ArticleProceedings of the National Academy of Sciences of the United States of America2004
Prodrugs of dynemicin analogs for selective chemotherapy mediated by an aldolase catalytic Ab.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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
9 citing papers in PubMed, 30 citations in OpenAlex.
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- Capturing Biological Activity in Natural Product Fragments by Chemical Synthesis.Angewandte Chemie (International ed. in English) · 2016Review
- Reversible Bergman cyclization by atomic manipulation.Nature chemistry · 2016Article
- Targeting cell surface alpha(v)beta(3) integrin increases therapeutic efficacies of a legumain protease-activated auristatin prodrug.Molecular pharmaceutics · 2012Article
- The legumain protease-activated auristatin prodrugs suppress tumor growth and metastasis without toxicity.ChemMedChem · 2011Article
- Studies toward the duocarmycin prodrugs for the antibody prodrug therapy approach.Tetrahedron letters · 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
- Identification of the adduct between a 4-Aza-3-ene-1,6-diyne and DNA using electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2006Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prodrugs of dynemicin analogs were synthesized, and their activation by aldolase antibody (Ab) 38C2 was evaluated by DNA-cleaving activity, as well as tumor cell growth inhibition. Further, we provide evidence that the activated enediynes underwent covalent crosscoupling with the aldolase Ab, which appears to be a limiting factor of their tumor cell growth-inhibiting activity and should be of general interest in the field of enediyne chemotherapy. These findings might open new avenues for defined conjugations of small molecule drugs to mAbs in general and aldolase Abs in particular.
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