ArticlemAbs2016
Rapid characterization of biotherapeutic proteins by size-exclusion chromatography coupled to native mass spectrometry.
Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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.
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
45 citing papers in PubMed, 137 citations in OpenAlex.
- Using mass spectrometry for robust identity release testing in a global quality control network.mAbs · 2026Article
- Quality by Design to Mitigate Aggregation: Mechanistic Insights and Analytical Strategies for Biopharmaceutical Manufacturing.Therapeutic innovation & regulatory science · 2026Review
- Understanding the Aggregation Mechanism of and Developing Stabilization Strategies for Recombinant Fibroblast Growth Factor 2.Biomolecules · 2026Article
- Article
- Nanoflow Size Exclusion Chromatography-Native Mass Spectrometry of Intact Proteoforms and Protein Complexes.Analytical chemistry · 2025Article
- Characterizing Monoclonal Antibody Aggregation Using Charge Detection Mass Spectrometry and Industry Standard Methods.Journal of the American Society for Mass Spectrometry · 2025Article
- Peptide Property Prediction for Mass Spectrometry Using AI: An Introduction to State of the Art Models.Proteomics · 2025Review
- Current advances in separation chemistry for antibody purification and analysis.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025Review
- Extensive Biotransformation Profiling of AZD8205, an Anti-B7-H4 Antibody-Drug Conjugate, Elucidates Pathways Underlying Its StabilityAnalytical chemistry · 2024Article
- Progress in mass spectrometry approaches to profiling protein-protein interactions in the studies of the innate immune system.Journal of proteins and proteomics · 2024Article
- Influence of pneumatic transportation on the stability of monoclonal antibodies.Scientific reports · 2023Article
- Discovery and Characterization of an Acid-Labile Serine-Lysine Cross-Link in Antibody High-Molecular-Weight Species Using a Multipronged Mass Spectrometry Approach.Analytical chemistry · 2023Article
- Characterizing Non-covalent Protein Complexes Using Asymmetrical Flow Field-Flow Fractionation On-Line Coupled to Native Mass Spectrometry.Analytical chemistry · 2023Article
- Continuous Validation Across Macromolecular Structure Determination Process.Nihon Kessho Gakkai shi · 2023Article
- Analytical Techniques for the Characterization and Quantification of Monoclonal Antibodies.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Identification of Hetero-aggregates in Antibody Co-formulations by Multi-dimensional Liquid Chromatography Coupled to Mass Spectrometry.Analytical chemistry · 2023Article
- Comprehensive Multidimensional Liquid Chromatography-Mass Spectrometry for the Characterization of Charge Variants of a Bispecific Antibody.Journal of the American Society for Mass Spectrometry · 2022Article
- High sensitivity glycomics in biomedicine.Mass spectrometry reviews · 2022Review
- Charting the Proteoform Landscape of Serum Proteins in Individual Donors by High-Resolution Native Mass Spectrometry.Analytical chemistry · 2022Article
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-molecular weight aggregates such as antibody dimers and other side products derived from incorrect light or heavy chain association typically represent critical product-related impurities for bispecific antibody formats. In this study, an approach employing ultra-pressure liquid chromatography size-exclusion separation combined with native electrospray ionization mass spectrometry for the simultaneous formation, identification and quantification of size variants in recombinant antibodies was developed. Samples exposed to storage and elevated temperature(s) enabled the identification of various bispecific antibody size variants. This test system hence allowed us to study the variants formed during formulation and bio-process development, and can thus be transferred to quality control units for routine in-process control and release analytics. In addition, native SEC-UV/MS not only facilitates the detailed analysis of low-abundant and non-covalent size variants during process characterization/validation studies, but is also essential for the SEC-UV method validation prior to admission to the market.
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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.