ArticleProceedings of the National Academy of Sciences of the United States of America1999
Multiple event activation of a generic prodrug trigger by antibody catalysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed.
- Stimuli-Responsive Silsesquioxane Nanozymes for Organocatalysis in Water and Prodrug Activation in Cells.Angewandte Chemie (International ed. in English) · 2026Article
- From Phytotoxin to Cell-Death Probe: Ophiobolin A and Related Sesterterpenoids in Membrane Stress and Non-Apoptotic Cell Death.Molecules (Basel, Switzerland) · 2026Review
- Reactivity of Biliatresone, a Natural Biliary Toxin, with Glutathione, Histamine, and Amino Acids.Chemical research in toxicology · 2016Article
- Preparation and activities of macromolecule conjugates of the CCR5 antagonist Maraviroc.ACS medicinal chemistry letters · 2014Article
- Chemically Programmed Antibodies AS HIV-1 Attachment Inhibitors.ACS medicinal chemistry letters · 2013Article
- Expanding the concept of chemically programmable antibodies to RNA aptamers: chemically programmed biotherapeutics.Angewandte Chemie (International ed. in English) · 2010Article
- Studies toward the duocarmycin prodrugs for the antibody prodrug therapy approach.Tetrahedron letters · 2009Article
- Instant immunity through chemically programmable vaccination and covalent self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Synthesis of the next-generation therapeutic antibodies that combine cell targeting and antibody-catalyzed prodrug activation.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Breaking the one antibody-one target axiom.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Prodrugs of dynemicin analogs for selective chemotherapy mediated by an aldolase catalytic Ab.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Chemically programmed monoclonal antibodies for cancer therapy: adaptor immunotherapy based on a covalent antibody catalyst.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Synthesis of an organoinsulin molecule that can be activated by antibody catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- An active immunization approach to generate protective catalytic antibodies.The Biochemical journal · 2001Article
- In vivo activity in a catalytic antibody-prodrug system: Antibody catalyzed etoposide prodrug activation for selective chemotherapy.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Chemotherapeutic regimes are typically limited by nonspecific toxicity. To address this problem we have developed a broadly applicable drug-masking chemistry that operates in conjunction with a unique broad-scope catalytic antibody. This masking chemistry is applicable to a wide range of drugs because it is compatible with virtually any heteroatom. We demonstrate that generic drug-masking groups may be selectively removed by sequential retro-aldol-retro-Michael reactions catalyzed by antibody 38C2. This reaction cascade is not catalyzed by any known natural enzyme. Application of this masking chemistry to the anticancer drugs doxorubicin and camptothecin produced prodrugs with substantially reduced toxicity. These prodrugs are selectively unmasked by the catalytic antibody when it is applied at therapeutically relevant concentrations. We have demonstrated the efficacy of this approach by using human colon and prostate cancer cell lines. The antibody demonstrated a long in vivo half-life after administration to mice. Based on these findings, we believe that the system described here has the potential to become a key tool in selective chemotherapeutic strategies.
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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.