Ontology highlight
ABSTRACT:
SUBMITTER: Curtis JM
PROVIDER: S-EPMC3463318 | biostudies-literature | 2012 Sep
REPOSITORIES: biostudies-literature
Curtis Jessica M JM Hahn Wendy S WS Stone Matthew D MD Inda Jacob J JJ Droullard David J DJ Kuzmicic Jovan P JP Donoghue Margaret A MA Long Eric K EK Armien Anibal G AG Lavandero Sergio S Arriaga Edgar E Griffin Timothy J TJ Bernlohr David A DA
The Journal of biological chemistry 20120721 39
Carbonylation is the covalent, non-reversible modification of the side chains of cysteine, histidine, and lysine residues by lipid peroxidation end products such as 4-hydroxy- and 4-oxononenal. In adipose tissue the effects of such modifications are associated with increased oxidative stress and metabolic dysregulation centered on mitochondrial energy metabolism. To address the role of protein carbonylation in the pathogenesis of mitochondrial dysfunction, quantitative proteomics was employed to ...[more]