Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans.

@article{Arnesen2009ProteomicsAR,
  title={Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans.},
  author={Thomas Arnesen and Petra Van Damme and Bogdan Polevoda and Kenny Helsens and Rune H Evjenth and Niklaas Colaert and Jan Erik Varhaug and Jo{\"e}l Vandekerckhove and Johan Richard Lillehaug and Fred Sherman and Kris Gevaert},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 20},
  pages={8157-62}
}
N(alpha)-terminal acetylation is one of the most common protein modifications in eukaryotes. The COmbined FRActional DIagonal Chromatography (COFRADIC) proteomics technology that can be specifically used to isolate N-terminal peptides was used to determine the N-terminal acetylation status of 742 human and 379 yeast protein N termini, representing the largest eukaryotic dataset of N-terminal acetylation. The major N-terminal acetyltransferase (NAT), NatA, acts on subclasses of proteins with Ser… CONTINUE READING
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