ArticleCatalysts (Basel, Switzerland)2020
Indole C6 Functionalization of Tryprostatin B Using Prenyltransferase CdpNPT.
Article in Catalysts (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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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
6 citing papers in PubMed.
- Chemoenzymatic Modification of Daptomycin: Aromatic Group Installation on Trp1.Chembiochem : a European journal of chemical biology · 2024Article
- Molecular authentication, metabolite profiling and in silico-in vitro cytotoxicity screening of endophytic3 Biotech · 2024Article
- Unlocking New Prenylation Modes: Azaindoles as a New Substrate Class for Indole Prenyltransferases.ChemCatChem · 2023Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides.Angewandte Chemie (International ed. in English) · 2023Article
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Tryprostatin A and B are prenylated, tryptophan-containing, diketopiperazine natural products, displaying cytotoxic activity through different mechanisms of action. The presence of the 6-methoxy substituent on the indole moiety of tryprostatin A was shown to be essential for the dual inhibition of topoisomerase II and tubulin polymerization. However, the inability to perform late-stage modification of the indole ring has limited the structure-activity relationship studies of this class of natural products. Herein, we describe an efficient chemoenzymatic approach for the late-stage modification of tryprostatin B using a cyclic dipeptide
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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 Socratic graph.