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Journal Article

Discovery and Characterization of Protein-Modifying Natural Products by MALDI Mass Spectrometry Reveal Potent SIRT1 and p300 Inhibitors

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Holzhauser,  Susanne
Nutrigenomics and Gene Regulation (Sascha Sauer), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Freiwald,  Anja
Nutrigenomics and Gene Regulation (Sascha Sauer), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Han,  Chung-Ting
Nutrigenomics and Gene Regulation (Sascha Sauer), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Sauer,  Sascha
Nutrigenomics and Gene Regulation (Sascha Sauer), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Citation

Holzhauser, S., Freiwald, A., Weise, C., Multhaup, G., Han, C.-T., & Sauer, S. (2013). Discovery and Characterization of Protein-Modifying Natural Products by MALDI Mass Spectrometry Reveal Potent SIRT1 and p300 Inhibitors. Angewandte Chemie International Edition, 52(19), 5171-5174. doi:10.1002/anie.201207325.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-112C-0
Abstract
A straightforward MALDI MS method facilitates the unbiased screening and characterization of compounds that modify protein activity. This procedure can be used to circumvent analytical problems deriving from compounds with autofluorescence. Various posttranslationally active enzymes like deacetylases, acetyltransferases, kinases, phosphatases, and methyltransferases can be studied in the presented way.