Discovery and characterization of protein-modifying natural products by MALDI mass spectrometry reveal potent SIRT1 and p300 inhibitors

Angew Chem Int Ed Engl. 2013 May 3;52(19):5171-4. doi: 10.1002/anie.201207325. Epub 2013 Apr 8.

Authors

Susanne Holzhauser¹, Anja Freiwald, Christoph Weise, Gerd Multhaup, Chung-Ting Han, Sascha Sauer

Affiliation

¹ Otto Warburg Laboratory, Max Planck Institute for Molecular Genetics, Ihnestrasse 63-73, 14195 Berlin, Germany.

PMID: 23568553
DOI: 10.1002/anie.201207325

No abstract available

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acetylation
Biological Products / pharmacology*
Cells, Cultured
E1A-Associated p300 Protein / antagonists & inhibitors*
E1A-Associated p300 Protein / metabolism
Enzyme Inhibitors / pharmacology*
Heterocyclic Compounds, 4 or More Rings / pharmacology
Humans
Molecular Structure
Monocytes / cytology
Monocytes / drug effects
Monocytes / metabolism
Optical Imaging
Peptide Fragments / metabolism*
Resveratrol
Sirtuin 1 / antagonists & inhibitors*
Sirtuin 1 / metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization*
Stilbenes / pharmacology

Substances

Biological Products
Enzyme Inhibitors
Heterocyclic Compounds, 4 or More Rings
Peptide Fragments
SRT1720
Stilbenes
E1A-Associated p300 Protein
EP300 protein, human
SIRT1 protein, human
Sirtuin 1
Resveratrol