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January 31, 2016

The team also discovered that acetylation modification occurs primarily on proteins that work together, and that these switches have much greater consequences for the organism's function than previously thought. In one example, the function of Cdc28, an important growth protein in yeast, can be disrupted by the addition of an acetylation button, ultimately affecting the organism's ability to survive.

The results of the team's research were published in the 17 July 2009 edition of Science.

Full bibliographic information: Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

Chunaram Choudhary (1), Chanchal Kumar (2), Florian Gnad (2), Michael L. Nielsen (1), Michael Rehman (3), Tobias Walther (3), Jesper V. Olsen (1), Matthias Mann (1)*

1. Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.; The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen, Denmark. 2. Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany. 3. Organelle Architecture and Dynamics, Max Planck Institute for Biochemistry, Martinsried, Germany

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