Carbonyl modified proteins in cellular regulation, aging, and disease.
By R. Levine. Free Radical Biology & Medicine, 2002
670 citations recorded by the source corpus.
Subfields: Cell Biology, Clinical Biochemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/225693fa9f03417c83335fe9d362ab4e618d5dfd
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
In Clinical Biochemistry
In Molecular Biology
Citations in the corpus
- Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells. (2004, background): “Proteins can be oxidatively modified, resulting in increases in the level of protein carbonyls (Levine, 2002), oxidized methionines (Stadtman and Levine, 2003) and/or cysteines (Stadtman, 2001; Davies, 2000), protein hydrophobicity (Meucci et al.”
- Cellular response to hyperosmotic stresses. (2007, background): “Instead, they undergo accelerated degradation by proteasomes and are replaced (169).”
- Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean? (2004, methodology): “Carbonyls can also be measured in other body fluids and in tissues (Chapman et al., 1989; Buss et al., 1997; Chevion et al., 2000; Frank et al., 2000; Schock et al., 2001; Levine, 2002; Tanaka et al., 2003).”
- Reactive oxygen species in cancer (2010, background): “Some ROS-induced modifications also increase protein carbonylation, nitration of tyrosine and phenylalanine residues, protein degradation [230], or lead to formation of cross-linked and glycated proteins [231, 232].”
- Biomarkers of oxidative damage in human disease. (2006, background): “As a marker of oxidative damage to proteins, carbonyls have been shown to accumulate during aging, ischemia/reperfusion injury, chronic inflammation, cystic fibrosis, and many of age-related diseases in a variety of organisms (4, 5, 11, 28, 118, 144).”
- Oxidation events and skin aging. (2015, background): “Carbonyl proteins may be regarded as a measure for the degree of oxidative damage and can be detected in a variety of diseases, as well as in aged tissue (Berlett and Stadtman, 1997; Levine, 2002).”
- Role of oxidative carbonylation in protein quality control and senescence (2005, methodology): “Biochemical analysis revealed that carbonyl groups introduced into the side chains of specific amino acids in the active center of the protein trigger the initial steps in the degradation of the enzyme (Levine, 1983, 2002).”
- Oxidative Stress Resistance in Deinococcus radiodurans (2011, background): “radiodurans from oxidative stress is determined by protection against protein oxidation, researchers still argue whether aging and cancer are a consequence of the accumulation of DNA damage (371, 542) or protein damage (117, 353), as both genomic instability and the accumulation of protein damage ar”
- Effects of Ionizing Radiation on Biological Molecules—Mechanisms of Damage and Emerging Methods of Detection (2014, background): “Repair processes for proteins modified by carbonylation have not been identified, and, instead, degradation is believed to be the primary mechanism for cellular regulation of proteome carbonylation (201).”
- Free radical-mediated oxidation of free amino acids and amino acid residues in proteins (2003, background): “Difficulties encoun- tered in the assay of protein carbonyl levels may reflect lack of attention to experimental details (Levine, 2002).”