ArticleBioconjugate chemistry2022
Impact of Drug Conjugation on Thermal and Metabolic Stabilities of Aglycosylated and
Article in Bioconjugate chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Innovative use of therapeutic antibodies in lung cancer: the current landscape of ADCs and other antibody-based therapies.Frontiers in oncology · 2026Review
- Article
- Antibody-Drug Conjugate Stability Probed by Variable-Temperature Electrospray Ionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Glycoscience in Advancing PD-1/PD-L1-Axis-Targeted Tumor Immunotherapy.International journal of molecular sciences · 2025Review
- Technical, preclinical, and clinical developments of Fc-glycan-specific antibody-drug conjugates.RSC medicinal chemistry · 2025Review
- Antibody Drug Conjugates (ADCs): Shaping the Future of Precision Oncology.Anti-cancer agents in medicinal chemistry · 2025Review
- Exploring the next generation of antibody-drug conjugates.Nature reviews. Clinical oncology · 2024Review
- Site-Specific Antibody Conjugation Using Modified BisectedBioconjugate chemistry · 2023Article
- Site-Specific Antibody Conjugation with Payloads beyond Cytotoxins.Molecules (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-linked glycosylation is one of the most common and complex posttranslational modifications that govern the biological functions and physicochemical properties of therapeutic antibodies. We evaluated thermal and metabolic stabilities of antibody-drug conjugates (ADCs) with payloads attached to the C'E loop in the immunoglobulin G (IgG) Fc CH2 domain, comparing the glycosylated and aglycosylated Fc ADC variants. Our study revealed that introduction of small-molecule drugs into an aglycosylated antibody can compensate for thermal destabilization originating from structural distortions caused by elimination of N-linked glycans. Depending on the conjugation site, glycans had both positive and negative effects on plasma stability of ADCs. The findings highlight the importance of consideration for selection of conjugation site to achieve desirable physicochemical properties and plasma stability.
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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.