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

Publication: Research - peer-reviewJournal article – Annual report year: 2012

View graph of relations

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.
Original languageEnglish
JournalAngewandte Chemie (International Edition)
Volume51
Issue number16
Pages (from-to)3755-3756
ISSN1433-7851
DOIs
StatePublished - 2012
Peer-reviewedYes

Bibliographical note

Financial support from the Lundbeck Foundation (Young Group Leader Fellowship) and the Danish Independent Research Council – Natural Sciences (Steno Grant No. 10-080907) is gratefully acknowledged.

CitationsWeb of Science® Times Cited: 20

Keywords

  • Acetylation, Crotonylation, Epigenetics, Protein modifications, Succinylation
Download as:
Download as PDF
Select render style:
APAAuthorCBE/CSEHarvardMLAStandardVancouverShortLong
PDF
Download as HTML
Select render style:
APAAuthorCBE/CSEHarvardMLAStandardVancouverShortLong
HTML
Download as Word
Select render style:
APAAuthorCBE/CSEHarvardMLAStandardVancouverShortLong
Word

ID: 7743047