ArticlemAbs
Correlated analytical and functional evaluation of higher order structure perturbations from oxidation of NISTmAb.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed.
- 2D NMR assessment of structural consistency and functional relationships in monoclonal antibodies.mAbs · 2026Article
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- Stereochemical and Structural Characterization of Methionine Oxidation in the IgG1 Fc Region by Integrated NMR and LC-MS Analysis.Analytical chemistry · 2026Article
- Toward site-specific characterization of structural perturbations on glycosylated Fc using NMR at natural abundance.Journal of biomolecular NMR · 2026Article
- Decoupling Protein Concentration and Aggregate Content Using Diffusion and Water NMR.Analytical chemistry · 2024Article
- Assessing Photostability of mAb Formulations In Situ Using Light-Coupled NMR Spectroscopy.Analytical chemistry · 2024Article
- Integration of NMR Spectroscopy in an Analytical Workflow to Evaluate the Effects of Oxidative Stress on Abituzumab: Beyond the Fingerprint of mAbs.Analytical chemistry · 2023Article
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Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The clinical efficacy and safety of protein-based drugs such as monoclonal antibodies (mAbs) rely on the integrity of the protein higher order structure (HOS) during product development, manufacturing, storage, and patient administration. As mAb-based drugs are becoming more prevalent in the treatment of many illnesses, the need to establish metrics for quality attributes of mAb therapeutics through high-resolution techniques is also becoming evident. To this end, here we used a forced degradation method, time-dependent oxidation by hydrogen peroxide, on the model biotherapeutic NISTmAb and evaluated the effects on HOS with orthogonal analytical methods and a functional assay. To monitor the oxidation process, the experimental workflow involved incubation of NISTmAb with hydrogen peroxide in a benchtop nuclear magnetic resonance spectrometer (NMR) that followed the reaction kinetics, in real-time through the water proton transverse relaxation rate
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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.