van der Burgt, Manfred Wuhrer, Simone Nicolardi

Abstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Top-Down and Middle-Down Mass Spectrometry of Antibodies.Molecular & cellular proteomics : MCP · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. High-throughput antibody screening from complex matrices using intact protein electrospray mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Article
  20. 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

10 authors.

Christoph GstöttnerLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.ORCID 0000-0003-4033-4024
Dietmar ReuschPharma Technical Development Penzberg, Roche Diagnostics GmbH, Penzberg, Germany.
Markus HabergerPharma Technical Development Penzberg, Roche Diagnostics GmbH, Penzberg, Germany.
Irina DraganLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Peter Van VeelenLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
David P A KilgourDepartment of Chemistry, Nottingham Trent University, Nottingham, U.K.ORCID 0000-0002-3860-7532
Yury O TsybinSpectroswiss, EPFL Innovation Park, Lausanne, Switzerland.ORCID 0000-0001-7533-0774
Yuri E M van der BurgtLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Manfred WuhrerLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.ORCID 0000-0002-0814-4995
Simone NicolardiLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.ORCID 0000-0001-8393-1625

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bispecific monoclonal antibodies (BsAbs) are engineered proteins with multiple functionalities and properties. The "bi-specificity" of these complex biopharmaceuticals is a key characteristic for the development of novel and more effective therapeutic strategies. The high structural complexity of BsAbs poses a challenge to the analytical methods needed for their characterization. Modifications of the BsAb structure, resulting from enzymatic and non-enzymatic processes, further complicate the analysis. An important example of the latter type of modification is glycation, which can occur in the manufacturing process, during storage in the formulation or

Indexed as

AngiotensinsAnimalsAntibodies, BispecificAntineoplastic Agents, ImmunologicalBioengineeringCyclotronsFourier AnalysisGlycosylationHumansImmunoglobulin SubunitsMiceSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationVascular Endothelial Growth Factor AAngiotensinsAntibodies, BispecificAntineoplastic Agents, ImmunologicalImmunoglobulin SubunitsVascular Endothelial Growth Factor AVEGFA protein, humanBispecific monoclonal antibodyFT-ICR mass spectrometryglycationIdeS digestionMALDI-ISDmiddle-downmiddle-uppost-translational modificationPTM

Identifiers

PMID31630606
PMCPMC6927770

What OpenQuestion holds

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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.