Posttranslational modification of proteins

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

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
Pages165-169
Number of pages5
ISBN (Electronic)9784431553335
ISBN (Print)9784431553328
DOIs
Publication statusPublished - Jan 1 2015

    Fingerprint

Keywords

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

ASJC Scopus subject areas

  • Medicine(all)
  • Engineering(all)

Cite this

Radak, Z. (2015). Posttranslational modification of proteins. In Physical Activity, Exercise, Sedentary Behavior and Health (pp. 165-169). Springer Japan. https://doi.org/10.1007/978-4-431-55333-5_14