Protein carbonylation, cellular dysfunction, and disease progression
By I. Dalle-Donne, G. Aldini, M. Carini, R. Colombo, R. Rossi, A. Milzani. Journal of Cellular and Molecular Medicine, 2006
850 citations recorded by the source corpus.
Carbonylation of proteins is an irreversible oxidative damage, often leading to a loss of protein function, which is considered a widespread indicator of severe oxidative damage and disease‐derived protein dysfunction. Whereas moderately carbonylated proteins are degraded by the proteasomal system, heavily carbonylated proteins tend to form high‐molecular‐weight aggregates that are resistant to degradation and accumulate as damaged or unfolded proteins. Such aggregates of carbonylated proteins can inhibit proteasome activity. A large number of neurodegenerative diseases are directly associated with the accumulation of proteolysis‐resistant aggregates of carbonylated proteins in tissues. Identification of specific carbonylated protein(s) functionally impaired and development of selective carbonyl blockers should lead to the definitive assessment of the causative, correlative or consequential role of protein carbonylation in disease onset and/or progression, possibly providing new therapeutic aproaches.
Subfields: Clinical Biochemistry, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/4b28b09dc1c8ee2b4f7aa570bc680bd917b64610
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Clinical Biochemistry
In Molecular Biology
In Physiology
Citations in the corpus
- Protein oxidation and peroxidation (2016, background): “The detection of high levels of carbonyls and alcohols in both normal and diseased tissue specimens [122,192] is consistent with the formation of hydroperoxides, with the yield of these species typically being in the low nmol/mg protein range in most cases, though some higher values have also been…”
- Oxidative stress in neurodegenerative diseases (2012, background): “Carbonyl groups can also be introduced in proteins by direct oxidation of lysine, arginine, proline and threonine residues, or from the cleavage of peptide bonds by the α-amidation pathway or by the oxidation of glutamyl residues [44] .”
- Oxidative Stress in Aging Human Skin (2015, background): “At the very least the increased formation of protein carbonyls may overburden the cell’s repair/degradation system resulting in an accumulation of more modified and inactivated proteins [199].”
- Redox Regulation of Cell Survival (2008, neutral): “Protein carbonylation is often used as an indicator for protein oxidations, as it accumulates in vivo at high levels relative to other oxidative modifications and is readily detectable (59).”
- Oxidative Stress Resistance in Deinococcus radiodurans (2011, neutral): “coli, yeast, and Arabidopsis thaliana (116).”