ArticleAnalytical chemistry2018
Chemical Structure and Composition of Major Glycans Covalently Linked to Therapeutic Monoclonal Antibodies by Middle-Down Nuclear Magnetic Resonance.
Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 36 citations in OpenAlex.
- Experimental and computational analysis of glycan processing at increased monoclonal antibody productivities.Metabolic engineering communications · 2026Article
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- Middle-Down Nuclear Magnetic Resonance for Therapeutic Monoclonal Antibody Glycan Profiling.Current protocols · 2025Article
- Assessment of monoclonal antibody glycosylation: a comparative study using HRMS, NMR, and HILIC-FLD.Analytical and bioanalytical chemistry · 2024Article
- The impact of glycosylation on the structure, function, and interactions of CD14.Glycobiology · 2024Article
- The NMR signature of maltose-based glycation in full-length proteins.Journal of biomolecular NMR · 2024Article
- Unambiguous Identification of Glucose-Induced Glycation in mAbs and other Proteins by NMR Spectroscopy.Pharmaceutical research · 2023Article
- A Precise qNMR Method for the Rapid Quantification of Lot-to-Lot Variations in Multiple Quality Attributes of Pentosan Polysulfate Sodium.The AAPS journal · 2023Article
- Analytical Techniques for the Characterization and Quantification of Monoclonal Antibodies.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Primary Structure of Glycans by NMR Spectroscopy.Chemical reviews · 2023Review
- Analytical Similarity Assessment of Biosimilars: Global Regulatory Landscape, Recent Studies and Major Advancements in Orthogonal Platforms.Frontiers in bioengineering and biotechnology · 2022Review
- Comprehensive Assessment of Protein and Excipient Stability in Biopharmaceutical Formulations UsingACS pharmacology & translational science · 2021Article
- Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy.Analytical chemistry · 2020Article
- Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020Review
- Characterizing Post-Translational Modifications and Their Effects on Protein Conformation Using NMR Spectroscopy.Biochemistry · 2020Review
- Regional Metabolic Patterns of Abnormal Postoperative Behavioral Performance in Aged Mice Assessed byNeuroscience bulletin · 2020Article
- Glycoprofile Analysis of an Intact Glycoprotein As Inferred by NMR Spectroscopy.ACS central science · 2019Article
- The NMR signature of gluconoylation: a frequent N-terminal modification of isotope-labeled proteins.Journal of biomolecular NMR · 2019Article
- Unambiguous identification of α-Gal epitopes in intact monoclonal antibodies by NMR spectroscopy.mAbsArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Glycosylation of monoclonal antibodies (mAbs) is a critical quality attribute that can impact mAb drug efficacy and safety. The mAb glycans are inherently heterogeneous in chemical structure and composition of monosaccharides. The established fluorescence or mass-spectrometry (MS) detection methods for glycosylation evaluation may require multiple steps of glycan cleavage or extensive digestion of the mAb, chemical labeling of the glycans, column separation and report the chemical identity of glycans indirectly through retention time and molecular weight values. In demonstrating chemical structure similarity and comparability among mAb drugs, orthogonal analytical methods for measuring glycan chemistry are needed to ensure the quality of drug products. Here, a "middle-down" NMR method is developed as a proof-of-concept approach to measure the domain-specific glycosylation of marketed mAb drugs without cleavage of the glycan moieties. Complete glycan
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What OpenQuestion holds
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.