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 |
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Keywords
- Acetylation
- Carbonylation
- Reactive oxygen species
- Sirtuins
- Ubiquitination
ASJC Scopus subject areas
- Medicine(all)
- Engineering(all)
Cite this
Posttranslational modification of proteins. / Radak, Zsolt.
Physical Activity, Exercise, Sedentary Behavior and Health. Springer Japan, 2015. p. 165-169.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Posttranslational modification of proteins
AU - Radak, Zsolt
PY - 2015/1/1
Y1 - 2015/1/1
N2 - 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.
AB - 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.
KW - Acetylation
KW - Carbonylation
KW - Reactive oxygen species
KW - Sirtuins
KW - Ubiquitination
UR - http://www.scopus.com/inward/record.url?scp=84943328759&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84943328759&partnerID=8YFLogxK
U2 - 10.1007/978-4-431-55333-5_14
DO - 10.1007/978-4-431-55333-5_14
M3 - Chapter
AN - SCOPUS:84943328759
SN - 9784431553328
SP - 165
EP - 169
BT - Physical Activity, Exercise, Sedentary Behavior and Health
PB - Springer Japan
ER -