ArticlemAbs2014
Versatile characterization of glycosylation modification in CTLA4-Ig fusion proteins by liquid chromatography-mass spectrometry.
Article in mAbs, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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.
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.
Who cites it
24 citing papers in PubMed.
- Post-translational modifications of immune checkpoints: molecular mechanisms, tumor microenvironment remodeling, and therapeutic implications.Journal of biomedical science · 2026Review
- A chemoenzymatic method for simultaneous profiling N- and O-glycans on glycoproteins using one-pot format.Cell reports methods · 2024Article
- Fragmentation stability and retention time-shift obtained by LC-MS/MS to distinguish sialylatedJournal of pharmaceutical analysis · 2023Article
- O-glycosylation and its role in therapeutic proteins.Bioscience reports · 2022Review
- Deep learning explains the biology of branched glycans from single-cell sequencing data.iScience · 2022Article
- Site-Specific Glycan Microheterogeneity Evaluation of Aflibercept Fusion Protein by Glycopeptide-Based LC-MSMS Mapping.International journal of molecular sciences · 2022Article
- An etanercept O-glycovariant with enhanced potency.Molecular therapy. Methods & clinical development · 2022Article
- Comparison of Three Complementary Analytical Techniques for the Evaluation of the Biosimilar Comparability of a Monoclonal Antibody and an Fc-Fusion Protein.Frontiers in chemistry · 2021Article
- At-line high throughput site-specific glycan profiling using targeted mass spectrometry.Biotechnology reports (Amsterdam, Netherlands) · 2020Article
- Computational insights into O-glycosylation in a CTLA4 Fc-fusion protein linker and its impact on protein quality attributes.Computational and structural biotechnology journal · 2020Article
- The Design, Characterizations, and Tumor Angiogenesis Inhibition of a Multi-Epitope Peptibody With bFGF/VEGFA.Frontiers in oncology · 2020Article
- Structure Prediction and Expression of Modified rCTLA4-Ig as a Blocker for B7 Molecules.Iranian journal of pharmaceutical research : IJPR · 2020Article
- Investigation of Site-Specific Differences in Glycan Microheterogeneity by N-Glycopeptide Mapping of VEGFR-IgG Fusion Protein.Molecules (Basel, Switzerland) · 2019Article
- Article
- A novel glycosylated anti-CD20 monoclonal antibody from transgenic cattle.Scientific reports · 2018Article
- Glycans as Key Checkpoints of T Cell Activity and Function.Frontiers in immunology · 2018Review
- Recent advances in mass spectrometric analysis of glycoproteins.Electrophoresis · 2017Review
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- Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CTLA4-Ig is a highly glycosylated therapeutic fusion protein that contains multiple N- and O-glycosylation sites. Glycosylation plays a vital role in protein solubility, stability, serum half-life, activity, and immunogenicity. For a CTLA4-Ig biosimilar development program, comparative analytical data, especially the glycosylation data, can influence decisions about the type and amount of animal and clinical data needed to establish biosimilarity. Because of the limited clinical experience with biosimilars before approval, a comprehensive level of knowledge about the biosimilar candidates is needed to achieve subsequent development. Liquid chromatography-mass spectrometry (LC-MS) is a versatile technique for characterizing N- and O-glycosylation modification of recombinant therapeutic proteins, including 3 levels: intact protein analysis, peptide mapping analysis, and released glycans analysis. In this report, an in-depth characterization of glycosylation of a candidate biosimilar was carried out using a systematic approach: N- and O-linked glycans were identified and electron-transfer dissociation was then used to pinpoint the 4 occupied O-glycosylation sites for the first time. As the results show, the approach provides a set of routine tools that combine accurate intact mass measurement, peptide mapping, and released glycan profiling. This approach can be used to comprehensively research a candidate biosimilar Fc-fusion protein and provides a basis for future studies addressing the similarity of CTLA4-Ig biosimilars.
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Registered trials
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.