Expansion of the lysine acylation landscape.
CA Olsen - Angewandte Chemie (International Ed. In English), 2012 - europepmc.org
Angewandte Chemie (International Ed. In English), 2012•europepmc.org
Leaving marks: the number of known posttranslational modifications for lysine has been
expanded considerably. In addition to acetylation of side-chain amino functionalities of
lysine residues in proteins, crotonylation, succinylation, and malonylation have now been
identified as posttranslational modifications in histone and in non-histone proteins.
expanded considerably. In addition to acetylation of side-chain amino functionalities of
lysine residues in proteins, crotonylation, succinylation, and malonylation have now been
identified as posttranslational modifications in histone and in non-histone proteins.
Leaving marks: the number of known posttranslational modifications for lysine has been expanded considerably. In addition to acetylation of side-chain amino functionalities of lysine residues in proteins, crotonylation, succinylation, and malonylation have now been identified as posttranslational modifications in histone and in non-histone proteins.
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