ArticleJournal of biomolecular screening2015
A Cell-Based Internalization and Degradation Assay with an Activatable Fluorescence-Quencher Probe as a Tool for Functional Antibody Screening.
Article in Journal of biomolecular screening, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- A Method for High-Throughput Screening of Monoclonal Antibody Internalization Using a DNA/Protein Molecular Staple.Small methods · 2025Article
- Recent Advances in Antibody Discovery Using Ultrahigh-Throughput Droplet Microfluidics: Challenges and Future Perspectives.Biosensors · 2025Review
- Long-term retention of antigens in germinal centers is controlled by the spatial organization of the follicular dendritic cell network.Nature immunology · 2023Article
- Quantification of Antibody Persistence for Cell Surface Protein Labeling.Cellular and molecular bioengineering · 2021Article
- Review
- Recent progress in the molecular imaging of therapeutic monoclonal antibodies.Journal of pharmaceutical analysis · 2020Review
- Novel Antibody Drug Conjugates Targeting Tumor-Associated Receptor Tyrosine Kinase ROR2 by Functional Screening of Fully Human Antibody Libraries Using Transpo-mAb Display on Progenitor B Cells.Frontiers in immunology · 2018Article
- A red-emissive antibody-AIEgen conjugate for turn-on and wash-free imaging of specific cancer cells.Chemical science · 2017Article
- Article
- Dose-Dependent Internalization and Externalization Integrity Study of Newly SynthesizedDose-response : a publication of International Hormesis SocietyArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For the development of therapeutically potent anti-cancer antibody drugs, it is often important to identify antibodies that internalize into cells efficiently, rather than just binding to antigens on the cell surface. Such antibodies can mediate receptor endocytosis, resulting in receptor downregulation on the cell surface and potentially inhibiting receptor function and tumor growth. Also, efficient antibody internalization is a prerequisite for the delivery of cytotoxic drugs into target cells and is critical for the development of antibody-drug conjugates. Here we describe a novel activatable fluorescence-quencher pair to quantify the extent of antibody internalization and degradation in the target cells. In this assay, candidate antibodies were labeled with a fluorescent dye and a quencher. Fluorescence is inhibited outside and on the surface of cells, but activated upon endocytosis and degradation of the antibody. This assay enabled the development of a process for rapid characterization of candidate antibodies potentially in a high-throughput format. By employing an activatable secondary antibody, primary antibodies in purified form or in culture supernatants can be screened for internalization and degradation. Because purification of candidate antibodies is not required, this method represents a direct functional screen to identify antibodies that internalize efficiently early in the discovery process.
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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.