Posttranslational modification of proteins

Zsolt Radak*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter


Proteins are subject to continuous reversible and irreversible modifications. These posttranslational modifications directly influence the stability and/or the function of proteins. Aging results in an increased half-life of proteins, which is associated with enhanced oxidative modifications of amino acid residues. Lysine residues are carbonylated, acetylated, and ubiquitinated, and cross talk between these modifications is crucial for the fate of proteins.

Original languageEnglish
Title of host publicationPhysical Activity, Exercise, Sedentary Behavior and Health
PublisherSpringer Japan
Number of pages5
ISBN (Electronic)9784431553335
ISBN (Print)9784431553328
Publication statusPublished - 2015 Jan 1
Externally publishedYes


  • Acetylation
  • Carbonylation
  • Reactive oxygen species
  • Sirtuins
  • Ubiquitination

ASJC Scopus subject areas

  • Medicine(all)
  • Engineering(all)


Dive into the research topics of 'Posttranslational modification of proteins'. Together they form a unique fingerprint.

Cite this