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Expansion of the Lysine Acylation Landscape
Author(s) -
Olsen Christian A.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201200316
Subject(s) - succinylation , lysine , acetylation , acylation , histone , posttranslational modification , biochemistry , chemistry , bromodomain , amino acid , enzyme , dna , gene , catalysis
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.