Evidence map›Paper›PMID 23563524›Full record

ArticlemAbs

Rapid and multi-level characterization of trastuzumab using sheathless capillary electrophoresis-tandem mass spectrometry.

Rabah Gahoual, Alicia Burr, Jean-Marc Busnel, Lauriane Kuhn, Phillipe Hammann, Alain Beck, Yannis-Nicolas François, Emmanuelle Leize-Wagner

Open access · goldAbstract 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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
10.6field-weighted citation impact, top 1% 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

20 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Glycoproteomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021
    Article
  4. Review
  5. Article
  6. Assessing Analytical Similarity of Proposed Amgen Biosimilar ABP 501 to Adalimumab.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2016
    Article
  7. Article
  8. Optimal Synthetic Glycosylation of a Therapeutic Antibody.Angewandte Chemie (International ed. in English) · 2016
    Article
  9. Optimal Synthetic Glycosylation of a Therapeutic Antibody.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

8 authors at 5 institutions in 2 countries.

Rabah GahoualLaboratoire de Spectrométrie de Masse des Interactions et des Systèmes (LSMIS); UDS-CNRS UMR 7140; Université de Strasbourg; Strasbourg, France.
Alicia BurrLaboratoire de Spectrométrie de Masse des Interactions et des Systèmes (LSMIS); UDS-CNRS UMR 7140; Université de Strasbourg; Strasbourg, France.
Jean-Marc BusnelBeckman Coulter Inc.; Brea, CA, USA.
Lauriane KuhnPlateforme Protéomique; Université de Strasbourg; Institut de Biologie Moléculaire et Cellulaire; Strasbourg, France.
Phillipe HammannPlateforme Protéomique; Université de Strasbourg; Institut de Biologie Moléculaire et Cellulaire; Strasbourg, France.
Alain BeckCentre d'immunologie Pierre Fabre; Saint-Julien-en-Genevois, France.
Yannis-Nicolas FrançoisLaboratoire de Spectrométrie de Masse des Interactions et des Systèmes (LSMIS); UDS-CNRS UMR 7140; Université de Strasbourg; Strasbourg, France.
Emmanuelle Leize-WagnerLaboratoire de Spectrométrie de Masse des Interactions et des Systèmes (LSMIS); UDS-CNRS UMR 7140; Université de Strasbourg; Strasbourg, France.
Université de Strasbourg · FRInstitut de Biologie Moléculaire et Cellulaire · FRBeckman Coulter Foundation · USCenter of Immunology Pierre Fabre · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoclonal antibodies (mAbs) are highly complex proteins that display a wide range of microheterogeneity that requires multiple analytical methods for full structure assessment and quality control. As a consequence, the characterization of mAbs on different levels is particularly product - and time - consuming. This work presents the characterization of trastuzumab sequence using sheathless capillary electrophoresis (referred as CESI) - tandem mass spectrometry (CESI-MS/MS). Using this bottom-up proteomic-like approach, CESI-MS/MS provided 100% sequence coverage for both heavy and light chain via peptide fragment fingerprinting (PFF) identification. The result was accomplished in a single shot, corresponding to the analysis of 100 fmoles of digest. The same analysis also enabled precise characterization of the post-translational hot spots of trastuzumab, used as a representative widely marketed therapeutic mAb, including the structural confirmation of the five major N-glycoforms.

Indexed as

Electrophoresis, CapillaryTandem Mass SpectrometryAmino Acid SequenceAntibodies, Monoclonal, HumanizedGlycosylationHumansPeptide MappingProtein IsoformsProtein Processing, Post-TranslationalProteomicsTrastuzumabAntibodies, Monoclonal, HumanizedProtein IsoformsTrastuzumabCESI-MS/MSmass spectrometrymicroheterogeneitymicrovariantmonoclonal antibodyN-linked glycosylationpeptide mappingposttranslational modificationssheathless capillary electrophoresis

Identifiers

PMID23563524
PMCPMC4169039
OpenAlexW1985476025

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.