Skip to main content

Protein Lysine Acylation: Abundance, Dynamics and Function

  • Pougovkina O
  • de Boer V
N/ACitations
Citations of this article
7Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Lysine acylation comprises a group of post-translational modifications which involve the transfer of an acyl group to $ε$-amino group of a lysine residue. Most studied acylation modification is acetylation, however recently, a number of new acylation modifications have been discovered. These include formylation, propionylation, butyrylation, malonylation, succinylation, glutarylation and crotonylation. In this chapter, we review the discovery of various acylation modifications and the current insight into their function, regulation and dynamics.

Cite

CITATION STYLE

APA

Pougovkina, O., & de Boer, V. C. J. (2016). Protein Lysine Acylation: Abundance, Dynamics and Function. In Sirtuins (pp. 41–69). Springer Netherlands. https://doi.org/10.1007/978-94-024-0962-8_3

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free