ArticleThe AAPS journal2026
Glycan Profiles of FDA-Approved Therapeutic Antibodies: Insights from Regulatory Submissions.
Article in The AAPS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Article
- Osmolality-Independent Impact of Sodium on Glycosylation of an Fc-Fusion Protein and the Hexosamine Biosynthesis Pathway in a Chinese Hamster Ovary Cell Line.Biotechnology journal · 2026Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation is a critical quality attribute of certain therapeutic proteins, influencing efficacy, safety, and pharmacokinetics. This study analyzed glycan characterization data and drug substance release specifications from 209 Biologics License Applications (BLAs) approved by the U.S. Food and Drug Administration (FDA) through May 2025. Ten predominant Fc N-glycans were identified across IgG antibodies expressed by CHO, NS0, and Sp2/0 cell lines, with six glycans common to all systems. Five low-abundance afucosylated glycans (< 10%) were tightly controlled within drug substance release specifications for antibodies with Fc effector functions, although acceptance criteria varied across products. Glycan profiles were strongly dependent on the expression system: CHO-derived antibodies predominantly contained human-compatible glycan structures, whereas NS0 and Sp2/0 antibodies introduced non-human epitopes. Fc fusion proteins exhibited higher branching and sialylation compared with conventional IgG antibodies. Notably, analysis of product labels revealed that Fc effector functions were described exclusively as in vitro observations or proposed mechanisms, with limited clinical validation. Overall, these findings establish a comprehensive benchmark for glycan profiles of FDA-approved therapeutic antibodies and underscore the need for harmonized control strategies and stronger correlation between in vitro Fc assays and clinical outcomes.
Indexed as
Identifiers
41577853What Socratic 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 Socratic graph.