ArticleBiomolecular NMR assignments2024
Backbone and methyl side-chain resonance assignments of the single chain Fab fragment of trastuzumab.
Article in Biomolecular NMR assignments, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- Complete and Rapid NMR Characterization of Therapeutic Monoclonal Antibodies via Differential Labeling of Fab Fragments inAnalytical chemistry · 2026Article
- An Integrated NMR Approach for Evaluating Linker-Payload Conjugation with Monoclonal Antibodies.Bioconjugate chemistry · 2026Article
- Toward site-specific characterization of structural perturbations on glycosylated Fc using NMR at natural abundance.Journal of biomolecular NMR · 2026Article
- A fast and efficient strategy for the NMR assignment of Fab methyl groups.Journal of biomolecular NMR · 2026Article
- Assessment of ADC Higher Order Structure Through 2D NMR Analysis.Molecules (Basel, Switzerland) · 2025Article
- Backbone and methyl side-chain resonance assignments of the Fab fragment of adalimumab.Biomolecular NMR assignments · 2024Article
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Authors and funding
3 authors.
Funding
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Abstract
Trastuzumab is a therapeutic monoclonal antibody developed to target human epidermal growth factor receptor 2 (HER2) present at higher levels in early cancers. Here we report the near complete resonance assignment of trastuzumab-scFab fragment backbone and the methyl groups of isoleucine, leucine and valine residues, as well as their stereo-assignments. The antibody fragment was produced using a single chain approach in Escherichia coli.
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