Publikation: Cell-Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP-Ribosylation
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Posttranslational modifications (PTMs) greatly enhance the functional diversity of proteins, surpassing the number of gene‐encoded variations. One intriguing PTM is ADP‐ribosylation, which utilizes nicotinamide adenine dinucleotide (NAD+) as a substrate and is essential in cell signaling pathways regulating cellular responses. Here, we report the first cell‐permeable NAD+ analogs and demonstrate their utility for investigating cellular ADP‐ribosylation. Using a desthiobiotin‐labelled analog for affinity enrichment of proteins that are ADP‐ribosylated in living cells under oxidative stress, we identified protein targets associated with host‐virus interactions, DNA damage and repair, protein biosynthesis, and ribosome biogenesis. Most of these targets have been noted in various literature sources, highlighting the potential of our probes for cellular ADP‐ribosylome studies.
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KASPRZYK, Renata, Sonja RIETH, Peter HEID, Florian STENGEL, Andreas MARX, 2024. Cell-Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP-Ribosylation. In: Angewandte Chemie International Edition. Wiley. 2024, 63(51), e202411203. ISSN 1433-7851. eISSN 1521-3773. Verfügbar unter: doi: 10.1002/anie.202411203BibTex
@article{Kasprzyk2024-12-16CellP-70926, year={2024}, doi={10.1002/anie.202411203}, title={Cell-Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP-Ribosylation}, number={51}, volume={63}, issn={1433-7851}, journal={Angewandte Chemie International Edition}, author={Kasprzyk, Renata and Rieth, Sonja and Heid, Peter and Stengel, Florian and Marx, Andreas}, note={Article Number: e202411203} }
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