title: Expansion of the lysine acylation landscape.
abstract: 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.
authors.affiliation: Department of Chemistry, Technical University of Denmark, Lyngby, Denmark. cao@kemi.dtu.dk
authors.forename: Christian A
authors.initials: CA
authors.lastname: Olsen
mesh_terms: D000215:Acylation; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008239:Lysine / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D037761:Sirtuins / Q000737:chemistry / Q000378:metabolism
chemical_list: D006657:Histones; D051548:Histone Acetyltransferases; C508544:SIRT5 protein, human; D037761:Sirtuins; D008239:Lysine