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 language | English |
---|---|
Title of host publication | Physical Activity, Exercise, Sedentary Behavior and Health |
Publisher | Springer Japan |
Pages | 165-169 |
Number of pages | 5 |
ISBN (Electronic) | 9784431553335 |
ISBN (Print) | 9784431553328 |
DOIs | |
Publication status | Published - 2015 Jan 1 |
Externally published | Yes |
Keywords
- Acetylation
- Carbonylation
- Reactive oxygen species
- Sirtuins
- Ubiquitination
ASJC Scopus subject areas
- Medicine(all)
- Engineering(all)