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Journal article

Expansion of the Lysine Acylation Landscape: In memory of Jerzy W. Jaroszewski

By Olsen, Christian A.1,2

From

Department of Chemistry, Technical University of Denmark1

Organic Chemistry, Department of Chemistry, Technical University of Denmark2

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.

Language: English
Publisher: WILEY‐VCH Verlag
Year: 2012
Pages: 3755-3756
ISSN: 15213773 and 14337851
Types: Journal article
DOI: 10.1002/anie.201200316
ORCIDs: 0000-0002-2953-8942
Keywords

Acetylation Crotonylation Epigenetics Protein modifications Succinylation

Other keywords

Acylation Histone Acetyltransferases Histones Humans Lysine Protein Processing, Post-Translational SIRT5 protein, human Sirtuins acetylation crotonylation epigenetics protein modifications succinylation

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