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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-112C-0 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-112F-A
Genre: Journal Article

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© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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 Creators:
Holzhauser, Susanne1, Author           
Freiwald, Anja1, Author           
Weise, Christoph, Author
Multhaup, Gerd, Author
Han, Chung-Ting1, Author           
Sauer, Sascha1, Author           
Affiliations:
1Nutrigenomics and Gene Regulation (Sascha Sauer), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, Ihnestr. 73, 14195 Berlin, Germany, ou_1479662              

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Free keywords: compound screening; enzymes; MALDI; mass spectrometry; natural products
 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.

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Language(s): eng - English
 Dates: 2013-04-082013-05-03
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201207325
ISSN: 1521-3773 (Electronic)1433-7851 (Print)
URI: http://www.ncbi.nlm.nih.gov/pubmed/23568553
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Title: Angewandte Chemie International Edition
  Other : Angewandte Chemie International Edition in English
  Other : Angewandte Chemie - International Edition
  Abbreviation : Angew. Chem. Int. Ed.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 52 (19) Sequence Number: - Start / End Page: 5171 - 5174 Identifier: Other: 1433-7851
CoNE: https://pure.mpg.de/cone/journals/resource/201310171