Protein carbonylation in human diseases.
By I. Dalle-Donne, D. Giustarini, R. Colombo, R. Rossi, A. Milzani. Trends in Molecular Medicine, 2003
935 citations recorded by the source corpus.
Subfields: Clinical Biochemistry, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/4ebe5e5f9d222a717924e1a6957f734773d18e7e
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Citations in the corpus
- Oxidative Stress Resistance in Deinococcus radiodurans (2011, background): “While there is some evidence that protein oxidation is a cause of cell death in oxidatively stressed bacteria (329), for human cells it is still unclear whether oxidative stress is a cause or a consequence of the primary disease process (117, 337, 465).”
- Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean? (2004, background): “Carbonyls can be readily measured spectrophotometrically and by ELISA techniques (Buss & Winterbourn, 2002; Levine, 2002), and tissue or plasma levels have been shown to be elevated in many human diseases (reviewed by Dalle-Donne et al., 2003).”
- Role of oxidative carbonylation in protein quality control and senescence (2005, background): “Compared to other oxidative modifications, carbonyls are relatively difficult to induce and in contrast to, for example, methionine sulfoxide and cysteine disulfide bond formation, carbonylation is an irreversible oxidative process (Dalle-Donne et al, 2003).”
- 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…”
- Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors (2008, background): “…of carbohydrates are precursors of advanced glycation end products (AGEs) and advanced lipid peroxidation end products (ALEs), which form cross-links on tissular proteins (carbonyl stress), and accumulate during ageing and in chronic diseases (Dalle-Donne et al., 2003; Smit and Lutgers, 2004).”
- Protein carbonylation, cellular dysfunction, and disease progression (2006, background): “The same studies in prokaryotes [32, 33] have raised the possibility that, in AD and other diseases, some proteins are more susceptible to carbonylation because they are misfolded (and, consequently, dysfunctional), rather than being dysfunctional because carbonylation has made them misfolded [16].”
- The role of oxidative stress during inflammatory processes (2013, background): “Oxidized proteins may be subject to accelerated degradation and loss of function, with potentially significant cytotoxic consequences (Dalle-Donne et al., 2003).”
- Effects of Ionizing Radiation on Biological Molecules—Mechanisms of Damage and Emerging Methods of Detection (2014, background): “Increased levels of protein carbonyls have been noted after IR exposure (10 Gy) (310, 317), and in addition, have been implicated in the pathophysiology of many human disease states, including chronic lung disease (357), neurodegenerative diseases (133), diabetes (2), and ischemiareperfusion injury ”